Browse entries in the PDBbind-CN Database
HEADER HYDROLASE/HYDROLASE INHIBITOR 14-SEP-07 2RA3 TITLE HUMAN CATIONIC TRYPSIN COMPLEXED WITH BOVINE PANCREATIC TITLE 2 TRYPSIN INHIBITOR (BPTI) COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRYPSIN-1; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: TRYPSIN I, CATIONIC TRYPSINOGEN, SERINE PROTEASE COMPND 5 1; COMPND 6 EC: 3.4.21.4; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: PANCREATIC TRYPSIN INHIBITOR; COMPND 11 CHAIN: I, C; COMPND 12 SYNONYM: BASIC PROTEASE INHIBITOR, BPI, BPTI, APROTININ SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: PRSS1, TRP1, TRY1, TRYP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3); SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 11 ORGANISM_COMMON: CATTLE; SOURCE 12 ORGANISM_TAXID: 9913; SOURCE 13 STRAIN: A1153 KEYWDS HUMAN CATIONIC TRYPSIN, SERINE PROTEASE, BOVINE PANCREATIC KEYWDS 2 TRYPSIN INHIBITOR, BPTI, CALCIUM, DIGESTION, DISEASE KEYWDS 3 MUTATION, HYDROLASE, METAL-BINDING, SECRETED, SULFATION, KEYWDS 4 ZYMOGEN, PHARMACEUTICAL, PROTEASE INHIBITOR, SERINE KEYWDS 5 PROTEASE INHIBITOR, HYDROLASE/HYDROLASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.A.SALAMEH,A.S.SOARES,E.S.RADISKY REVDAT 4 24-FEB-09 2RA3 1 VERSN REVDAT 3 18-MAR-08 2RA3 1 REMARK REVDAT 2 26-FEB-08 2RA3 1 JRNL REVDAT 1 11-DEC-07 2RA3 0 JRNL AUTH M.A.SALAMEH,A.S.SOARES,A.HOCKLA,E.S.RADISKY JRNL TITL STRUCTURAL BASIS FOR ACCELERATED CLEAVAGE OF JRNL TITL 2 BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) BY JRNL TITL 3 HUMAN MESOTRYPSIN. JRNL REF J.BIOL.CHEM. V. 283 4115 2008 JRNL REFN ISSN 0021-9258 JRNL PMID 18077447 JRNL DOI 10.1074/JBC.M708268200 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.46 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.13 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.8 REMARK 3 NUMBER OF REFLECTIONS : 115064 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.154 REMARK 3 R VALUE (WORKING SET) : 0.153 REMARK 3 FREE R VALUE : 0.178 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 11506 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.34 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.36 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2RA3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-07. REMARK 100 THE RCSB ID CODE IS RCSB044614. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-OCT-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X12B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.95 REMARK 200 MONOCHROMATOR : SI 111 CHANNEL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115118 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460 REMARK 200 RESOLUTION RANGE LOW (A) : 26.144 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.1 REMARK 200 DATA REDUNDANCY : 7.500 REMARK 200 R MERGE (I) : 0.05700 REMARK 200 R SYM (I) : 0.05700 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 46.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.46500 REMARK 200 R SYM FOR SHELL (I) : 0.46500 REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: PDB ENTRIES 1TRN AND 2PTC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HYDROCHLORIDE PH 8.5, REMARK 280 1.6M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 298.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.09350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.09350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 45.59150 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 93.27300 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.59150 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 93.27300 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.09350 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.59150 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 93.27300 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.09350 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.59150 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 93.27300 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 23350 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 40830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -746.2 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 1 -1.000000 0.000000 0.000000 45.59150 REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 -93.27300 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 -45.09350 REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -45.59150 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -93.27300 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -45.09350 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B 340 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY C 57 REMARK 465 ALA C 58 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLU A 23 CD OE1 OE2 REMARK 480 LYS A 236 NZ REMARK 480 ARG C 53 CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR C 23 O HOH C 105 1.94 REMARK 500 O HOH C 71 O HOH C 122 1.98 REMARK 500 O ALA C 25 O HOH C 105 2.01 REMARK 500 O PRO B 128 O HOH B 361 2.11 REMARK 500 O ALA C 27 N LEU C 29 2.11 REMARK 500 CE2 TYR C 23 O HOH C 85 2.14 REMARK 500 NE ARG C 42 O4 SO4 C 60 2.18 REMARK 500 O4 SO4 A 14 O HOH A 346 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OE1 GLN A 64 NH1 ARG C 53 3655 2.10 REMARK 500 OE1 GLN A 64 NH1 ARG C 53 3655 2.17 REMARK 500 OD1 ASN A 34 NH1 ARG C 53 3655 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS A 117 C VAL A 118 N 0.251 REMARK 500 GLU B 74 C GLU B 74 O 0.223 REMARK 500 GLU B 74 C VAL B 75 N 0.186 REMARK 500 GLU B 77 CD GLU B 77 OE2 0.066 REMARK 500 HIS B 117 C VAL B 118 N 0.174 REMARK 500 CYS C 55 CB CYS C 55 SG -0.140 REMARK 500 CYS C 55 CB CYS C 55 SG 0.122 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG B 62 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 GLU B 74 O - C - N ANGL. DEV. = -12.9 DEGREES REMARK 500 ASP B 189 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 ASN C 24 N - CA - C ANGL. DEV. = 29.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 HIS A 71 -65.87 -120.43 REMARK 500 SER A 214 -79.61 -122.79 REMARK 500 ASP B 150 78.23 -153.11 REMARK 500 SER B 214 -76.69 -124.32 REMARK 500 ASN I 44 108.69 -160.33 REMARK 500 PHE C 4 -8.59 -46.41 REMARK 500 ALA C 25 -131.42 51.26 REMARK 500 LYS C 26 33.66 -95.61 REMARK 500 ASN C 44 110.95 -164.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 1 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 70 OE2 REMARK 620 2 ASN A 72 O 89.6 REMARK 620 3 VAL A 75 O 162.0 83.7 REMARK 620 4 GLU A 80 OE2 102.3 160.5 88.9 REMARK 620 5 HOH A 274 O 89.5 83.2 106.2 81.6 REMARK 620 6 HOH A 311 O 79.6 106.8 86.3 90.6 165.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 1 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 70 OE2 REMARK 620 2 ASN B 72 O 87.4 REMARK 620 3 VAL B 75 O 163.3 85.3 REMARK 620 4 GLU B 77 OE2 90.3 82.5 103.6 REMARK 620 5 GLU B 80 OE2 101.6 163.3 89.3 83.4 REMARK 620 6 HOH B 291 O 80.0 103.4 87.1 168.4 92.1 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 6 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 10 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 12 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 14 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 247 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 248 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 249 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 7 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 8 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 11 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 15 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 247 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 248 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 249 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 250 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 59 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 60 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 61 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 62 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 63 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 59 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 60 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2R9P RELATED DB: PDB REMARK 900 HUMAN MESOTRYPSIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN REMARK 900 INHIBITOR DBREF 2RA3 A 16 246 UNP P07477 TRY1_HUMAN 24 247 DBREF 2RA3 B 16 246 UNP P07477 TRY1_HUMAN 24 247 DBREF 2RA3 I 1 58 UNP P00974 BPT1_BOVIN 36 93 DBREF 2RA3 C 1 58 UNP P00974 BPT1_BOVIN 36 93 SEQADV 2RA3 HIS A 117 UNP P07477 ARG 122 ENGINEERED SEQADV 2RA3 ALA A 195 UNP P07477 SER 200 ENGINEERED SEQADV 2RA3 HIS B 117 UNP P07477 ARG 122 ENGINEERED SEQADV 2RA3 ALA B 195 UNP P07477 SER 200 ENGINEERED SEQRES 1 A 224 ILE VAL GLY GLY TYR ASN CYS GLU GLU ASN SER VAL PRO SEQRES 2 A 224 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY SEQRES 3 A 224 GLY SER LEU ILE ASN GLU GLN TRP VAL VAL SER ALA GLY SEQRES 4 A 224 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU SEQRES 5 A 224 HIS ASN ILE GLU VAL LEU GLU GLY ASN GLU GLN PHE ILE SEQRES 6 A 224 ASN ALA ALA LYS ILE ILE ARG HIS PRO GLN TYR ASP ARG SEQRES 7 A 224 LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER SEQRES 8 A 224 SER ARG ALA VAL ILE ASN ALA HIS VAL SER THR ILE SER SEQRES 9 A 224 LEU PRO THR ALA PRO PRO ALA THR GLY THR LYS CYS LEU SEQRES 10 A 224 ILE SER GLY TRP GLY ASN THR ALA SER SER GLY ALA ASP SEQRES 11 A 224 TYR PRO ASP GLU LEU GLN CYS LEU ASP ALA PRO VAL LEU SEQRES 12 A 224 SER GLN ALA LYS CYS GLU ALA SER TYR PRO GLY LYS ILE SEQRES 13 A 224 THR SER ASN MET PHE CYS VAL GLY PHE LEU GLU GLY GLY SEQRES 14 A 224 LYS ASP SER CYS GLN GLY ASP ALA GLY GLY PRO VAL VAL SEQRES 15 A 224 CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY ASP SEQRES 16 A 224 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS SEQRES 17 A 224 VAL TYR ASN TYR VAL LYS TRP ILE LYS ASN THR ILE ALA SEQRES 18 A 224 ALA ASN SER SEQRES 1 B 224 ILE VAL GLY GLY TYR ASN CYS GLU GLU ASN SER VAL PRO SEQRES 2 B 224 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY SEQRES 3 B 224 GLY SER LEU ILE ASN GLU GLN TRP VAL VAL SER ALA GLY SEQRES 4 B 224 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU SEQRES 5 B 224 HIS ASN ILE GLU VAL LEU GLU GLY ASN GLU GLN PHE ILE SEQRES 6 B 224 ASN ALA ALA LYS ILE ILE ARG HIS PRO GLN TYR ASP ARG SEQRES 7 B 224 LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER SEQRES 8 B 224 SER ARG ALA VAL ILE ASN ALA HIS VAL SER THR ILE SER SEQRES 9 B 224 LEU PRO THR ALA PRO PRO ALA THR GLY THR LYS CYS LEU SEQRES 10 B 224 ILE SER GLY TRP GLY ASN THR ALA SER SER GLY ALA ASP SEQRES 11 B 224 TYR PRO ASP GLU LEU GLN CYS LEU ASP ALA PRO VAL LEU SEQRES 12 B 224 SER GLN ALA LYS CYS GLU ALA SER TYR PRO GLY LYS ILE SEQRES 13 B 224 THR SER ASN MET PHE CYS VAL GLY PHE LEU GLU GLY GLY SEQRES 14 B 224 LYS ASP SER CYS GLN GLY ASP ALA GLY GLY PRO VAL VAL SEQRES 15 B 224 CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY ASP SEQRES 16 B 224 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS SEQRES 17 B 224 VAL TYR ASN TYR VAL LYS TRP ILE LYS ASN THR ILE ALA SEQRES 18 B 224 ALA ASN SER SEQRES 1 I 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO SEQRES 2 I 58 CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS SEQRES 3 I 58 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG SEQRES 4 I 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET SEQRES 5 I 58 ARG THR CYS GLY GLY ALA SEQRES 1 C 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO SEQRES 2 C 58 CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS SEQRES 3 C 58 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG SEQRES 4 C 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET SEQRES 5 C 58 ARG THR CYS GLY GLY ALA HET CA A 1 1 HET SO4 A 6 5 HET SO4 A 10 5 HET SO4 A 12 5 HET SO4 A 14 5 HET SO4 A 247 5 HET SO4 A 248 5 HET SO4 A 249 5 HET CA B 1 1 HET SO4 B 4 5 HET SO4 B 5 5 HET SO4 B 7 5 HET SO4 B 8 5 HET SO4 B 11 5 HET SO4 B 15 5 HET SO4 B 247 5 HET SO4 B 248 5 HET SO4 B 249 5 HET SO4 B 250 5 HET SO4 I 59 5 HET SO4 I 60 5 HET SO4 I 61 5 HET SO4 I 62 5 HET SO4 I 63 5 HET SO4 C 59 5 HET SO4 C 60 10 HETNAM CA CALCIUM ION HETNAM SO4 SULFATE ION FORMUL 5 CA 2(CA 2+) FORMUL 6 SO4 24(O4 S 2-) FORMUL 31 HOH *643(H2 O) HELIX 1 1 ALA A 55 TYR A 59 5 5 HELIX 2 2 SER A 164 TYR A 172 1 9 HELIX 3 3 TYR A 234 ASN A 245 1 12 HELIX 4 4 GLU B 23 ASN B 25 5 3 HELIX 5 5 ALA B 55 TYR B 59 5 5 HELIX 6 6 SER B 164 TYR B 172 1 9 HELIX 7 7 TYR B 234 ASN B 245 1 12 HELIX 8 8 PRO I 2 GLU I 7 5 6 HELIX 9 9 SER I 47 GLY I 56 1 10 HELIX 10 10 PRO C 2 GLU C 7 5 6 HELIX 11 11 ALA C 25 GLY C 28 5 4 HELIX 12 12 SER C 47 GLY C 56 1 10 SHEET 1 A 7 TYR A 20 ASN A 21 0 SHEET 2 A 7 GLN A 156 PRO A 161 -1 O CYS A 157 N TYR A 20 SHEET 3 A 7 LYS A 135 GLY A 140 -1 N ILE A 138 O LEU A 158 SHEET 4 A 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137 SHEET 5 A 7 GLN A 204 TRP A 215 -1 O GLN A 204 N CYS A 201 SHEET 6 A 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215 SHEET 7 A 7 MET A 180 VAL A 183 -1 N PHE A 181 O TYR A 228 SHEET 1 B 7 GLN A 30 ASN A 34 0 SHEET 2 B 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33 SHEET 3 B 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45 SHEET 4 B 7 MET A 104 LEU A 108 -1 O ILE A 106 N VAL A 52 SHEET 5 B 7 GLN A 81 ARG A 90 -1 N ALA A 86 O LYS A 107 SHEET 6 B 7 GLN A 64 LEU A 67 -1 N LEU A 67 O GLN A 81 SHEET 7 B 7 GLN A 30 ASN A 34 -1 N SER A 32 O ARG A 66 SHEET 1 C 7 TYR B 20 ASN B 21 0 SHEET 2 C 7 GLN B 156 PRO B 161 -1 O CYS B 157 N TYR B 20 SHEET 3 C 7 LYS B 135 GLY B 140 -1 N CYS B 136 O ALA B 160 SHEET 4 C 7 PRO B 198 CYS B 201 -1 O VAL B 200 N LEU B 137 SHEET 5 C 7 GLN B 204 TRP B 215 -1 O GLN B 204 N CYS B 201 SHEET 6 C 7 GLY B 226 LYS B 230 -1 O VAL B 227 N TRP B 215 SHEET 7 C 7 MET B 180 VAL B 183 -1 N PHE B 181 O TYR B 228 SHEET 1 D 7 GLN B 30 ASN B 34 0 SHEET 2 D 7 HIS B 40 ASN B 48 -1 O CYS B 42 N LEU B 33 SHEET 3 D 7 TRP B 51 SER B 54 -1 O VAL B 53 N SER B 45 SHEET 4 D 7 MET B 104 LEU B 108 -1 O ILE B 106 N VAL B 52 SHEET 5 D 7 GLN B 81 ARG B 90 -1 N ILE B 89 O LEU B 105 SHEET 6 D 7 GLN B 64 LEU B 67 -1 N LEU B 67 O GLN B 81 SHEET 7 D 7 GLN B 30 ASN B 34 -1 N SER B 32 O ARG B 66 SHEET 1 E 2 ILE I 18 ASN I 24 0 SHEET 2 E 2 LEU I 29 TYR I 35 -1 O TYR I 35 N ILE I 18 SHEET 1 F 2 ILE C 18 TYR C 23 0 SHEET 2 F 2 CYS C 30 TYR C 35 -1 O TYR C 35 N ILE C 18 SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.03 SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.06 SSBOND 3 CYS A 136 CYS A 201 1555 1555 2.06 SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.06 SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.11 SSBOND 6 CYS B 22 CYS B 157 1555 1555 2.04 SSBOND 7 CYS B 42 CYS B 58 1555 1555 2.05 SSBOND 8 CYS B 136 CYS B 201 1555 1555 2.07 SSBOND 9 CYS B 168 CYS B 182 1555 1555 2.09 SSBOND 10 CYS B 191 CYS B 220 1555 1555 2.14 SSBOND 11 CYS I 5 CYS I 55 1555 1555 2.05 SSBOND 12 CYS I 14 CYS I 38 1555 1555 2.10 SSBOND 13 CYS I 30 CYS I 51 1555 1555 2.10 SSBOND 14 CYS C 5 CYS C 55 1555 1555 2.03 SSBOND 15 CYS C 14 CYS C 38 1555 1555 2.06 SSBOND 16 CYS C 30 CYS C 51 1555 1555 2.09 LINK OE2 GLU A 70 CA CA A 1 1555 1555 2.24 LINK O ASN A 72 CA CA A 1 1555 1555 2.34 LINK O VAL A 75 CA CA A 1 1555 1555 2.34 LINK OE2 GLU A 80 CA CA A 1 1555 1555 2.39 LINK OE2 GLU B 70 CA CA B 1 1555 1555 2.26 LINK O ASN B 72 CA CA B 1 1555 1555 2.30 LINK O VAL B 75 CA CA B 1 1555 1555 2.31 LINK OE2 GLU B 77 CA CA B 1 1555 1555 2.40 LINK OE2 GLU B 80 CA CA B 1 1555 1555 2.39 LINK CA CA A 1 O HOH A 274 1555 1555 2.44 LINK CA CA A 1 O HOH A 311 1555 1555 2.47 LINK CA CA B 1 O HOH B 291 1555 1555 2.40 SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80 SITE 2 AC1 6 HOH A 274 HOH A 311 SITE 1 AC2 6 LYS A 60 SER A 61 HOH A 398 HOH A 462 SITE 2 AC2 6 HOH A 468 LYS C 46 SITE 1 AC3 4 THR A 132 SER A 164 GLN A 165 HOH A 351 SITE 1 AC4 4 THR A 177 SER A 178 SO4 A 247 HOH A 465 SITE 1 AC5 3 ARG A 90 HOH A 346 HOH A 383 SITE 1 AC6 6 SO4 A 12 ASN A 100 SER A 178 ASN A 179 SITE 2 AC6 6 HOH A 338 HOH A 465 SITE 1 AC7 3 SER A 110 ARG A 111 HOH A 381 SITE 1 AC8 5 LYS A 97 LEU A 99 TRP A 215 HOH A 337 SITE 2 AC8 5 ARG C 39 SITE 1 AC9 6 GLU B 70 ASN B 72 VAL B 75 GLU B 77 SITE 2 AC9 6 GLU B 80 HOH B 291 SITE 1 BC1 8 PHE B 184 LEU B 185 GLU B 186 HOH B 268 SITE 2 BC1 8 HOH B 329 HOH B 334 HOH B 400 HOH B 427 SITE 1 BC2 8 PRO A 173 LYS A 175 LYS A 224 HOH A 367 SITE 2 BC2 8 HOH A 394 ASN B 115 ALA B 116 HOH B 384 SITE 1 BC3 7 LYS B 60 SER B 61 HOH B 399 HOH B 489 SITE 2 BC3 7 HOH B 513 HOH B 517 LYS I 46 SITE 1 BC4 4 LYS B 87 HOH B 368 HOH B 418 ARG I 42 SITE 1 BC5 10 ASN B 100 PRO B 129 ALA B 130 THR B 132 SITE 2 BC5 10 ASN B 179 SO4 B 248 HOH B 383 HOH B 387 SITE 3 BC5 10 HOH B 389 HOH B 485 SITE 1 BC6 3 SER B 110 ARG B 111 HOH B 501 SITE 1 BC7 2 ASN B 21 GLN B 156 SITE 1 BC8 7 SO4 B 11 THR B 132 GLN B 165 THR B 177 SITE 2 BC8 7 SER B 178 HOH B 288 HOH B 405 SITE 1 BC9 5 LYS B 97 LEU B 99 LYS B 175 TRP B 215 SITE 2 BC9 5 ARG I 39 SITE 1 CC1 6 ILE B 47 ASN B 48 LYS B 239 ILE B 242 SITE 2 CC1 6 HOH B 330 HOH B 511 SITE 1 CC2 7 GLU I 7 ARG I 42 HOH I 66 HOH I 80 SITE 2 CC2 7 HOH I 88 HOH I 91 HOH I 107 SITE 1 CC3 9 ARG I 20 TYR I 35 GLY I 37 ALA I 40 SITE 2 CC3 9 HOH I 72 HOH I 79 HOH I 104 HOH I 120 SITE 3 CC3 9 HOH I 128 SITE 1 CC4 6 ASN B 84 SER B 109 SER B 110 HOH B 490 SITE 2 CC4 6 ARG I 1 PRO I 2 SITE 1 CC5 3 TYR I 10 THR I 11 GLY I 12 SITE 1 CC6 10 TYR A 151 PRO A 152 ASP A 153 HOH A 251 SITE 2 CC6 10 HOH A 291 ARG C 17 TYR I 23 GLY I 28 SITE 3 CC6 10 HOH I 100 HOH I 121 SITE 1 CC7 6 ARG C 20 TYR C 35 GLY C 37 ALA C 40 SITE 2 CC7 6 HOH C 73 HOH C 77 SITE 1 CC8 5 PHE C 4 LYS C 41 ARG C 42 HOH C 84 SITE 2 CC8 5 HOH C 109 CRYST1 91.183 186.546 90.187 90.00 90.00 90.00 C 2 2 21 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010967 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005361 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011088 0.00000 ATOM 1 N ILE A 16 19.370 -43.232 20.964 1.00 18.97 N ANISOU 1 N ILE A 16 2488 2287 2434 25 180 64 N ATOM 2 CA ILE A 16 18.063 -42.531 20.908 1.00 18.63 C ANISOU 2 CA ILE A 16 2365 2275 2438 9 258 61 C ATOM 3 C ILE A 16 17.128 -43.218 21.889 1.00 18.76 C ANISOU 3 C ILE A 16 2415 2259 2452 -51 342 86 C ATOM 4 O ILE A 16 16.811 -44.418 21.742 1.00 19.65 O ANISOU 4 O ILE A 16 2535 2340 2589 -96 330 100 O ATOM 5 CB ILE A 16 17.469 -42.554 19.473 1.00 16.43 C ANISOU 5 CB ILE A 16 1976 2029 2238 16 221 43 C ATOM 6 CG1 ILE A 16 18.432 -41.955 18.448 1.00 17.51 C ANISOU 6 CG1 ILE A 16 2095 2194 2365 70 147 23 C ATOM 7 CG2 ILE A 16 16.103 -41.853 19.544 1.00 21.76 C ANISOU 7 CG2 ILE A 16 2564 2730 2973 4 296 41 C ATOM 8 CD1 ILE A 16 18.661 -40.423 18.524 1.00 18.74 C ANISOU 8 CD1 ILE A 16 2236 2379 2507 112 168 16 C ATOM 9 N VAL A 17 16.684 -42.476 22.900 1.00 19.18 N ANISOU 9 N VAL A 17 2496 2316 2475 -56 432 92 N ATOM 10 CA VAL A 17 15.719 -42.956 23.888 1.00 19.99 C ANISOU 10 CA VAL A 17 2629 2394 2571 -116 540 115 C ATOM 11 C VAL A 17 14.335 -42.511 23.451 1.00 22.29 C ANISOU 11 C VAL A 17 2783 2722 2963 -129 613 99 C ATOM 12 O VAL A 17 14.164 -41.367 23.121 1.00 20.92 O ANISOU 12 O VAL A 17 2545 2586 2818 -81 621 75 O ATOM 13 CB VAL A 17 15.976 -42.319 25.263 1.00 22.50 C ANISOU 13 CB VAL A 17 3059 2697 2793 -109 610 122 C ATOM 14 CG1 VAL A 17 14.991 -42.837 26.277 1.00 23.49 C ANISOU 14 CG1 VAL A 17 3228 2797 2902 -175 737 147 C ATOM 15 CG2 VAL A 17 17.368 -42.648 25.738 1.00 24.15 C ANISOU 15 CG2 VAL A 17 3399 2870 2908 -90 522 134 C ATOM 16 N GLY A 18 13.355 -43.411 23.467 1.00 20.29 N ANISOU 16 N GLY A 18 2485 2454 2770 -195 664 114 N ATOM 17 CA GLY A 18 11.994 -43.043 23.173 1.00 23.49 C ANISOU 17 CA GLY A 18 2749 2891 3283 -212 737 98 C ATOM 18 C GLY A 18 11.675 -42.860 21.705 1.00 21.47 C ANISOU 18 C GLY A 18 2361 2672 3126 -183 644 72 C ATOM 19 O GLY A 18 10.635 -42.284 21.377 1.00 24.04 O ANISOU 19 O GLY A 18 2560 3029 3545 -175 682 54 O ATOM 20 N GLY A 19 12.548 -43.377 20.842 1.00 23.21 N ANISOU 20 N GLY A 19 2613 2883 3323 -167 523 70 N ATOM 21 CA GLY A 19 12.381 -43.270 19.421 1.00 22.30 C ANISOU 21 CA GLY A 19 2402 2796 3274 -140 426 46 C ATOM 22 C GLY A 19 11.804 -44.517 18.799 1.00 23.72 C ANISOU 22 C GLY A 19 2538 2955 3521 -201 383 45 C ATOM 23 O GLY A 19 11.124 -45.314 19.471 1.00 25.77 O ANISOU 23 O GLY A 19 2797 3183 3812 -273 453 63 O ATOM 24 N TYR A 20 12.084 -44.702 17.516 1.00 21.45 N ANISOU 24 N TYR A 20 2220 2678 3251 -176 270 24 N ATOM 25 CA TYR A 20 11.521 -45.810 16.749 1.00 21.38 C ANISOU 25 CA TYR A 20 2167 2649 3309 -229 209 12 C ATOM 26 C TYR A 20 12.525 -46.264 15.707 1.00 22.98 C ANISOU 26 C TYR A 20 2428 2842 3462 -196 94 -7 C ATOM 27 O TYR A 20 13.464 -45.523 15.397 1.00 21.26 O ANISOU 27 O TYR A 20 2249 2649 3179 -129 63 -13 O ATOM 28 CB TYR A 20 10.214 -45.377 16.038 1.00 22.69 C ANISOU 28 CB TYR A 20 2181 2850 3591 -236 194 -8 C ATOM 29 CG TYR A 20 10.319 -44.136 15.177 1.00 23.48 C ANISOU 29 CG TYR A 20 2233 3000 3690 -155 135 -26 C ATOM 30 CD1 TYR A 20 10.160 -42.876 15.720 1.00 24.71 C ANISOU 30 CD1 TYR A 20 2360 3184 3846 -107 204 -20 C ATOM 31 CD2 TYR A 20 10.542 -44.230 13.817 1.00 25.22 C ANISOU 31 CD2 TYR A 20 2444 3231 3906 -128 14 -48 C ATOM 32 CE1 TYR A 20 10.245 -41.739 14.947 1.00 26.55 C ANISOU 32 CE1 TYR A 20 2557 3451 4079 -35 149 -31 C ATOM 33 CE2 TYR A 20 10.641 -43.101 13.038 1.00 25.11 C ANISOU 33 CE2 TYR A 20 2401 3255 3882 -57 -38 -57 C ATOM 34 CZ TYR A 20 10.485 -41.855 13.605 1.00 25.47 C ANISOU 34 CZ TYR A 20 2419 3326 3935 -12 28 -46 C ATOM 35 OH TYR A 20 10.558 -40.704 12.840 1.00 28.12 O ANISOU 35 OH TYR A 20 2733 3688 4262 57 -24 -50 O ATOM 36 N ASN A 21 12.356 -47.486 15.194 1.00 22.71 N ANISOU 36 N ASN A 21 2403 2769 3456 -244 37 -19 N ATOM 37 CA ASN A 21 13.253 -47.979 14.160 1.00 20.33 C ANISOU 37 CA ASN A 21 2158 2457 3111 -210 -65 -46 C ATOM 38 C ASN A 21 13.038 -47.125 12.889 1.00 23.21 C ANISOU 38 C ASN A 21 2454 2876 3490 -160 -135 -74 C ATOM 39 O ASN A 21 11.930 -47.018 12.394 1.00 24.92 O ANISOU 39 O ASN A 21 2575 3108 3785 -184 -161 -85 O ATOM 40 CB ASN A 21 12.928 -49.444 13.797 1.00 23.92 C ANISOU 40 CB ASN A 21 2631 2853 3604 -274 -115 -60 C ATOM 41 CG ASN A 21 13.202 -50.443 14.925 1.00 28.78 C ANISOU 41 CG ASN A 21 3336 3399 4200 -325 -62 -28 C ATOM 42 OD1 ASN A 21 14.056 -50.254 15.765 1.00 27.03 O ANISOU 42 OD1 ASN A 21 3196 3168 3908 -296 -23 -4 O ATOM 43 ND2 ASN A 21 12.468 -51.559 14.903 1.00 36.09 N ANISOU 43 ND2 ASN A 21 4252 4271 5189 -405 -72 -29 N ATOM 44 N CYS A 22 14.100 -46.518 12.364 1.00 22.13 N ANISOU 44 N CYS A 22 2366 2763 3277 -92 -168 -83 N ATOM 45 CA CYS A 22 14.009 -45.726 11.130 1.00 20.66 C ANISOU 45 CA CYS A 22 2143 2622 3086 -45 -234 -103 C ATOM 46 C CYS A 22 13.657 -46.679 9.994 1.00 21.63 C ANISOU 46 C CYS A 22 2264 2726 3228 -70 -329 -138 C ATOM 47 O CYS A 22 14.126 -47.827 9.937 1.00 24.37 O ANISOU 47 O CYS A 22 2676 3029 3557 -94 -351 -154 O ATOM 48 CB CYS A 22 15.363 -45.102 10.792 1.00 19.94 C ANISOU 48 CB CYS A 22 2121 2550 2904 20 -241 -105 C ATOM 49 SG CYS A 22 16.082 -43.957 11.959 1.00 23.37 S ANISOU 49 SG CYS A 22 2579 3001 3299 55 -154 -73 S ATOM 50 N GLU A 23 12.829 -46.210 9.081 1.00 26.17 N ANISOU 50 N GLU A 23 2772 3330 3842 -62 -392 -152 N ATOM 51 CA GLU A 23 12.550 -47.015 7.891 1.00 28.81 C ANISOU 51 CA GLU A 23 3118 3648 4180 -80 -498 -191 C ATOM 52 C GLU A 23 13.842 -47.175 7.086 1.00 30.91 C ANISOU 52 C GLU A 23 3492 3913 4337 -32 -531 -215 C ATOM 53 O GLU A 23 14.648 -46.251 7.023 1.00 28.38 O ANISOU 53 O GLU A 23 3203 3626 3953 24 -499 -200 O ATOM 54 CB GLU A 23 11.455 -46.366 7.048 1.00 34.96 C ANISOU 54 CB GLU A 23 3809 4460 5014 -72 -575 -200 C ATOM 55 CG GLU A 23 10.172 -45.999 7.828 1.00 41.29 C ANISOU 55 CG GLU A 23 4480 5271 5937 -107 -531 -181 C ATOM 56 CD GLU A 23 9.160 -45.258 6.975 0.00 40.37 C ANISOU 56 CD GLU A 23 4270 5186 5882 -83 -619 -190 C ATOM 57 OE1 GLU A 23 8.016 -45.069 7.439 0.00 40.31 O ANISOU 57 OE1 GLU A 23 4137 5185 5993 -112 -599 -184 O ATOM 58 OE2 GLU A 23 9.509 -44.867 5.842 0.00 39.72 O ANISOU 58 OE2 GLU A 23 4240 5120 5729 -35 -708 -203 O ATOM 59 N GLU A 24 14.068 -48.337 6.475 1.00 33.68 N ANISOU 59 N GLU A 24 3901 4225 4669 -53 -588 -253 N ATOM 60 CA GLU A 24 15.307 -48.542 5.712 1.00 37.91 C ANISOU 60 CA GLU A 24 4538 4760 5107 -3 -605 -283 C ATOM 61 C GLU A 24 15.408 -47.512 4.564 1.00 35.09 C ANISOU 61 C GLU A 24 4192 4455 4687 48 -648 -289 C ATOM 62 O GLU A 24 14.414 -47.195 3.896 1.00 37.67 O ANISOU 62 O GLU A 24 4473 4797 5041 38 -720 -294 O ATOM 63 CB GLU A 24 15.428 -49.988 5.198 1.00 45.42 C ANISOU 63 CB GLU A 24 5552 5653 6053 -32 -662 -332 C ATOM 64 CG GLU A 24 16.312 -50.861 6.087 1.00 52.03 C ANISOU 64 CG GLU A 24 6445 6438 6885 -35 -608 -329 C ATOM 65 CD GLU A 24 16.611 -52.231 5.494 1.00 60.69 C ANISOU 65 CD GLU A 24 7619 7471 7969 -47 -663 -382 C ATOM 66 OE1 GLU A 24 15.757 -53.133 5.650 1.00 63.29 O ANISOU 66 OE1 GLU A 24 7934 7748 8365 -114 -702 -392 O ATOM 67 OE2 GLU A 24 17.708 -52.406 4.902 1.00 62.91 O ANISOU 67 OE2 GLU A 24 7973 7751 8179 10 -663 -417 O ATOM 68 N ASN A 25 16.596 -46.927 4.406 1.00 38.52 N ANISOU 68 N ASN A 25 4682 4914 5042 102 -600 -283 N ATOM 69 CA ASN A 25 16.847 -45.877 3.402 1.00 38.02 C ANISOU 69 CA ASN A 25 4645 4894 4906 148 -621 -278 C ATOM 70 C ASN A 25 16.237 -44.510 3.682 1.00 33.06 C ANISOU 70 C ASN A 25 3951 4303 4309 163 -608 -232 C ATOM 71 O ASN A 25 16.316 -43.628 2.829 1.00 34.89 O ANISOU 71 O ASN A 25 4210 4562 4484 198 -635 -222 O ATOM 72 CB ASN A 25 16.367 -46.305 1.987 1.00 47.16 C ANISOU 72 CB ASN A 25 5849 6048 6021 145 -724 -320 C ATOM 73 CG ASN A 25 16.964 -47.634 1.515 1.00 52.61 C ANISOU 73 CG ASN A 25 6620 6699 6672 138 -743 -377 C ATOM 74 OD1 ASN A 25 16.348 -48.338 0.703 1.00 57.43 O ANISOU 74 OD1 ASN A 25 7258 7286 7277 115 -833 -418 O ATOM 75 ND2 ASN A 25 18.154 -47.979 2.004 1.00 50.09 N ANISOU 75 ND2 ASN A 25 6337 6366 6328 160 -666 -384 N ATOM 76 N SER A 26 15.596 -44.307 4.836 1.00 28.57 N ANISOU 76 N SER A 26 3302 3728 3825 139 -566 -203 N ATOM 77 CA SER A 26 14.965 -43.028 5.101 1.00 28.56 C ANISOU 77 CA SER A 26 3236 3756 3861 160 -553 -167 C ATOM 78 C SER A 26 15.928 -41.956 5.624 1.00 22.93 C ANISOU 78 C SER A 26 2549 3060 3102 199 -473 -136 C ATOM 79 O SER A 26 15.611 -40.772 5.558 1.00 26.81 O ANISOU 79 O SER A 26 3014 3571 3602 228 -471 -109 O ATOM 80 CB SER A 26 13.785 -43.153 6.064 1.00 31.11 C ANISOU 80 CB SER A 26 3457 4068 4296 121 -533 -155 C ATOM 81 OG SER A 26 14.191 -43.578 7.337 1.00 28.91 O ANISOU 81 OG SER A 26 3182 3769 4034 95 -444 -143 O ATOM 82 N VAL A 27 17.099 -42.386 6.084 1.00 19.89 N ANISOU 82 N VAL A 27 2217 2664 2676 200 -417 -143 N ATOM 83 CA VAL A 27 18.109 -41.475 6.597 1.00 17.73 C ANISOU 83 CA VAL A 27 1966 2403 2366 229 -349 -119 C ATOM 84 C VAL A 27 19.459 -41.727 5.879 1.00 18.33 C ANISOU 84 C VAL A 27 2117 2485 2365 251 -340 -141 C ATOM 85 O VAL A 27 20.468 -42.090 6.497 1.00 18.02 O ANISOU 85 O VAL A 27 2097 2433 2315 254 -294 -148 O ATOM 86 CB VAL A 27 18.305 -41.622 8.120 1.00 18.19 C ANISOU 86 CB VAL A 27 2005 2443 2463 211 -281 -105 C ATOM 87 CG1 VAL A 27 18.980 -40.405 8.643 1.00 19.00 C ANISOU 87 CG1 VAL A 27 2115 2559 2544 238 -227 -80 C ATOM 88 CG2 VAL A 27 16.965 -41.774 8.835 1.00 23.32 C ANISOU 88 CG2 VAL A 27 2585 3082 3192 178 -275 -94 C ATOM 89 N PRO A 28 19.487 -41.483 4.561 1.00 16.99 N ANISOU 89 N PRO A 28 1987 2332 2137 270 -382 -151 N ATOM 90 CA PRO A 28 20.638 -41.884 3.760 1.00 16.94 C ANISOU 90 CA PRO A 28 2050 2330 2057 287 -366 -180 C ATOM 91 C PRO A 28 21.902 -41.055 3.944 1.00 17.35 C ANISOU 91 C PRO A 28 2119 2399 2076 309 -291 -163 C ATOM 92 O PRO A 28 22.972 -41.453 3.478 1.00 16.51 O ANISOU 92 O PRO A 28 2052 2296 1925 323 -259 -191 O ATOM 93 CB PRO A 28 20.095 -41.776 2.320 1.00 18.77 C ANISOU 93 CB PRO A 28 2328 2574 2229 296 -435 -191 C ATOM 94 CG PRO A 28 19.104 -40.687 2.369 1.00 19.30 C ANISOU 94 CG PRO A 28 2354 2653 2328 301 -468 -150 C ATOM 95 CD PRO A 28 18.405 -40.959 3.704 1.00 19.91 C ANISOU 95 CD PRO A 28 2345 2713 2506 275 -453 -140 C ATOM 96 N TYR A 29 21.783 -39.954 4.679 1.00 16.08 N ANISOU 96 N TYR A 29 1922 2245 1945 311 -261 -123 N ATOM 97 CA TYR A 29 22.901 -39.068 5.015 1.00 15.48 C ANISOU 97 CA TYR A 29 1852 2178 1854 322 -195 -105 C ATOM 98 C TYR A 29 23.552 -39.454 6.341 1.00 16.13 C ANISOU 98 C TYR A 29 1905 2244 1982 315 -158 -111 C ATOM 99 O TYR A 29 24.570 -38.889 6.684 1.00 15.49 O ANISOU 99 O TYR A 29 1822 2166 1897 321 -113 -105 O ATOM 100 CB TYR A 29 22.431 -37.605 5.057 1.00 16.14 C ANISOU 100 CB TYR A 29 1924 2267 1941 330 -190 -61 C ATOM 101 CG TYR A 29 21.203 -37.395 5.907 1.00 15.08 C ANISOU 101 CG TYR A 29 1736 2120 1872 324 -214 -44 C ATOM 102 CD1 TYR A 29 21.326 -37.202 7.266 1.00 14.97 C ANISOU 102 CD1 TYR A 29 1690 2094 1905 316 -171 -36 C ATOM 103 CD2 TYR A 29 19.928 -37.453 5.371 1.00 16.48 C ANISOU 103 CD2 TYR A 29 1894 2300 2069 327 -277 -41 C ATOM 104 CE1 TYR A 29 20.203 -37.069 8.082 1.00 15.57 C ANISOU 104 CE1 TYR A 29 1717 2160 2039 310 -174 -26 C ATOM 105 CE2 TYR A 29 18.799 -37.328 6.170 1.00 16.88 C ANISOU 105 CE2 TYR A 29 1878 2341 2194 321 -287 -31 C ATOM 106 CZ TYR A 29 18.940 -37.139 7.520 1.00 17.68 C ANISOU 106 CZ TYR A 29 1951 2431 2336 312 -227 -24 C ATOM 107 OH TYR A 29 17.799 -37.042 8.281 1.00 17.63 O ANISOU 107 OH TYR A 29 1881 2417 2400 305 -221 -18 O ATOM 108 N GLN A 30 22.937 -40.376 7.090 1.00 15.22 N ANISOU 108 N GLN A 30 1769 2106 1909 298 -181 -121 N ATOM 109 CA GLN A 30 23.485 -40.799 8.377 1.00 14.55 C ANISOU 109 CA GLN A 30 1675 1998 1856 291 -156 -122 C ATOM 110 C GLN A 30 24.683 -41.684 8.133 1.00 14.10 C ANISOU 110 C GLN A 30 1642 1932 1785 306 -152 -156 C ATOM 111 O GLN A 30 24.587 -42.643 7.335 1.00 16.15 O ANISOU 111 O GLN A 30 1925 2184 2029 310 -179 -188 O ATOM 112 CB GLN A 30 22.441 -41.618 9.131 1.00 16.24 C ANISOU 112 CB GLN A 30 1873 2185 2111 263 -176 -119 C ATOM 113 CG GLN A 30 22.997 -42.296 10.400 1.00 15.54 C ANISOU 113 CG GLN A 30 1800 2064 2041 254 -161 -119 C ATOM 114 CD GLN A 30 23.063 -41.389 11.623 1.00 17.22 C ANISOU 114 CD GLN A 30 2005 2274 2262 251 -123 -90 C ATOM 115 OE1 GLN A 30 24.108 -41.300 12.337 1.00 18.71 O ANISOU 115 OE1 GLN A 30 2214 2453 2443 262 -113 -91 O ATOM 116 NE2 GLN A 30 21.979 -40.809 11.946 1.00 14.75 N ANISOU 116 NE2 GLN A 30 1666 1967 1969 236 -106 -70 N ATOM 117 N VAL A 31 25.782 -41.396 8.824 1.00 13.94 N ANISOU 117 N VAL A 31 1613 1908 1774 318 -123 -155 N ATOM 118 CA VAL A 31 26.914 -42.310 8.836 1.00 15.50 C ANISOU 118 CA VAL A 31 1818 2090 1980 339 -124 -189 C ATOM 119 C VAL A 31 27.241 -42.781 10.249 1.00 14.35 C ANISOU 119 C VAL A 31 1674 1910 1870 336 -139 -182 C ATOM 120 O VAL A 31 26.856 -42.173 11.254 1.00 13.85 O ANISOU 120 O VAL A 31 1608 1840 1815 318 -134 -151 O ATOM 121 CB VAL A 31 28.164 -41.743 8.129 1.00 17.87 C ANISOU 121 CB VAL A 31 2105 2419 2266 360 -82 -205 C ATOM 122 CG1 VAL A 31 27.800 -41.217 6.749 1.00 18.99 C ANISOU 122 CG1 VAL A 31 2268 2592 2355 359 -64 -205 C ATOM 123 CG2 VAL A 31 28.805 -40.693 8.956 1.00 16.78 C ANISOU 123 CG2 VAL A 31 1938 2287 2151 354 -59 -182 C ATOM 124 N SER A 32 27.955 -43.903 10.300 1.00 13.76 N ANISOU 124 N SER A 32 1611 1806 1811 358 -161 -212 N ATOM 125 CA SER A 32 28.542 -44.440 11.530 1.00 16.09 C ANISOU 125 CA SER A 32 1917 2061 2135 367 -188 -208 C ATOM 126 C SER A 32 30.042 -44.228 11.471 1.00 14.96 C ANISOU 126 C SER A 32 1739 1929 2017 403 -182 -233 C ATOM 127 O SER A 32 30.692 -44.521 10.456 1.00 18.60 O ANISOU 127 O SER A 32 2181 2405 2481 430 -162 -271 O ATOM 128 CB SER A 32 28.196 -45.923 11.649 1.00 17.31 C ANISOU 128 CB SER A 32 2112 2164 2300 368 -228 -223 C ATOM 129 OG SER A 32 28.994 -46.501 12.668 1.00 17.47 O ANISOU 129 OG SER A 32 2152 2142 2346 388 -263 -222 O ATOM 130 N LEU A 33 30.609 -43.680 12.527 1.00 15.41 N ANISOU 130 N LEU A 33 1785 1978 2091 402 -195 -215 N ATOM 131 CA LEU A 33 32.034 -43.591 12.658 1.00 15.73 C ANISOU 131 CA LEU A 33 1782 2021 2174 434 -204 -240 C ATOM 132 C LEU A 33 32.514 -44.776 13.463 1.00 16.65 C ANISOU 132 C LEU A 33 1924 2083 2320 464 -269 -251 C ATOM 133 O LEU A 33 32.022 -45.062 14.557 1.00 16.24 O ANISOU 133 O LEU A 33 1926 1993 2253 448 -309 -221 O ATOM 134 CB LEU A 33 32.450 -42.270 13.335 1.00 16.24 C ANISOU 134 CB LEU A 33 1821 2104 2245 414 -197 -218 C ATOM 135 CG LEU A 33 31.887 -40.983 12.690 1.00 17.09 C ANISOU 135 CG LEU A 33 1917 2252 2323 383 -139 -197 C ATOM 136 CD1 LEU A 33 32.513 -39.771 13.415 1.00 18.58 C ANISOU 136 CD1 LEU A 33 2083 2446 2531 366 -139 -184 C ATOM 137 CD2 LEU A 33 32.138 -40.970 11.211 1.00 16.79 C ANISOU 137 CD2 LEU A 33 1853 2248 2277 393 -89 -220 C ATOM 138 N ASN A 34 33.535 -45.440 12.931 1.00 16.19 N ANISOU 138 N ASN A 34 1827 2017 2306 510 -277 -295 N ATOM 139 CA ASN A 34 34.002 -46.709 13.472 1.00 18.49 C ANISOU 139 CA ASN A 34 2144 2249 2633 552 -344 -312 C ATOM 140 C ASN A 34 35.526 -46.688 13.672 1.00 19.03 C ANISOU 140 C ASN A 34 2139 2316 2774 601 -373 -345 C ATOM 141 O ASN A 34 36.274 -46.324 12.754 1.00 23.34 O ANISOU 141 O ASN A 34 2610 2903 3354 620 -318 -382 O ATOM 142 CB ASN A 34 33.566 -47.799 12.501 1.00 17.45 C ANISOU 142 CB ASN A 34 2041 2098 2492 569 -331 -344 C ATOM 143 CG ASN A 34 33.895 -49.185 12.967 1.00 20.55 C ANISOU 143 CG ASN A 34 2474 2416 2919 611 -399 -360 C ATOM 144 OD1 ASN A 34 35.057 -49.578 13.020 1.00 22.04 O ANISOU 144 OD1 ASN A 34 2620 2586 3167 669 -428 -395 O ATOM 145 ND2 ASN A 34 32.866 -49.973 13.250 1.00 20.05 N ANISOU 145 ND2 ASN A 34 2490 2304 2824 583 -425 -337 N ATOM 146 N SER A 37 35.911 -47.080 14.877 1.00 22.50 N ANISOU 146 N SER A 37 2606 2705 3236 619 -458 -330 N ATOM 147 CA SER A 37 37.281 -47.202 15.366 1.00 30.13 C ANISOU 147 CA SER A 37 3512 3655 4282 670 -521 -356 C ATOM 148 C SER A 37 37.548 -48.620 15.800 1.00 31.56 C ANISOU 148 C SER A 37 3739 3759 4492 725 -604 -367 C ATOM 149 O SER A 37 38.272 -48.815 16.773 1.00 37.31 O ANISOU 149 O SER A 37 4470 4449 5259 756 -697 -361 O ATOM 150 CB SER A 37 37.347 -46.449 16.676 1.00 34.69 C ANISOU 150 CB SER A 37 4117 4222 4840 641 -581 -316 C ATOM 151 OG SER A 37 36.365 -47.073 17.531 1.00 31.45 O ANISOU 151 OG SER A 37 3828 3759 4362 620 -622 -272 O ATOM 152 N GLY A 38 36.949 -49.614 15.147 1.00 26.23 N ANISOU 152 N GLY A 38 3112 3056 3799 737 -583 -381 N ATOM 153 CA GLY A 38 36.879 -50.974 15.651 1.00 29.30 C ANISOU 153 CA GLY A 38 3578 3357 4198 774 -661 -377 C ATOM 154 C GLY A 38 35.491 -51.366 16.130 1.00 28.27 C ANISOU 154 C GLY A 38 3566 3187 3987 714 -664 -324 C ATOM 155 O GLY A 38 35.193 -52.523 16.376 1.00 31.64 O ANISOU 155 O GLY A 38 4071 3539 4413 728 -710 -317 O ATOM 156 N TYR A 39 34.630 -50.337 16.276 1.00 22.79 N ANISOU 156 N TYR A 39 2881 2545 3232 645 -609 -287 N ATOM 157 CA TYR A 39 33.261 -50.494 16.742 1.00 20.06 C ANISOU 157 CA TYR A 39 2626 2177 2819 580 -592 -237 C ATOM 158 C TYR A 39 32.633 -49.117 16.465 1.00 17.77 C ANISOU 158 C TYR A 39 2294 1966 2491 528 -516 -221 C ATOM 159 O TYR A 39 33.357 -48.103 16.329 1.00 17.33 O ANISOU 159 O TYR A 39 2168 1962 2455 539 -499 -235 O ATOM 160 CB TYR A 39 33.144 -50.920 18.238 1.00 19.45 C ANISOU 160 CB TYR A 39 2650 2030 2711 569 -665 -185 C ATOM 161 CG TYR A 39 33.821 -49.962 19.198 1.00 19.18 C ANISOU 161 CG TYR A 39 2603 2015 2667 573 -702 -168 C ATOM 162 CD1 TYR A 39 35.154 -50.109 19.536 1.00 21.48 C ANISOU 162 CD1 TYR A 39 2860 2286 3016 636 -786 -192 C ATOM 163 CD2 TYR A 39 33.125 -48.895 19.762 1.00 18.87 C ANISOU 163 CD2 TYR A 39 2587 2014 2568 515 -657 -133 C ATOM 164 CE1 TYR A 39 35.777 -49.200 20.388 1.00 21.47 C ANISOU 164 CE1 TYR A 39 2846 2303 3011 635 -831 -181 C ATOM 165 CE2 TYR A 39 33.751 -48.012 20.586 1.00 18.42 C ANISOU 165 CE2 TYR A 39 2526 1972 2502 518 -695 -125 C ATOM 166 CZ TYR A 39 35.063 -48.182 20.898 1.00 20.81 C ANISOU 166 CZ TYR A 39 2796 2253 2859 574 -786 -148 C ATOM 167 OH TYR A 39 35.666 -47.264 21.709 1.00 24.22 O ANISOU 167 OH TYR A 39 3222 2697 3282 570 -832 -143 O ATOM 168 N HIS A 40 31.307 -49.054 16.476 1.00 17.40 N ANISOU 168 N HIS A 40 2290 1923 2397 470 -474 -190 N ATOM 169 CA HIS A 40 30.598 -47.764 16.322 1.00 16.15 C ANISOU 169 CA HIS A 40 2101 1830 2207 425 -409 -172 C ATOM 170 C HIS A 40 30.783 -46.921 17.564 1.00 17.47 C ANISOU 170 C HIS A 40 2292 1998 2348 410 -423 -139 C ATOM 171 O HIS A 40 30.439 -47.358 18.655 1.00 17.00 O ANISOU 171 O HIS A 40 2313 1889 2256 392 -452 -105 O ATOM 172 CB HIS A 40 29.124 -48.037 16.128 1.00 16.63 C ANISOU 172 CB HIS A 40 2194 1886 2239 373 -371 -149 C ATOM 173 CG HIS A 40 28.294 -46.815 16.263 1.00 15.75 C ANISOU 173 CG HIS A 40 2061 1824 2100 332 -315 -124 C ATOM 174 ND1 HIS A 40 28.028 -45.983 15.188 1.00 16.12 N ANISOU 174 ND1 HIS A 40 2047 1930 2149 329 -272 -140 N ATOM 175 CD2 HIS A 40 27.712 -46.258 17.342 1.00 17.92 C ANISOU 175 CD2 HIS A 40 2372 2094 2342 298 -294 -86 C ATOM 176 CE1 HIS A 40 27.309 -44.958 15.616 1.00 16.95 C ANISOU 176 CE1 HIS A 40 2146 2062 2233 299 -233 -112 C ATOM 177 NE2 HIS A 40 27.113 -45.095 16.916 1.00 17.63 N ANISOU 177 NE2 HIS A 40 2288 2113 2299 280 -241 -82 N ATOM 178 N PHE A 41 31.308 -45.703 17.413 1.00 15.40 N ANISOU 178 N PHE A 41 1971 1787 2094 414 -401 -148 N ATOM 179 CA PHE A 41 31.501 -44.800 18.566 1.00 15.57 C ANISOU 179 CA PHE A 41 2020 1808 2089 398 -418 -125 C ATOM 180 C PHE A 41 30.804 -43.432 18.458 1.00 15.29 C ANISOU 180 C PHE A 41 1963 1820 2026 361 -351 -111 C ATOM 181 O PHE A 41 30.663 -42.703 19.461 1.00 16.09 O ANISOU 181 O PHE A 41 2105 1914 2092 341 -353 -91 O ATOM 182 CB PHE A 41 32.978 -44.627 18.887 1.00 14.99 C ANISOU 182 CB PHE A 41 1908 1728 2059 438 -484 -149 C ATOM 183 CG PHE A 41 33.721 -43.769 17.910 1.00 17.11 C ANISOU 183 CG PHE A 41 2073 2052 2376 449 -448 -181 C ATOM 184 CD1 PHE A 41 33.902 -42.441 18.140 1.00 19.05 C ANISOU 184 CD1 PHE A 41 2292 2328 2617 424 -427 -176 C ATOM 185 CD2 PHE A 41 34.303 -44.344 16.776 1.00 17.47 C ANISOU 185 CD2 PHE A 41 2053 2112 2472 485 -432 -220 C ATOM 186 CE1 PHE A 41 34.602 -41.647 17.226 1.00 18.08 C ANISOU 186 CE1 PHE A 41 2079 2251 2539 425 -387 -201 C ATOM 187 CE2 PHE A 41 34.994 -43.556 15.873 1.00 18.80 C ANISOU 187 CE2 PHE A 41 2133 2332 2680 488 -383 -247 C ATOM 188 CZ PHE A 41 35.134 -42.233 16.088 1.00 18.28 C ANISOU 188 CZ PHE A 41 2041 2295 2609 456 -361 -234 C ATOM 189 N CYS A 42 30.408 -43.048 17.242 1.00 15.02 N ANISOU 189 N CYS A 42 1871 1830 2004 355 -295 -124 N ATOM 190 CA CYS A 42 29.720 -41.770 17.016 1.00 14.37 C ANISOU 190 CA CYS A 42 1769 1787 1903 328 -238 -110 C ATOM 191 C CYS A 42 29.045 -41.838 15.695 1.00 14.45 C ANISOU 191 C CYS A 42 1744 1829 1919 325 -197 -117 C ATOM 192 O CYS A 42 29.306 -42.744 14.867 1.00 14.95 O ANISOU 192 O CYS A 42 1793 1890 1998 344 -209 -141 O ATOM 193 CB CYS A 42 30.752 -40.635 16.937 1.00 15.69 C ANISOU 193 CB CYS A 42 1890 1979 2093 336 -239 -123 C ATOM 194 SG CYS A 42 31.233 -39.906 18.543 1.00 17.43 S ANISOU 194 SG CYS A 42 2159 2171 2294 325 -282 -112 S ATOM 195 N GLY A 43 28.150 -40.887 15.485 1.00 14.03 N ANISOU 195 N GLY A 43 1680 1801 1849 303 -154 -100 N ATOM 196 CA GLY A 43 27.566 -40.683 14.174 1.00 13.79 C ANISOU 196 CA GLY A 43 1617 1803 1818 302 -126 -105 C ATOM 197 C GLY A 43 28.164 -39.492 13.432 1.00 14.05 C ANISOU 197 C GLY A 43 1614 1870 1852 309 -99 -108 C ATOM 198 O GLY A 43 29.143 -38.882 13.874 1.00 15.01 O ANISOU 198 O GLY A 43 1724 1991 1987 313 -102 -112 O ATOM 199 N GLY A 44 27.604 -39.240 12.250 1.00 13.59 N ANISOU 199 N GLY A 44 1544 1839 1782 309 -79 -107 N ATOM 200 CA GLY A 44 28.019 -38.136 11.413 1.00 14.85 C ANISOU 200 CA GLY A 44 1685 2026 1933 311 -49 -101 C ATOM 201 C GLY A 44 26.982 -37.981 10.325 1.00 14.28 C ANISOU 201 C GLY A 44 1620 1972 1835 310 -44 -91 C ATOM 202 O GLY A 44 26.033 -38.791 10.199 1.00 14.36 O ANISOU 202 O GLY A 44 1637 1976 1844 307 -69 -95 O ATOM 203 N SER A 45 27.143 -36.911 9.537 1.00 14.48 N ANISOU 203 N SER A 45 1645 2015 1840 310 -19 -76 N ATOM 204 CA SER A 45 26.244 -36.582 8.442 1.00 14.72 C ANISOU 204 CA SER A 45 1692 2061 1840 313 -26 -61 C ATOM 205 C SER A 45 27.018 -36.318 7.166 1.00 15.02 C ANISOU 205 C SER A 45 1749 2120 1837 317 2 -66 C ATOM 206 O SER A 45 27.960 -35.519 7.162 1.00 15.64 O ANISOU 206 O SER A 45 1822 2202 1919 309 42 -57 O ATOM 207 CB SER A 45 25.406 -35.345 8.776 1.00 14.80 C ANISOU 207 CB SER A 45 1701 2063 1859 311 -24 -26 C ATOM 208 OG SER A 45 24.624 -35.531 9.945 1.00 16.52 O ANISOU 208 OG SER A 45 1902 2263 2111 307 -34 -24 O ATOM 209 N LEU A 46 26.626 -36.957 6.081 1.00 13.22 N ANISOU 209 N LEU A 46 1549 1905 1569 326 -16 -80 N ATOM 210 CA LEU A 46 27.235 -36.730 4.781 1.00 15.01 C ANISOU 210 CA LEU A 46 1814 2152 1738 329 17 -84 C ATOM 211 C LEU A 46 26.719 -35.444 4.171 1.00 15.48 C ANISOU 211 C LEU A 46 1907 2212 1761 324 18 -39 C ATOM 212 O LEU A 46 25.527 -35.341 3.874 1.00 15.75 O ANISOU 212 O LEU A 46 1959 2243 1783 332 -36 -22 O ATOM 213 CB LEU A 46 26.971 -37.943 3.855 1.00 17.24 C ANISOU 213 CB LEU A 46 2130 2442 1979 342 -9 -122 C ATOM 214 CG LEU A 46 27.726 -37.916 2.531 1.00 17.04 C ANISOU 214 CG LEU A 46 2155 2438 1883 348 39 -138 C ATOM 215 CD1 LEU A 46 29.214 -38.155 2.782 1.00 16.85 C ANISOU 215 CD1 LEU A 46 2092 2420 1890 351 110 -167 C ATOM 216 CD2 LEU A 46 27.199 -38.936 1.579 1.00 19.11 C ANISOU 216 CD2 LEU A 46 2469 2700 2090 360 -1 -174 C ATOM 217 N ILE A 47 27.606 -34.471 3.960 1.00 15.62 N ANISOU 217 N ILE A 47 1935 2232 1768 311 75 -18 N ATOM 218 CA ILE A 47 27.176 -33.177 3.388 1.00 16.98 C ANISOU 218 CA ILE A 47 2153 2395 1904 305 75 32 C ATOM 219 C ILE A 47 27.640 -32.959 1.969 1.00 18.75 C ANISOU 219 C ILE A 47 2447 2633 2044 299 114 43 C ATOM 220 O ILE A 47 27.159 -32.044 1.297 1.00 22.49 O ANISOU 220 O ILE A 47 2981 3094 2470 299 100 87 O ATOM 221 CB ILE A 47 27.588 -32.003 4.314 1.00 18.52 C ANISOU 221 CB ILE A 47 2321 2566 2151 288 104 59 C ATOM 222 CG1 ILE A 47 29.090 -31.953 4.513 1.00 19.69 C ANISOU 222 CG1 ILE A 47 2438 2721 2323 262 172 42 C ATOM 223 CG2 ILE A 47 26.875 -32.094 5.631 1.00 18.20 C ANISOU 223 CG2 ILE A 47 2235 2507 2172 298 63 53 C ATOM 224 CD1 ILE A 47 29.620 -30.531 4.930 1.00 23.47 C ANISOU 224 CD1 ILE A 47 2915 3171 2831 232 206 76 C ATOM 225 N ASN A 48 28.525 -33.788 1.469 1.00 20.34 N ANISOU 225 N ASN A 48 2651 2858 2221 297 162 4 N ATOM 226 CA ASN A 48 29.089 -33.667 0.148 1.00 22.59 C ANISOU 226 CA ASN A 48 3007 3159 2418 288 221 6 C ATOM 227 C ASN A 48 29.602 -35.063 -0.164 1.00 22.76 C ANISOU 227 C ASN A 48 3018 3201 2429 305 242 -59 C ATOM 228 O ASN A 48 29.767 -35.864 0.760 1.00 20.97 O ANISOU 228 O ASN A 48 2721 2971 2276 317 221 -95 O ATOM 229 CB ASN A 48 30.224 -32.633 0.307 1.00 29.90 C ANISOU 229 CB ASN A 48 3912 4079 3370 253 311 32 C ATOM 230 CG ASN A 48 31.005 -32.441 -0.870 1.00 39.63 C ANISOU 230 CG ASN A 48 5203 5327 4525 234 399 37 C ATOM 231 OD1 ASN A 48 30.708 -31.573 -1.708 1.00 47.34 O ANISOU 231 OD1 ASN A 48 6270 6292 5425 220 410 88 O ATOM 232 ND2 ASN A 48 32.093 -33.164 -0.945 1.00 36.70 N ANISOU 232 ND2 ASN A 48 4786 4981 4178 232 474 -13 N ATOM 233 N GLU A 49 29.872 -35.362 -1.433 1.00 22.50 N ANISOU 233 N GLU A 49 3062 3185 2302 309 283 -75 N ATOM 234 CA GLU A 49 30.366 -36.691 -1.790 1.00 24.64 C ANISOU 234 CA GLU A 49 3330 3471 2561 331 307 -145 C ATOM 235 C GLU A 49 31.649 -37.022 -1.052 1.00 23.47 C ANISOU 235 C GLU A 49 3085 3330 2504 332 378 -180 C ATOM 236 O GLU A 49 31.992 -38.193 -0.922 1.00 24.95 O ANISOU 236 O GLU A 49 3243 3518 2720 359 377 -239 O ATOM 237 CB GLU A 49 30.649 -36.815 -3.297 1.00 29.78 C ANISOU 237 CB GLU A 49 4089 4140 3087 332 366 -159 C ATOM 238 CG GLU A 49 29.440 -36.872 -4.154 1.00 38.34 C ANISOU 238 CG GLU A 49 5279 5216 4072 342 276 -144 C ATOM 239 CD GLU A 49 29.798 -36.944 -5.641 1.00 43.82 C ANISOU 239 CD GLU A 49 6100 5925 4624 341 339 -158 C ATOM 240 OE1 GLU A 49 28.863 -36.865 -6.461 1.00 50.25 O ANISOU 240 OE1 GLU A 49 7019 6731 5340 347 260 -141 O ATOM 241 OE2 GLU A 49 31.005 -37.081 -5.984 1.00 41.18 O ANISOU 241 OE2 GLU A 49 5760 5611 4277 336 466 -188 O ATOM 242 N GLN A 50 32.391 -36.016 -0.600 1.00 22.71 N ANISOU 242 N GLN A 50 2938 3234 2456 302 436 -148 N ATOM 243 CA GLN A 50 33.671 -36.278 0.054 1.00 21.05 C ANISOU 243 CA GLN A 50 2626 3031 2340 302 496 -183 C ATOM 244 C GLN A 50 33.792 -35.804 1.493 1.00 20.64 C ANISOU 244 C GLN A 50 2490 2960 2393 289 451 -164 C ATOM 245 O GLN A 50 34.866 -35.905 2.064 1.00 20.86 O ANISOU 245 O GLN A 50 2433 2991 2503 286 486 -190 O ATOM 246 CB GLN A 50 34.811 -35.609 -0.705 1.00 27.40 C ANISOU 246 CB GLN A 50 3428 3856 3128 271 624 -178 C ATOM 247 CG GLN A 50 35.030 -36.080 -2.083 1.00 36.31 C ANISOU 247 CG GLN A 50 4636 5006 4154 282 699 -207 C ATOM 248 CD GLN A 50 36.233 -35.393 -2.689 1.00 40.24 C ANISOU 248 CD GLN A 50 5117 5524 4650 244 844 -200 C ATOM 249 OE1 GLN A 50 37.311 -35.953 -2.690 1.00 35.86 O ANISOU 249 OE1 GLN A 50 4482 4987 4155 257 923 -255 O ATOM 250 NE2 GLN A 50 36.060 -34.135 -3.139 1.00 43.16 N ANISOU 250 NE2 GLN A 50 5553 5886 4962 196 878 -131 N ATOM 251 N TRP A 51 32.728 -35.260 2.068 1.00 18.18 N ANISOU 251 N TRP A 51 2202 2627 2079 282 375 -121 N ATOM 252 CA TRP A 51 32.826 -34.642 3.396 1.00 18.60 C ANISOU 252 CA TRP A 51 2194 2658 2214 267 342 -101 C ATOM 253 C TRP A 51 31.678 -35.015 4.319 1.00 16.99 C ANISOU 253 C TRP A 51 1993 2434 2027 285 249 -96 C ATOM 254 O TRP A 51 30.512 -35.031 3.908 1.00 16.82 O ANISOU 254 O TRP A 51 2025 2409 1956 294 206 -77 O ATOM 255 CB TRP A 51 32.905 -33.120 3.306 1.00 18.71 C ANISOU 255 CB TRP A 51 2228 2660 2221 227 375 -47 C ATOM 256 CG TRP A 51 34.167 -32.594 2.659 1.00 19.14 C ANISOU 256 CG TRP A 51 2264 2728 2282 192 479 -47 C ATOM 257 CD1 TRP A 51 34.404 -32.432 1.334 1.00 20.22 C ANISOU 257 CD1 TRP A 51 2462 2883 2340 180 555 -37 C ATOM 258 CD2 TRP A 51 35.348 -32.174 3.335 1.00 18.22 C ANISOU 258 CD2 TRP A 51 2060 2607 2257 162 517 -59 C ATOM 259 NE1 TRP A 51 35.672 -31.914 1.133 1.00 23.02 N ANISOU 259 NE1 TRP A 51 2768 3245 2735 139 655 -39 N ATOM 260 CE2 TRP A 51 36.274 -31.764 2.355 1.00 21.66 C ANISOU 260 CE2 TRP A 51 2495 3059 2675 128 628 -55 C ATOM 261 CE3 TRP A 51 35.719 -32.132 4.672 1.00 18.98 C ANISOU 261 CE3 TRP A 51 2080 2685 2446 159 466 -74 C ATOM 262 CZ2 TRP A 51 37.537 -31.278 2.681 1.00 24.11 C ANISOU 262 CZ2 TRP A 51 2717 3370 3074 87 689 -65 C ATOM 263 CZ3 TRP A 51 36.974 -31.635 5.006 1.00 21.57 C ANISOU 263 CZ3 TRP A 51 2328 3011 2856 122 511 -86 C ATOM 264 CH2 TRP A 51 37.863 -31.204 4.003 1.00 22.85 C ANISOU 264 CH2 TRP A 51 2476 3191 3014 84 623 -82 C ATOM 265 N VAL A 52 32.052 -35.282 5.574 1.00 17.53 N ANISOU 265 N VAL A 52 2003 2488 2170 288 219 -112 N ATOM 266 CA VAL A 52 31.138 -35.621 6.664 1.00 16.76 C ANISOU 266 CA VAL A 52 1905 2369 2095 298 147 -106 C ATOM 267 C VAL A 52 31.307 -34.604 7.801 1.00 16.23 C ANISOU 267 C VAL A 52 1815 2280 2073 277 137 -83 C ATOM 268 O VAL A 52 32.447 -34.227 8.112 1.00 15.64 O ANISOU 268 O VAL A 52 1698 2203 2041 261 163 -93 O ATOM 269 CB VAL A 52 31.464 -37.057 7.179 1.00 15.97 C ANISOU 269 CB VAL A 52 1777 2261 2028 324 115 -150 C ATOM 270 CG1 VAL A 52 30.844 -37.330 8.546 1.00 15.53 C ANISOU 270 CG1 VAL A 52 1720 2178 2003 325 56 -142 C ATOM 271 CG2 VAL A 52 31.009 -38.097 6.162 1.00 17.58 C ANISOU 271 CG2 VAL A 52 2018 2475 2186 345 110 -176 C ATOM 272 N VAL A 53 30.188 -34.168 8.394 1.00 15.65 N ANISOU 272 N VAL A 53 1767 2188 1992 277 102 -57 N ATOM 273 CA VAL A 53 30.144 -33.372 9.608 1.00 14.23 C ANISOU 273 CA VAL A 53 1580 1981 1845 264 86 -43 C ATOM 274 C VAL A 53 29.898 -34.261 10.813 1.00 16.01 C ANISOU 274 C VAL A 53 1800 2193 2093 275 42 -62 C ATOM 275 O VAL A 53 29.011 -35.093 10.787 1.00 15.87 O ANISOU 275 O VAL A 53 1796 2176 2059 289 20 -65 O ATOM 276 CB VAL A 53 29.037 -32.273 9.533 1.00 17.39 C ANISOU 276 CB VAL A 53 2016 2366 2225 262 84 -5 C ATOM 277 CG1 VAL A 53 28.893 -31.594 10.880 1.00 20.31 C ANISOU 277 CG1 VAL A 53 2388 2704 2624 255 69 -2 C ATOM 278 CG2 VAL A 53 29.324 -31.258 8.424 1.00 19.50 C ANISOU 278 CG2 VAL A 53 2307 2635 2466 247 122 23 C ATOM 279 N SER A 54 30.667 -34.078 11.881 1.00 16.00 N ANISOU 279 N SER A 54 1782 2172 2124 266 25 -73 N ATOM 280 CA SER A 54 30.415 -34.768 13.127 1.00 13.88 C ANISOU 280 CA SER A 54 1529 1882 1862 274 -17 -83 C ATOM 281 C SER A 54 30.752 -33.822 14.292 1.00 16.14 C ANISOU 281 C SER A 54 1829 2141 2162 257 -33 -79 C ATOM 282 O SER A 54 30.915 -32.619 14.088 1.00 16.36 O ANISOU 282 O SER A 54 1856 2163 2196 239 -9 -67 O ATOM 283 CB SER A 54 31.275 -36.028 13.154 1.00 14.81 C ANISOU 283 CB SER A 54 1622 2002 2002 291 -44 -113 C ATOM 284 OG SER A 54 30.972 -36.859 14.263 1.00 16.46 O ANISOU 284 OG SER A 54 1862 2184 2208 300 -89 -116 O ATOM 285 N ALA A 55 30.837 -34.366 15.511 1.00 14.72 N ANISOU 285 N ALA A 55 1675 1938 1981 261 -75 -90 N ATOM 286 CA ALA A 55 31.133 -33.555 16.675 1.00 14.17 C ANISOU 286 CA ALA A 55 1634 1838 1911 246 -98 -93 C ATOM 287 C ALA A 55 32.611 -33.529 16.928 1.00 16.22 C ANISOU 287 C ALA A 55 1854 2092 2215 238 -140 -116 C ATOM 288 O ALA A 55 33.306 -34.527 16.700 1.00 17.15 O ANISOU 288 O ALA A 55 1936 2220 2360 256 -166 -133 O ATOM 289 CB ALA A 55 30.414 -34.144 17.885 1.00 17.04 C ANISOU 289 CB ALA A 55 2060 2178 2237 252 -121 -89 C ATOM 290 N GLY A 56 33.107 -32.444 17.509 1.00 16.50 N ANISOU 290 N GLY A 56 1898 2106 2265 214 -156 -122 N ATOM 291 CA GLY A 56 34.514 -32.400 17.868 1.00 19.28 C ANISOU 291 CA GLY A 56 2205 2449 2673 202 -209 -148 C ATOM 292 C GLY A 56 34.947 -33.355 18.940 1.00 17.02 C ANISOU 292 C GLY A 56 1941 2142 2383 222 -292 -165 C ATOM 293 O GLY A 56 36.079 -33.872 18.926 1.00 17.23 O ANISOU 293 O GLY A 56 1907 2171 2468 233 -341 -188 O ATOM 294 N HIS A 57 34.064 -33.695 19.879 1.00 16.51 N ANISOU 294 N HIS A 57 1966 2055 2254 232 -309 -153 N ATOM 295 CA HIS A 57 34.459 -34.658 20.900 1.00 17.36 C ANISOU 295 CA HIS A 57 2115 2136 2346 251 -391 -162 C ATOM 296 C HIS A 57 34.489 -36.093 20.365 1.00 18.35 C ANISOU 296 C HIS A 57 2213 2273 2486 284 -398 -160 C ATOM 297 O HIS A 57 34.945 -36.977 21.069 1.00 19.63 O ANISOU 297 O HIS A 57 2403 2408 2646 305 -472 -166 O ATOM 298 CB HIS A 57 33.576 -34.521 22.153 1.00 19.17 C ANISOU 298 CB HIS A 57 2462 2332 2491 244 -400 -149 C ATOM 299 CG HIS A 57 32.220 -35.121 21.998 1.00 16.93 C ANISOU 299 CG HIS A 57 2219 2056 2157 251 -333 -123 C ATOM 300 ND1 HIS A 57 31.105 -34.386 21.639 1.00 17.17 N ANISOU 300 ND1 HIS A 57 2256 2100 2167 241 -251 -110 N ATOM 301 CD2 HIS A 57 31.795 -36.386 22.213 1.00 18.82 C ANISOU 301 CD2 HIS A 57 2495 2286 2369 266 -343 -109 C ATOM 302 CE1 HIS A 57 30.056 -35.193 21.605 1.00 18.47 C ANISOU 302 CE1 HIS A 57 2447 2270 2303 246 -212 -91 C ATOM 303 NE2 HIS A 57 30.458 -36.414 21.941 1.00 17.75 N ANISOU 303 NE2 HIS A 57 2377 2163 2204 258 -264 -88 N ATOM 304 N CYS A 58 34.073 -36.296 19.124 1.00 16.89 N ANISOU 304 N CYS A 58 1980 2122 2315 289 -328 -155 N ATOM 305 CA CYS A 58 34.200 -37.582 18.413 1.00 18.39 C ANISOU 305 CA CYS A 58 2138 2323 2527 320 -329 -163 C ATOM 306 C CYS A 58 35.539 -37.702 17.714 1.00 20.79 C ANISOU 306 C CYS A 58 2345 2645 2910 337 -341 -194 C ATOM 307 O CYS A 58 35.801 -38.660 16.967 1.00 20.76 O ANISOU 307 O CYS A 58 2304 2652 2933 367 -331 -211 O ATOM 308 CB CYS A 58 33.088 -37.714 17.392 1.00 18.30 C ANISOU 308 CB CYS A 58 2129 2337 2487 317 -254 -147 C ATOM 309 SG CYS A 58 31.427 -37.898 18.118 1.00 18.12 S ANISOU 309 SG CYS A 58 2197 2296 2393 302 -231 -114 S ATOM 310 N TYR A 59 36.436 -36.762 17.943 1.00 18.51 N ANISOU 310 N TYR A 59 2009 2357 2665 317 -360 -208 N ATOM 311 CA TYR A 59 37.719 -36.825 17.274 1.00 16.46 C ANISOU 311 CA TYR A 59 1642 2118 2495 327 -358 -240 C ATOM 312 C TYR A 59 38.507 -38.054 17.659 1.00 17.83 C ANISOU 312 C TYR A 59 1788 2271 2717 375 -437 -266 C ATOM 313 O TYR A 59 38.666 -38.354 18.843 1.00 20.00 O ANISOU 313 O TYR A 59 2111 2506 2980 387 -533 -264 O ATOM 314 CB TYR A 59 38.566 -35.559 17.559 1.00 17.74 C ANISOU 314 CB TYR A 59 1754 2278 2708 286 -371 -250 C ATOM 315 CG TYR A 59 39.928 -35.625 16.930 1.00 19.23 C ANISOU 315 CG TYR A 59 1815 2488 3003 290 -363 -285 C ATOM 316 CD1 TYR A 59 40.112 -35.273 15.611 1.00 22.59 C ANISOU 316 CD1 TYR A 59 2178 2952 3451 273 -256 -287 C ATOM 317 CD2 TYR A 59 41.006 -36.143 17.607 1.00 23.48 C ANISOU 317 CD2 TYR A 59 2295 3007 3618 316 -459 -317 C ATOM 318 CE1 TYR A 59 41.331 -35.435 14.987 1.00 25.90 C ANISOU 318 CE1 TYR A 59 2478 3395 3970 279 -228 -322 C ATOM 319 CE2 TYR A 59 42.233 -36.327 16.975 1.00 28.30 C ANISOU 319 CE2 TYR A 59 2772 3640 4341 328 -443 -354 C ATOM 320 CZ TYR A 59 42.376 -35.943 15.664 1.00 27.37 C ANISOU 320 CZ TYR A 59 2591 3565 4245 306 -317 -357 C ATOM 321 OH TYR A 59 43.593 -36.083 15.034 1.00 32.84 O ANISOU 321 OH TYR A 59 3146 4281 5049 314 -282 -397 O ATOM 322 N LYS A 60 39.053 -38.711 16.644 1.00 20.09 N ANISOU 322 N LYS A 60 1996 2580 3055 406 -397 -293 N ATOM 323 CA LYS A 60 40.073 -39.741 16.802 1.00 21.57 C ANISOU 323 CA LYS A 60 2124 2750 3320 459 -464 -329 C ATOM 324 C LYS A 60 41.012 -39.550 15.623 1.00 21.24 C ANISOU 324 C LYS A 60 1958 2751 3363 464 -385 -365 C ATOM 325 O LYS A 60 40.593 -39.022 14.580 1.00 22.17 O ANISOU 325 O LYS A 60 2071 2905 3446 435 -277 -355 O ATOM 326 CB LYS A 60 39.477 -41.159 16.753 1.00 22.29 C ANISOU 326 CB LYS A 60 2279 2815 3374 507 -484 -326 C ATOM 327 CG LYS A 60 38.730 -41.546 18.002 1.00 22.14 C ANISOU 327 CG LYS A 60 2380 2747 3284 504 -564 -291 C ATOM 328 CD LYS A 60 38.196 -42.985 17.896 1.00 26.55 C ANISOU 328 CD LYS A 60 2999 3271 3816 544 -580 -288 C ATOM 329 CE LYS A 60 37.392 -43.338 19.141 1.00 30.35 C ANISOU 329 CE LYS A 60 3610 3703 4220 531 -642 -246 C ATOM 330 NZ LYS A 60 38.251 -43.480 20.394 1.00 35.24 N ANISOU 330 NZ LYS A 60 4253 4276 4860 554 -769 -246 N ATOM 331 N SER A 61 42.258 -39.970 15.760 1.00 22.10 N ANISOU 331 N SER A 61 1965 2854 3579 501 -435 -406 N ATOM 332 CA SER A 61 43.215 -39.743 14.676 1.00 23.22 C ANISOU 332 CA SER A 61 1976 3037 3808 501 -344 -444 C ATOM 333 C SER A 61 42.949 -40.608 13.434 1.00 22.36 C ANISOU 333 C SER A 61 1869 2950 3675 539 -249 -465 C ATOM 334 O SER A 61 43.377 -40.252 12.352 1.00 25.23 O ANISOU 334 O SER A 61 2165 3355 4067 524 -137 -485 O ATOM 335 CB SER A 61 44.633 -39.965 15.131 1.00 26.37 C ANISOU 335 CB SER A 61 2247 3425 4347 533 -419 -489 C ATOM 336 OG SER A 61 44.885 -41.314 15.397 1.00 30.04 O ANISOU 336 OG SER A 61 2712 3856 4844 613 -494 -515 O ATOM 337 N ARG A 62 42.234 -41.720 13.585 1.00 20.76 N ANISOU 337 N ARG A 62 1753 2716 3418 583 -290 -461 N ATOM 338 CA ARG A 62 41.906 -42.588 12.458 1.00 23.96 C ANISOU 338 CA ARG A 62 2178 3134 3793 619 -214 -485 C ATOM 339 C ARG A 62 40.458 -42.932 12.620 1.00 23.51 C ANISOU 339 C ARG A 62 2256 3055 3622 604 -231 -444 C ATOM 340 O ARG A 62 40.041 -43.338 13.701 1.00 24.91 O ANISOU 340 O ARG A 62 2500 3188 3777 611 -326 -419 O ATOM 341 CB ARG A 62 42.734 -43.883 12.460 1.00 24.26 C ANISOU 341 CB ARG A 62 2161 3142 3917 702 -259 -538 C ATOM 342 CG ARG A 62 44.215 -43.669 12.418 1.00 22.89 C ANISOU 342 CG ARG A 62 1832 2984 3880 726 -255 -585 C ATOM 343 CD ARG A 62 44.756 -43.067 11.154 1.00 25.73 C ANISOU 343 CD ARG A 62 2103 3403 4269 702 -105 -614 C ATOM 344 NE ARG A 62 46.159 -42.831 11.419 1.00 26.90 N ANISOU 344 NE ARG A 62 2093 3560 4566 718 -123 -654 N ATOM 345 CZ ARG A 62 47.065 -42.547 10.502 1.00 30.82 C ANISOU 345 CZ ARG A 62 2467 4101 5142 715 -4 -697 C ATOM 346 NH1 ARG A 62 46.682 -42.379 9.253 1.00 32.34 N ANISOU 346 NH1 ARG A 62 2697 4333 5258 692 143 -699 N ATOM 347 NH2 ARG A 62 48.353 -42.449 10.829 1.00 32.24 N ANISOU 347 NH2 ARG A 62 2487 4285 5479 734 -33 -738 N ATOM 348 N ILE A 63 39.684 -42.779 11.559 1.00 20.93 N ANISOU 348 N ILE A 63 1971 2758 3222 582 -141 -436 N ATOM 349 CA ILE A 63 38.254 -43.073 11.624 1.00 19.27 C ANISOU 349 CA ILE A 63 1875 2531 2916 564 -155 -400 C ATOM 350 C ILE A 63 37.854 -43.706 10.308 1.00 19.37 C ANISOU 350 C ILE A 63 1914 2560 2886 581 -87 -426 C ATOM 351 O ILE A 63 38.235 -43.217 9.220 1.00 20.28 O ANISOU 351 O ILE A 63 1991 2718 2996 572 5 -445 O ATOM 352 CB ILE A 63 37.418 -41.791 11.797 1.00 19.45 C ANISOU 352 CB ILE A 63 1938 2576 2877 500 -130 -349 C ATOM 353 CG1 ILE A 63 37.737 -41.120 13.124 1.00 19.29 C ANISOU 353 CG1 ILE A 63 1910 2536 2885 479 -198 -327 C ATOM 354 CG2 ILE A 63 35.939 -42.077 11.745 1.00 21.82 C ANISOU 354 CG2 ILE A 63 2333 2865 3094 483 -134 -318 C ATOM 355 CD1 ILE A 63 37.023 -39.796 13.343 1.00 19.16 C ANISOU 355 CD1 ILE A 63 1928 2533 2817 423 -171 -284 C ATOM 356 N GLN A 64 37.072 -44.795 10.377 1.00 18.71 N ANISOU 356 N GLN A 64 1904 2438 2767 601 -129 -428 N ATOM 357 CA GLN A 64 36.448 -45.385 9.198 1.00 19.88 C ANISOU 357 CA GLN A 64 2099 2594 2860 609 -81 -451 C ATOM 358 C GLN A 64 34.995 -44.938 9.177 1.00 19.23 C ANISOU 358 C GLN A 64 2091 2518 2697 556 -85 -403 C ATOM 359 O GLN A 64 34.287 -45.115 10.162 1.00 20.40 O ANISOU 359 O GLN A 64 2281 2634 2836 538 -145 -368 O ATOM 360 CB GLN A 64 36.488 -46.903 9.254 1.00 21.43 C ANISOU 360 CB GLN A 64 2328 2734 3079 661 -131 -489 C ATOM 361 CG GLN A 64 35.999 -47.528 7.999 1.00 22.91 C ANISOU 361 CG GLN A 64 2564 2927 3215 671 -86 -525 C ATOM 362 CD GLN A 64 36.083 -49.020 8.066 1.00 26.92 C ANISOU 362 CD GLN A 64 3108 3369 3752 723 -137 -566 C ATOM 363 OE1 GLN A 64 35.310 -49.650 8.748 1.00 27.67 O ANISOU 363 OE1 GLN A 64 3266 3413 3835 709 -207 -539 O ATOM 364 NE2 GLN A 64 37.048 -49.584 7.384 1.00 30.14 N ANISOU 364 NE2 GLN A 64 3475 3774 4202 783 -98 -631 N ATOM 365 N VAL A 65 34.585 -44.301 8.089 1.00 18.40 N ANISOU 365 N VAL A 65 2000 2456 2536 532 -19 -399 N ATOM 366 CA VAL A 65 33.210 -43.818 7.883 1.00 16.94 C ANISOU 366 CA VAL A 65 1874 2281 2282 489 -24 -358 C ATOM 367 C VAL A 65 32.442 -44.948 7.229 1.00 18.94 C ANISOU 367 C VAL A 65 2186 2511 2499 501 -46 -384 C ATOM 368 O VAL A 65 32.864 -45.521 6.202 1.00 19.12 O ANISOU 368 O VAL A 65 2218 2540 2506 530 -12 -432 O ATOM 369 CB VAL A 65 33.162 -42.598 7.031 1.00 18.02 C ANISOU 369 CB VAL A 65 2006 2465 2376 462 42 -338 C ATOM 370 CG1 VAL A 65 31.727 -42.120 6.853 1.00 19.29 C ANISOU 370 CG1 VAL A 65 2220 2631 2478 428 22 -297 C ATOM 371 CG2 VAL A 65 34.025 -41.522 7.711 1.00 20.43 C ANISOU 371 CG2 VAL A 65 2249 2783 2729 446 61 -318 C ATOM 372 N ARG A 66 31.329 -45.315 7.854 1.00 16.22 N ANISOU 372 N ARG A 66 1881 2137 2144 477 -101 -356 N ATOM 373 CA ARG A 66 30.464 -46.335 7.300 1.00 16.81 C ANISOU 373 CA ARG A 66 2010 2184 2192 475 -132 -377 C ATOM 374 C ARG A 66 29.147 -45.729 6.858 1.00 16.72 C ANISOU 374 C ARG A 66 2024 2196 2133 432 -137 -345 C ATOM 375 O ARG A 66 28.386 -45.183 7.667 1.00 15.45 O ANISOU 375 O ARG A 66 1855 2034 1981 400 -153 -299 O ATOM 376 CB ARG A 66 30.251 -47.450 8.318 1.00 16.93 C ANISOU 376 CB ARG A 66 2050 2136 2247 478 -193 -374 C ATOM 377 CG ARG A 66 31.559 -48.131 8.670 1.00 17.04 C ANISOU 377 CG ARG A 66 2042 2120 2314 531 -204 -410 C ATOM 378 CD ARG A 66 31.379 -49.357 9.567 1.00 18.27 C ANISOU 378 CD ARG A 66 2241 2199 2502 540 -271 -407 C ATOM 379 NE ARG A 66 32.619 -50.110 9.622 1.00 18.53 N ANISOU 379 NE ARG A 66 2254 2199 2588 605 -288 -451 N ATOM 380 CZ ARG A 66 32.745 -51.349 10.093 1.00 21.17 C ANISOU 380 CZ ARG A 66 2632 2458 2956 634 -347 -465 C ATOM 381 NH1 ARG A 66 31.685 -52.005 10.574 1.00 22.71 N ANISOU 381 NH1 ARG A 66 2896 2601 3132 593 -389 -435 N ATOM 382 NH2 ARG A 66 33.942 -51.965 10.043 1.00 26.41 N ANISOU 382 NH2 ARG A 66 3265 3093 3677 705 -362 -512 N ATOM 383 N LEU A 67 28.907 -45.810 5.565 1.00 17.00 N ANISOU 383 N LEU A 67 2091 2252 2117 436 -123 -372 N ATOM 384 CA LEU A 67 27.747 -45.191 4.926 1.00 17.22 C ANISOU 384 CA LEU A 67 2142 2303 2097 405 -138 -346 C ATOM 385 C LEU A 67 26.793 -46.301 4.459 1.00 17.16 C ANISOU 385 C LEU A 67 2180 2264 2078 393 -198 -375 C ATOM 386 O LEU A 67 27.205 -47.452 4.240 1.00 19.12 O ANISOU 386 O LEU A 67 2456 2475 2333 415 -210 -423 O ATOM 387 CB LEU A 67 28.161 -44.339 3.725 1.00 17.30 C ANISOU 387 CB LEU A 67 2171 2359 2043 414 -87 -351 C ATOM 388 CG LEU A 67 29.270 -43.306 3.955 1.00 18.99 C ANISOU 388 CG LEU A 67 2342 2602 2271 421 -19 -332 C ATOM 389 CD1 LEU A 67 30.645 -43.806 3.593 1.00 22.79 C ANISOU 389 CD1 LEU A 67 2806 3087 2765 457 37 -382 C ATOM 390 CD2 LEU A 67 29.000 -42.009 3.186 1.00 24.32 C ANISOU 390 CD2 LEU A 67 3039 3315 2888 403 13 -295 C ATOM 391 N GLY A 69 25.521 -45.968 4.279 1.00 18.07 N ANISOU 391 N GLY A 69 2299 2386 2181 359 -238 -348 N ATOM 392 CA GLY A 69 24.541 -46.954 3.834 1.00 18.99 C ANISOU 392 CA GLY A 69 2449 2471 2297 338 -304 -375 C ATOM 393 C GLY A 69 24.178 -48.023 4.842 1.00 20.34 C ANISOU 393 C GLY A 69 2611 2584 2532 315 -336 -376 C ATOM 394 O GLY A 69 23.685 -49.071 4.445 1.00 21.85 O ANISOU 394 O GLY A 69 2838 2737 2728 301 -384 -410 O ATOM 395 N GLU A 70 24.406 -47.766 6.119 1.00 18.81 N ANISOU 395 N GLU A 70 2383 2382 2383 309 -311 -337 N ATOM 396 CA GLU A 70 24.122 -48.691 7.186 1.00 17.09 C ANISOU 396 CA GLU A 70 2171 2108 2216 285 -333 -327 C ATOM 397 C GLU A 70 22.692 -48.589 7.658 1.00 19.05 C ANISOU 397 C GLU A 70 2393 2350 2497 229 -353 -292 C ATOM 398 O GLU A 70 22.159 -47.491 7.844 1.00 21.89 O ANISOU 398 O GLU A 70 2710 2750 2857 217 -332 -257 O ATOM 399 CB GLU A 70 25.034 -48.395 8.397 1.00 19.22 C ANISOU 399 CB GLU A 70 2426 2371 2507 305 -300 -299 C ATOM 400 CG GLU A 70 26.471 -48.823 8.218 1.00 21.61 C ANISOU 400 CG GLU A 70 2740 2660 2808 360 -290 -337 C ATOM 401 CD GLU A 70 26.690 -50.280 8.409 1.00 22.54 C ANISOU 401 CD GLU A 70 2903 2707 2953 372 -329 -367 C ATOM 402 OE1 GLU A 70 27.855 -50.655 8.651 1.00 22.72 O ANISOU 402 OE1 GLU A 70 2927 2710 2996 421 -327 -390 O ATOM 403 OE2 GLU A 70 25.706 -51.064 8.335 1.00 19.90 O ANISOU 403 OE2 GLU A 70 2600 2333 2629 333 -366 -370 O ATOM 404 N HIS A 71 22.120 -49.750 7.960 1.00 21.50 N ANISOU 404 N HIS A 71 2725 2602 2842 193 -387 -300 N ATOM 405 CA HIS A 71 20.888 -49.802 8.732 1.00 21.57 C ANISOU 405 CA HIS A 71 2702 2595 2899 132 -388 -263 C ATOM 406 C HIS A 71 21.136 -50.597 9.999 1.00 20.97 C ANISOU 406 C HIS A 71 2660 2457 2849 113 -373 -239 C ATOM 407 O HIS A 71 21.082 -50.036 11.079 1.00 21.30 O ANISOU 407 O HIS A 71 2689 2509 2897 102 -330 -196 O ATOM 408 CB HIS A 71 19.683 -50.390 7.979 1.00 24.61 C ANISOU 408 CB HIS A 71 3074 2963 3312 85 -443 -285 C ATOM 409 CG HIS A 71 18.421 -50.237 8.766 1.00 25.70 C ANISOU 409 CG HIS A 71 3155 3097 3512 23 -427 -246 C ATOM 410 ND1 HIS A 71 17.808 -51.294 9.414 1.00 30.30 N ANISOU 410 ND1 HIS A 71 3748 3616 4147 -38 -432 -237 N ATOM 411 CD2 HIS A 71 17.772 -49.118 9.179 1.00 29.10 C ANISOU 411 CD2 HIS A 71 3519 3575 3963 15 -390 -210 C ATOM 412 CE1 HIS A 71 16.772 -50.836 10.104 1.00 30.51 C ANISOU 412 CE1 HIS A 71 3710 3659 4225 -85 -394 -200 C ATOM 413 NE2 HIS A 71 16.729 -49.521 9.977 1.00 32.64 N ANISOU 413 NE2 HIS A 71 3930 3995 4478 -49 -369 -186 N ATOM 414 N ASN A 72 21.412 -51.885 9.882 1.00 20.50 N ANISOU 414 N ASN A 72 2656 2332 2801 111 -410 -267 N ATOM 415 CA ASN A 72 21.876 -52.712 10.995 1.00 19.74 C ANISOU 415 CA ASN A 72 2615 2168 2720 106 -407 -245 C ATOM 416 C ASN A 72 23.400 -52.714 11.004 1.00 19.95 C ANISOU 416 C ASN A 72 2668 2192 2720 183 -410 -267 C ATOM 417 O ASN A 72 24.030 -53.216 10.066 1.00 21.65 O ANISOU 417 O ASN A 72 2902 2397 2927 226 -436 -320 O ATOM 418 CB ASN A 72 21.300 -54.115 10.828 1.00 24.39 C ANISOU 418 CB ASN A 72 3250 2675 3344 61 -451 -264 C ATOM 419 CG ASN A 72 21.667 -55.040 11.954 1.00 22.23 C ANISOU 419 CG ASN A 72 3047 2317 3083 51 -455 -234 C ATOM 420 OD1 ASN A 72 22.769 -54.999 12.496 1.00 22.24 O ANISOU 420 OD1 ASN A 72 3080 2307 3065 106 -455 -227 O ATOM 421 ND2 ASN A 72 20.753 -55.950 12.274 1.00 27.55 N ANISOU 421 ND2 ASN A 72 3749 2923 3795 -22 -467 -218 N ATOM 422 N ILE A 73 23.996 -52.077 12.024 1.00 19.45 N ANISOU 422 N ILE A 73 2600 2143 2646 202 -382 -230 N ATOM 423 CA ILE A 73 25.456 -51.917 12.063 1.00 18.24 C ANISOU 423 CA ILE A 73 2450 1997 2483 273 -388 -250 C ATOM 424 C ILE A 73 26.223 -53.191 12.422 1.00 19.84 C ANISOU 424 C ILE A 73 2714 2115 2707 307 -435 -266 C ATOM 425 O ILE A 73 27.449 -53.214 12.327 1.00 23.33 O ANISOU 425 O ILE A 73 3148 2558 3158 373 -448 -294 O ATOM 426 CB ILE A 73 25.943 -50.800 12.976 1.00 20.44 C ANISOU 426 CB ILE A 73 2705 2316 2747 285 -359 -213 C ATOM 427 CG1 ILE A 73 25.279 -50.862 14.336 1.00 19.92 C ANISOU 427 CG1 ILE A 73 2676 2214 2676 236 -349 -157 C ATOM 428 CG2 ILE A 73 25.867 -49.451 12.244 1.00 23.03 C ANISOU 428 CG2 ILE A 73 2967 2728 3055 291 -318 -218 C ATOM 429 CD1 ILE A 73 25.964 -49.908 15.359 1.00 24.66 C ANISOU 429 CD1 ILE A 73 3277 2839 3255 256 -335 -128 C ATOM 430 N GLU A 74 25.502 -54.257 12.782 1.00 20.14 N ANISOU 430 N GLU A 74 2811 2079 2764 262 -462 -252 N ATOM 431 CA GLU A 74 26.146 -55.506 13.170 1.00 22.98 C ANISOU 431 CA GLU A 74 3242 2344 3146 293 -514 -262 C ATOM 432 C GLU A 74 26.262 -56.486 12.022 1.00 24.65 C ANISOU 432 C GLU A 74 3474 2514 3376 319 -546 -328 C ATOM 433 O GLU A 74 27.066 -57.388 12.075 1.00 30.07 O ANISOU 433 O GLU A 74 4207 3132 4086 372 -587 -355 O ATOM 434 CB GLU A 74 25.401 -56.179 14.346 1.00 25.18 C ANISOU 434 CB GLU A 74 3593 2546 3427 229 -523 -201 C ATOM 435 CG GLU A 74 26.098 -57.423 14.912 1.00 26.87 C ANISOU 435 CG GLU A 74 3898 2650 3660 263 -585 -198 C ATOM 436 CD GLU A 74 25.524 -58.754 14.426 1.00 29.87 C ANISOU 436 CD GLU A 74 4337 2939 4072 229 -619 -221 C ATOM 437 OE1 GLU A 74 24.340 -58.832 14.010 1.00 35.84 O ANISOU 437 OE1 GLU A 74 5077 3704 4837 152 -596 -220 O ATOM 438 OE2 GLU A 74 26.292 -59.739 14.395 1.00 30.43 O ANISOU 438 OE2 GLU A 74 4468 2928 4167 285 -676 -246 O ATOM 439 N VAL A 75 25.470 -56.336 10.987 1.00 23.09 N ANISOU 439 N VAL A 75 3250 2353 3169 286 -534 -358 N ATOM 440 CA VAL A 75 25.580 -57.288 9.868 1.00 24.65 C ANISOU 440 CA VAL A 75 3483 2508 3375 310 -568 -429 C ATOM 441 C VAL A 75 25.701 -56.613 8.492 1.00 25.71 C ANISOU 441 C VAL A 75 3575 2722 3472 338 -544 -483 C ATOM 442 O VAL A 75 25.146 -55.553 8.313 1.00 22.55 O ANISOU 442 O VAL A 75 3123 2400 3047 307 -514 -457 O ATOM 443 CB VAL A 75 24.399 -58.224 9.905 1.00 32.11 C ANISOU 443 CB VAL A 75 4475 3380 4345 230 -603 -420 C ATOM 444 CG1 VAL A 75 23.168 -57.502 9.874 1.00 29.97 C ANISOU 444 CG1 VAL A 75 4151 3165 4070 154 -579 -387 C ATOM 445 CG2 VAL A 75 24.445 -59.159 8.717 1.00 32.05 C ANISOU 445 CG2 VAL A 75 4512 3325 4340 251 -645 -500 C ATOM 446 N LEU A 76 26.449 -57.215 7.544 1.00 27.58 N ANISOU 446 N LEU A 76 3841 2938 3701 399 -554 -556 N ATOM 447 CA ALEU A 76 26.462 -56.684 6.178 0.50 29.63 C ANISOU 447 CA ALEU A 76 4085 3266 3909 417 -529 -608 C ATOM 448 CA BLEU A 76 26.461 -56.720 6.160 0.50 30.04 C ANISOU 448 CA BLEU A 76 4138 3315 3961 418 -530 -609 C ATOM 449 C LEU A 76 25.128 -56.954 5.526 1.00 31.57 C ANISOU 449 C LEU A 76 4355 3500 4139 347 -570 -618 C ATOM 450 O LEU A 76 24.672 -58.123 5.473 1.00 39.65 O ANISOU 450 O LEU A 76 5437 4437 5190 320 -623 -644 O ATOM 451 CB ALEU A 76 27.532 -57.363 5.322 0.50 31.45 C ANISOU 451 CB ALEU A 76 4349 3468 4130 498 -521 -691 C ATOM 452 CB BLEU A 76 27.460 -57.503 5.306 0.50 32.34 C ANISOU 452 CB BLEU A 76 4471 3571 4245 495 -528 -694 C ATOM 453 CG ALEU A 76 29.006 -57.060 5.527 0.50 28.33 C ANISOU 453 CG ALEU A 76 3912 3098 3754 582 -474 -707 C ATOM 454 CG BLEU A 76 28.835 -56.888 5.184 0.50 26.97 C ANISOU 454 CG BLEU A 76 3741 2945 3563 574 -466 -714 C ATOM 455 CD1ALEU A 76 29.790 -57.926 4.551 0.50 28.14 C ANISOU 455 CD1ALEU A 76 3930 3036 3727 655 -464 -800 C ATOM 456 CD1BLEU A 76 29.417 -56.962 6.571 0.50 31.31 C ANISOU 456 CD1BLEU A 76 4264 3461 4173 593 -481 -664 C ATOM 457 CD2ALEU A 76 29.384 -55.559 5.356 0.50 19.03 C ANISOU 457 CD2ALEU A 76 2658 2029 2542 586 -406 -679 C ATOM 458 CD2BLEU A 76 29.707 -57.624 4.160 0.50 27.39 C ANISOU 458 CD2BLEU A 76 3829 2971 3606 650 -446 -808 C ATOM 459 N GLU A 77 24.540 -55.932 4.955 1.00 32.58 N ANISOU 459 N GLU A 77 4444 3709 4227 321 -555 -604 N ATOM 460 CA GLU A 77 23.235 -56.037 4.318 1.00 32.96 C ANISOU 460 CA GLU A 77 4500 3757 4267 256 -605 -613 C ATOM 461 C GLU A 77 23.344 -55.748 2.808 1.00 39.50 C ANISOU 461 C GLU A 77 5360 4630 5018 286 -612 -673 C ATOM 462 O GLU A 77 22.372 -55.927 2.048 1.00 41.94 O ANISOU 462 O GLU A 77 5692 4935 5310 243 -672 -696 O ATOM 463 CB GLU A 77 22.228 -55.126 5.026 1.00 38.85 C ANISOU 463 CB GLU A 77 5173 4548 5039 195 -596 -539 C ATOM 464 CG GLU A 77 21.940 -55.599 6.471 1.00 42.27 C ANISOU 464 CG GLU A 77 5599 4925 5539 152 -590 -485 C ATOM 465 CD GLU A 77 20.841 -54.796 7.169 1.00 43.34 C ANISOU 465 CD GLU A 77 5664 5100 5704 88 -570 -420 C ATOM 466 OE1 GLU A 77 20.975 -53.543 7.284 1.00 35.91 O ANISOU 466 OE1 GLU A 77 4671 4235 4739 109 -527 -390 O ATOM 467 OE2 GLU A 77 19.847 -55.424 7.619 1.00 45.94 O ANISOU 467 OE2 GLU A 77 5989 5379 6087 16 -592 -402 O ATOM 468 N GLY A 78 24.540 -55.338 2.381 1.00 33.34 N ANISOU 468 N GLY A 78 4586 3889 4192 358 -552 -699 N ATOM 469 CA GLY A 78 24.849 -55.189 0.964 1.00 31.75 C ANISOU 469 CA GLY A 78 4437 3722 3906 393 -540 -761 C ATOM 470 C GLY A 78 24.937 -53.803 0.365 1.00 28.37 C ANISOU 470 C GLY A 78 3983 3387 3409 401 -494 -734 C ATOM 471 O GLY A 78 25.407 -53.646 -0.762 1.00 32.95 O ANISOU 471 O GLY A 78 4616 3996 3907 436 -465 -782 O ATOM 472 N ASN A 79 24.521 -52.794 1.120 1.00 28.74 N ANISOU 472 N ASN A 79 3957 3478 3485 371 -482 -659 N ATOM 473 CA ASN A 79 24.492 -51.444 0.625 1.00 27.74 C ANISOU 473 CA ASN A 79 3810 3430 3302 374 -448 -626 C ATOM 474 C ASN A 79 25.517 -50.548 1.307 1.00 24.36 C ANISOU 474 C ASN A 79 3323 3042 2891 404 -363 -586 C ATOM 475 O ASN A 79 25.562 -49.331 1.083 1.00 25.07 O ANISOU 475 O ASN A 79 3390 3191 2946 403 -328 -548 O ATOM 476 CB ASN A 79 23.099 -50.883 0.848 1.00 31.93 C ANISOU 476 CB ASN A 79 4301 3977 3855 316 -507 -575 C ATOM 477 CG ASN A 79 22.034 -51.668 0.078 1.00 39.43 C ANISOU 477 CG ASN A 79 5298 4890 4792 280 -603 -615 C ATOM 478 OD1 ASN A 79 22.270 -52.098 -1.043 1.00 41.54 O ANISOU 478 OD1 ASN A 79 5646 5150 4987 302 -623 -676 O ATOM 479 ND2 ASN A 79 20.876 -51.873 0.695 1.00 43.15 N ANISOU 479 ND2 ASN A 79 5720 5338 5338 222 -661 -586 N ATOM 480 N GLU A 80 26.344 -51.137 2.144 1.00 22.01 N ANISOU 480 N GLU A 80 3004 2709 2651 431 -339 -595 N ATOM 481 CA GLU A 80 27.336 -50.377 2.871 1.00 20.29 C ANISOU 481 CA GLU A 80 2726 2522 2461 457 -275 -563 C ATOM 482 C GLU A 80 28.469 -49.884 1.980 1.00 20.48 C ANISOU 482 C GLU A 80 2754 2592 2437 503 -197 -596 C ATOM 483 O GLU A 80 28.892 -50.564 1.013 1.00 21.96 O ANISOU 483 O GLU A 80 2995 2767 2584 536 -180 -663 O ATOM 484 CB GLU A 80 27.957 -51.220 3.988 1.00 21.93 C ANISOU 484 CB GLU A 80 2916 2673 2745 479 -287 -566 C ATOM 485 CG GLU A 80 27.011 -51.672 5.070 1.00 21.24 C ANISOU 485 CG GLU A 80 2827 2537 2706 431 -344 -523 C ATOM 486 CD GLU A 80 26.313 -52.988 4.784 1.00 22.38 C ANISOU 486 CD GLU A 80 3031 2611 2861 410 -405 -559 C ATOM 487 OE1 GLU A 80 26.410 -53.524 3.659 1.00 24.09 O ANISOU 487 OE1 GLU A 80 3297 2817 3038 431 -415 -621 O ATOM 488 OE2 GLU A 80 25.721 -53.558 5.736 1.00 23.93 O ANISOU 488 OE2 GLU A 80 3232 2754 3105 371 -442 -527 O ATOM 489 N GLN A 81 29.019 -48.734 2.378 1.00 19.77 N ANISOU 489 N GLN A 81 2605 2549 2356 503 -143 -553 N ATOM 490 CA GLN A 81 30.309 -48.254 1.862 1.00 19.63 C ANISOU 490 CA GLN A 81 2566 2570 2324 541 -54 -577 C ATOM 491 C GLN A 81 31.167 -47.971 3.043 1.00 18.84 C ANISOU 491 C GLN A 81 2386 2467 2307 555 -37 -553 C ATOM 492 O GLN A 81 30.729 -47.281 3.944 1.00 20.56 O ANISOU 492 O GLN A 81 2571 2691 2549 522 -61 -495 O ATOM 493 CB GLN A 81 30.167 -47.003 1.005 1.00 19.76 C ANISOU 493 CB GLN A 81 2599 2646 2264 519 -6 -548 C ATOM 494 CG GLN A 81 29.353 -47.236 -0.230 1.00 20.46 C ANISOU 494 CG GLN A 81 2778 2737 2258 509 -34 -573 C ATOM 495 CD GLN A 81 29.078 -45.981 -0.996 1.00 21.05 C ANISOU 495 CD GLN A 81 2883 2862 2254 486 -5 -531 C ATOM 496 OE1 GLN A 81 29.996 -45.182 -1.262 1.00 23.24 O ANISOU 496 OE1 GLN A 81 3142 3174 2513 494 85 -520 O ATOM 497 NE2 GLN A 81 27.818 -45.777 -1.341 1.00 23.80 N ANISOU 497 NE2 GLN A 81 3274 3208 2560 457 -82 -506 N ATOM 498 N PHE A 82 32.367 -48.534 3.079 1.00 18.36 N ANISOU 498 N PHE A 82 2292 2391 2291 606 -2 -601 N ATOM 499 CA PHE A 82 33.293 -48.240 4.168 1.00 19.00 C ANISOU 499 CA PHE A 82 2292 2470 2456 622 3 -582 C ATOM 500 C PHE A 82 34.445 -47.434 3.580 1.00 20.41 C ANISOU 500 C PHE A 82 2413 2701 2639 639 101 -599 C ATOM 501 O PHE A 82 35.177 -47.963 2.712 1.00 20.16 O ANISOU 501 O PHE A 82 2385 2674 2602 682 160 -663 O ATOM 502 CB PHE A 82 33.890 -49.516 4.783 1.00 22.25 C ANISOU 502 CB PHE A 82 2694 2817 2941 674 -42 -622 C ATOM 503 CG PHE A 82 32.907 -50.430 5.501 1.00 19.58 C ANISOU 503 CG PHE A 82 2414 2414 2613 656 -134 -603 C ATOM 504 CD1 PHE A 82 31.579 -50.095 5.731 1.00 22.23 C ANISOU 504 CD1 PHE A 82 2786 2753 2908 593 -170 -552 C ATOM 505 CD2 PHE A 82 33.363 -51.653 5.994 1.00 23.36 C ANISOU 505 CD2 PHE A 82 2905 2822 3150 702 -182 -636 C ATOM 506 CE1 PHE A 82 30.722 -50.979 6.428 1.00 22.96 C ANISOU 506 CE1 PHE A 82 2924 2782 3018 569 -242 -535 C ATOM 507 CE2 PHE A 82 32.485 -52.523 6.678 1.00 25.72 C ANISOU 507 CE2 PHE A 82 3264 3051 3457 677 -261 -613 C ATOM 508 CZ PHE A 82 31.186 -52.171 6.887 1.00 24.90 C ANISOU 508 CZ PHE A 82 3192 2956 3313 607 -284 -562 C ATOM 509 N ILE A 83 34.615 -46.200 4.063 1.00 18.38 N ANISOU 509 N ILE A 83 2107 2480 2396 604 122 -547 N ATOM 510 CA ILE A 83 35.611 -45.272 3.512 1.00 17.51 C ANISOU 510 CA ILE A 83 1943 2420 2291 601 220 -552 C ATOM 511 C ILE A 83 36.397 -44.651 4.637 1.00 19.48 C ANISOU 511 C ILE A 83 2100 2671 2630 595 207 -527 C ATOM 512 O ILE A 83 35.845 -44.071 5.562 1.00 21.53 O ANISOU 512 O ILE A 83 2362 2923 2897 561 151 -474 O ATOM 513 CB ILE A 83 34.951 -44.170 2.671 1.00 18.44 C ANISOU 513 CB ILE A 83 2112 2579 2315 553 264 -511 C ATOM 514 CG1 ILE A 83 34.047 -44.794 1.595 1.00 20.00 C ANISOU 514 CG1 ILE A 83 2412 2771 2416 557 251 -535 C ATOM 515 CG2 ILE A 83 36.039 -43.328 2.020 1.00 20.72 C ANISOU 515 CG2 ILE A 83 2355 2911 2605 545 378 -518 C ATOM 516 CD1 ILE A 83 33.220 -43.805 0.742 1.00 23.37 C ANISOU 516 CD1 ILE A 83 2908 3229 2741 515 267 -491 C ATOM 517 N ASN A 84 37.705 -44.802 4.591 1.00 21.46 N ANISOU 517 N ASN A 84 2268 2931 2956 630 255 -569 N ATOM 518 CA ASN A 84 38.535 -44.239 5.630 1.00 21.50 C ANISOU 518 CA ASN A 84 2179 2936 3056 624 231 -552 C ATOM 519 C ASN A 84 38.622 -42.725 5.487 1.00 25.19 C ANISOU 519 C ASN A 84 2622 3444 3504 562 288 -506 C ATOM 520 O ASN A 84 38.608 -42.179 4.384 1.00 26.83 O ANISOU 520 O ASN A 84 2854 3688 3651 539 381 -504 O ATOM 521 CB ASN A 84 39.909 -44.886 5.612 1.00 23.11 C ANISOU 521 CB ASN A 84 2286 3133 3363 683 257 -617 C ATOM 522 CG ASN A 84 39.864 -46.352 5.983 1.00 25.95 C ANISOU 522 CG ASN A 84 2669 3434 3755 749 179 -656 C ATOM 523 OD1 ASN A 84 39.126 -46.764 6.884 1.00 32.39 O ANISOU 523 OD1 ASN A 84 3540 4206 4559 744 77 -624 O ATOM 524 ND2 ASN A 84 40.683 -47.148 5.325 1.00 30.14 N ANISOU 524 ND2 ASN A 84 3160 3961 4331 811 230 -728 N ATOM 525 N ALA A 85 38.710 -42.055 6.628 1.00 21.42 N ANISOU 525 N ALA A 85 2108 2956 3074 536 229 -468 N ATOM 526 CA ALA A 85 38.955 -40.640 6.670 1.00 23.62 C ANISOU 526 CA ALA A 85 2356 3262 3358 479 273 -430 C ATOM 527 C ALA A 85 40.360 -40.385 6.128 1.00 27.91 C ANISOU 527 C ALA A 85 2794 3833 3976 482 364 -468 C ATOM 528 O ALA A 85 41.306 -41.107 6.450 1.00 29.66 O ANISOU 528 O ALA A 85 2932 4045 4293 529 346 -517 O ATOM 529 CB ALA A 85 38.813 -40.151 8.053 1.00 24.13 C ANISOU 529 CB ALA A 85 2408 3300 3460 458 183 -395 C ATOM 530 N ALA A 86 40.485 -39.389 5.259 1.00 23.06 N ANISOU 530 N ALA A 86 2185 3253 3322 434 465 -447 N ATOM 531 CA ALA A 86 41.773 -38.910 4.789 1.00 22.62 C ANISOU 531 CA ALA A 86 2027 3225 3341 416 568 -472 C ATOM 532 C ALA A 86 42.268 -37.712 5.593 1.00 27.48 C ANISOU 532 C ALA A 86 2575 3837 4029 358 547 -438 C ATOM 533 O ALA A 86 43.475 -37.565 5.838 1.00 28.45 O ANISOU 533 O ALA A 86 2572 3967 4269 353 572 -469 O ATOM 534 CB ALA A 86 41.697 -38.533 3.310 1.00 23.45 C ANISOU 534 CB ALA A 86 2189 3366 3354 390 704 -467 C ATOM 535 N LYS A 87 41.328 -36.865 5.966 1.00 24.98 N ANISOU 535 N LYS A 87 2339 3506 3648 315 503 -378 N ATOM 536 CA LYS A 87 41.598 -35.688 6.787 1.00 25.59 C ANISOU 536 CA LYS A 87 2379 3567 3777 259 470 -344 C ATOM 537 C LYS A 87 40.525 -35.576 7.835 1.00 22.30 C ANISOU 537 C LYS A 87 2040 3117 3317 262 355 -309 C ATOM 538 O LYS A 87 39.343 -35.849 7.575 1.00 23.76 O ANISOU 538 O LYS A 87 2324 3298 3408 278 337 -286 O ATOM 539 CB LYS A 87 41.561 -34.417 5.955 1.00 28.68 C ANISOU 539 CB LYS A 87 2803 3971 4122 191 570 -301 C ATOM 540 CG LYS A 87 42.646 -34.249 4.943 1.00 34.92 C ANISOU 540 CG LYS A 87 3522 4794 4953 167 707 -324 C ATOM 541 CD LYS A 87 42.317 -32.976 4.123 1.00 47.62 C ANISOU 541 CD LYS A 87 5208 6404 6483 96 795 -263 C ATOM 542 CE LYS A 87 43.043 -32.903 2.775 1.00 52.16 C ANISOU 542 CE LYS A 87 5768 7013 7037 72 958 -275 C ATOM 543 NZ LYS A 87 44.480 -32.661 2.984 1.00 53.97 N ANISOU 543 NZ LYS A 87 5842 7255 7411 38 1022 -310 N ATOM 544 N ILE A 88 40.929 -35.169 9.030 1.00 22.96 N ANISOU 544 N ILE A 88 2078 3174 3471 246 276 -308 N ATOM 545 CA ILE A 88 40.000 -35.016 10.133 1.00 21.80 C ANISOU 545 CA ILE A 88 2005 2993 3283 247 176 -279 C ATOM 546 C ILE A 88 40.323 -33.675 10.738 1.00 23.88 C ANISOU 546 C ILE A 88 2251 3238 3584 188 162 -257 C ATOM 547 O ILE A 88 41.400 -33.519 11.308 1.00 25.37 O ANISOU 547 O ILE A 88 2351 3419 3869 175 129 -284 O ATOM 548 CB ILE A 88 40.138 -36.147 11.166 1.00 22.94 C ANISOU 548 CB ILE A 88 2137 3115 3464 300 71 -308 C ATOM 549 CG1 ILE A 88 39.897 -37.510 10.510 1.00 24.17 C ANISOU 549 CG1 ILE A 88 2310 3280 3594 358 86 -336 C ATOM 550 CG2 ILE A 88 39.135 -35.955 12.298 1.00 24.11 C ANISOU 550 CG2 ILE A 88 2375 3228 3558 294 -14 -276 C ATOM 551 CD1 ILE A 88 40.308 -38.709 11.346 1.00 25.57 C ANISOU 551 CD1 ILE A 88 2462 3428 3824 414 -8 -369 C ATOM 552 N ILE A 89 39.405 -32.712 10.607 1.00 20.72 N ANISOU 552 N ILE A 89 1933 2827 3113 154 182 -211 N ATOM 553 CA ILE A 89 39.636 -31.317 10.933 1.00 19.87 C ANISOU 553 CA ILE A 89 1825 2695 3031 94 188 -187 C ATOM 554 C ILE A 89 38.608 -30.877 11.974 1.00 19.25 C ANISOU 554 C ILE A 89 1834 2579 2903 96 113 -163 C ATOM 555 O ILE A 89 37.456 -30.591 11.647 1.00 20.63 O ANISOU 555 O ILE A 89 2090 2750 2999 103 133 -129 O ATOM 556 CB ILE A 89 39.561 -30.435 9.700 1.00 23.58 C ANISOU 556 CB ILE A 89 2318 3176 3465 51 296 -152 C ATOM 557 CG1 ILE A 89 40.572 -30.912 8.649 1.00 26.04 C ANISOU 557 CG1 ILE A 89 2550 3527 3816 49 389 -179 C ATOM 558 CG2 ILE A 89 39.832 -28.973 10.054 1.00 26.05 C ANISOU 558 CG2 ILE A 89 2635 3452 3811 -16 300 -126 C ATOM 559 CD1 ILE A 89 40.273 -30.351 7.265 1.00 31.10 C ANISOU 559 CD1 ILE A 89 3250 4184 4383 20 501 -141 C ATOM 560 N ARG A 90 39.032 -30.833 13.239 1.00 21.30 N ANISOU 560 N ARG A 90 2075 2810 3207 93 26 -184 N ATOM 561 CA ARG A 90 38.157 -30.342 14.303 1.00 21.57 C ANISOU 561 CA ARG A 90 2196 2807 3193 92 -35 -168 C ATOM 562 C ARG A 90 38.186 -28.820 14.327 1.00 23.08 C ANISOU 562 C ARG A 90 2409 2966 3393 36 -11 -147 C ATOM 563 O ARG A 90 39.187 -28.187 13.968 1.00 23.38 O ANISOU 563 O ARG A 90 2381 3002 3500 -11 19 -154 O ATOM 564 CB ARG A 90 38.640 -30.865 15.636 1.00 20.92 C ANISOU 564 CB ARG A 90 2104 2701 3142 109 -141 -199 C ATOM 565 CG ARG A 90 37.734 -30.426 16.769 1.00 22.74 C ANISOU 565 CG ARG A 90 2437 2893 3309 110 -192 -187 C ATOM 566 CD ARG A 90 37.900 -31.302 17.911 1.00 24.16 C ANISOU 566 CD ARG A 90 2641 3057 3483 140 -286 -208 C ATOM 567 NE ARG A 90 39.219 -31.207 18.497 1.00 25.39 N ANISOU 567 NE ARG A 90 2729 3197 3719 124 -364 -241 N ATOM 568 CZ ARG A 90 39.654 -32.025 19.440 1.00 28.21 C ANISOU 568 CZ ARG A 90 3094 3537 4086 154 -465 -262 C ATOM 569 NH1 ARG A 90 38.873 -33.027 19.877 1.00 26.80 N ANISOU 569 NH1 ARG A 90 2993 3353 3836 197 -488 -250 N ATOM 570 NH2 ARG A 90 40.856 -31.851 19.939 1.00 31.57 N ANISOU 570 NH2 ARG A 90 3453 3948 4595 140 -547 -294 N ATOM 571 N HIS A 91 37.082 -28.197 14.725 1.00 20.33 N ANISOU 571 N HIS A 91 2152 2589 2982 40 -18 -123 N ATOM 572 CA HIS A 91 37.048 -26.764 14.798 1.00 22.60 C ANISOU 572 CA HIS A 91 2473 2836 3278 -6 -2 -105 C ATOM 573 C HIS A 91 38.192 -26.265 15.665 1.00 21.94 C ANISOU 573 C HIS A 91 2345 2721 3270 -50 -62 -138 C ATOM 574 O HIS A 91 38.435 -26.797 16.761 1.00 22.71 O ANISOU 574 O HIS A 91 2445 2809 3375 -31 -147 -169 O ATOM 575 CB HIS A 91 35.736 -26.258 15.370 1.00 20.10 C ANISOU 575 CB HIS A 91 2256 2486 2894 16 -15 -88 C ATOM 576 CG HIS A 91 35.506 -24.819 15.061 1.00 21.47 C ANISOU 576 CG HIS A 91 2472 2617 3070 -19 20 -61 C ATOM 577 ND1 HIS A 91 36.117 -23.798 15.767 1.00 22.04 N ANISOU 577 ND1 HIS A 91 2554 2636 3184 -65 -13 -77 N ATOM 578 CD2 HIS A 91 34.833 -24.219 14.044 1.00 22.95 C ANISOU 578 CD2 HIS A 91 2695 2799 3226 -18 80 -19 C ATOM 579 CE1 HIS A 91 35.777 -22.639 15.230 1.00 22.51 C ANISOU 579 CE1 HIS A 91 2657 2657 3239 -90 31 -45 C ATOM 580 NE2 HIS A 91 35.018 -22.868 14.171 1.00 25.43 N ANISOU 580 NE2 HIS A 91 3043 3054 3564 -60 86 -7 N ATOM 581 N PRO A 92 38.912 -25.253 15.179 1.00 23.74 N ANISOU 581 N PRO A 92 2536 2929 3554 -111 -23 -129 N ATOM 582 CA PRO A 92 40.112 -24.822 15.911 1.00 26.84 C ANISOU 582 CA PRO A 92 2867 3295 4038 -161 -84 -165 C ATOM 583 C PRO A 92 39.832 -24.214 17.281 1.00 24.39 C ANISOU 583 C PRO A 92 2634 2926 3706 -167 -176 -185 C ATOM 584 O PRO A 92 40.745 -24.145 18.110 1.00 28.97 O ANISOU 584 O PRO A 92 3172 3485 4348 -193 -260 -224 O ATOM 585 CB PRO A 92 40.743 -23.795 14.963 1.00 28.46 C ANISOU 585 CB PRO A 92 3029 3485 4299 -233 -2 -142 C ATOM 586 CG PRO A 92 39.646 -23.350 14.071 1.00 27.84 C ANISOU 586 CG PRO A 92 3037 3403 4137 -219 77 -90 C ATOM 587 CD PRO A 92 38.792 -24.571 13.868 1.00 26.09 C ANISOU 587 CD PRO A 92 2840 3231 3843 -142 79 -87 C ATOM 588 N GLN A 93 38.618 -23.740 17.512 1.00 22.36 N ANISOU 588 N GLN A 93 2487 2642 3367 -143 -161 -164 N ATOM 589 CA AGLN A 93 38.206 -23.161 18.788 0.50 22.92 C ANISOU 589 CA AGLN A 93 2650 2658 3402 -141 -230 -187 C ATOM 590 CA BGLN A 93 38.323 -23.236 18.855 0.50 23.10 C ANISOU 590 CA BGLN A 93 2665 2682 3430 -142 -239 -191 C ATOM 591 C GLN A 93 37.433 -24.174 19.668 1.00 21.62 C ANISOU 591 C GLN A 93 2545 2509 3158 -77 -275 -199 C ATOM 592 O GLN A 93 36.808 -23.792 20.679 1.00 23.39 O ANISOU 592 O GLN A 93 2867 2694 3327 -64 -308 -214 O ATOM 593 CB AGLN A 93 37.360 -21.891 18.528 0.50 20.76 C ANISOU 593 CB AGLN A 93 2460 2334 3096 -154 -177 -160 C ATOM 594 CB BGLN A 93 37.788 -21.806 18.828 0.50 22.74 C ANISOU 594 CB BGLN A 93 2698 2574 3370 -171 -207 -175 C ATOM 595 CG AGLN A 93 38.180 -20.659 18.022 0.50 25.99 C ANISOU 595 CG AGLN A 93 3093 2950 3833 -232 -154 -151 C ATOM 596 CG BGLN A 93 38.857 -20.749 18.491 0.50 25.84 C ANISOU 596 CG BGLN A 93 3040 2926 3851 -254 -202 -178 C ATOM 597 CD AGLN A 93 37.424 -19.673 17.103 0.50 31.27 C ANISOU 597 CD AGLN A 93 3819 3585 4476 -238 -72 -101 C ATOM 598 CD BGLN A 93 39.151 -20.655 17.001 0.50 26.86 C ANISOU 598 CD BGLN A 93 3103 3086 4016 -282 -103 -134 C ATOM 599 OE1AGLN A 93 36.202 -19.474 17.192 0.50 32.81 O ANISOU 599 OE1AGLN A 93 4097 3764 4604 -187 -56 -85 O ATOM 600 OE1BGLN A 93 38.240 -20.547 16.176 0.50 26.92 O ANISOU 600 OE1BGLN A 93 3158 3103 3967 -253 -32 -90 O ATOM 601 NE2AGLN A 93 38.189 -19.021 16.222 0.50 34.74 N ANISOU 601 NE2AGLN A 93 4213 4010 4977 -305 -22 -76 N ATOM 602 NE2BGLN A 93 40.433 -20.679 16.653 0.50 29.91 N ANISOU 602 NE2BGLN A 93 3380 3486 4497 -340 -97 -147 N ATOM 603 N TYR A 94 37.441 -25.448 19.291 1.00 22.18 N ANISOU 603 N TYR A 94 2569 2635 3224 -39 -267 -194 N ATOM 604 CA TYR A 94 36.813 -26.474 20.124 1.00 18.77 C ANISOU 604 CA TYR A 94 2194 2214 2725 12 -310 -202 C ATOM 605 C TYR A 94 37.340 -26.392 21.545 1.00 22.87 C ANISOU 605 C TYR A 94 2760 2692 3236 3 -416 -239 C ATOM 606 O TYR A 94 38.538 -26.310 21.747 1.00 23.20 O ANISOU 606 O TYR A 94 2737 2726 3351 -28 -483 -265 O ATOM 607 CB TYR A 94 37.123 -27.861 19.569 1.00 19.71 C ANISOU 607 CB TYR A 94 2243 2385 2863 46 -308 -199 C ATOM 608 CG TYR A 94 36.721 -28.996 20.476 1.00 20.72 C ANISOU 608 CG TYR A 94 2425 2514 2935 89 -365 -207 C ATOM 609 CD1 TYR A 94 35.400 -29.339 20.615 1.00 21.38 C ANISOU 609 CD1 TYR A 94 2584 2601 2939 119 -323 -185 C ATOM 610 CD2 TYR A 94 37.658 -29.722 21.183 1.00 21.41 C ANISOU 610 CD2 TYR A 94 2487 2595 3054 99 -460 -233 C ATOM 611 CE1 TYR A 94 35.010 -30.368 21.421 1.00 22.38 C ANISOU 611 CE1 TYR A 94 2766 2723 3012 150 -363 -186 C ATOM 612 CE2 TYR A 94 37.262 -30.765 21.992 1.00 23.10 C ANISOU 612 CE2 TYR A 94 2767 2801 3208 137 -511 -232 C ATOM 613 CZ TYR A 94 35.947 -31.088 22.094 1.00 21.86 C ANISOU 613 CZ TYR A 94 2691 2648 2968 159 -456 -207 C ATOM 614 OH TYR A 94 35.525 -32.115 22.917 1.00 24.92 O ANISOU 614 OH TYR A 94 3152 3022 3293 188 -496 -201 O ATOM 615 N ASP A 95 36.436 -26.453 22.531 1.00 20.68 N ANISOU 615 N ASP A 95 2596 2391 2871 28 -432 -243 N ATOM 616 CA ASP A 95 36.818 -26.386 23.944 1.00 21.56 C ANISOU 616 CA ASP A 95 2783 2460 2947 22 -533 -278 C ATOM 617 C ASP A 95 36.315 -27.635 24.651 1.00 24.14 C ANISOU 617 C ASP A 95 3173 2799 3198 67 -562 -271 C ATOM 618 O ASP A 95 35.119 -27.877 24.701 1.00 22.86 O ANISOU 618 O ASP A 95 3074 2645 2966 94 -492 -250 O ATOM 619 CB ASP A 95 36.189 -25.148 24.576 1.00 22.60 C ANISOU 619 CB ASP A 95 3019 2539 3030 6 -515 -291 C ATOM 620 CG ASP A 95 36.674 -24.900 25.987 1.00 27.97 C ANISOU 620 CG ASP A 95 3790 3168 3670 -9 -624 -334 C ATOM 621 OD1 ASP A 95 36.683 -25.823 26.824 1.00 25.42 O ANISOU 621 OD1 ASP A 95 3523 2849 3287 17 -685 -340 O ATOM 622 OD2 ASP A 95 37.030 -23.739 26.274 1.00 32.46 O ANISOU 622 OD2 ASP A 95 4385 3687 4261 -49 -651 -361 O ATOM 623 N ARG A 96 37.233 -28.453 25.137 1.00 24.23 N ANISOU 623 N ARG A 96 3163 2812 3232 75 -663 -287 N ATOM 624 CA ARG A 96 36.872 -29.771 25.630 1.00 25.51 C ANISOU 624 CA ARG A 96 3377 2984 3334 117 -690 -273 C ATOM 625 C ARG A 96 36.193 -29.739 27.002 1.00 27.01 C ANISOU 625 C ARG A 96 3727 3132 3403 124 -719 -278 C ATOM 626 O ARG A 96 35.714 -30.793 27.468 1.00 27.15 O ANISOU 626 O ARG A 96 3810 3152 3355 153 -725 -258 O ATOM 627 CB ARG A 96 38.116 -30.651 25.667 1.00 25.13 C ANISOU 627 CB ARG A 96 3250 2942 3356 131 -796 -287 C ATOM 628 CG ARG A 96 39.083 -30.294 26.742 1.00 26.53 C ANISOU 628 CG ARG A 96 3461 3076 3544 113 -935 -323 C ATOM 629 CD ARG A 96 40.326 -31.200 26.664 1.00 36.35 C ANISOU 629 CD ARG A 96 4603 4329 4880 136 -1042 -338 C ATOM 630 NE ARG A 96 41.067 -31.150 27.921 1.00 52.48 N ANISOU 630 NE ARG A 96 6709 6323 6906 132 -1202 -367 N ATOM 631 CZ ARG A 96 41.081 -32.122 28.838 1.00 63.80 C ANISOU 631 CZ ARG A 96 8238 7731 8271 171 -1301 -359 C ATOM 632 NH1 ARG A 96 40.410 -33.266 28.640 1.00 64.16 N ANISOU 632 NH1 ARG A 96 8320 7791 8266 214 -1252 -323 N ATOM 633 NH2 ARG A 96 41.786 -31.953 29.960 1.00 68.71 N ANISOU 633 NH2 ARG A 96 8927 8307 8874 165 -1458 -387 N ATOM 634 N LYS A 97 36.161 -28.566 27.649 1.00 25.75 N ANISOU 634 N LYS A 97 3638 2932 3213 96 -732 -305 N ATOM 635 CA LYS A 97 35.541 -28.405 28.960 1.00 27.16 C ANISOU 635 CA LYS A 97 3981 3069 3269 101 -748 -317 C ATOM 636 C LYS A 97 34.151 -27.794 28.821 1.00 27.60 C ANISOU 636 C LYS A 97 4090 3126 3272 109 -611 -306 C ATOM 637 O LYS A 97 33.204 -28.300 29.409 1.00 27.89 O ANISOU 637 O LYS A 97 4219 3161 3216 130 -559 -293 O ATOM 638 CB LYS A 97 36.417 -27.560 29.889 1.00 33.97 C ANISOU 638 CB LYS A 97 4904 3879 4125 70 -864 -364 C ATOM 639 CG LYS A 97 37.769 -28.222 30.232 1.00 45.74 C ANISOU 639 CG LYS A 97 6350 5364 5667 69 -1022 -379 C ATOM 640 CD LYS A 97 37.573 -29.603 30.906 1.00 61.43 C ANISOU 640 CD LYS A 97 8419 7351 7571 109 -1071 -354 C ATOM 641 CE LYS A 97 38.792 -30.536 30.755 1.00 65.11 C ANISOU 641 CE LYS A 97 8789 7826 8125 127 -1199 -355 C ATOM 642 NZ LYS A 97 38.408 -31.995 30.883 1.00 65.26 N ANISOU 642 NZ LYS A 97 8850 7854 8091 172 -1200 -316 N ATOM 643 N THR A 98 34.027 -26.709 28.058 1.00 26.28 N ANISOU 643 N THR A 98 3862 2957 3165 92 -552 -312 N ATOM 644 CA THR A 98 32.729 -26.049 27.846 1.00 23.66 C ANISOU 644 CA THR A 98 3566 2621 2801 108 -431 -303 C ATOM 645 C THR A 98 31.909 -26.643 26.680 1.00 22.34 C ANISOU 645 C THR A 98 3311 2509 2669 133 -335 -260 C ATOM 646 O THR A 98 30.693 -26.412 26.552 1.00 23.46 O ANISOU 646 O THR A 98 3475 2655 2783 155 -239 -249 O ATOM 647 CB THR A 98 32.907 -24.576 27.550 1.00 25.65 C ANISOU 647 CB THR A 98 3809 2837 3101 84 -418 -325 C ATOM 648 OG1 THR A 98 33.553 -24.447 26.281 1.00 24.79 O ANISOU 648 OG1 THR A 98 3568 2755 3097 63 -415 -304 O ATOM 649 CG2 THR A 98 33.730 -23.875 28.633 1.00 29.53 C ANISOU 649 CG2 THR A 98 4386 3268 3567 52 -519 -375 C ATOM 650 N LEU A 99 32.591 -27.382 25.803 1.00 20.78 N ANISOU 650 N LEU A 99 3008 2350 2537 130 -364 -240 N ATOM 651 CA LEU A 99 32.019 -27.993 24.628 1.00 20.62 C ANISOU 651 CA LEU A 99 2904 2378 2551 149 -294 -205 C ATOM 652 C LEU A 99 31.583 -26.975 23.562 1.00 20.15 C ANISOU 652 C LEU A 99 2793 2324 2539 145 -222 -192 C ATOM 653 O LEU A 99 30.876 -27.270 22.619 1.00 19.65 O ANISOU 653 O LEU A 99 2680 2294 2491 163 -161 -164 O ATOM 654 CB LEU A 99 30.883 -28.970 24.990 1.00 23.38 C ANISOU 654 CB LEU A 99 3303 2744 2836 176 -244 -186 C ATOM 655 CG LEU A 99 31.254 -29.818 26.216 1.00 31.32 C ANISOU 655 CG LEU A 99 4395 3729 3775 177 -314 -194 C ATOM 656 CD1 LEU A 99 30.125 -30.741 26.614 1.00 34.08 C ANISOU 656 CD1 LEU A 99 4802 4087 4060 193 -254 -171 C ATOM 657 CD2 LEU A 99 32.533 -30.589 25.922 1.00 31.32 C ANISOU 657 CD2 LEU A 99 4330 3741 3830 175 -410 -196 C ATOM 658 N ASN A 100 32.040 -25.728 23.688 1.00 19.22 N ANISOU 658 N ASN A 100 2691 2166 2447 119 -238 -211 N ATOM 659 CA ASN A 100 31.831 -24.722 22.638 1.00 17.38 C ANISOU 659 CA ASN A 100 2415 1927 2264 110 -183 -193 C ATOM 660 C ASN A 100 32.552 -25.138 21.350 1.00 17.89 C ANISOU 660 C ASN A 100 2372 2034 2393 95 -179 -169 C ATOM 661 O ASN A 100 33.653 -25.702 21.412 1.00 20.39 O ANISOU 661 O ASN A 100 2640 2366 2743 76 -235 -181 O ATOM 662 CB ASN A 100 32.315 -23.350 23.131 1.00 18.95 C ANISOU 662 CB ASN A 100 2661 2061 2478 78 -212 -221 C ATOM 663 CG ASN A 100 31.796 -22.175 22.311 1.00 21.04 C ANISOU 663 CG ASN A 100 2922 2297 2774 77 -151 -202 C ATOM 664 OD1 ASN A 100 32.465 -21.123 22.223 1.00 25.94 O ANISOU 664 OD1 ASN A 100 3548 2870 3438 37 -172 -212 O ATOM 665 ND2 ASN A 100 30.636 -22.297 21.779 1.00 15.85 N ANISOU 665 ND2 ASN A 100 2261 1661 2101 119 -84 -175 N ATOM 666 N ASN A 101 31.925 -24.917 20.196 1.00 19.21 N ANISOU 666 N ASN A 101 2504 2221 2574 108 -113 -135 N ATOM 667 CA ASN A 101 32.507 -25.229 18.871 1.00 18.56 C ANISOU 667 CA ASN A 101 2337 2178 2537 94 -92 -111 C ATOM 668 C ASN A 101 32.699 -26.737 18.729 1.00 16.88 C ANISOU 668 C ASN A 101 2080 2016 2318 114 -108 -113 C ATOM 669 O ASN A 101 33.743 -27.213 18.273 1.00 17.48 O ANISOU 669 O ASN A 101 2088 2115 2437 98 -126 -120 O ATOM 670 CB ASN A 101 33.811 -24.469 18.618 1.00 18.38 C ANISOU 670 CB ASN A 101 2272 2133 2577 39 -112 -120 C ATOM 671 CG ASN A 101 33.632 -22.945 18.740 1.00 19.26 C ANISOU 671 CG ASN A 101 2437 2181 2698 14 -98 -117 C ATOM 672 OD1 ASN A 101 32.792 -22.331 18.081 1.00 19.94 O ANISOU 672 OD1 ASN A 101 2550 2254 2771 31 -46 -87 O ATOM 673 ND2 ASN A 101 34.378 -22.357 19.639 1.00 23.00 N ANISOU 673 ND2 ASN A 101 2933 2610 3195 -22 -154 -151 N ATOM 674 N ASP A 102 31.712 -27.495 19.190 1.00 16.63 N ANISOU 674 N ASP A 102 2087 1996 2236 149 -102 -110 N ATOM 675 CA ASP A 102 31.757 -28.965 19.139 1.00 16.40 C ANISOU 675 CA ASP A 102 2033 2003 2197 170 -120 -110 C ATOM 676 C ASP A 102 31.364 -29.476 17.761 1.00 15.67 C ANISOU 676 C ASP A 102 1888 1952 2114 185 -74 -87 C ATOM 677 O ASP A 102 30.276 -30.013 17.513 1.00 16.43 O ANISOU 677 O ASP A 102 1997 2064 2182 208 -46 -72 O ATOM 678 CB ASP A 102 30.859 -29.585 20.207 1.00 16.99 C ANISOU 678 CB ASP A 102 2175 2066 2213 191 -126 -114 C ATOM 679 CG ASP A 102 31.082 -31.071 20.366 1.00 19.16 C ANISOU 679 CG ASP A 102 2440 2360 2479 206 -160 -115 C ATOM 680 OD1 ASP A 102 32.125 -31.555 19.892 1.00 17.21 O ANISOU 680 OD1 ASP A 102 2136 2130 2275 203 -195 -123 O ATOM 681 OD2 ASP A 102 30.222 -31.742 20.993 1.00 17.83 O ANISOU 681 OD2 ASP A 102 2324 2187 2264 219 -148 -107 O ATOM 682 N ILE A 103 32.297 -29.316 16.826 1.00 18.16 N ANISOU 682 N ILE A 103 2144 2284 2471 166 -64 -86 N ATOM 683 CA ILE A 103 32.062 -29.700 15.438 1.00 16.44 C ANISOU 683 CA ILE A 103 1890 2103 2252 177 -19 -67 C ATOM 684 C ILE A 103 33.396 -30.093 14.786 1.00 18.58 C ANISOU 684 C ILE A 103 2092 2398 2569 162 -16 -82 C ATOM 685 O ILE A 103 34.482 -29.597 15.155 1.00 16.89 O ANISOU 685 O ILE A 103 1845 2169 2404 133 -36 -99 O ATOM 686 CB ILE A 103 31.331 -28.565 14.675 1.00 15.10 C ANISOU 686 CB ILE A 103 1746 1923 2069 172 27 -36 C ATOM 687 CG1 ILE A 103 30.856 -29.039 13.296 1.00 17.32 C ANISOU 687 CG1 ILE A 103 2013 2240 2328 188 61 -15 C ATOM 688 CG2 ILE A 103 32.231 -27.350 14.534 1.00 17.67 C ANISOU 688 CG2 ILE A 103 2063 2220 2429 131 39 -32 C ATOM 689 CD1 ILE A 103 29.810 -28.118 12.668 1.00 18.87 C ANISOU 689 CD1 ILE A 103 2247 2422 2500 199 85 20 C ATOM 690 N MET A 104 33.304 -30.999 13.818 1.00 17.05 N ANISOU 690 N MET A 104 1873 2240 2365 182 10 -81 N ATOM 691 CA MET A 104 34.474 -31.494 13.105 1.00 19.07 C ANISOU 691 CA MET A 104 2061 2521 2662 178 29 -101 C ATOM 692 C MET A 104 34.045 -31.866 11.680 1.00 16.56 C ANISOU 692 C MET A 104 1748 2236 2307 191 86 -88 C ATOM 693 O MET A 104 32.913 -32.252 11.461 1.00 17.41 O ANISOU 693 O MET A 104 1899 2349 2366 214 81 -74 O ATOM 694 CB MET A 104 35.075 -32.648 13.915 1.00 24.25 C ANISOU 694 CB MET A 104 2688 3176 3349 203 -32 -135 C ATOM 695 CG MET A 104 35.790 -33.685 13.234 1.00 28.68 C ANISOU 695 CG MET A 104 3193 3764 3941 226 -20 -161 C ATOM 696 SD MET A 104 36.238 -34.992 14.427 1.00 23.22 S ANISOU 696 SD MET A 104 2494 3051 3279 265 -115 -192 S ATOM 697 CE MET A 104 35.004 -36.227 14.266 1.00 22.38 C ANISOU 697 CE MET A 104 2451 2944 3109 300 -120 -182 C ATOM 698 N LEU A 105 34.968 -31.724 10.733 1.00 17.00 N ANISOU 698 N LEU A 105 1759 2313 2385 174 141 -95 N ATOM 699 CA LEU A 105 34.801 -32.174 9.359 1.00 16.65 C ANISOU 699 CA LEU A 105 1725 2301 2298 186 198 -91 C ATOM 700 C LEU A 105 35.755 -33.335 9.091 1.00 17.61 C ANISOU 700 C LEU A 105 1786 2448 2458 210 209 -136 C ATOM 701 O LEU A 105 36.926 -33.368 9.491 1.00 19.14 O ANISOU 701 O LEU A 105 1905 2641 2727 201 208 -164 O ATOM 702 CB LEU A 105 35.130 -31.032 8.392 1.00 17.28 C ANISOU 702 CB LEU A 105 1818 2384 2365 145 271 -61 C ATOM 703 CG LEU A 105 34.049 -29.969 8.229 1.00 19.56 C ANISOU 703 CG LEU A 105 2182 2647 2604 135 267 -12 C ATOM 704 CD1 LEU A 105 34.600 -28.732 7.518 1.00 21.05 C ANISOU 704 CD1 LEU A 105 2384 2821 2792 86 332 21 C ATOM 705 CD2 LEU A 105 32.903 -30.582 7.449 1.00 22.03 C ANISOU 705 CD2 LEU A 105 2550 2978 2844 171 257 0 C ATOM 706 N ILE A 106 35.219 -34.317 8.400 1.00 15.94 N ANISOU 706 N ILE A 106 1603 2254 2200 243 215 -148 N ATOM 707 CA ILE A 106 36.005 -35.435 7.924 1.00 18.53 C ANISOU 707 CA ILE A 106 1886 2601 2553 274 237 -194 C ATOM 708 C ILE A 106 35.982 -35.432 6.402 1.00 20.21 C ANISOU 708 C ILE A 106 2130 2844 2706 272 321 -194 C ATOM 709 O ILE A 106 34.912 -35.451 5.802 1.00 19.36 O ANISOU 709 O ILE A 106 2098 2738 2519 277 314 -172 O ATOM 710 CB ILE A 106 35.406 -36.767 8.412 1.00 18.17 C ANISOU 710 CB ILE A 106 1863 2542 2498 318 169 -216 C ATOM 711 CG1 ILE A 106 35.589 -36.889 9.929 1.00 19.55 C ANISOU 711 CG1 ILE A 106 2017 2685 2725 322 90 -218 C ATOM 712 CG2 ILE A 106 36.024 -37.968 7.667 1.00 20.46 C ANISOU 712 CG2 ILE A 106 2128 2846 2801 357 197 -266 C ATOM 713 CD1 ILE A 106 34.731 -37.961 10.554 1.00 20.94 C ANISOU 713 CD1 ILE A 106 2242 2838 2878 350 25 -220 C ATOM 714 N LYS A 107 37.156 -35.449 5.766 1.00 20.08 N ANISOU 714 N LYS A 107 2056 2848 2724 265 399 -221 N ATOM 715 CA LYS A 107 37.232 -35.636 4.334 1.00 20.58 C ANISOU 715 CA LYS A 107 2159 2941 2721 268 487 -231 C ATOM 716 C LYS A 107 37.477 -37.115 4.053 1.00 20.24 C ANISOU 716 C LYS A 107 2101 2906 2685 324 483 -291 C ATOM 717 O LYS A 107 38.409 -37.706 4.589 1.00 21.26 O ANISOU 717 O LYS A 107 2142 3031 2903 349 475 -334 O ATOM 718 CB LYS A 107 38.371 -34.798 3.738 1.00 22.49 C ANISOU 718 CB LYS A 107 2350 3200 2994 225 597 -227 C ATOM 719 CG LYS A 107 38.388 -34.854 2.212 1.00 22.77 C ANISOU 719 CG LYS A 107 2452 3263 2937 221 701 -229 C ATOM 720 CD LYS A 107 39.521 -34.056 1.585 1.00 27.14 C ANISOU 720 CD LYS A 107 2959 3834 3518 170 829 -223 C ATOM 721 CE LYS A 107 39.428 -34.142 0.087 1.00 32.72 C ANISOU 721 CE LYS A 107 3758 4565 4109 167 933 -221 C ATOM 722 NZ LYS A 107 40.653 -33.601 -0.604 1.00 37.84 N ANISOU 722 NZ LYS A 107 4355 5236 4786 120 1085 -226 N ATOM 723 N LEU A 108 36.636 -37.712 3.217 1.00 19.19 N ANISOU 723 N LEU A 108 2053 2777 2460 346 481 -297 N ATOM 724 CA LEU A 108 36.756 -39.111 2.852 1.00 21.07 C ANISOU 724 CA LEU A 108 2296 3014 2694 398 476 -357 C ATOM 725 C LEU A 108 37.903 -39.353 1.891 1.00 22.61 C ANISOU 725 C LEU A 108 2456 3238 2898 411 592 -405 C ATOM 726 O LEU A 108 38.263 -38.499 1.074 1.00 22.34 O ANISOU 726 O LEU A 108 2437 3228 2822 374 689 -384 O ATOM 727 CB LEU A 108 35.458 -39.571 2.210 1.00 19.78 C ANISOU 727 CB LEU A 108 2242 2846 2430 407 432 -349 C ATOM 728 CG LEU A 108 34.180 -39.369 3.025 1.00 20.87 C ANISOU 728 CG LEU A 108 2413 2959 2559 394 330 -304 C ATOM 729 CD1 LEU A 108 32.937 -39.816 2.279 1.00 22.21 C ANISOU 729 CD1 LEU A 108 2673 3125 2640 400 287 -301 C ATOM 730 CD2 LEU A 108 34.258 -40.137 4.322 1.00 21.87 C ANISOU 730 CD2 LEU A 108 2489 3055 2766 416 257 -321 C ATOM 731 N SER A 109 38.500 -40.535 1.998 1.00 20.39 N ANISOU 731 N SER A 109 2128 2948 2672 465 588 -469 N ATOM 732 CA SER A 109 39.643 -40.898 1.158 1.00 23.96 C ANISOU 732 CA SER A 109 2531 3424 3149 489 705 -528 C ATOM 733 C SER A 109 39.263 -41.162 -0.291 1.00 26.00 C ANISOU 733 C SER A 109 2899 3701 3278 495 782 -548 C ATOM 734 O SER A 109 40.106 -41.065 -1.178 1.00 27.37 O ANISOU 734 O SER A 109 3057 3904 3440 495 911 -580 O ATOM 735 CB SER A 109 40.396 -42.079 1.773 1.00 26.60 C ANISOU 735 CB SER A 109 2778 3736 3592 556 667 -594 C ATOM 736 OG SER A 109 39.596 -43.249 1.749 1.00 33.13 O ANISOU 736 OG SER A 109 3684 4530 4376 600 590 -620 O ATOM 737 N SER A 110 37.988 -41.487 -0.515 1.00 26.49 N ANISOU 737 N SER A 110 3074 3747 3246 498 703 -530 N ATOM 738 CA SER A 110 37.382 -41.550 -1.852 1.00 31.33 C ANISOU 738 CA SER A 110 3816 4373 3716 493 744 -535 C ATOM 739 C SER A 110 35.960 -41.039 -1.806 1.00 27.44 C ANISOU 739 C SER A 110 3413 3868 3145 461 647 -471 C ATOM 740 O SER A 110 35.364 -40.915 -0.723 1.00 24.52 O ANISOU 740 O SER A 110 3008 3476 2833 453 548 -437 O ATOM 741 CB SER A 110 37.370 -42.965 -2.391 1.00 34.36 C ANISOU 741 CB SER A 110 4244 4740 4073 552 740 -615 C ATOM 742 OG SER A 110 36.589 -43.815 -1.582 1.00 34.04 O ANISOU 742 OG SER A 110 4208 4658 4069 575 607 -621 O ATOM 743 N ARG A 111 35.401 -40.728 -2.970 1.00 26.68 N ANISOU 743 N ARG A 111 3434 3785 2918 445 673 -456 N ATOM 744 CA ARG A 111 34.079 -40.112 -3.020 1.00 25.83 C ANISOU 744 CA ARG A 111 3404 3667 2743 418 580 -393 C ATOM 745 C ARG A 111 33.037 -41.196 -2.747 1.00 25.11 C ANISOU 745 C ARG A 111 3342 3547 2651 445 458 -421 C ATOM 746 O ARG A 111 33.102 -42.290 -3.296 1.00 29.92 O ANISOU 746 O ARG A 111 3993 4147 3228 478 459 -486 O ATOM 747 CB ARG A 111 33.810 -39.454 -4.369 1.00 28.98 C ANISOU 747 CB ARG A 111 3928 4084 2999 395 631 -366 C ATOM 748 CG ARG A 111 34.677 -38.244 -4.641 1.00 34.83 C ANISOU 748 CG ARG A 111 4655 4846 3734 354 750 -322 C ATOM 749 CD ARG A 111 34.700 -37.857 -6.121 1.00 42.84 C ANISOU 749 CD ARG A 111 5808 5876 4593 337 832 -309 C ATOM 750 NE ARG A 111 35.158 -36.472 -6.316 1.00 51.51 N ANISOU 750 NE ARG A 111 6915 6981 5676 283 916 -240 N ATOM 751 CZ ARG A 111 36.428 -36.057 -6.238 1.00 57.75 C ANISOU 751 CZ ARG A 111 7624 7788 6529 255 1052 -245 C ATOM 752 NH1 ARG A 111 37.419 -36.910 -5.963 1.00 60.18 N ANISOU 752 NH1 ARG A 111 7827 8113 6927 283 1119 -319 N ATOM 753 NH2 ARG A 111 36.712 -34.777 -6.435 1.00 58.55 N ANISOU 753 NH2 ARG A 111 7748 7886 6612 197 1118 -176 N ATOM 754 N ALA A 112 32.097 -40.884 -1.876 1.00 22.17 N ANISOU 754 N ALA A 112 2947 3157 2321 429 360 -375 N ATOM 755 CA ALA A 112 30.969 -41.770 -1.631 1.00 20.06 C ANISOU 755 CA ALA A 112 2705 2861 2054 440 247 -390 C ATOM 756 C ALA A 112 30.185 -41.892 -2.937 1.00 22.01 C ANISOU 756 C ALA A 112 3073 3113 2178 439 216 -399 C ATOM 757 O ALA A 112 30.075 -40.915 -3.699 1.00 25.14 O ANISOU 757 O ALA A 112 3530 3529 2492 420 246 -358 O ATOM 758 CB ALA A 112 30.072 -41.209 -0.577 1.00 23.77 C ANISOU 758 CB ALA A 112 3132 3318 2582 417 168 -334 C ATOM 759 N VAL A 113 29.657 -43.089 -3.192 1.00 23.00 N ANISOU 759 N VAL A 113 3238 3214 2288 457 152 -451 N ATOM 760 CA VAL A 113 28.770 -43.340 -4.327 1.00 22.63 C ANISOU 760 CA VAL A 113 3304 3163 2130 454 91 -466 C ATOM 761 C VAL A 113 27.355 -42.956 -3.877 1.00 22.84 C ANISOU 761 C VAL A 113 3317 3178 2185 429 -30 -415 C ATOM 762 O VAL A 113 26.855 -43.445 -2.857 1.00 22.18 O ANISOU 762 O VAL A 113 3162 3069 2196 423 -89 -413 O ATOM 763 CB VAL A 113 28.823 -44.797 -4.723 1.00 24.25 C ANISOU 763 CB VAL A 113 3553 3340 2321 482 68 -550 C ATOM 764 CG1 VAL A 113 27.844 -45.093 -5.866 1.00 26.09 C ANISOU 764 CG1 VAL A 113 3910 3564 2440 475 -15 -571 C ATOM 765 CG2 VAL A 113 30.228 -45.165 -5.186 1.00 26.95 C ANISOU 765 CG2 VAL A 113 3902 3694 2644 515 196 -608 C ATOM 766 N ILE A 114 26.750 -42.023 -4.594 1.00 23.83 N ANISOU 766 N ILE A 114 3506 3317 2230 416 -59 -369 N ATOM 767 CA ILE A 114 25.438 -41.502 -4.244 1.00 23.01 C ANISOU 767 CA ILE A 114 3379 3204 2159 399 -168 -319 C ATOM 768 C ILE A 114 24.373 -42.345 -4.923 1.00 25.66 C ANISOU 768 C ILE A 114 3776 3520 2453 398 -284 -356 C ATOM 769 O ILE A 114 24.400 -42.531 -6.158 1.00 28.63 O ANISOU 769 O ILE A 114 4268 3901 2710 406 -296 -384 O ATOM 770 CB ILE A 114 25.287 -40.049 -4.717 1.00 21.94 C ANISOU 770 CB ILE A 114 3287 3086 1964 391 -156 -249 C ATOM 771 CG1 ILE A 114 26.398 -39.176 -4.144 1.00 23.29 C ANISOU 771 CG1 ILE A 114 3405 3271 2173 383 -39 -215 C ATOM 772 CG2 ILE A 114 23.930 -39.521 -4.411 1.00 24.40 C ANISOU 772 CG2 ILE A 114 3569 3385 2316 384 -270 -204 C ATOM 773 CD1 ILE A 114 26.502 -39.186 -2.628 1.00 24.85 C ANISOU 773 CD1 ILE A 114 3477 3460 2506 378 -34 -206 C ATOM 774 N ASN A 115 23.476 -42.900 -4.114 1.00 25.16 N ANISOU 774 N ASN A 115 3639 3433 2486 384 -367 -360 N ATOM 775 CA ASN A 115 22.442 -43.799 -4.620 1.00 25.66 C ANISOU 775 CA ASN A 115 3739 3472 2537 373 -484 -400 C ATOM 776 C ASN A 115 21.213 -43.764 -3.685 1.00 26.81 C ANISOU 776 C ASN A 115 3784 3603 2801 348 -569 -369 C ATOM 777 O ASN A 115 21.050 -42.833 -2.909 1.00 28.63 O ANISOU 777 O ASN A 115 3942 3846 3091 345 -545 -313 O ATOM 778 CB ASN A 115 23.014 -45.194 -4.788 1.00 27.79 C ANISOU 778 CB ASN A 115 4044 3716 2799 382 -464 -479 C ATOM 779 CG ASN A 115 23.563 -45.740 -3.505 1.00 26.57 C ANISOU 779 CG ASN A 115 3795 3543 2758 382 -410 -485 C ATOM 780 OD1 ASN A 115 23.084 -45.402 -2.407 1.00 26.86 O ANISOU 780 OD1 ASN A 115 3739 3575 2890 363 -425 -440 O ATOM 781 ND2 ASN A 115 24.576 -46.583 -3.617 1.00 28.83 N ANISOU 781 ND2 ASN A 115 4107 3814 3033 407 -346 -542 N ATOM 782 N ALA A 116 20.335 -44.770 -3.768 1.00 30.61 N ANISOU 782 N ALA A 116 4260 4054 3318 326 -665 -409 N ATOM 783 CA ALA A 116 19.128 -44.759 -2.931 1.00 33.52 C ANISOU 783 CA ALA A 116 4525 4409 3802 296 -736 -382 C ATOM 784 C ALA A 116 19.433 -44.896 -1.433 1.00 33.14 C ANISOU 784 C ALA A 116 4379 4351 3861 284 -660 -361 C ATOM 785 O ALA A 116 18.628 -44.490 -0.582 1.00 35.85 O ANISOU 785 O ALA A 116 4633 4695 4294 265 -676 -323 O ATOM 786 CB ALA A 116 18.176 -45.862 -3.368 1.00 39.53 C ANISOU 786 CB ALA A 116 5300 5136 4585 266 -851 -432 C ATOM 787 N HIS A 117 20.602 -45.444 -1.103 1.00 26.77 N ANISOU 787 N HIS A 117 3592 3535 3045 298 -578 -387 N ATOM 788 CA HIS A 117 20.908 -45.782 0.291 1.00 23.61 C ANISOU 788 CA HIS A 117 3118 3115 2736 286 -525 -373 C ATOM 789 C HIS A 117 21.746 -44.734 0.940 1.00 22.58 C ANISOU 789 C HIS A 117 2955 3013 2610 307 -437 -329 C ATOM 790 O HIS A 117 22.104 -44.645 2.225 1.00 23.12 O ANISOU 790 O HIS A 117 2965 3074 2746 302 -387 -305 O ATOM 791 CB HIS A 117 21.631 -47.107 0.392 1.00 26.91 C ANISOU 791 CB HIS A 117 3571 3493 3159 292 -507 -428 C ATOM 792 CG HIS A 117 20.973 -48.166 -0.428 1.00 30.22 C ANISOU 792 CG HIS A 117 4045 3878 3558 274 -593 -482 C ATOM 793 ND1 HIS A 117 19.683 -48.595 -0.184 1.00 34.38 N ANISOU 793 ND1 HIS A 117 4532 4379 4152 227 -677 -478 N ATOM 794 CD2 HIS A 117 21.362 -48.766 -1.576 1.00 32.17 C ANISOU 794 CD2 HIS A 117 4386 4115 3722 295 -611 -543 C ATOM 795 CE1 HIS A 117 19.338 -49.479 -1.108 1.00 35.35 C ANISOU 795 CE1 HIS A 117 4721 4472 4239 216 -752 -536 C ATOM 796 NE2 HIS A 117 20.336 -49.597 -1.968 1.00 36.47 N ANISOU 796 NE2 HIS A 117 4952 4622 4284 259 -714 -577 N ATOM 797 N VAL A 118 22.635 -43.854 -0.036 1.00 22.42 N ANISOU 797 N VAL A 118 2995 3029 2493 337 -384 -324 N ATOM 798 CA VAL A 118 23.651 -42.959 0.474 1.00 19.76 C ANISOU 798 CA VAL A 118 2631 2714 2162 352 -294 -293 C ATOM 799 C VAL A 118 23.461 -41.683 -0.297 1.00 20.23 C ANISOU 799 C VAL A 118 2727 2802 2158 357 -293 -252 C ATOM 800 O VAL A 118 23.470 -41.684 -1.516 1.00 21.52 O ANISOU 800 O VAL A 118 2971 2975 2230 366 -309 -268 O ATOM 801 CB VAL A 118 25.046 -43.533 0.220 1.00 18.66 C ANISOU 801 CB VAL A 118 2520 2576 1996 376 -221 -337 C ATOM 802 CG1 VAL A 118 26.097 -42.552 0.609 1.00 18.62 C ANISOU 802 CG1 VAL A 118 2481 2594 1998 384 -134 -307 C ATOM 803 CG2 VAL A 118 25.253 -44.839 0.956 1.00 22.29 C ANISOU 803 CG2 VAL A 118 2955 2996 2519 378 -234 -377 C ATOM 804 N SER A 119 23.257 -40.576 0.417 1.00 16.78 N ANISOU 804 N SER A 119 2239 2373 1763 352 -276 -198 N ATOM 805 CA SER A 119 23.092 -39.286 -0.200 1.00 16.86 C ANISOU 805 CA SER A 119 2284 2399 1723 358 -275 -152 C ATOM 806 C SER A 119 23.290 -38.205 0.853 1.00 18.72 C ANISOU 806 C SER A 119 2459 2633 2019 355 -229 -106 C ATOM 807 O SER A 119 23.413 -38.480 2.021 1.00 18.26 O ANISOU 807 O SER A 119 2338 2565 2035 347 -209 -110 O ATOM 808 CB SER A 119 21.760 -39.156 -0.914 1.00 21.17 C ANISOU 808 CB SER A 119 2857 2941 2247 360 -380 -140 C ATOM 809 OG SER A 119 20.649 -39.316 -0.036 1.00 24.24 O ANISOU 809 OG SER A 119 3161 3315 2733 349 -437 -132 O ATOM 810 N THR A 120 23.318 -36.969 0.390 1.00 17.52 N ANISOU 810 N THR A 120 2342 2488 1828 360 -216 -61 N ATOM 811 CA THR A 120 23.750 -35.864 1.226 1.00 16.58 C ANISOU 811 CA THR A 120 2185 2362 1752 356 -162 -22 C ATOM 812 C THR A 120 22.579 -35.116 1.863 1.00 16.86 C ANISOU 812 C THR A 120 2177 2382 1849 364 -213 13 C ATOM 813 O THR A 120 21.425 -35.162 1.381 1.00 20.66 O ANISOU 813 O THR A 120 2662 2859 2328 376 -294 19 O ATOM 814 CB THR A 120 24.580 -34.846 0.435 1.00 19.04 C ANISOU 814 CB THR A 120 2562 2680 1995 352 -104 10 C ATOM 815 OG1 THR A 120 23.799 -34.240 -0.615 1.00 21.56 O ANISOU 815 OG1 THR A 120 2954 2993 2246 364 -162 43 O ATOM 816 CG2 THR A 120 25.830 -35.486 -0.189 1.00 20.98 C ANISOU 816 CG2 THR A 120 2841 2944 2187 345 -29 -27 C ATOM 817 N ILE A 121 22.911 -34.408 2.933 1.00 16.19 N ANISOU 817 N ILE A 121 2048 2286 1819 359 -167 31 N ATOM 818 CA ILE A 121 21.965 -33.507 3.615 1.00 15.46 C ANISOU 818 CA ILE A 121 1916 2174 1784 372 -192 62 C ATOM 819 C ILE A 121 22.467 -32.063 3.405 1.00 15.72 C ANISOU 819 C ILE A 121 1990 2189 1793 376 -157 106 C ATOM 820 O ILE A 121 23.666 -31.772 3.502 1.00 17.34 O ANISOU 820 O ILE A 121 2213 2395 1980 356 -90 107 O ATOM 821 CB ILE A 121 21.827 -33.871 5.107 1.00 15.36 C ANISOU 821 CB ILE A 121 1834 2153 1850 362 -167 45 C ATOM 822 CG1 ILE A 121 20.718 -33.057 5.801 1.00 16.14 C ANISOU 822 CG1 ILE A 121 1889 2232 2010 380 -185 66 C ATOM 823 CG2 ILE A 121 23.121 -33.724 5.834 1.00 17.20 C ANISOU 823 CG2 ILE A 121 2066 2382 2086 346 -100 38 C ATOM 824 CD1 ILE A 121 19.329 -33.415 5.350 1.00 18.71 C ANISOU 824 CD1 ILE A 121 2181 2561 2365 394 -258 64 C ATOM 825 N SER A 122 21.529 -31.155 3.105 1.00 16.67 N ANISOU 825 N SER A 122 2123 2290 1922 401 -206 141 N ATOM 826 CA SER A 122 21.821 -29.754 2.864 1.00 17.79 C ANISOU 826 CA SER A 122 2313 2402 2043 407 -186 187 C ATOM 827 C SER A 122 22.176 -29.014 4.126 1.00 16.77 C ANISOU 827 C SER A 122 2145 2248 1978 400 -134 190 C ATOM 828 O SER A 122 21.631 -29.285 5.200 1.00 17.17 O ANISOU 828 O SER A 122 2131 2297 2095 408 -135 168 O ATOM 829 CB SER A 122 20.599 -29.056 2.254 1.00 18.29 C ANISOU 829 CB SER A 122 2398 2443 2109 447 -271 222 C ATOM 830 OG SER A 122 20.380 -29.497 0.918 1.00 21.41 O ANISOU 830 OG SER A 122 2858 2853 2422 452 -329 227 O ATOM 831 N LEU A 123 23.124 -28.087 3.991 1.00 16.15 N ANISOU 831 N LEU A 123 2113 2149 1875 380 -83 217 N ATOM 832 CA LEU A 123 23.417 -27.183 5.077 1.00 16.83 C ANISOU 832 CA LEU A 123 2179 2201 2016 373 -46 222 C ATOM 833 C LEU A 123 22.254 -26.210 5.300 1.00 17.64 C ANISOU 833 C LEU A 123 2280 2262 2159 416 -91 247 C ATOM 834 O LEU A 123 21.467 -25.923 4.395 1.00 20.12 O ANISOU 834 O LEU A 123 2628 2567 2452 447 -149 276 O ATOM 835 CB LEU A 123 24.697 -26.428 4.776 1.00 19.12 C ANISOU 835 CB LEU A 123 2515 2473 2276 334 14 244 C ATOM 836 CG LEU A 123 25.980 -27.271 4.790 1.00 20.53 C ANISOU 836 CG LEU A 123 2671 2688 2440 295 70 212 C ATOM 837 CD1 LEU A 123 27.210 -26.419 4.477 1.00 26.17 C ANISOU 837 CD1 LEU A 123 3419 3384 3142 250 136 235 C ATOM 838 CD2 LEU A 123 26.133 -28.014 6.078 1.00 24.88 C ANISOU 838 CD2 LEU A 123 3152 3253 3050 293 73 166 C ATOM 839 N PRO A 124 22.150 -25.681 6.537 1.00 18.01 N ANISOU 839 N PRO A 124 2293 2281 2268 422 -66 233 N ATOM 840 CA PRO A 124 21.011 -24.813 6.872 1.00 17.63 C ANISOU 840 CA PRO A 124 2233 2193 2272 471 -98 246 C ATOM 841 C PRO A 124 21.131 -23.425 6.281 1.00 17.43 C ANISOU 841 C PRO A 124 2281 2110 2231 484 -109 294 C ATOM 842 O PRO A 124 22.225 -22.851 6.203 1.00 20.63 O ANISOU 842 O PRO A 124 2737 2494 2609 443 -65 311 O ATOM 843 CB PRO A 124 21.059 -24.718 8.389 1.00 19.11 C ANISOU 843 CB PRO A 124 2379 2367 2513 467 -52 210 C ATOM 844 CG PRO A 124 22.488 -24.952 8.729 1.00 19.41 C ANISOU 844 CG PRO A 124 2436 2416 2523 412 -4 196 C ATOM 845 CD PRO A 124 23.040 -25.916 7.703 1.00 17.84 C ANISOU 845 CD PRO A 124 2244 2263 2270 388 -11 200 C ATOM 846 N THR A 125 19.979 -22.880 5.884 1.00 17.61 N ANISOU 846 N THR A 125 2306 2105 2280 541 -171 316 N ATOM 847 CA THR A 125 19.903 -21.545 5.319 1.00 18.61 C ANISOU 847 CA THR A 125 2509 2165 2398 565 -196 367 C ATOM 848 C THR A 125 19.228 -20.541 6.297 1.00 18.57 C ANISOU 848 C THR A 125 2479 2099 2476 613 -193 356 C ATOM 849 O THR A 125 18.953 -19.425 5.940 1.00 19.69 O ANISOU 849 O THR A 125 2677 2177 2629 648 -224 394 O ATOM 850 CB THR A 125 19.184 -21.550 3.948 1.00 20.35 C ANISOU 850 CB THR A 125 2773 2385 2575 601 -285 409 C ATOM 851 OG1 THR A 125 17.906 -22.161 4.061 1.00 21.95 O ANISOU 851 OG1 THR A 125 2891 2615 2835 650 -348 382 O ATOM 852 CG2 THR A 125 19.988 -22.278 2.904 1.00 23.07 C ANISOU 852 CG2 THR A 125 3175 2773 2819 552 -276 423 C ATOM 853 N ALA A 127 18.994 -20.989 7.518 1.00 17.40 N ANISOU 853 N ALA A 127 2256 1972 2382 615 -152 304 N ATOM 854 CA ALA A 127 18.523 -20.182 8.621 1.00 18.58 C ANISOU 854 CA ALA A 127 2386 2073 2601 652 -124 278 C ATOM 855 C ALA A 127 18.973 -20.872 9.917 1.00 17.53 C ANISOU 855 C ALA A 127 2211 1973 2475 614 -55 224 C ATOM 856 O ALA A 127 19.233 -22.075 9.911 1.00 18.29 O ANISOU 856 O ALA A 127 2272 2133 2546 578 -47 208 O ATOM 857 CB ALA A 127 17.028 -20.053 8.568 1.00 19.13 C ANISOU 857 CB ALA A 127 2393 2134 2743 730 -172 272 C ATOM 858 N PRO A 128 19.068 -20.118 11.017 1.00 19.52 N ANISOU 858 N PRO A 128 2479 2177 2759 622 -11 197 N ATOM 859 CA PRO A 128 19.419 -20.775 12.281 1.00 19.47 C ANISOU 859 CA PRO A 128 2448 2200 2750 590 46 147 C ATOM 860 C PRO A 128 18.171 -21.547 12.772 1.00 18.87 C ANISOU 860 C PRO A 128 2288 2162 2720 627 58 117 C ATOM 861 O PRO A 128 17.069 -21.445 12.199 1.00 20.24 O ANISOU 861 O PRO A 128 2414 2336 2941 680 22 129 O ATOM 862 CB PRO A 128 19.753 -19.588 13.188 1.00 19.16 C ANISOU 862 CB PRO A 128 2465 2088 2726 595 78 128 C ATOM 863 CG PRO A 128 18.890 -18.490 12.681 1.00 20.29 C ANISOU 863 CG PRO A 128 2623 2170 2916 662 48 151 C ATOM 864 CD PRO A 128 18.933 -18.674 11.170 1.00 21.78 C ANISOU 864 CD PRO A 128 2820 2379 3077 658 -13 208 C ATOM 865 N PRO A 129 18.293 -22.267 13.892 1.00 18.73 N ANISOU 865 N PRO A 129 2251 2171 2693 601 110 77 N ATOM 866 CA PRO A 129 17.169 -23.054 14.399 1.00 19.65 C ANISOU 866 CA PRO A 129 2291 2323 2852 622 138 51 C ATOM 867 C PRO A 129 16.001 -22.201 14.799 1.00 19.57 C ANISOU 867 C PRO A 129 2246 2275 2916 691 163 33 C ATOM 868 O PRO A 129 16.210 -21.113 15.349 1.00 23.39 O ANISOU 868 O PRO A 129 2785 2700 3403 713 189 19 O ATOM 869 CB PRO A 129 17.765 -23.759 15.618 1.00 20.35 C ANISOU 869 CB PRO A 129 2402 2429 2899 575 194 18 C ATOM 870 CG PRO A 129 19.212 -23.797 15.355 1.00 21.02 C ANISOU 870 CG PRO A 129 2548 2514 2926 525 168 32 C ATOM 871 CD PRO A 129 19.543 -22.539 14.609 1.00 19.92 C ANISOU 871 CD PRO A 129 2450 2325 2792 542 137 60 C ATOM 872 N ALA A 130 14.797 -22.648 14.466 1.00 19.88 N ANISOU 872 N ALA A 130 2193 2341 3019 726 150 31 N ATOM 873 CA ALA A 130 13.601 -21.898 14.768 1.00 20.99 C ANISOU 873 CA ALA A 130 2278 2450 3249 799 172 11 C ATOM 874 C ALA A 130 12.751 -22.645 15.775 1.00 21.59 C ANISOU 874 C ALA A 130 2276 2559 3368 796 256 -31 C ATOM 875 O ALA A 130 12.354 -23.776 15.566 1.00 21.59 O ANISOU 875 O ALA A 130 2209 2613 3382 764 249 -29 O ATOM 876 CB ALA A 130 12.797 -21.592 13.489 1.00 20.16 C ANISOU 876 CB ALA A 130 2118 2338 3204 854 79 44 C ATOM 877 N THR A 132 12.453 -21.958 16.866 1.00 21.57 N ANISOU 877 N THR A 132 2290 2520 3386 828 340 -71 N ATOM 878 CA THR A 132 11.667 -22.544 17.941 1.00 21.53 C ANISOU 878 CA THR A 132 2227 2540 3413 823 444 -112 C ATOM 879 C THR A 132 10.371 -23.138 17.424 1.00 22.32 C ANISOU 879 C THR A 132 2183 2679 3618 847 431 -111 C ATOM 880 O THR A 132 9.623 -22.487 16.687 1.00 24.60 O ANISOU 880 O THR A 132 2405 2948 3994 915 374 -104 O ATOM 881 CB THR A 132 11.363 -21.488 18.993 1.00 22.18 C ANISOU 881 CB THR A 132 2345 2567 3513 875 532 -158 C ATOM 882 OG1 THR A 132 12.604 -20.974 19.448 1.00 25.93 O ANISOU 882 OG1 THR A 132 2956 3004 3893 844 529 -161 O ATOM 883 CG2 THR A 132 10.574 -22.037 20.147 1.00 25.79 C ANISOU 883 CG2 THR A 132 2756 3049 3993 868 659 -202 C ATOM 884 N GLY A 133 10.114 -24.366 17.854 1.00 23.51 N ANISOU 884 N GLY A 133 2288 2880 3764 790 480 -119 N ATOM 885 CA GLY A 133 8.892 -25.048 17.526 1.00 26.10 C ANISOU 885 CA GLY A 133 2473 3246 4197 795 481 -125 C ATOM 886 C GLY A 133 8.938 -25.841 16.251 1.00 25.21 C ANISOU 886 C GLY A 133 2320 3169 4091 766 360 -88 C ATOM 887 O GLY A 133 8.011 -26.607 15.989 1.00 27.00 O ANISOU 887 O GLY A 133 2431 3429 4399 752 351 -93 O ATOM 888 N THR A 134 9.961 -25.648 15.436 1.00 22.64 N ANISOU 888 N THR A 134 2085 2833 3684 755 270 -54 N ATOM 889 CA THR A 134 10.048 -26.447 14.222 1.00 22.19 C ANISOU 889 CA THR A 134 2006 2810 3617 726 162 -24 C ATOM 890 C THR A 134 10.366 -27.906 14.565 1.00 22.97 C ANISOU 890 C THR A 134 2107 2949 3671 643 193 -29 C ATOM 891 O THR A 134 11.010 -28.215 15.567 1.00 23.23 O ANISOU 891 O THR A 134 2206 2980 3640 603 273 -39 O ATOM 892 CB THR A 134 11.035 -25.890 13.167 1.00 22.72 C ANISOU 892 CB THR A 134 2170 2856 3606 735 67 14 C ATOM 893 OG1 THR A 134 12.352 -25.828 13.678 1.00 23.26 O ANISOU 893 OG1 THR A 134 2351 2915 3573 694 108 18 O ATOM 894 CG2 THR A 134 10.618 -24.514 12.708 1.00 26.99 C ANISOU 894 CG2 THR A 134 2711 3348 4196 817 22 26 C ATOM 895 N LYS A 135 9.924 -28.806 13.686 1.00 22.14 N ANISOU 895 N LYS A 135 1939 2875 3597 619 118 -19 N ATOM 896 CA LYS A 135 10.059 -30.250 13.874 1.00 21.69 C ANISOU 896 CA LYS A 135 1876 2850 3517 544 133 -23 C ATOM 897 C LYS A 135 11.399 -30.778 13.336 1.00 21.35 C ANISOU 897 C LYS A 135 1941 2812 3358 505 82 -4 C ATOM 898 O LYS A 135 11.805 -30.425 12.221 1.00 22.95 O ANISOU 898 O LYS A 135 2179 3013 3527 527 -7 16 O ATOM 899 CB LYS A 135 8.894 -30.942 13.154 1.00 22.90 C ANISOU 899 CB LYS A 135 1905 3026 3769 536 70 -30 C ATOM 900 CG LYS A 135 7.485 -30.669 13.686 1.00 30.32 C ANISOU 900 CG LYS A 135 2705 3967 4847 564 127 -55 C ATOM 901 CD LYS A 135 6.406 -31.259 12.733 1.00 41.41 C ANISOU 901 CD LYS A 135 3983 5393 6359 560 27 -60 C ATOM 902 CE LYS A 135 4.976 -30.962 13.190 1.00 46.70 C ANISOU 902 CE LYS A 135 4489 6066 7189 591 79 -88 C ATOM 903 NZ LYS A 135 4.613 -29.505 13.127 1.00 51.56 N ANISOU 903 NZ LYS A 135 5078 6654 7859 692 69 -92 N ATOM 904 N CYS A 136 12.103 -31.598 14.126 1.00 20.77 N ANISOU 904 N CYS A 136 1924 2744 3225 450 139 -9 N ATOM 905 CA CYS A 136 13.384 -32.139 13.711 1.00 18.16 C ANISOU 905 CA CYS A 136 1683 2418 2799 418 98 3 C ATOM 906 C CYS A 136 13.350 -33.656 13.808 1.00 19.48 C ANISOU 906 C CYS A 136 1840 2600 2961 358 97 -3 C ATOM 907 O CYS A 136 12.509 -34.223 14.528 1.00 20.52 O ANISOU 907 O CYS A 136 1915 2733 3146 330 153 -14 O ATOM 908 CB CYS A 136 14.520 -31.643 14.586 1.00 18.19 C ANISOU 908 CB CYS A 136 1781 2402 2729 414 151 3 C ATOM 909 SG CYS A 136 14.596 -29.828 14.734 1.00 21.96 S ANISOU 909 SG CYS A 136 2285 2845 3214 476 168 6 S ATOM 910 N LEU A 137 14.243 -34.285 13.044 1.00 16.23 N ANISOU 910 N LEU A 137 1482 2197 2489 339 36 3 N ATOM 911 CA LEU A 137 14.500 -35.712 13.041 1.00 16.70 C ANISOU 911 CA LEU A 137 1557 2260 2528 288 24 -5 C ATOM 912 C LEU A 137 15.934 -35.931 13.526 1.00 14.49 C ANISOU 912 C LEU A 137 1372 1970 2165 276 44 -2 C ATOM 913 O LEU A 137 16.926 -35.464 12.918 1.00 16.58 O ANISOU 913 O LEU A 137 1684 2237 2378 296 11 3 O ATOM 914 CB LEU A 137 14.336 -36.284 11.633 1.00 20.08 C ANISOU 914 CB LEU A 137 1968 2702 2958 286 -73 -8 C ATOM 915 CG LEU A 137 14.574 -37.794 11.591 1.00 18.49 C ANISOU 915 CG LEU A 137 1788 2497 2743 235 -89 -21 C ATOM 916 CD1 LEU A 137 13.407 -38.542 12.291 1.00 20.47 C ANISOU 916 CD1 LEU A 137 1965 2738 3073 190 -52 -28 C ATOM 917 CD2 LEU A 137 14.697 -38.291 10.164 1.00 21.09 C ANISOU 917 CD2 LEU A 137 2130 2835 3047 237 -184 -32 C ATOM 918 N ILE A 138 16.054 -36.620 14.650 1.00 16.10 N ANISOU 918 N ILE A 138 1602 2158 2357 241 98 -5 N ATOM 919 CA ILE A 138 17.343 -36.947 15.248 1.00 14.62 C ANISOU 919 CA ILE A 138 1499 1956 2101 230 107 -4 C ATOM 920 C ILE A 138 17.514 -38.439 15.082 1.00 16.09 C ANISOU 920 C ILE A 138 1701 2134 2280 192 77 -9 C ATOM 921 O ILE A 138 16.540 -39.194 15.244 1.00 16.83 O ANISOU 921 O ILE A 138 1754 2220 2418 159 91 -9 O ATOM 922 CB ILE A 138 17.384 -36.617 16.728 1.00 15.83 C ANISOU 922 CB ILE A 138 1694 2089 2233 222 181 -2 C ATOM 923 CG1 ILE A 138 16.914 -35.183 16.947 1.00 19.06 C ANISOU 923 CG1 ILE A 138 2079 2499 2664 259 219 -4 C ATOM 924 CG2 ILE A 138 18.770 -36.823 17.298 1.00 17.04 C ANISOU 924 CG2 ILE A 138 1932 2225 2318 217 167 -2 C ATOM 925 CD1 ILE A 138 16.712 -34.755 18.428 1.00 26.31 C ANISOU 925 CD1 ILE A 138 3038 3396 3561 255 305 -10 C ATOM 926 N SER A 139 18.710 -38.887 14.700 1.00 14.97 N ANISOU 926 N SER A 139 1608 1987 2091 198 35 -14 N ATOM 927 CA SER A 139 18.898 -40.312 14.432 1.00 15.63 C ANISOU 927 CA SER A 139 1712 2056 2173 171 0 -24 C ATOM 928 C SER A 139 20.258 -40.790 14.928 1.00 14.88 C ANISOU 928 C SER A 139 1686 1939 2030 177 -11 -27 C ATOM 929 O SER A 139 21.201 -39.991 15.086 1.00 14.65 O ANISOU 929 O SER A 139 1678 1917 1970 203 -9 -27 O ATOM 930 CB SER A 139 18.724 -40.585 12.942 1.00 15.98 C ANISOU 930 CB SER A 139 1726 2119 2228 181 -62 -39 C ATOM 931 OG SER A 139 19.503 -39.753 12.165 1.00 15.74 O ANISOU 931 OG SER A 139 1708 2110 2163 218 -81 -42 O ATOM 932 N GLY A 140 20.346 -42.089 15.185 1.00 15.55 N ANISOU 932 N GLY A 140 1801 1992 2114 151 -28 -30 N ATOM 933 CA GLY A 140 21.597 -42.699 15.624 1.00 14.52 C ANISOU 933 CA GLY A 140 1733 1835 1949 163 -53 -34 C ATOM 934 C GLY A 140 21.469 -44.083 16.192 1.00 14.52 C ANISOU 934 C GLY A 140 1779 1785 1951 132 -65 -28 C ATOM 935 O GLY A 140 20.359 -44.628 16.335 1.00 15.02 O ANISOU 935 O GLY A 140 1829 1834 2044 89 -43 -17 O ATOM 936 N TRP A 141 22.634 -44.685 16.427 1.00 15.08 N ANISOU 936 N TRP A 141 1902 1829 2000 154 -104 -35 N ATOM 937 CA TRP A 141 22.736 -46.004 17.042 1.00 16.12 C ANISOU 937 CA TRP A 141 2097 1900 2127 133 -126 -25 C ATOM 938 C TRP A 141 23.091 -45.948 18.533 1.00 16.94 C ANISOU 938 C TRP A 141 2276 1970 2189 126 -113 4 C ATOM 939 O TRP A 141 23.628 -46.911 19.091 1.00 17.66 O ANISOU 939 O TRP A 141 2438 2007 2265 127 -152 14 O ATOM 940 CB TRP A 141 23.739 -46.863 16.274 1.00 15.78 C ANISOU 940 CB TRP A 141 2065 1837 2093 169 -189 -56 C ATOM 941 CG TRP A 141 23.317 -47.261 14.865 1.00 15.00 C ANISOU 941 CG TRP A 141 1923 1755 2021 169 -207 -88 C ATOM 942 CD1 TRP A 141 22.568 -48.332 14.507 1.00 15.99 C ANISOU 942 CD1 TRP A 141 2059 1844 2172 135 -225 -95 C ATOM 943 CD2 TRP A 141 23.653 -46.586 13.655 1.00 15.45 C ANISOU 943 CD2 TRP A 141 1932 1864 2076 202 -211 -117 C ATOM 944 NE1 TRP A 141 22.427 -48.386 13.158 1.00 17.36 N ANISOU 944 NE1 TRP A 141 2197 2044 2355 148 -249 -131 N ATOM 945 CE2 TRP A 141 23.062 -47.306 12.601 1.00 16.28 C ANISOU 945 CE2 TRP A 141 2027 1963 2196 189 -238 -143 C ATOM 946 CE3 TRP A 141 24.393 -45.444 13.359 1.00 15.51 C ANISOU 946 CE3 TRP A 141 1910 1917 2066 236 -196 -122 C ATOM 947 CZ2 TRP A 141 23.226 -46.920 11.251 1.00 16.60 C ANISOU 947 CZ2 TRP A 141 2041 2045 2223 215 -249 -174 C ATOM 948 CZ3 TRP A 141 24.572 -45.058 12.027 1.00 15.63 C ANISOU 948 CZ3 TRP A 141 1894 1971 2073 257 -198 -148 C ATOM 949 CH2 TRP A 141 23.992 -45.812 10.996 1.00 14.78 C ANISOU 949 CH2 TRP A 141 1789 1859 1968 249 -225 -173 C ATOM 950 N GLY A 142 22.755 -44.860 19.193 1.00 16.01 N ANISOU 950 N GLY A 142 2155 1878 2050 119 -63 18 N ATOM 951 CA GLY A 142 23.058 -44.745 20.610 1.00 16.67 C ANISOU 951 CA GLY A 142 2325 1930 2080 111 -51 43 C ATOM 952 C GLY A 142 22.139 -45.503 21.531 1.00 16.28 C ANISOU 952 C GLY A 142 2339 1836 2009 57 -3 77 C ATOM 953 O GLY A 142 21.188 -46.143 21.108 1.00 16.83 O ANISOU 953 O GLY A 142 2376 1899 2119 19 25 82 O ATOM 954 N ASN A 143 22.401 -45.385 22.826 1.00 18.77 N ANISOU 954 N ASN A 143 2751 2121 2259 50 10 100 N ATOM 955 CA ASN A 143 21.648 -46.082 23.836 1.00 19.98 C ANISOU 955 CA ASN A 143 2989 2227 2374 -5 65 139 C ATOM 956 C ASN A 143 20.179 -45.736 23.716 1.00 17.65 C ANISOU 956 C ASN A 143 2626 1963 2119 -50 172 142 C ATOM 957 O ASN A 143 19.852 -44.574 23.467 1.00 18.66 O ANISOU 957 O ASN A 143 2683 2142 2264 -31 211 122 O ATOM 958 CB ASN A 143 22.167 -45.592 25.173 1.00 19.43 C ANISOU 958 CB ASN A 143 3032 2136 2214 3 69 156 C ATOM 959 CG ASN A 143 21.832 -46.493 26.315 1.00 21.50 C ANISOU 959 CG ASN A 143 3426 2332 2410 -44 98 201 C ATOM 960 OD1 ASN A 143 21.034 -47.428 26.210 1.00 21.11 O ANISOU 960 OD1 ASN A 143 3380 2253 2388 -95 139 224 O ATOM 961 ND2 ASN A 143 22.420 -46.187 27.463 1.00 21.73 N ANISOU 961 ND2 ASN A 143 3575 2334 2346 -33 78 216 N ATOM 962 N THR A 144 19.304 -46.714 23.937 1.00 18.37 N ANISOU 962 N THR A 144 2736 2017 2227 -111 217 168 N ATOM 963 CA THR A 144 17.864 -46.501 23.902 1.00 21.62 C ANISOU 963 CA THR A 144 3072 2453 2691 -162 322 171 C ATOM 964 C THR A 144 17.202 -46.481 25.290 1.00 20.36 C ANISOU 964 C THR A 144 2996 2267 2472 -212 436 205 C ATOM 965 O THR A 144 15.989 -46.302 25.401 1.00 25.04 O ANISOU 965 O THR A 144 3524 2879 3113 -256 540 207 O ATOM 966 CB THR A 144 17.119 -47.531 23.035 1.00 19.27 C ANISOU 966 CB THR A 144 2705 2140 2478 -208 310 170 C ATOM 967 OG1 THR A 144 17.167 -48.834 23.620 1.00 23.42 O ANISOU 967 OG1 THR A 144 3333 2589 2977 -258 304 206 O ATOM 968 CG2 THR A 144 17.685 -47.582 21.628 1.00 19.95 C ANISOU 968 CG2 THR A 144 2718 2250 2611 -160 207 132 C ATOM 969 N ALA A 145 18.011 -46.664 26.320 1.00 21.75 N ANISOU 969 N ALA A 145 3318 2399 2547 -205 414 230 N ATOM 970 CA ALA A 145 17.560 -46.641 27.715 1.00 23.38 C ANISOU 970 CA ALA A 145 3641 2575 2667 -248 516 264 C ATOM 971 C ALA A 145 17.999 -45.346 28.426 1.00 25.98 C ANISOU 971 C ALA A 145 4019 2933 2920 -202 536 244 C ATOM 972 O ALA A 145 19.148 -44.913 28.291 1.00 25.30 O ANISOU 972 O ALA A 145 3956 2852 2804 -144 432 225 O ATOM 973 CB ALA A 145 18.120 -47.856 28.433 1.00 23.56 C ANISOU 973 CB ALA A 145 3821 2515 2616 -276 467 311 C ATOM 974 N SER A 146 17.097 -44.752 29.216 1.00 25.94 N ANISOU 974 N SER A 146 4031 2942 2884 -231 672 246 N ATOM 975 CA SER A 146 17.393 -43.502 29.949 1.00 26.91 C ANISOU 975 CA SER A 146 4210 3085 2931 -191 703 221 C ATOM 976 C SER A 146 18.165 -43.794 31.220 1.00 31.67 C ANISOU 976 C SER A 146 5016 3631 3388 -197 673 250 C ATOM 977 O SER A 146 18.822 -42.913 31.792 1.00 33.99 O ANISOU 977 O SER A 146 5382 3927 3605 -156 642 228 O ATOM 978 CB SER A 146 16.091 -42.758 30.286 1.00 30.10 C ANISOU 978 CB SER A 146 4553 3522 3363 -212 868 204 C ATOM 979 OG SER A 146 15.172 -43.582 30.956 1.00 35.25 O ANISOU 979 OG SER A 146 5253 4144 3997 -288 988 241 O ATOM 980 N SER A 147 18.065 -45.029 31.693 1.00 31.91 N ANISOU 980 N SER A 147 5146 3602 3376 -250 678 300 N ATOM 981 CA SER A 147 18.983 -45.519 32.705 1.00 33.54 C ANISOU 981 CA SER A 147 5550 3745 3451 -247 603 335 C ATOM 982 C SER A 147 19.419 -46.924 32.350 1.00 30.78 C ANISOU 982 C SER A 147 5232 3337 3126 -264 505 374 C ATOM 983 O SER A 147 18.647 -47.750 31.862 1.00 32.35 O ANISOU 983 O SER A 147 5368 3523 3399 -315 556 394 O ATOM 984 CB SER A 147 18.374 -45.475 34.118 1.00 41.85 C ANISOU 984 CB SER A 147 6766 4764 4372 -298 735 365 C ATOM 985 OG SER A 147 17.163 -46.198 34.182 1.00 48.42 O ANISOU 985 OG SER A 147 7573 5583 5241 -376 875 398 O ATOM 986 N GLY A 148 20.674 -47.199 32.625 1.00 29.95 N ANISOU 986 N GLY A 148 5225 3191 2962 -219 359 383 N ATOM 987 CA GLY A 148 21.245 -48.456 32.234 1.00 28.27 C ANISOU 987 CA GLY A 148 5038 2920 2782 -215 248 411 C ATOM 988 C GLY A 148 21.513 -48.434 30.743 1.00 28.12 C ANISOU 988 C GLY A 148 4834 2949 2904 -174 181 367 C ATOM 989 O GLY A 148 21.626 -47.376 30.126 1.00 26.84 O ANISOU 989 O GLY A 148 4551 2857 2792 -135 182 318 O ATOM 990 N ALA A 149 21.606 -49.620 30.167 1.00 28.86 N ANISOU 990 N ALA A 149 4915 2996 3054 -185 125 384 N ATOM 991 CA ALA A 149 22.069 -49.741 28.787 1.00 29.08 C ANISOU 991 CA ALA A 149 4798 3056 3196 -138 43 341 C ATOM 992 C ALA A 149 21.196 -50.695 27.962 1.00 27.08 C ANISOU 992 C ALA A 149 4473 2785 3031 -189 82 347 C ATOM 993 O ALA A 149 20.875 -51.828 28.384 1.00 27.69 O ANISOU 993 O ALA A 149 4646 2785 3089 -240 91 393 O ATOM 994 CB ALA A 149 23.528 -50.213 28.780 1.00 30.90 C ANISOU 994 CB ALA A 149 5083 3243 3414 -69 -115 336 C ATOM 995 N ASP A 150 20.817 -50.224 26.779 1.00 24.81 N ANISOU 995 N ASP A 150 4024 2565 2838 -177 99 302 N ATOM 996 CA ASP A 150 20.121 -51.028 25.801 1.00 24.05 C ANISOU 996 CA ASP A 150 3844 2460 2835 -214 107 293 C ATOM 997 C ASP A 150 20.516 -50.493 24.426 1.00 23.31 C ANISOU 997 C ASP A 150 3609 2431 2815 -155 49 234 C ATOM 998 O ASP A 150 19.909 -49.583 23.895 1.00 24.37 O ANISOU 998 O ASP A 150 3634 2636 2990 -155 102 208 O ATOM 999 CB ASP A 150 18.623 -50.935 26.052 1.00 29.55 C ANISOU 999 CB ASP A 150 4498 3171 3557 -297 245 311 C ATOM 1000 CG ASP A 150 17.831 -51.916 25.246 1.00 36.40 C ANISOU 1000 CG ASP A 150 5300 4013 4517 -354 250 309 C ATOM 1001 OD1 ASP A 150 18.374 -52.483 24.273 1.00 32.54 O ANISOU 1001 OD1 ASP A 150 4778 3510 4077 -319 150 281 O ATOM 1002 OD2 ASP A 150 16.645 -52.107 25.592 1.00 44.34 O ANISOU 1002 OD2 ASP A 150 6286 5011 5550 -435 358 333 O ATOM 1003 N TYR A 151 21.561 -51.065 23.839 1.00 22.32 N ANISOU 1003 N TYR A 151 3492 2280 2708 -101 -60 213 N ATOM 1004 CA TYR A 151 22.121 -50.521 22.593 1.00 19.67 C ANISOU 1004 CA TYR A 151 3042 2005 2426 -41 -110 159 C ATOM 1005 C TYR A 151 21.577 -51.293 21.404 1.00 20.67 C ANISOU 1005 C TYR A 151 3101 2125 2627 -62 -124 134 C ATOM 1006 O TYR A 151 21.574 -52.518 21.421 1.00 22.23 O ANISOU 1006 O TYR A 151 3359 2249 2838 -84 -159 146 O ATOM 1007 CB TYR A 151 23.655 -50.567 22.641 1.00 21.16 C ANISOU 1007 CB TYR A 151 3267 2177 2593 35 -211 142 C ATOM 1008 CG TYR A 151 24.233 -49.473 23.469 1.00 21.85 C ANISOU 1008 CG TYR A 151 3383 2296 2624 63 -210 147 C ATOM 1009 CD1 TYR A 151 24.696 -48.291 22.871 1.00 19.53 C ANISOU 1009 CD1 TYR A 151 2995 2075 2351 104 -212 110 C ATOM 1010 CD2 TYR A 151 24.268 -49.556 24.848 1.00 23.62 C ANISOU 1010 CD2 TYR A 151 3732 2473 2767 42 -203 190 C ATOM 1011 CE1 TYR A 151 25.181 -47.264 23.610 1.00 20.26 C ANISOU 1011 CE1 TYR A 151 3112 2189 2396 123 -213 111 C ATOM 1012 CE2 TYR A 151 24.756 -48.476 25.613 1.00 23.71 C ANISOU 1012 CE2 TYR A 151 3775 2514 2722 65 -205 188 C ATOM 1013 CZ TYR A 151 25.207 -47.346 24.968 1.00 22.22 C ANISOU 1013 CZ TYR A 151 3482 2393 2566 104 -212 146 C ATOM 1014 OH TYR A 151 25.700 -46.289 25.678 1.00 24.83 O ANISOU 1014 OH TYR A 151 3843 2745 2848 123 -220 140 O ATOM 1015 N PRO A 152 21.136 -50.564 20.365 1.00 18.21 N ANISOU 1015 N PRO A 152 2672 1885 2362 -53 -104 98 N ATOM 1016 CA PRO A 152 20.449 -51.187 19.245 1.00 17.70 C ANISOU 1016 CA PRO A 152 2544 1819 2363 -80 -118 71 C ATOM 1017 C PRO A 152 21.353 -51.556 18.094 1.00 18.70 C ANISOU 1017 C PRO A 152 2650 1947 2509 -21 -199 24 C ATOM 1018 O PRO A 152 22.419 -50.983 17.918 1.00 22.46 O ANISOU 1018 O PRO A 152 3117 2454 2963 44 -230 4 O ATOM 1019 CB PRO A 152 19.486 -50.087 18.803 1.00 20.28 C ANISOU 1019 CB PRO A 152 2763 2222 2720 -96 -59 61 C ATOM 1020 CG PRO A 152 20.283 -48.837 18.989 1.00 21.13 C ANISOU 1020 CG PRO A 152 2860 2383 2787 -36 -56 54 C ATOM 1021 CD PRO A 152 21.066 -49.091 20.272 1.00 19.02 C ANISOU 1021 CD PRO A 152 2704 2067 2456 -28 -64 85 C ATOM 1022 N ASP A 153 20.922 -52.545 17.317 1.00 19.00 N ANISOU 1022 N ASP A 153 2681 1947 2590 -47 -231 2 N ATOM 1023 CA ASP A 153 21.593 -52.869 16.053 1.00 20.97 C ANISOU 1023 CA ASP A 153 2907 2204 2856 6 -295 -53 C ATOM 1024 C ASP A 153 21.077 -51.964 14.922 1.00 19.29 C ANISOU 1024 C ASP A 153 2597 2073 2661 12 -282 -85 C ATOM 1025 O ASP A 153 21.815 -51.593 14.013 1.00 19.79 O ANISOU 1025 O ASP A 153 2633 2174 2711 69 -309 -124 O ATOM 1026 CB ASP A 153 21.402 -54.345 15.651 1.00 20.51 C ANISOU 1026 CB ASP A 153 2898 2062 2831 -20 -343 -71 C ATOM 1027 CG ASP A 153 22.085 -55.325 16.606 1.00 21.28 C ANISOU 1027 CG ASP A 153 3106 2067 2913 -10 -375 -42 C ATOM 1028 OD1 ASP A 153 23.074 -54.906 17.267 1.00 22.58 O ANISOU 1028 OD1 ASP A 153 3301 2239 3041 44 -386 -28 O ATOM 1029 OD2 ASP A 153 21.618 -56.455 16.654 1.00 22.13 O ANISOU 1029 OD2 ASP A 153 3266 2094 3047 -57 -394 -35 O ATOM 1030 N GLU A 154 19.781 -51.668 14.983 1.00 19.48 N ANISOU 1030 N GLU A 154 2568 2118 2715 -48 -242 -68 N ATOM 1031 CA GLU A 154 19.124 -50.920 13.900 1.00 19.71 C ANISOU 1031 CA GLU A 154 2508 2212 2767 -46 -246 -94 C ATOM 1032 C GLU A 154 19.035 -49.439 14.209 1.00 18.82 C ANISOU 1032 C GLU A 154 2344 2170 2638 -23 -196 -75 C ATOM 1033 O GLU A 154 18.787 -49.046 15.341 1.00 18.55 O ANISOU 1033 O GLU A 154 2320 2133 2595 -44 -137 -39 O ATOM 1034 CB GLU A 154 17.700 -51.424 13.653 1.00 21.96 C ANISOU 1034 CB GLU A 154 2747 2481 3116 -121 -246 -94 C ATOM 1035 CG GLU A 154 17.596 -52.847 13.107 1.00 27.27 C ANISOU 1035 CG GLU A 154 3462 3083 3816 -153 -306 -122 C ATOM 1036 CD GLU A 154 16.138 -53.214 12.880 1.00 37.88 C ANISOU 1036 CD GLU A 154 4742 4415 5234 -235 -308 -122 C ATOM 1037 OE1 GLU A 154 15.742 -54.300 13.334 1.00 44.81 O ANISOU 1037 OE1 GLU A 154 5661 5219 6148 -299 -307 -109 O ATOM 1038 OE2 GLU A 154 15.388 -52.388 12.281 1.00 39.39 O ANISOU 1038 OE2 GLU A 154 4843 4669 5456 -237 -312 -134 O ATOM 1039 N LEU A 155 19.251 -48.634 13.182 1.00 17.17 N ANISOU 1039 N LEU A 155 2090 2016 2417 19 -217 -102 N ATOM 1040 CA LEU A 155 19.209 -47.195 13.296 1.00 16.63 C ANISOU 1040 CA LEU A 155 1976 2007 2335 46 -179 -87 C ATOM 1041 C LEU A 155 17.861 -46.729 13.870 1.00 16.04 C ANISOU 1041 C LEU A 155 1842 1945 2305 1 -128 -62 C ATOM 1042 O LEU A 155 16.808 -47.154 13.422 1.00 19.19 O ANISOU 1042 O LEU A 155 2193 2339 2758 -39 -144 -70 O ATOM 1043 CB LEU A 155 19.436 -46.566 11.914 1.00 17.53 C ANISOU 1043 CB LEU A 155 2059 2169 2434 87 -217 -116 C ATOM 1044 CG LEU A 155 19.541 -45.037 11.909 1.00 16.07 C ANISOU 1044 CG LEU A 155 1838 2036 2231 120 -185 -101 C ATOM 1045 CD1 LEU A 155 20.724 -44.531 12.698 1.00 15.45 C ANISOU 1045 CD1 LEU A 155 1797 1958 2115 150 -155 -89 C ATOM 1046 CD2 LEU A 155 19.612 -44.423 10.513 1.00 20.49 C ANISOU 1046 CD2 LEU A 155 2378 2637 2772 152 -222 -121 C ATOM 1047 N GLN A 156 17.955 -45.881 14.883 1.00 16.58 N ANISOU 1047 N GLN A 156 1917 2027 2355 10 -67 -35 N ATOM 1048 CA GLN A 156 16.821 -45.276 15.557 1.00 17.83 C ANISOU 1048 CA GLN A 156 2023 2201 2551 -20 1 -15 C ATOM 1049 C GLN A 156 16.599 -43.807 15.169 1.00 17.01 C ANISOU 1049 C GLN A 156 1858 2150 2454 23 14 -19 C ATOM 1050 O GLN A 156 17.552 -43.063 14.888 1.00 15.35 O ANISOU 1050 O GLN A 156 1674 1960 2199 72 -5 -24 O ATOM 1051 CB GLN A 156 17.010 -45.301 17.052 1.00 17.34 C ANISOU 1051 CB GLN A 156 2025 2110 2453 -39 70 15 C ATOM 1052 CG GLN A 156 17.229 -46.668 17.611 1.00 18.24 C ANISOU 1052 CG GLN A 156 2217 2162 2553 -81 62 29 C ATOM 1053 CD GLN A 156 15.998 -47.521 17.507 1.00 21.10 C ANISOU 1053 CD GLN A 156 2535 2499 2983 -151 81 34 C ATOM 1054 OE1 GLN A 156 14.961 -47.266 18.138 1.00 21.66 O ANISOU 1054 OE1 GLN A 156 2562 2576 3090 -194 161 52 O ATOM 1055 NE2 GLN A 156 16.087 -48.528 16.678 1.00 21.09 N ANISOU 1055 NE2 GLN A 156 2540 2469 3006 -165 11 15 N ATOM 1056 N CYS A 157 15.313 -43.439 15.169 1.00 16.42 N ANISOU 1056 N CYS A 157 1701 2093 2446 3 46 -16 N ATOM 1057 CA CYS A 157 14.854 -42.095 14.784 1.00 16.86 C ANISOU 1057 CA CYS A 157 1690 2189 2526 44 53 -19 C ATOM 1058 C CYS A 157 13.995 -41.531 15.926 1.00 19.21 C ANISOU 1058 C CYS A 157 1951 2489 2860 30 151 -6 C ATOM 1059 O CYS A 157 13.299 -42.260 16.646 1.00 19.37 O ANISOU 1059 O CYS A 157 1959 2487 2914 -25 207 3 O ATOM 1060 CB CYS A 157 14.000 -42.173 13.484 1.00 16.84 C ANISOU 1060 CB CYS A 157 1606 2207 2585 45 -20 -37 C ATOM 1061 SG CYS A 157 14.985 -42.250 11.971 1.00 21.57 S ANISOU 1061 SG CYS A 157 2254 2819 3122 85 -123 -57 S ATOM 1062 N LEU A 158 13.976 -40.213 15.999 1.00 16.99 N ANISOU 1062 N LEU A 158 1650 2231 2576 78 175 -6 N ATOM 1063 CA LEU A 158 13.194 -39.472 16.995 1.00 17.06 C ANISOU 1063 CA LEU A 158 1622 2242 2617 81 272 -3 C ATOM 1064 C LEU A 158 12.745 -38.153 16.403 1.00 19.23 C ANISOU 1064 C LEU A 158 1830 2543 2935 139 256 -12 C ATOM 1065 O LEU A 158 13.538 -37.410 15.849 1.00 18.99 O ANISOU 1065 O LEU A 158 1836 2519 2860 184 206 -11 O ATOM 1066 CB LEU A 158 14.004 -39.190 18.242 1.00 19.26 C ANISOU 1066 CB LEU A 158 2004 2500 2813 83 336 7 C ATOM 1067 CG LEU A 158 13.327 -38.362 19.324 1.00 20.29 C ANISOU 1067 CG LEU A 158 2123 2630 2957 91 445 4 C ATOM 1068 CD1 LEU A 158 12.185 -39.085 19.959 1.00 24.02 C ANISOU 1068 CD1 LEU A 158 2547 3094 3484 35 532 9 C ATOM 1069 CD2 LEU A 158 14.326 -37.933 20.387 1.00 22.80 C ANISOU 1069 CD2 LEU A 158 2562 2928 3175 104 480 8 C ATOM 1070 N ASP A 159 11.449 -37.898 16.483 1.00 20.11 N ANISOU 1070 N ASP A 159 1836 2664 3141 138 295 -20 N ATOM 1071 CA ASP A 159 10.864 -36.606 16.140 1.00 19.14 C ANISOU 1071 CA ASP A 159 1643 2557 3073 200 291 -28 C ATOM 1072 C ASP A 159 10.854 -35.704 17.370 1.00 21.91 C ANISOU 1072 C ASP A 159 2025 2896 3404 224 402 -33 C ATOM 1073 O ASP A 159 10.331 -36.077 18.391 1.00 21.63 O ANISOU 1073 O ASP A 159 1981 2853 3384 188 503 -36 O ATOM 1074 CB ASP A 159 9.457 -36.788 15.612 1.00 23.97 C ANISOU 1074 CB ASP A 159 2113 3183 3811 193 271 -40 C ATOM 1075 CG ASP A 159 9.376 -37.756 14.446 1.00 35.91 C ANISOU 1075 CG ASP A 159 3601 4701 5341 162 157 -42 C ATOM 1076 OD1 ASP A 159 10.190 -37.655 13.516 1.00 37.81 O ANISOU 1076 OD1 ASP A 159 3904 4946 5516 187 66 -37 O ATOM 1077 OD2 ASP A 159 8.432 -38.572 14.432 1.00 43.98 O ANISOU 1077 OD2 ASP A 159 4536 5724 6449 111 162 -50 O ATOM 1078 N ALA A 160 11.417 -34.507 17.256 1.00 19.40 N ANISOU 1078 N ALA A 160 1749 2573 3049 283 385 -34 N ATOM 1079 CA ALA A 160 11.467 -33.618 18.413 1.00 21.96 C ANISOU 1079 CA ALA A 160 2117 2880 3347 307 483 -46 C ATOM 1080 C ALA A 160 11.552 -32.181 17.981 1.00 21.30 C ANISOU 1080 C ALA A 160 2029 2787 3278 380 453 -52 C ATOM 1081 O ALA A 160 12.144 -31.901 16.961 1.00 21.59 O ANISOU 1081 O ALA A 160 2084 2826 3293 401 358 -38 O ATOM 1082 CB ALA A 160 12.673 -33.933 19.246 1.00 21.33 C ANISOU 1082 CB ALA A 160 2170 2782 3153 278 505 -38 C ATOM 1083 N PRO A 161 10.984 -31.259 18.772 1.00 21.67 N ANISOU 1083 N PRO A 161 2059 2818 3356 418 539 -73 N ATOM 1084 CA PRO A 161 10.981 -29.852 18.378 1.00 20.15 C ANISOU 1084 CA PRO A 161 1863 2605 3187 491 509 -79 C ATOM 1085 C PRO A 161 12.166 -29.044 18.914 1.00 19.71 C ANISOU 1085 C PRO A 161 1937 2518 3035 504 518 -81 C ATOM 1086 O PRO A 161 12.677 -29.330 19.992 1.00 21.22 O ANISOU 1086 O PRO A 161 2211 2700 3154 470 581 -91 O ATOM 1087 CB PRO A 161 9.692 -29.353 19.045 1.00 23.82 C ANISOU 1087 CB PRO A 161 2239 3065 3747 528 609 -109 C ATOM 1088 CG PRO A 161 9.656 -30.058 20.315 1.00 21.60 C ANISOU 1088 CG PRO A 161 2000 2786 3420 473 726 -121 C ATOM 1089 CD PRO A 161 10.205 -31.462 19.998 1.00 22.04 C ANISOU 1089 CD PRO A 161 2085 2862 3427 398 672 -93 C ATOM 1090 N VAL A 162 12.576 -28.029 18.159 1.00 19.06 N ANISOU 1090 N VAL A 162 1875 2416 2952 549 449 -71 N ATOM 1091 CA VAL A 162 13.509 -27.026 18.642 1.00 18.60 C ANISOU 1091 CA VAL A 162 1921 2318 2830 566 458 -79 C ATOM 1092 C VAL A 162 12.863 -26.290 19.830 1.00 18.71 C ANISOU 1092 C VAL A 162 1942 2301 2864 601 565 -117 C ATOM 1093 O VAL A 162 11.716 -25.780 19.786 1.00 21.57 O ANISOU 1093 O VAL A 162 2219 2657 3318 653 602 -135 O ATOM 1094 CB VAL A 162 13.884 -26.001 17.540 1.00 18.30 C ANISOU 1094 CB VAL A 162 1895 2256 2803 608 372 -57 C ATOM 1095 CG1 VAL A 162 14.845 -24.928 18.050 1.00 18.90 C ANISOU 1095 CG1 VAL A 162 2075 2283 2822 617 382 -66 C ATOM 1096 CG2 VAL A 162 14.479 -26.677 16.366 1.00 20.30 C ANISOU 1096 CG2 VAL A 162 2147 2538 3027 577 281 -23 C ATOM 1097 N LEU A 163 13.651 -26.162 20.879 1.00 19.04 N ANISOU 1097 N LEU A 163 2093 2321 2819 576 610 -134 N ATOM 1098 CA LEU A 163 13.228 -25.424 22.061 1.00 22.00 C ANISOU 1098 CA LEU A 163 2509 2663 3188 606 713 -176 C ATOM 1099 C LEU A 163 13.773 -24.003 22.060 1.00 20.10 C ANISOU 1099 C LEU A 163 2339 2365 2933 651 685 -191 C ATOM 1100 O LEU A 163 14.782 -23.709 21.474 1.00 22.09 O ANISOU 1100 O LEU A 163 2639 2603 3150 636 600 -168 O ATOM 1101 CB LEU A 163 13.727 -26.136 23.323 1.00 23.02 C ANISOU 1101 CB LEU A 163 2736 2793 3216 550 777 -189 C ATOM 1102 CG LEU A 163 13.088 -27.510 23.546 1.00 23.50 C ANISOU 1102 CG LEU A 163 2744 2897 3289 502 828 -176 C ATOM 1103 CD1 LEU A 163 13.816 -28.226 24.646 1.00 26.06 C ANISOU 1103 CD1 LEU A 163 3190 3215 3497 445 860 -176 C ATOM 1104 CD2 LEU A 163 11.630 -27.403 23.864 1.00 28.99 C ANISOU 1104 CD2 LEU A 163 3340 3601 4074 531 937 -201 C ATOM 1105 N SER A 164 13.073 -23.105 22.749 1.00 22.05 N ANISOU 1105 N SER A 164 2591 2575 3213 705 766 -233 N ATOM 1106 CA SER A 164 13.522 -21.720 22.813 1.00 23.31 C ANISOU 1106 CA SER A 164 2823 2668 3364 749 744 -252 C ATOM 1107 C SER A 164 14.883 -21.612 23.497 1.00 22.71 C ANISOU 1107 C SER A 164 2888 2566 3174 697 719 -260 C ATOM 1108 O SER A 164 15.248 -22.431 24.340 1.00 24.02 O ANISOU 1108 O SER A 164 3111 2755 3263 646 754 -269 O ATOM 1109 CB SER A 164 12.534 -20.848 23.587 1.00 27.33 C ANISOU 1109 CB SER A 164 3324 3137 3922 819 848 -307 C ATOM 1110 OG SER A 164 12.557 -21.161 24.974 1.00 25.01 O ANISOU 1110 OG SER A 164 3111 2843 3550 791 954 -348 O ATOM 1111 N GLN A 165 15.606 -20.539 23.178 1.00 26.72 N ANISOU 1111 N GLN A 165 3457 3020 3676 712 658 -260 N ATOM 1112 CA GLN A 165 16.849 -20.227 23.856 1.00 28.43 C ANISOU 1112 CA GLN A 165 3798 3201 3804 668 629 -277 C ATOM 1113 C GLN A 165 16.617 -20.095 25.374 1.00 25.59 C ANISOU 1113 C GLN A 165 3528 2815 3379 673 724 -336 C ATOM 1114 O GLN A 165 17.437 -20.566 26.171 1.00 27.34 O ANISOU 1114 O GLN A 165 3841 3040 3507 620 713 -346 O ATOM 1115 CB GLN A 165 17.378 -18.915 23.316 1.00 35.59 C ANISOU 1115 CB GLN A 165 4746 4040 4738 691 569 -273 C ATOM 1116 CG GLN A 165 18.812 -18.584 23.640 1.00 42.81 C ANISOU 1116 CG GLN A 165 5762 4919 5584 633 508 -279 C ATOM 1117 CD GLN A 165 19.120 -17.132 23.233 1.00 48.87 C ANISOU 1117 CD GLN A 165 6575 5604 6391 658 469 -282 C ATOM 1118 OE1 GLN A 165 18.616 -16.651 22.207 1.00 47.90 O ANISOU 1118 OE1 GLN A 165 6394 5467 6338 700 447 -249 O ATOM 1119 NE2 GLN A 165 19.907 -16.424 24.052 1.00 52.23 N ANISOU 1119 NE2 GLN A 165 7109 5968 6769 633 457 -322 N ATOM 1120 N ALA A 166 15.524 -19.472 25.768 1.00 25.64 N ANISOU 1120 N ALA A 166 3514 2794 3433 738 813 -375 N ATOM 1121 CA ALA A 166 15.266 -19.334 27.205 1.00 24.35 C ANISOU 1121 CA ALA A 166 3447 2607 3199 744 918 -435 C ATOM 1122 C ALA A 166 15.119 -20.677 27.916 1.00 25.94 C ANISOU 1122 C ALA A 166 3659 2867 3331 691 979 -428 C ATOM 1123 O ALA A 166 15.602 -20.855 29.038 1.00 26.59 O ANISOU 1123 O ALA A 166 3869 2934 3302 658 1009 -456 O ATOM 1124 CB ALA A 166 14.045 -18.481 27.450 1.00 28.83 C ANISOU 1124 CB ALA A 166 3973 3138 3841 830 1018 -483 C ATOM 1125 N LYS A 167 14.399 -21.608 27.294 1.00 25.24 N ANISOU 1125 N LYS A 167 3443 2839 3307 684 996 -390 N ATOM 1126 CA LYS A 167 14.262 -22.939 27.892 1.00 24.73 C ANISOU 1126 CA LYS A 167 3390 2824 3183 626 1050 -375 C ATOM 1127 C LYS A 167 15.617 -23.662 27.944 1.00 22.88 C ANISOU 1127 C LYS A 167 3240 2600 2854 557 947 -343 C ATOM 1128 O LYS A 167 15.893 -24.362 28.927 1.00 23.78 O ANISOU 1128 O LYS A 167 3449 2719 2869 513 982 -348 O ATOM 1129 CB LYS A 167 13.221 -23.775 27.145 1.00 26.07 C ANISOU 1129 CB LYS A 167 3400 3050 3454 627 1080 -344 C ATOM 1130 CG LYS A 167 11.785 -23.340 27.405 1.00 28.77 C ANISOU 1130 CG LYS A 167 3654 3391 3888 687 1207 -382 C ATOM 1131 CD LYS A 167 10.816 -24.118 26.563 1.00 32.86 C ANISOU 1131 CD LYS A 167 4002 3963 4522 684 1211 -351 C ATOM 1132 CE LYS A 167 9.418 -23.641 26.721 1.00 38.25 C ANISOU 1132 CE LYS A 167 4570 4643 5318 748 1324 -390 C ATOM 1133 NZ LYS A 167 8.557 -24.315 25.720 1.00 39.39 N ANISOU 1133 NZ LYS A 167 4538 4837 5592 745 1291 -359 N ATOM 1134 N CYS A 168 16.451 -23.530 26.899 1.00 22.38 N ANISOU 1134 N CYS A 168 3142 2539 2821 547 824 -309 N ATOM 1135 CA CYS A 168 17.761 -24.167 26.856 1.00 21.54 C ANISOU 1135 CA CYS A 168 3094 2443 2646 489 726 -283 C ATOM 1136 C CYS A 168 18.627 -23.614 27.986 1.00 21.99 C ANISOU 1136 C CYS A 168 3301 2449 2603 473 711 -322 C ATOM 1137 O CYS A 168 19.249 -24.395 28.726 1.00 22.43 O ANISOU 1137 O CYS A 168 3440 2512 2570 429 689 -318 O ATOM 1138 CB CYS A 168 18.436 -23.919 25.490 1.00 25.07 C ANISOU 1138 CB CYS A 168 3473 2898 3154 488 617 -247 C ATOM 1139 SG CYS A 168 19.725 -25.091 25.089 1.00 29.19 S ANISOU 1139 SG CYS A 168 4001 3457 3634 424 515 -208 S ATOM 1140 N GLU A 169 18.685 -22.284 28.096 1.00 23.93 N ANISOU 1140 N GLU A 169 3588 2640 2865 510 712 -359 N ATOM 1141 CA GLU A 169 19.459 -21.650 29.160 1.00 23.27 C ANISOU 1141 CA GLU A 169 3651 2500 2690 496 691 -404 C ATOM 1142 C GLU A 169 18.954 -22.046 30.548 1.00 24.48 C ANISOU 1142 C GLU A 169 3910 2648 2742 492 791 -440 C ATOM 1143 O GLU A 169 19.751 -22.298 31.440 1.00 27.09 O ANISOU 1143 O GLU A 169 4366 2961 2967 454 749 -454 O ATOM 1144 CB GLU A 169 19.503 -20.136 28.945 1.00 27.23 C ANISOU 1144 CB GLU A 169 4173 2935 3238 537 678 -438 C ATOM 1145 CG GLU A 169 20.367 -19.817 27.753 1.00 31.78 C ANISOU 1145 CG GLU A 169 4688 3508 3879 518 566 -398 C ATOM 1146 CD GLU A 169 20.262 -18.377 27.348 1.00 36.55 C ANISOU 1146 CD GLU A 169 5299 4044 4544 559 558 -418 C ATOM 1147 OE1 GLU A 169 19.429 -17.679 27.966 1.00 37.07 O ANISOU 1147 OE1 GLU A 169 5406 4068 4612 612 640 -465 O ATOM 1148 OE2 GLU A 169 21.006 -17.966 26.427 1.00 38.03 O ANISOU 1148 OE2 GLU A 169 5456 4217 4778 537 475 -385 O ATOM 1149 N ALA A 170 17.641 -22.124 30.730 1.00 23.84 N ANISOU 1149 N ALA A 170 3779 2584 2695 529 921 -453 N ATOM 1150 CA ALA A 170 17.086 -22.566 32.008 1.00 23.28 C ANISOU 1150 CA ALA A 170 3806 2513 2527 520 1039 -482 C ATOM 1151 C ALA A 170 17.445 -24.004 32.348 1.00 23.30 C ANISOU 1151 C ALA A 170 3844 2557 2453 456 1018 -438 C ATOM 1152 O ALA A 170 17.572 -24.335 33.524 1.00 23.76 O ANISOU 1152 O ALA A 170 4044 2598 2387 430 1061 -456 O ATOM 1153 CB ALA A 170 15.581 -22.372 32.019 1.00 27.04 C ANISOU 1153 CB ALA A 170 4193 3003 3079 572 1192 -504 C ATOM 1154 N SER A 171 17.605 -24.843 31.335 1.00 23.41 N ANISOU 1154 N SER A 171 3742 2618 2537 432 951 -381 N ATOM 1155 CA SER A 171 17.918 -26.230 31.563 1.00 23.68 C ANISOU 1155 CA SER A 171 3802 2683 2512 377 927 -338 C ATOM 1156 C SER A 171 19.386 -26.395 31.903 1.00 20.46 C ANISOU 1156 C SER A 171 3504 2252 2019 342 791 -332 C ATOM 1157 O SER A 171 19.745 -27.369 32.559 1.00 21.74 O ANISOU 1157 O SER A 171 3751 2417 2094 302 772 -310 O ATOM 1158 CB SER A 171 17.590 -27.024 30.310 1.00 23.07 C ANISOU 1158 CB SER A 171 3564 2658 2544 368 897 -287 C ATOM 1159 OG SER A 171 16.192 -27.152 30.125 1.00 27.66 O ANISOU 1159 OG SER A 171 4043 3265 3201 388 1018 -289 O ATOM 1160 N TYR A 172 20.233 -25.457 31.473 1.00 22.04 N ANISOU 1160 N TYR A 172 3701 2425 2250 356 694 -350 N ATOM 1161 CA TYR A 172 21.682 -25.553 31.688 1.00 20.96 C ANISOU 1161 CA TYR A 172 3639 2267 2059 322 554 -348 C ATOM 1162 C TYR A 172 22.302 -24.192 32.006 1.00 20.80 C ANISOU 1162 C TYR A 172 3690 2188 2023 335 505 -399 C ATOM 1163 O TYR A 172 22.961 -23.576 31.182 1.00 24.43 O ANISOU 1163 O TYR A 172 4085 2639 2558 335 425 -395 O ATOM 1164 CB TYR A 172 22.379 -26.111 30.434 1.00 21.79 C ANISOU 1164 CB TYR A 172 3619 2409 2249 306 453 -301 C ATOM 1165 CG TYR A 172 21.925 -27.522 30.061 1.00 20.19 C ANISOU 1165 CG TYR A 172 3352 2257 2064 288 478 -253 C ATOM 1166 CD1 TYR A 172 22.494 -28.637 30.656 1.00 20.96 C ANISOU 1166 CD1 TYR A 172 3522 2355 2085 254 429 -231 C ATOM 1167 CD2 TYR A 172 20.935 -27.743 29.094 1.00 20.71 C ANISOU 1167 CD2 TYR A 172 3285 2361 2222 306 541 -230 C ATOM 1168 CE1 TYR A 172 22.077 -29.947 30.320 1.00 20.02 C ANISOU 1168 CE1 TYR A 172 3352 2272 1984 235 450 -188 C ATOM 1169 CE2 TYR A 172 20.499 -28.993 28.797 1.00 19.46 C ANISOU 1169 CE2 TYR A 172 3074 2240 2080 285 561 -193 C ATOM 1170 CZ TYR A 172 21.103 -30.107 29.385 1.00 19.28 C ANISOU 1170 CZ TYR A 172 3128 2214 1983 247 516 -171 C ATOM 1171 OH TYR A 172 20.702 -31.402 29.076 1.00 19.71 O ANISOU 1171 OH TYR A 172 3137 2296 2055 222 531 -132 O ATOM 1172 N PRO A 173 22.015 -23.678 33.194 1.00 21.50 N ANISOU 1172 N PRO A 173 3918 2234 2016 346 565 -449 N ATOM 1173 CA PRO A 173 22.387 -22.301 33.523 1.00 27.42 C ANISOU 1173 CA PRO A 173 4742 2920 2757 363 536 -507 C ATOM 1174 C PRO A 173 23.886 -22.042 33.384 1.00 25.27 C ANISOU 1174 C PRO A 173 4494 2621 2487 324 371 -508 C ATOM 1175 O PRO A 173 24.700 -22.795 33.940 1.00 27.44 O ANISOU 1175 O PRO A 173 4837 2900 2688 287 284 -498 O ATOM 1176 CB PRO A 173 21.935 -22.185 34.966 1.00 27.60 C ANISOU 1176 CB PRO A 173 4934 2907 2644 370 621 -557 C ATOM 1177 CG PRO A 173 20.890 -23.214 35.116 1.00 27.50 C ANISOU 1177 CG PRO A 173 4890 2946 2615 372 746 -524 C ATOM 1178 CD PRO A 173 21.362 -24.367 34.298 1.00 23.77 C ANISOU 1178 CD PRO A 173 4312 2525 2193 338 663 -455 C ATOM 1179 N GLY A 174 24.214 -21.015 32.611 1.00 25.13 N ANISOU 1179 N GLY A 174 4412 2575 2562 333 330 -518 N ATOM 1180 CA GLY A 174 25.587 -20.546 32.421 1.00 26.52 C ANISOU 1180 CA GLY A 174 4596 2720 2762 293 188 -526 C ATOM 1181 C GLY A 174 26.396 -21.387 31.434 1.00 30.83 C ANISOU 1181 C GLY A 174 5016 3318 3378 260 102 -469 C ATOM 1182 O GLY A 174 27.568 -21.088 31.176 1.00 29.88 O ANISOU 1182 O GLY A 174 4876 3180 3296 223 -8 -472 O ATOM 1183 N LYS A 175 25.768 -22.399 30.843 1.00 24.92 N ANISOU 1183 N LYS A 175 4178 2635 2657 273 158 -420 N ATOM 1184 CA LYS A 175 26.502 -23.338 29.990 1.00 24.17 C ANISOU 1184 CA LYS A 175 3980 2590 2615 247 84 -371 C ATOM 1185 C LYS A 175 26.193 -23.332 28.501 1.00 22.00 C ANISOU 1185 C LYS A 175 3557 2355 2449 260 111 -329 C ATOM 1186 O LYS A 175 26.890 -24.007 27.730 1.00 22.90 O ANISOU 1186 O LYS A 175 3588 2505 2608 239 53 -296 O ATOM 1187 CB LYS A 175 26.226 -24.773 30.466 1.00 21.32 C ANISOU 1187 CB LYS A 175 3643 2268 2189 242 100 -345 C ATOM 1188 CG LYS A 175 26.714 -25.039 31.860 1.00 22.80 C ANISOU 1188 CG LYS A 175 3984 2422 2258 224 49 -372 C ATOM 1189 CD LYS A 175 26.141 -26.356 32.379 1.00 27.32 C ANISOU 1189 CD LYS A 175 4600 3023 2757 222 97 -341 C ATOM 1190 CE LYS A 175 26.706 -26.667 33.758 1.00 30.03 C ANISOU 1190 CE LYS A 175 5114 3328 2968 203 31 -361 C ATOM 1191 NZ LYS A 175 26.119 -27.920 34.317 1.00 29.86 N ANISOU 1191 NZ LYS A 175 5156 3324 2866 197 85 -325 N ATOM 1192 N ILE A 176 25.136 -22.653 28.095 1.00 21.66 N ANISOU 1192 N ILE A 176 3482 2304 2446 299 199 -332 N ATOM 1193 CA ILE A 176 24.719 -22.655 26.704 1.00 21.18 C ANISOU 1193 CA ILE A 176 3296 2278 2476 316 220 -290 C ATOM 1194 C ILE A 176 25.282 -21.421 26.002 1.00 22.49 C ANISOU 1194 C ILE A 176 3442 2401 2704 310 179 -292 C ATOM 1195 O ILE A 176 24.925 -20.264 26.339 1.00 24.63 O ANISOU 1195 O ILE A 176 3768 2612 2979 334 208 -325 O ATOM 1196 CB ILE A 176 23.187 -22.642 26.588 1.00 22.35 C ANISOU 1196 CB ILE A 176 3407 2439 2644 366 328 -287 C ATOM 1197 CG1 ILE A 176 22.556 -23.815 27.330 1.00 22.72 C ANISOU 1197 CG1 ILE A 176 3477 2522 2632 362 384 -284 C ATOM 1198 CG2 ILE A 176 22.764 -22.624 25.160 1.00 26.07 C ANISOU 1198 CG2 ILE A 176 3759 2942 3204 385 330 -246 C ATOM 1199 CD1 ILE A 176 23.067 -25.218 26.897 1.00 22.66 C ANISOU 1199 CD1 ILE A 176 3419 2567 2622 328 331 -243 C ATOM 1200 N THR A 177 26.181 -21.659 25.062 1.00 20.87 N ANISOU 1200 N THR A 177 3165 2219 2545 278 118 -260 N ATOM 1201 CA THR A 177 26.707 -20.588 24.240 1.00 21.28 C ANISOU 1201 CA THR A 177 3191 2234 2658 263 90 -250 C ATOM 1202 C THR A 177 25.816 -20.333 23.008 1.00 21.95 C ANISOU 1202 C THR A 177 3204 2335 2800 301 138 -209 C ATOM 1203 O THR A 177 24.863 -21.095 22.727 1.00 21.03 O ANISOU 1203 O THR A 177 3040 2266 2684 334 182 -190 O ATOM 1204 CB THR A 177 28.119 -20.861 23.776 1.00 22.57 C ANISOU 1204 CB THR A 177 3312 2413 2850 208 13 -235 C ATOM 1205 OG1 THR A 177 28.096 -21.832 22.743 1.00 20.70 O ANISOU 1205 OG1 THR A 177 2983 2243 2640 210 21 -192 O ATOM 1206 CG2 THR A 177 29.041 -21.342 24.910 1.00 24.72 C ANISOU 1206 CG2 THR A 177 3638 2678 3075 174 -56 -270 C ATOM 1207 N SER A 178 26.137 -19.284 22.251 1.00 23.10 N ANISOU 1207 N SER A 178 3343 2438 2994 292 122 -193 N ATOM 1208 CA SER A 178 25.372 -18.983 21.054 1.00 19.90 C ANISOU 1208 CA SER A 178 2885 2040 2636 328 150 -150 C ATOM 1209 C SER A 178 25.569 -20.069 19.992 1.00 20.60 C ANISOU 1209 C SER A 178 2889 2204 2733 314 138 -106 C ATOM 1210 O SER A 178 24.867 -20.083 18.998 1.00 22.64 O ANISOU 1210 O SER A 178 3105 2482 3018 344 152 -70 O ATOM 1211 CB SER A 178 25.771 -17.640 20.455 1.00 25.54 C ANISOU 1211 CB SER A 178 3627 2684 3392 315 133 -135 C ATOM 1212 OG SER A 178 27.120 -17.671 20.048 1.00 30.14 O ANISOU 1212 OG SER A 178 4194 3272 3988 246 88 -120 O ATOM 1213 N ASN A 179 26.538 -20.955 20.182 1.00 18.20 N ANISOU 1213 N ASN A 179 2567 1940 2410 270 103 -110 N ATOM 1214 CA ASN A 179 26.798 -22.028 19.220 1.00 18.14 C ANISOU 1214 CA ASN A 179 2486 1998 2408 258 94 -77 C ATOM 1215 C ASN A 179 26.142 -23.364 19.583 1.00 17.15 C ANISOU 1215 C ASN A 179 2337 1927 2254 279 108 -82 C ATOM 1216 O ASN A 179 26.476 -24.405 19.021 1.00 17.78 O ANISOU 1216 O ASN A 179 2368 2056 2332 267 93 -66 O ATOM 1217 CB ASN A 179 28.294 -22.256 19.067 1.00 18.88 C ANISOU 1217 CB ASN A 179 2559 2102 2514 202 50 -79 C ATOM 1218 CG ASN A 179 29.001 -21.025 18.579 1.00 22.18 C ANISOU 1218 CG ASN A 179 2990 2470 2969 167 42 -68 C ATOM 1219 OD1 ASN A 179 28.581 -20.396 17.613 1.00 23.09 O ANISOU 1219 OD1 ASN A 179 3102 2570 3102 179 67 -33 O ATOM 1220 ND2 ASN A 179 30.078 -20.650 19.258 1.00 22.60 N ANISOU 1220 ND2 ASN A 179 3061 2489 3035 120 2 -97 N ATOM 1221 N MET A 180 25.198 -23.295 20.522 1.00 17.33 N ANISOU 1221 N MET A 180 2398 1934 2254 310 145 -106 N ATOM 1222 CA MET A 180 24.425 -24.426 21.014 1.00 17.42 C ANISOU 1222 CA MET A 180 2397 1983 2238 325 175 -110 C ATOM 1223 C MET A 180 22.959 -24.111 20.991 1.00 17.86 C ANISOU 1223 C MET A 180 2435 2036 2317 373 236 -110 C ATOM 1224 O MET A 180 22.529 -22.948 21.115 1.00 19.96 O ANISOU 1224 O MET A 180 2726 2254 2603 403 259 -124 O ATOM 1225 CB MET A 180 24.824 -24.717 22.474 1.00 17.85 C ANISOU 1225 CB MET A 180 2529 2019 2233 307 168 -145 C ATOM 1226 CG MET A 180 26.305 -25.016 22.667 1.00 17.84 C ANISOU 1226 CG MET A 180 2544 2017 2218 264 93 -151 C ATOM 1227 SD MET A 180 26.713 -25.121 24.410 1.00 20.33 S ANISOU 1227 SD MET A 180 2973 2296 2455 248 67 -193 S ATOM 1228 CE MET A 180 28.473 -25.191 24.324 1.00 21.63 C ANISOU 1228 CE MET A 180 3122 2455 2641 203 -39 -200 C ATOM 1229 N PHE A 181 22.167 -25.173 20.863 1.00 17.03 N ANISOU 1229 N PHE A 181 2281 1974 2214 382 262 -99 N ATOM 1230 CA PHE A 181 20.731 -25.097 21.021 1.00 16.71 C ANISOU 1230 CA PHE A 181 2207 1937 2204 422 325 -106 C ATOM 1231 C PHE A 181 20.175 -26.409 21.548 1.00 16.38 C ANISOU 1231 C PHE A 181 2148 1933 2142 406 362 -106 C ATOM 1232 O PHE A 181 20.862 -27.443 21.468 1.00 17.51 O ANISOU 1232 O PHE A 181 2295 2102 2256 370 323 -93 O ATOM 1233 CB PHE A 181 20.030 -24.662 19.731 1.00 17.38 C ANISOU 1233 CB PHE A 181 2219 2031 2356 458 311 -79 C ATOM 1234 CG PHE A 181 20.014 -25.657 18.622 1.00 16.74 C ANISOU 1234 CG PHE A 181 2073 2000 2289 443 270 -47 C ATOM 1235 CD1 PHE A 181 21.179 -26.039 17.941 1.00 16.21 C ANISOU 1235 CD1 PHE A 181 2013 1950 2196 408 216 -28 C ATOM 1236 CD2 PHE A 181 18.802 -26.177 18.194 1.00 17.87 C ANISOU 1236 CD2 PHE A 181 2141 2172 2477 467 286 -39 C ATOM 1237 CE1 PHE A 181 21.113 -26.919 16.891 1.00 16.34 C ANISOU 1237 CE1 PHE A 181 1979 2008 2221 400 184 -5 C ATOM 1238 CE2 PHE A 181 18.751 -27.048 17.161 1.00 16.29 C ANISOU 1238 CE2 PHE A 181 1891 2012 2287 454 242 -15 C ATOM 1239 CZ PHE A 181 19.911 -27.429 16.521 1.00 15.52 C ANISOU 1239 CZ PHE A 181 1816 1929 2152 422 193 1 C ATOM 1240 N CYS A 182 18.944 -26.364 22.039 1.00 18.32 N ANISOU 1240 N CYS A 182 2371 2178 2410 432 437 -121 N ATOM 1241 CA CYS A 182 18.278 -27.546 22.592 1.00 16.91 C ANISOU 1241 CA CYS A 182 2177 2029 2219 410 489 -120 C ATOM 1242 C CYS A 182 17.136 -27.961 21.715 1.00 18.35 C ANISOU 1242 C CYS A 182 2245 2244 2482 427 503 -103 C ATOM 1243 O CYS A 182 16.406 -27.122 21.163 1.00 19.88 O ANISOU 1243 O CYS A 182 2380 2430 2743 474 510 -107 O ATOM 1244 CB CYS A 182 17.767 -27.347 24.023 1.00 21.09 C ANISOU 1244 CB CYS A 182 2775 2534 2705 414 584 -153 C ATOM 1245 SG CYS A 182 19.039 -27.028 25.278 1.00 22.95 S ANISOU 1245 SG CYS A 182 3166 2727 2827 388 559 -178 S ATOM 1246 N VAL A 183 16.984 -29.283 21.620 1.00 18.31 N ANISOU 1246 N VAL A 183 2212 2272 2473 389 499 -86 N ATOM 1247 CA VAL A 183 15.901 -29.936 20.923 1.00 18.03 C ANISOU 1247 CA VAL A 183 2071 2268 2511 390 508 -74 C ATOM 1248 C VAL A 183 15.416 -31.037 21.854 1.00 18.99 C ANISOU 1248 C VAL A 183 2206 2398 2612 346 579 -75 C ATOM 1249 O VAL A 183 16.233 -31.745 22.423 1.00 20.19 O ANISOU 1249 O VAL A 183 2440 2542 2690 308 565 -67 O ATOM 1250 CB VAL A 183 16.419 -30.508 19.578 1.00 18.78 C ANISOU 1250 CB VAL A 183 2129 2389 2619 378 409 -48 C ATOM 1251 CG1 VAL A 183 15.279 -31.158 18.789 1.00 21.92 C ANISOU 1251 CG1 VAL A 183 2420 2815 3095 377 400 -39 C ATOM 1252 CG2 VAL A 183 17.128 -29.419 18.757 1.00 20.29 C ANISOU 1252 CG2 VAL A 183 2336 2566 2808 410 348 -41 C ATOM 1253 N GLY A 184A 14.118 -31.224 21.962 1.00 19.40 N ANISOU 1253 N GLY A 184A 2175 2462 2733 349 650 -82 N ATOM 1254 CA GLY A 184A 13.592 -32.289 22.794 1.00 20.21 C ANISOU 1254 CA GLY A 184A 2288 2569 2822 297 728 -78 C ATOM 1255 C GLY A 184A 12.424 -31.799 23.637 1.00 21.11 C ANISOU 1255 C GLY A 184A 2366 2679 2977 314 860 -104 C ATOM 1256 O GLY A 184A 11.573 -31.029 23.181 1.00 23.12 O ANISOU 1256 O GLY A 184A 2520 2939 3324 363 877 -122 O ATOM 1257 N PHE A 184 12.392 -32.304 24.860 1.00 23.53 N ANISOU 1257 N PHE A 184 2757 2971 3212 273 953 -106 N ATOM 1258 CA PHE A 184 11.221 -32.231 25.722 1.00 26.71 C ANISOU 1258 CA PHE A 184 3127 3374 3649 268 1103 -127 C ATOM 1259 C PHE A 184 11.679 -31.963 27.150 1.00 24.74 C ANISOU 1259 C PHE A 184 3037 3093 3272 258 1186 -143 C ATOM 1260 O PHE A 184 12.505 -32.710 27.703 1.00 28.04 O ANISOU 1260 O PHE A 184 3577 3494 3582 211 1158 -120 O ATOM 1261 CB PHE A 184 10.437 -33.555 25.677 1.00 27.95 C ANISOU 1261 CB PHE A 184 3213 3551 3858 200 1149 -103 C ATOM 1262 CG PHE A 184 10.009 -33.956 24.279 1.00 24.24 C ANISOU 1262 CG PHE A 184 2598 3109 3504 201 1053 -90 C ATOM 1263 CD1 PHE A 184 10.847 -34.700 23.472 1.00 26.39 C ANISOU 1263 CD1 PHE A 184 2896 3384 3747 177 925 -63 C ATOM 1264 CD2 PHE A 184 8.805 -33.521 23.757 1.00 26.94 C ANISOU 1264 CD2 PHE A 184 2781 3471 3982 234 1083 -110 C ATOM 1265 CE1 PHE A 184 10.478 -35.012 22.174 1.00 23.41 C ANISOU 1265 CE1 PHE A 184 2403 3030 3463 181 833 -56 C ATOM 1266 CE2 PHE A 184 8.417 -33.864 22.475 1.00 26.42 C ANISOU 1266 CE2 PHE A 184 2594 3428 4016 236 979 -100 C ATOM 1267 CZ PHE A 184 9.247 -34.585 21.704 1.00 25.07 C ANISOU 1267 CZ PHE A 184 2465 3259 3800 209 858 -74 C ATOM 1268 N LEU A 185 11.136 -30.908 27.738 1.00 28.04 N ANISOU 1268 N LEU A 185 3458 3497 3700 306 1283 -185 N ATOM 1269 CA LEU A 185 11.464 -30.607 29.115 1.00 30.91 C ANISOU 1269 CA LEU A 185 3981 3827 3936 299 1369 -208 C ATOM 1270 C LEU A 185 10.903 -31.700 30.014 1.00 30.46 C ANISOU 1270 C LEU A 185 3967 3774 3832 229 1491 -189 C ATOM 1271 O LEU A 185 11.418 -31.948 31.098 1.00 31.27 O ANISOU 1271 O LEU A 185 4235 3850 3797 197 1530 -186 O ATOM 1272 CB LEU A 185 10.960 -29.215 29.513 1.00 31.38 C ANISOU 1272 CB LEU A 185 4036 3866 4020 370 1452 -264 C ATOM 1273 CG LEU A 185 11.595 -27.971 28.866 1.00 30.61 C ANISOU 1273 CG LEU A 185 3939 3746 3946 437 1344 -284 C ATOM 1274 CD1 LEU A 185 11.151 -26.654 29.576 1.00 32.81 C ANISOU 1274 CD1 LEU A 185 4257 3987 4223 504 1443 -346 C ATOM 1275 CD2 LEU A 185 13.074 -28.063 28.903 1.00 32.21 C ANISOU 1275 CD2 LEU A 185 4269 3929 4041 411 1218 -265 C ATOM 1276 N GLU A 186 9.875 -32.412 29.545 1.00 28.22 N ANISOU 1276 N GLU A 186 3540 3521 3661 199 1544 -173 N ATOM 1277 CA GLU A 186 9.296 -33.493 30.315 1.00 35.57 C ANISOU 1277 CA GLU A 186 4502 4452 4562 122 1665 -149 C ATOM 1278 C GLU A 186 10.110 -34.790 30.254 1.00 35.35 C ANISOU 1278 C GLU A 186 4562 4412 4458 52 1571 -94 C ATOM 1279 O GLU A 186 9.813 -35.744 30.943 1.00 39.93 O ANISOU 1279 O GLU A 186 5202 4980 4991 -18 1655 -66 O ATOM 1280 CB GLU A 186 7.836 -33.732 29.894 1.00 43.44 C ANISOU 1280 CB GLU A 186 5302 5482 5723 110 1764 -158 C ATOM 1281 CG GLU A 186 7.626 -34.095 28.447 1.00 45.06 C ANISOU 1281 CG GLU A 186 5341 5715 6065 113 1634 -140 C ATOM 1282 CD GLU A 186 7.349 -32.888 27.520 1.00 47.22 C ANISOU 1282 CD GLU A 186 5489 6003 6449 207 1567 -175 C ATOM 1283 OE1 GLU A 186 6.567 -33.100 26.566 1.00 54.54 O ANISOU 1283 OE1 GLU A 186 6245 6958 7521 211 1527 -172 O ATOM 1284 OE2 GLU A 186 7.907 -31.768 27.700 1.00 37.57 O ANISOU 1284 OE2 GLU A 186 4341 4761 5173 273 1543 -202 O ATOM 1285 N GLY A 187 11.170 -34.800 29.454 1.00 28.95 N ANISOU 1285 N GLY A 187 3766 3600 3634 73 1400 -80 N ATOM 1286 CA GLY A 187 12.058 -35.937 29.346 1.00 29.89 C ANISOU 1286 CA GLY A 187 3966 3703 3688 24 1298 -36 C ATOM 1287 C GLY A 187 11.402 -37.059 28.548 1.00 30.08 C ANISOU 1287 C GLY A 187 3869 3745 3816 -27 1285 -6 C ATOM 1288 O GLY A 187 10.416 -36.817 27.844 1.00 34.40 O ANISOU 1288 O GLY A 187 4253 4323 4496 -14 1315 -23 O ATOM 1289 N GLY A 188A 11.956 -38.260 28.644 1.00 28.69 N ANISOU 1289 N GLY A 188A 3773 3544 3585 -82 1229 34 N ATOM 1290 CA GLY A 188A 11.356 -39.437 28.029 1.00 28.36 C ANISOU 1290 CA GLY A 188A 3641 3505 3629 -142 1220 62 C ATOM 1291 C GLY A 188A 11.869 -39.758 26.635 1.00 27.33 C ANISOU 1291 C GLY A 188A 3429 3390 3565 -121 1061 64 C ATOM 1292 O GLY A 188A 11.856 -40.903 26.215 1.00 28.01 O ANISOU 1292 O GLY A 188A 3503 3461 3678 -170 1015 89 O ATOM 1293 N LYS A 188 12.280 -38.730 25.901 1.00 23.61 N ANISOU 1293 N LYS A 188 2906 2944 3119 -50 985 37 N ATOM 1294 CA LYS A 188 12.743 -38.871 24.535 1.00 23.12 C ANISOU 1294 CA LYS A 188 2773 2901 3112 -25 847 35 C ATOM 1295 C LYS A 188 13.942 -37.947 24.371 1.00 22.10 C ANISOU 1295 C LYS A 188 2707 2773 2919 36 764 22 C ATOM 1296 O LYS A 188 13.864 -36.751 24.684 1.00 22.10 O ANISOU 1296 O LYS A 188 2708 2778 2911 81 804 -2 O ATOM 1297 CB LYS A 188 11.662 -38.452 23.556 1.00 26.69 C ANISOU 1297 CB LYS A 188 3054 3389 3698 -5 848 15 C ATOM 1298 CG LYS A 188 10.399 -39.271 23.551 1.00 28.38 C ANISOU 1298 CG LYS A 188 3170 3607 4008 -66 919 22 C ATOM 1299 CD LYS A 188 9.424 -38.589 22.626 1.00 35.13 C ANISOU 1299 CD LYS A 188 3856 4498 4995 -27 903 -4 C ATOM 1300 CE LYS A 188 8.197 -39.358 22.388 1.00 39.64 C ANISOU 1300 CE LYS A 188 4299 5077 5686 -85 945 -4 C ATOM 1301 NZ LYS A 188 7.174 -38.381 21.889 1.00 43.70 N ANISOU 1301 NZ LYS A 188 4655 5623 6325 -32 959 -35 N ATOM 1302 N ASP A 189 15.042 -38.473 23.850 1.00 19.75 N ANISOU 1302 N ASP A 189 2454 2466 2585 39 651 33 N ATOM 1303 CA ASP A 189 16.281 -37.712 23.765 1.00 17.16 C ANISOU 1303 CA ASP A 189 2185 2135 2199 84 576 22 C ATOM 1304 C ASP A 189 17.325 -38.511 22.986 1.00 20.08 C ANISOU 1304 C ASP A 189 2569 2501 2558 83 460 33 C ATOM 1305 O ASP A 189 17.134 -39.675 22.710 1.00 20.66 O ANISOU 1305 O ASP A 189 2633 2564 2652 47 441 48 O ATOM 1306 CB ASP A 189 16.805 -37.431 25.201 1.00 20.06 C ANISOU 1306 CB ASP A 189 2692 2471 2460 80 619 22 C ATOM 1307 CG ASP A 189 17.716 -36.225 25.340 1.00 21.03 C ANISOU 1307 CG ASP A 189 2860 2590 2540 126 576 -1 C ATOM 1308 OD1 ASP A 189 18.145 -35.564 24.349 1.00 20.30 O ANISOU 1308 OD1 ASP A 189 2703 2517 2493 162 510 -13 O ATOM 1309 OD2 ASP A 189 18.000 -35.945 26.537 1.00 24.06 O ANISOU 1309 OD2 ASP A 189 3358 2946 2837 122 613 -7 O ATOM 1310 N SER A 190 18.419 -37.866 22.640 1.00 17.25 N ANISOU 1310 N SER A 190 2232 2147 2174 121 389 21 N ATOM 1311 CA SER A 190 19.621 -38.530 22.136 1.00 17.74 C ANISOU 1311 CA SER A 190 2322 2202 2217 126 291 25 C ATOM 1312 C SER A 190 20.449 -38.970 23.323 1.00 18.68 C ANISOU 1312 C SER A 190 2561 2282 2254 113 274 35 C ATOM 1313 O SER A 190 20.280 -38.454 24.429 1.00 20.05 O ANISOU 1313 O SER A 190 2805 2439 2374 108 329 34 O ATOM 1314 CB SER A 190 20.410 -37.600 21.214 1.00 19.26 C ANISOU 1314 CB SER A 190 2472 2418 2427 168 233 9 C ATOM 1315 OG SER A 190 20.758 -36.454 21.921 1.00 18.95 O ANISOU 1315 OG SER A 190 2477 2370 2353 187 253 -3 O ATOM 1316 N CYS A 191 21.348 -39.927 23.085 1.00 17.37 N ANISOU 1316 N CYS A 191 2424 2098 2077 112 195 42 N ATOM 1317 CA CYS A 191 22.081 -40.558 24.158 1.00 17.55 C ANISOU 1317 CA CYS A 191 2563 2077 2029 102 162 57 C ATOM 1318 C CYS A 191 23.473 -41.023 23.700 1.00 17.46 C ANISOU 1318 C CYS A 191 2556 2055 2024 131 51 49 C ATOM 1319 O CYS A 191 23.860 -40.811 22.544 1.00 17.78 O ANISOU 1319 O CYS A 191 2511 2127 2118 155 16 30 O ATOM 1320 CB CYS A 191 21.217 -41.687 24.741 1.00 18.69 C ANISOU 1320 CB CYS A 191 2756 2187 2156 53 214 88 C ATOM 1321 SG CYS A 191 21.688 -42.185 26.464 1.00 25.36 S ANISOU 1321 SG CYS A 191 3784 2970 2882 32 211 117 S ATOM 1322 N GLN A 192 24.251 -41.612 24.601 1.00 18.06 N ANISOU 1322 N GLN A 192 2731 2087 2044 132 -4 61 N ATOM 1323 CA GLN A 192 25.593 -42.053 24.232 1.00 17.42 C ANISOU 1323 CA GLN A 192 2643 1995 1982 166 -110 49 C ATOM 1324 C GLN A 192 25.571 -42.983 23.046 1.00 16.58 C ANISOU 1324 C GLN A 192 2465 1895 1940 173 -132 43 C ATOM 1325 O GLN A 192 24.808 -43.972 22.996 1.00 17.60 O ANISOU 1325 O GLN A 192 2612 2000 2075 144 -107 62 O ATOM 1326 CB GLN A 192 26.293 -42.718 25.426 1.00 18.10 C ANISOU 1326 CB GLN A 192 2853 2022 2002 167 -176 68 C ATOM 1327 CG GLN A 192 26.916 -41.746 26.425 1.00 19.06 C ANISOU 1327 CG GLN A 192 3042 2135 2063 178 -207 59 C ATOM 1328 CD GLN A 192 25.856 -40.961 27.200 1.00 19.85 C ANISOU 1328 CD GLN A 192 3197 2241 2103 147 -102 65 C ATOM 1329 OE1 GLN A 192 24.836 -41.506 27.621 1.00 23.09 O ANISOU 1329 OE1 GLN A 192 3655 2636 2482 111 -25 92 O ATOM 1330 NE2 GLN A 192 26.093 -39.692 27.387 1.00 20.16 N ANISOU 1330 NE2 GLN A 192 3228 2301 2133 159 -96 39 N ATOM 1331 N GLY A 193 26.445 -42.673 22.084 1.00 16.47 N ANISOU 1331 N GLY A 193 2374 1910 1973 209 -177 14 N ATOM 1332 CA GLY A 193 26.477 -43.335 20.799 1.00 16.47 C ANISOU 1332 CA GLY A 193 2304 1925 2029 221 -191 -2 C ATOM 1333 C GLY A 193 25.824 -42.567 19.678 1.00 15.94 C ANISOU 1333 C GLY A 193 2150 1912 1996 218 -140 -15 C ATOM 1334 O GLY A 193 26.021 -42.874 18.507 1.00 17.70 O ANISOU 1334 O GLY A 193 2317 2154 2254 235 -156 -35 O ATOM 1335 N ASP A 194 25.066 -41.546 20.039 1.00 16.27 N ANISOU 1335 N ASP A 194 2187 1974 2023 202 -83 -6 N ATOM 1336 CA ASP A 194 24.432 -40.675 19.064 1.00 14.58 C ANISOU 1336 CA ASP A 194 1897 1804 1840 206 -44 -14 C ATOM 1337 C ASP A 194 25.271 -39.455 18.665 1.00 15.14 C ANISOU 1337 C ASP A 194 1935 1902 1916 231 -55 -29 C ATOM 1338 O ASP A 194 24.967 -38.833 17.634 1.00 13.81 O ANISOU 1338 O ASP A 194 1710 1765 1771 239 -38 -34 O ATOM 1339 CB ASP A 194 23.083 -40.221 19.572 1.00 13.96 C ANISOU 1339 CB ASP A 194 1817 1729 1758 180 26 1 C ATOM 1340 CG ASP A 194 22.055 -41.337 19.640 1.00 16.40 C ANISOU 1340 CG ASP A 194 2128 2020 2083 145 50 15 C ATOM 1341 OD1 ASP A 194 22.072 -42.235 18.760 1.00 15.87 O ANISOU 1341 OD1 ASP A 194 2033 1951 2045 142 13 8 O ATOM 1342 OD2 ASP A 194 21.230 -41.327 20.581 1.00 17.79 O ANISOU 1342 OD2 ASP A 194 2335 2181 2244 116 111 32 O ATOM 1343 N ALA A 195 26.253 -39.053 19.482 1.00 14.77 N ANISOU 1343 N ALA A 195 1927 1837 1846 239 -85 -34 N ATOM 1344 CA ALA A 195 27.048 -37.853 19.213 1.00 15.22 C ANISOU 1344 CA ALA A 195 1954 1912 1915 252 -92 -47 C ATOM 1345 C ALA A 195 27.618 -37.826 17.829 1.00 14.74 C ANISOU 1345 C ALA A 195 1825 1882 1892 267 -102 -61 C ATOM 1346 O ALA A 195 28.027 -38.848 17.287 1.00 15.19 O ANISOU 1346 O ALA A 195 1867 1940 1965 279 -129 -71 O ATOM 1347 CB ALA A 195 28.163 -37.686 20.207 1.00 15.81 C ANISOU 1347 CB ALA A 195 2074 1961 1973 256 -145 -57 C ATOM 1348 N GLY A 196 27.588 -36.628 17.264 1.00 14.30 N ANISOU 1348 N GLY A 196 1739 1848 1847 268 -74 -60 N ATOM 1349 CA GLY A 196 28.075 -36.403 15.917 1.00 14.02 C ANISOU 1349 CA GLY A 196 1652 1842 1835 277 -68 -67 C ATOM 1350 C GLY A 196 27.040 -36.534 14.856 1.00 14.24 C ANISOU 1350 C GLY A 196 1659 1891 1860 279 -44 -58 C ATOM 1351 O GLY A 196 27.246 -36.064 13.744 1.00 15.66 O ANISOU 1351 O GLY A 196 1814 2094 2043 285 -31 -57 O ATOM 1352 N GLY A 197 25.953 -37.239 15.158 1.00 14.56 N ANISOU 1352 N GLY A 197 1712 1923 1896 273 -40 -50 N ATOM 1353 CA GLY A 197 24.921 -37.447 14.179 1.00 14.34 C ANISOU 1353 CA GLY A 197 1659 1914 1875 273 -33 -45 C ATOM 1354 C GLY A 197 24.023 -36.258 13.978 1.00 14.92 C ANISOU 1354 C GLY A 197 1716 1997 1955 277 -7 -28 C ATOM 1355 O GLY A 197 24.187 -35.215 14.618 1.00 14.69 O ANISOU 1355 O GLY A 197 1700 1958 1925 280 13 -22 O ATOM 1356 N PRO A 198 23.073 -36.426 13.074 1.00 14.72 N ANISOU 1356 N PRO A 198 1664 1988 1942 281 -16 -24 N ATOM 1357 CA PRO A 198 22.258 -35.320 12.561 1.00 14.80 C ANISOU 1357 CA PRO A 198 1654 2007 1965 296 -8 -7 C ATOM 1358 C PRO A 198 21.040 -34.994 13.391 1.00 15.75 C ANISOU 1358 C PRO A 198 1752 2116 2118 296 19 0 C ATOM 1359 O PRO A 198 20.333 -35.875 13.901 1.00 16.97 O ANISOU 1359 O PRO A 198 1891 2265 2291 277 29 -5 O ATOM 1360 CB PRO A 198 21.797 -35.866 11.218 1.00 16.76 C ANISOU 1360 CB PRO A 198 1885 2274 2209 300 -47 -10 C ATOM 1361 CG PRO A 198 21.778 -37.379 11.379 1.00 18.01 C ANISOU 1361 CG PRO A 198 2045 2427 2371 281 -64 -30 C ATOM 1362 CD PRO A 198 22.916 -37.667 12.286 1.00 16.35 C ANISOU 1362 CD PRO A 198 1864 2201 2147 275 -47 -38 C ATOM 1363 N VAL A 199 20.769 -33.688 13.414 1.00 15.38 N ANISOU 1363 N VAL A 199 1701 2062 2082 317 36 11 N ATOM 1364 CA VAL A 199 19.482 -33.135 13.774 1.00 15.54 C ANISOU 1364 CA VAL A 199 1683 2075 2145 333 60 15 C ATOM 1365 C VAL A 199 19.036 -32.399 12.529 1.00 15.62 C ANISOU 1365 C VAL A 199 1671 2093 2170 362 20 31 C ATOM 1366 O VAL A 199 19.591 -31.377 12.168 1.00 16.15 O ANISOU 1366 O VAL A 199 1769 2149 2218 379 16 44 O ATOM 1367 CB VAL A 199 19.541 -32.161 14.964 1.00 16.23 C ANISOU 1367 CB VAL A 199 1799 2137 2232 342 112 11 C ATOM 1368 CG1 VAL A 199 18.153 -31.617 15.247 1.00 19.09 C ANISOU 1368 CG1 VAL A 199 2111 2493 2649 367 146 10 C ATOM 1369 CG2 VAL A 199 20.157 -32.862 16.186 1.00 20.10 C ANISOU 1369 CG2 VAL A 199 2335 2615 2688 313 139 -1 C ATOM 1370 N VAL A 200 18.039 -32.928 11.853 1.00 13.56 N ANISOU 1370 N VAL A 200 1362 1848 1943 366 -15 30 N ATOM 1371 CA VAL A 200 17.547 -32.350 10.583 1.00 16.26 C ANISOU 1371 CA VAL A 200 1690 2196 2292 396 -74 46 C ATOM 1372 C VAL A 200 16.174 -31.734 10.794 1.00 17.55 C ANISOU 1372 C VAL A 200 1787 2351 2531 428 -75 49 C ATOM 1373 O VAL A 200 15.251 -32.370 11.345 1.00 17.29 O ANISOU 1373 O VAL A 200 1690 2324 2555 415 -56 33 O ATOM 1374 CB VAL A 200 17.494 -33.435 9.482 1.00 18.18 C ANISOU 1374 CB VAL A 200 1933 2462 2514 380 -135 39 C ATOM 1375 CG1 VAL A 200 16.721 -32.951 8.244 1.00 19.54 C ANISOU 1375 CG1 VAL A 200 2092 2638 2694 411 -210 54 C ATOM 1376 CG2 VAL A 200 18.896 -33.873 9.125 1.00 17.15 C ANISOU 1376 CG2 VAL A 200 1866 2339 2313 361 -129 34 C ATOM 1377 N CYS A 201 16.021 -30.460 10.413 1.00 16.67 N ANISOU 1377 N CYS A 201 1687 2219 2428 471 -92 68 N ATOM 1378 CA CYS A 201 14.788 -29.705 10.582 1.00 18.42 C ANISOU 1378 CA CYS A 201 1844 2426 2730 516 -96 68 C ATOM 1379 C CYS A 201 14.565 -28.999 9.255 1.00 19.37 C ANISOU 1379 C CYS A 201 1982 2536 2842 556 -183 97 C ATOM 1380 O CYS A 201 15.525 -28.474 8.661 1.00 19.47 O ANISOU 1380 O CYS A 201 2077 2536 2783 554 -196 120 O ATOM 1381 CB CYS A 201 14.922 -28.711 11.713 1.00 21.24 C ANISOU 1381 CB CYS A 201 2219 2751 3102 536 -21 62 C ATOM 1382 SG CYS A 201 15.829 -29.210 13.199 1.00 23.48 S ANISOU 1382 SG CYS A 201 2550 3033 3340 488 70 39 S ATOM 1383 N ASN A 202 13.357 -29.080 8.731 1.00 21.37 N ANISOU 1383 N ASN A 202 2162 2795 3163 585 -246 96 N ATOM 1384 CA ASN A 202 13.013 -28.435 7.454 1.00 21.49 C ANISOU 1384 CA ASN A 202 2200 2796 3169 628 -348 125 C ATOM 1385 C ASN A 202 13.921 -28.965 6.322 1.00 21.12 C ANISOU 1385 C ASN A 202 2243 2767 3014 596 -397 141 C ATOM 1386 O ASN A 202 14.252 -28.268 5.378 1.00 20.96 O ANISOU 1386 O ASN A 202 2299 2728 2936 618 -446 175 O ATOM 1387 CB ASN A 202 13.092 -26.907 7.547 1.00 22.32 C ANISOU 1387 CB ASN A 202 2345 2853 3283 682 -339 151 C ATOM 1388 CG ASN A 202 12.153 -26.317 8.594 1.00 21.59 C ANISOU 1388 CG ASN A 202 2166 2738 3297 725 -288 128 C ATOM 1389 OD1 ASN A 202 11.167 -26.940 9.024 1.00 24.10 O ANISOU 1389 OD1 ASN A 202 2378 3080 3701 725 -277 99 O ATOM 1390 ND2 ASN A 202 12.472 -25.087 9.008 1.00 25.25 N ANISOU 1390 ND2 ASN A 202 2680 3155 3760 760 -251 139 N ATOM 1391 N GLY A 203 14.355 -30.228 6.420 1.00 17.90 N ANISOU 1391 N GLY A 203 1836 2391 2575 544 -377 116 N ATOM 1392 CA GLY A 203 15.220 -30.797 5.394 1.00 19.32 C ANISOU 1392 CA GLY A 203 2098 2587 2656 518 -409 121 C ATOM 1393 C GLY A 203 16.667 -30.339 5.322 1.00 17.80 C ANISOU 1393 C GLY A 203 1997 2387 2378 501 -350 138 C ATOM 1394 O GLY A 203 17.341 -30.503 4.321 1.00 20.00 O ANISOU 1394 O GLY A 203 2351 2676 2575 490 -372 149 O ATOM 1395 N GLN A 204 17.145 -29.743 6.389 1.00 16.28 N ANISOU 1395 N GLN A 204 1801 2178 2208 498 -274 139 N ATOM 1396 CA GLN A 204 18.503 -29.253 6.466 1.00 16.86 C ANISOU 1396 CA GLN A 204 1944 2241 2222 477 -218 151 C ATOM 1397 C GLN A 204 19.141 -29.632 7.792 1.00 16.93 C ANISOU 1397 C GLN A 204 1931 2252 2250 448 -145 124 C ATOM 1398 O GLN A 204 18.448 -29.872 8.774 1.00 16.21 O ANISOU 1398 O GLN A 204 1784 2158 2216 452 -124 105 O ATOM 1399 CB GLN A 204 18.536 -27.743 6.333 1.00 20.41 C ANISOU 1399 CB GLN A 204 2434 2648 2673 507 -217 188 C ATOM 1400 CG GLN A 204 17.827 -27.230 5.112 1.00 18.57 C ANISOU 1400 CG GLN A 204 2232 2400 2421 544 -300 222 C ATOM 1401 CD GLN A 204 17.863 -25.727 5.008 1.00 19.16 C ANISOU 1401 CD GLN A 204 2358 2422 2500 575 -302 262 C ATOM 1402 OE1 GLN A 204 17.827 -25.020 6.017 1.00 20.26 O ANISOU 1402 OE1 GLN A 204 2476 2530 2693 587 -256 255 O ATOM 1403 NE2 GLN A 204 17.864 -25.218 3.778 1.00 21.91 N ANISOU 1403 NE2 GLN A 204 2784 2752 2789 590 -359 305 N ATOM 1404 N LEU A 209 20.459 -29.690 7.781 1.00 15.93 N ANISOU 1404 N LEU A 209 1848 2129 2075 419 -107 123 N ATOM 1405 CA LEU A 209 21.234 -30.079 8.961 1.00 14.93 C ANISOU 1405 CA LEU A 209 1712 2003 1959 392 -55 98 C ATOM 1406 C LEU A 209 21.336 -28.933 9.956 1.00 16.52 C ANISOU 1406 C LEU A 209 1922 2168 2188 399 -18 103 C ATOM 1407 O LEU A 209 22.231 -28.095 9.844 1.00 18.68 O ANISOU 1407 O LEU A 209 2235 2421 2442 388 0 117 O ATOM 1408 CB LEU A 209 22.630 -30.600 8.546 1.00 16.36 C ANISOU 1408 CB LEU A 209 1923 2201 2092 362 -36 89 C ATOM 1409 CG LEU A 209 23.463 -31.172 9.706 1.00 16.09 C ANISOU 1409 CG LEU A 209 1875 2167 2072 338 -3 62 C ATOM 1410 CD1 LEU A 209 22.824 -32.492 10.198 1.00 16.46 C ANISOU 1410 CD1 LEU A 209 1891 2227 2136 335 -18 38 C ATOM 1411 CD2 LEU A 209 24.900 -31.353 9.306 1.00 18.37 C ANISOU 1411 CD2 LEU A 209 2180 2466 2332 317 18 54 C ATOM 1412 N GLN A 210 20.421 -28.851 10.897 1.00 16.11 N ANISOU 1412 N GLN A 210 1835 2104 2183 416 -4 90 N ATOM 1413 CA GLN A 210 20.466 -27.800 11.918 1.00 16.07 C ANISOU 1413 CA GLN A 210 1847 2060 2199 427 35 86 C ATOM 1414 C GLN A 210 21.425 -28.088 13.057 1.00 16.57 C ANISOU 1414 C GLN A 210 1934 2118 2243 394 70 62 C ATOM 1415 O GLN A 210 22.000 -27.159 13.610 1.00 16.80 O ANISOU 1415 O GLN A 210 2000 2114 2268 390 89 59 O ATOM 1416 CB GLN A 210 19.084 -27.520 12.525 1.00 17.33 C ANISOU 1416 CB GLN A 210 1962 2207 2416 464 49 75 C ATOM 1417 CG GLN A 210 18.128 -26.745 11.611 1.00 19.15 C ANISOU 1417 CG GLN A 210 2171 2423 2682 512 6 99 C ATOM 1418 CD GLN A 210 18.570 -25.334 11.392 1.00 20.76 C ANISOU 1418 CD GLN A 210 2432 2578 2877 531 4 121 C ATOM 1419 OE1 GLN A 210 19.313 -24.779 12.188 1.00 20.26 O ANISOU 1419 OE1 GLN A 210 2410 2486 2801 515 44 110 O ATOM 1420 NE2 GLN A 210 18.078 -24.729 10.324 1.00 19.48 N ANISOU 1420 NE2 GLN A 210 2278 2400 2724 566 -50 153 N ATOM 1421 N GLY A 211 21.583 -29.357 13.448 1.00 16.10 N ANISOU 1421 N GLY A 211 1859 2086 2172 371 72 44 N ATOM 1422 CA GLY A 211 22.373 -29.691 14.625 1.00 15.26 C ANISOU 1422 CA GLY A 211 1781 1970 2047 346 93 23 C ATOM 1423 C GLY A 211 23.256 -30.866 14.475 1.00 16.82 C ANISOU 1423 C GLY A 211 1978 2191 2222 321 72 15 C ATOM 1424 O GLY A 211 22.992 -31.734 13.625 1.00 15.48 O ANISOU 1424 O GLY A 211 1783 2048 2051 321 51 18 O ATOM 1425 N VAL A 212 24.269 -30.883 15.330 1.00 14.47 N ANISOU 1425 N VAL A 212 1711 1879 1908 302 72 0 N ATOM 1426 CA VAL A 212 25.079 -32.069 15.572 1.00 13.39 C ANISOU 1426 CA VAL A 212 1576 1754 1759 286 50 -13 C ATOM 1427 C VAL A 212 24.826 -32.507 17.007 1.00 14.32 C ANISOU 1427 C VAL A 212 1730 1851 1860 278 59 -24 C ATOM 1428 O VAL A 212 24.912 -31.690 17.963 1.00 15.07 O ANISOU 1428 O VAL A 212 1865 1920 1943 276 73 -32 O ATOM 1429 CB VAL A 212 26.562 -31.745 15.419 1.00 13.20 C ANISOU 1429 CB VAL A 212 1554 1726 1735 272 31 -21 C ATOM 1430 CG1 VAL A 212 27.433 -32.978 15.708 1.00 15.86 C ANISOU 1430 CG1 VAL A 212 1885 2070 2069 265 0 -39 C ATOM 1431 CG2 VAL A 212 26.846 -31.216 13.993 1.00 17.37 C ANISOU 1431 CG2 VAL A 212 2059 2271 2268 273 39 -6 C ATOM 1432 N VAL A 213 24.511 -33.784 17.198 1.00 14.65 N ANISOU 1432 N VAL A 213 1771 1900 1896 271 52 -26 N ATOM 1433 CA VAL A 213 24.313 -34.299 18.549 1.00 15.26 C ANISOU 1433 CA VAL A 213 1899 1954 1946 258 63 -30 C ATOM 1434 C VAL A 213 25.617 -34.050 19.364 1.00 13.87 C ANISOU 1434 C VAL A 213 1771 1756 1745 253 25 -43 C ATOM 1435 O VAL A 213 26.716 -34.481 18.965 1.00 14.82 O ANISOU 1435 O VAL A 213 1874 1882 1876 253 -21 -50 O ATOM 1436 CB VAL A 213 23.967 -35.812 18.565 1.00 15.48 C ANISOU 1436 CB VAL A 213 1926 1983 1971 245 53 -25 C ATOM 1437 CG1 VAL A 213 23.820 -36.303 19.978 1.00 15.14 C ANISOU 1437 CG1 VAL A 213 1953 1910 1889 228 68 -21 C ATOM 1438 CG2 VAL A 213 22.748 -36.127 17.734 1.00 15.07 C ANISOU 1438 CG2 VAL A 213 1821 1952 1953 244 75 -17 C ATOM 1439 N SER A 214 25.492 -33.397 20.522 1.00 15.85 N ANISOU 1439 N SER A 214 2079 1978 1963 248 43 -50 N ATOM 1440 CA SER A 214 26.646 -32.971 21.291 1.00 16.00 C ANISOU 1440 CA SER A 214 2146 1973 1961 242 -4 -66 C ATOM 1441 C SER A 214 26.646 -33.527 22.705 1.00 16.54 C ANISOU 1441 C SER A 214 2303 2011 1969 232 -16 -69 C ATOM 1442 O SER A 214 27.385 -34.461 23.008 1.00 18.93 O ANISOU 1442 O SER A 214 2629 2304 2259 229 -74 -68 O ATOM 1443 CB SER A 214 26.785 -31.454 21.237 1.00 16.56 C ANISOU 1443 CB SER A 214 2217 2030 2044 244 11 -77 C ATOM 1444 OG SER A 214 27.944 -30.931 21.851 1.00 17.73 O ANISOU 1444 OG SER A 214 2399 2153 2185 231 -43 -96 O ATOM 1445 N TRP A 215 25.872 -32.919 23.607 1.00 16.56 N ANISOU 1445 N TRP A 215 2367 1993 1931 230 37 -75 N ATOM 1446 CA TRP A 215 25.937 -33.285 25.033 1.00 16.64 C ANISOU 1446 CA TRP A 215 2488 1970 1864 218 29 -79 C ATOM 1447 C TRP A 215 24.603 -33.084 25.756 1.00 17.12 C ANISOU 1447 C TRP A 215 2598 2023 1886 215 130 -78 C ATOM 1448 O TRP A 215 23.618 -32.590 25.199 1.00 18.09 O ANISOU 1448 O TRP A 215 2658 2165 2052 227 200 -78 O ATOM 1449 CB TRP A 215 27.044 -32.478 25.715 1.00 17.66 C ANISOU 1449 CB TRP A 215 2673 2069 1966 215 -38 -105 C ATOM 1450 CG TRP A 215 26.843 -30.987 25.779 1.00 19.24 C ANISOU 1450 CG TRP A 215 2880 2255 2174 221 -4 -129 C ATOM 1451 CD1 TRP A 215 27.104 -30.082 24.794 1.00 17.74 C ANISOU 1451 CD1 TRP A 215 2613 2076 2050 226 -6 -133 C ATOM 1452 CD2 TRP A 215 26.381 -30.226 26.908 1.00 17.40 C ANISOU 1452 CD2 TRP A 215 2748 1988 1877 221 37 -152 C ATOM 1453 NE1 TRP A 215 26.821 -28.795 25.229 1.00 18.58 N ANISOU 1453 NE1 TRP A 215 2764 2152 2145 231 25 -156 N ATOM 1454 CE2 TRP A 215 26.373 -28.859 26.520 1.00 17.70 C ANISOU 1454 CE2 TRP A 215 2758 2012 1954 231 53 -173 C ATOM 1455 CE3 TRP A 215 25.932 -30.559 28.186 1.00 20.86 C ANISOU 1455 CE3 TRP A 215 3303 2401 2222 215 69 -158 C ATOM 1456 CZ2 TRP A 215 25.963 -27.831 27.387 1.00 19.56 C ANISOU 1456 CZ2 TRP A 215 3077 2209 2145 239 95 -205 C ATOM 1457 CZ3 TRP A 215 25.503 -29.511 29.045 1.00 22.89 C ANISOU 1457 CZ3 TRP A 215 3645 2624 2427 222 121 -191 C ATOM 1458 CH2 TRP A 215 25.541 -28.174 28.633 1.00 21.10 C ANISOU 1458 CH2 TRP A 215 3385 2383 2248 236 130 -217 C ATOM 1459 N GLY A 216 24.558 -33.522 26.999 1.00 19.47 N ANISOU 1459 N GLY A 216 3006 2290 2101 200 138 -76 N ATOM 1460 CA GLY A 216 23.412 -33.261 27.859 1.00 21.86 C ANISOU 1460 CA GLY A 216 3371 2582 2355 194 245 -81 C ATOM 1461 C GLY A 216 23.703 -33.819 29.253 1.00 23.00 C ANISOU 1461 C GLY A 216 3666 2686 2386 174 232 -76 C ATOM 1462 O GLY A 216 24.686 -34.514 29.456 1.00 23.57 O ANISOU 1462 O GLY A 216 3781 2742 2431 167 132 -64 O ATOM 1463 N ASP A 217 22.883 -33.470 30.241 1.00 20.13 N ANISOU 1463 N ASP A 217 3390 2305 1954 167 330 -87 N ATOM 1464 CA ASP A 217 23.001 -34.089 31.550 1.00 20.25 C ANISOU 1464 CA ASP A 217 3565 2283 1847 143 332 -75 C ATOM 1465 C ASP A 217 22.147 -35.350 31.595 1.00 22.51 C ANISOU 1465 C ASP A 217 3850 2575 2129 112 405 -33 C ATOM 1466 O ASP A 217 20.923 -35.302 31.740 1.00 25.29 O ANISOU 1466 O ASP A 217 4179 2939 2490 99 540 -31 O ATOM 1467 CB ASP A 217 22.577 -33.080 32.624 1.00 23.56 C ANISOU 1467 CB ASP A 217 4096 2677 2181 149 411 -113 C ATOM 1468 CG ASP A 217 23.646 -31.992 32.893 1.00 29.08 C ANISOU 1468 CG ASP A 217 4844 3349 2855 168 311 -155 C ATOM 1469 OD1 ASP A 217 24.801 -32.129 32.450 1.00 28.98 O ANISOU 1469 OD1 ASP A 217 4797 3336 2878 170 177 -151 O ATOM 1470 OD2 ASP A 217 23.341 -30.955 33.542 1.00 31.56 O ANISOU 1470 OD2 ASP A 217 5230 3641 3120 180 368 -196 O ATOM 1471 N GLY A 219 22.802 -36.483 31.389 1.00 26.04 N ANISOU 1471 N GLY A 219 4306 3011 2578 99 314 0 N ATOM 1472 CA GLY A 219 22.104 -37.735 31.208 1.00 26.53 C ANISOU 1472 CA GLY A 219 4350 3072 2657 67 363 42 C ATOM 1473 C GLY A 219 21.382 -37.740 29.870 1.00 23.71 C ANISOU 1473 C GLY A 219 3816 2762 2430 72 405 40 C ATOM 1474 O GLY A 219 21.694 -36.943 28.963 1.00 24.90 O ANISOU 1474 O GLY A 219 3865 2943 2654 105 365 14 O ATOM 1475 N CYS A 220 20.401 -38.625 29.770 1.00 24.76 N ANISOU 1475 N CYS A 220 3921 2896 2589 35 484 68 N ATOM 1476 CA CYS A 220 19.547 -38.719 28.604 1.00 24.57 C ANISOU 1476 CA CYS A 220 3740 2913 2683 34 524 66 C ATOM 1477 C CYS A 220 18.087 -38.859 29.016 1.00 24.15 C ANISOU 1477 C CYS A 220 3665 2865 2645 -4 674 74 C ATOM 1478 O CYS A 220 17.752 -39.671 29.865 1.00 25.56 O ANISOU 1478 O CYS A 220 3938 3012 2762 -50 732 104 O ATOM 1479 CB CYS A 220 19.900 -39.914 27.707 1.00 27.80 C ANISOU 1479 CB CYS A 220 4097 3320 3146 22 441 89 C ATOM 1480 SG CYS A 220 21.661 -40.322 27.463 1.00 34.25 S ANISOU 1480 SG CYS A 220 4960 4115 3940 54 274 88 S ATOM 1481 N ALA A 221A 17.232 -38.046 28.401 1.00 22.83 N ANISOU 1481 N ALA A 221A 3373 2737 2566 18 736 48 N ATOM 1482 CA ALA A 221A 15.798 -38.146 28.545 1.00 22.77 C ANISOU 1482 CA ALA A 221A 3297 2743 2612 -12 873 49 C ATOM 1483 C ALA A 221A 15.368 -37.820 29.952 1.00 25.67 C ANISOU 1483 C ALA A 221A 3780 3088 2887 -28 999 43 C ATOM 1484 O ALA A 221A 14.288 -38.211 30.393 1.00 26.83 O ANISOU 1484 O ALA A 221A 3908 3235 3050 -71 1130 54 O ATOM 1485 CB ALA A 221A 15.296 -39.519 28.112 1.00 24.36 C ANISOU 1485 CB ALA A 221A 3450 2940 2867 -67 874 83 C ATOM 1486 N GLN A 221 16.178 -37.018 30.635 1.00 24.88 N ANISOU 1486 N GLN A 221 3793 2969 2690 4 967 22 N ATOM 1487 CA GLN A 221 15.869 -36.634 31.997 1.00 25.86 C ANISOU 1487 CA GLN A 221 4053 3068 2706 -6 1081 10 C ATOM 1488 C GLN A 221 14.997 -35.382 32.009 1.00 25.57 C ANISOU 1488 C GLN A 221 3938 3054 2723 35 1191 -39 C ATOM 1489 O GLN A 221 15.066 -34.538 31.100 1.00 26.37 O ANISOU 1489 O GLN A 221 3927 3179 2915 85 1137 -66 O ATOM 1490 CB GLN A 221 17.146 -36.411 32.812 1.00 26.51 C ANISOU 1490 CB GLN A 221 4310 3111 2652 7 984 6 C ATOM 1491 CG GLN A 221 17.975 -37.650 32.985 1.00 27.02 C ANISOU 1491 CG GLN A 221 4466 3144 2657 -27 880 53 C ATOM 1492 CD GLN A 221 17.193 -38.825 33.544 1.00 30.35 C ANISOU 1492 CD GLN A 221 4945 3543 3043 -92 980 100 C ATOM 1493 OE1 GLN A 221 16.717 -38.794 34.669 1.00 32.08 O ANISOU 1493 OE1 GLN A 221 5290 3740 3161 -120 1096 104 O ATOM 1494 NE2 GLN A 221 17.085 -39.899 32.750 1.00 32.76 N ANISOU 1494 NE2 GLN A 221 5167 3851 3428 -121 937 134 N ATOM 1495 N LYS A 222 14.219 -35.212 33.066 1.00 30.12 N ANISOU 1495 N LYS A 222 4586 3617 3239 17 1347 -52 N ATOM 1496 CA LYS A 222 13.374 -34.044 33.170 1.00 33.15 C ANISOU 1496 CA LYS A 222 4904 4018 3676 63 1462 -104 C ATOM 1497 C LYS A 222 14.193 -32.761 33.238 1.00 27.26 C ANISOU 1497 C LYS A 222 4216 3255 2889 126 1383 -149 C ATOM 1498 O LYS A 222 15.182 -32.687 33.971 1.00 28.92 O ANISOU 1498 O LYS A 222 4590 3430 2969 121 1316 -151 O ATOM 1499 CB LYS A 222 12.466 -34.144 34.406 1.00 55.96 C ANISOU 1499 CB LYS A 222 7880 6893 6491 31 1658 -114 C ATOM 1500 CG LYS A 222 11.205 -34.983 34.182 1.00 82.17 C ANISOU 1500 CG LYS A 222 11069 10237 9912 -21 1786 -89 C ATOM 1501 CD LYS A 222 10.072 -34.576 35.131 1.00104.80 C ANISOU 1501 CD LYS A 222 13950 13105 12764 -27 2010 -123 C ATOM 1502 CE LYS A 222 8.823 -35.421 34.913 1.00120.14 C ANISOU 1502 CE LYS A 222 15749 15074 14826 -87 2140 -99 C ATOM 1503 NZ LYS A 222 9.144 -36.874 34.836 1.00127.09 N ANISOU 1503 NZ LYS A 222 16680 15936 15672 -171 2081 -29 N ATOM 1504 N AASN A 223 13.773 -31.774 32.453 0.50 26.92 N ANISOU 1504 N AASN A 223 4036 3230 2961 183 1384 -184 N ATOM 1505 N BASN A 223 13.765 -31.761 32.463 0.50 26.91 N ANISOU 1505 N BASN A 223 4036 3229 2960 183 1386 -184 N ATOM 1506 CA AASN A 223 14.372 -30.459 32.412 0.50 25.41 C ANISOU 1506 CA AASN A 223 3880 3018 2757 242 1325 -227 C ATOM 1507 CA BASN A 223 14.380 -30.438 32.360 0.50 24.82 C ANISOU 1507 CA BASN A 223 3800 2944 2687 244 1321 -228 C ATOM 1508 C AASN A 223 15.825 -30.503 31.945 0.50 23.63 C ANISOU 1508 C AASN A 223 3700 2782 2498 239 1141 -209 C ATOM 1509 C BASN A 223 15.792 -30.430 31.785 0.50 23.74 C ANISOU 1509 C BASN A 223 3693 2798 2529 245 1135 -210 C ATOM 1510 O AASN A 223 16.610 -29.589 32.217 0.50 25.04 O ANISOU 1510 O AASN A 223 3959 2929 2626 267 1078 -241 O ATOM 1511 O BASN A 223 16.520 -29.428 31.842 0.50 23.20 O ANISOU 1511 O BASN A 223 3677 2704 2434 278 1069 -241 O ATOM 1512 CB AASN A 223 14.208 -29.736 33.765 0.50 29.84 C ANISOU 1512 CB AASN A 223 4594 3542 3202 257 1436 -276 C ATOM 1513 CB BASN A 223 14.315 -29.669 33.686 0.50 28.70 C ANISOU 1513 CB BASN A 223 4447 3396 3060 260 1419 -276 C ATOM 1514 CG AASN A 223 12.795 -29.148 33.956 0.50 33.75 C ANISOU 1514 CG AASN A 223 5001 4048 3774 292 1615 -317 C ATOM 1515 CG BASN A 223 14.576 -28.174 33.511 0.50 32.34 C ANISOU 1515 CG BASN A 223 4906 3832 3549 327 1385 -331 C ATOM 1516 OD1AASN A 223 12.408 -28.187 33.280 0.50 31.79 O ANISOU 1516 OD1AASN A 223 4637 3804 3638 354 1611 -349 O ATOM 1517 OD1BASN A 223 14.238 -27.571 32.479 0.50 34.49 O ANISOU 1517 OD1BASN A 223 5032 4120 3953 372 1356 -338 O ATOM 1518 ND2AASN A 223 12.025 -29.742 34.847 0.50 40.25 N ANISOU 1518 ND2AASN A 223 5874 4874 4544 253 1773 -314 N ATOM 1519 ND2BASN A 223 15.195 -27.565 34.527 0.50 33.63 N ANISOU 1519 ND2BASN A 223 5245 3950 3584 334 1379 -369 N ATOM 1520 N LYS A 224 16.159 -31.549 31.177 1.00 21.87 N ANISOU 1520 N LYS A 224 3414 2582 2316 207 1055 -162 N ATOM 1521 CA LYS A 224 17.481 -31.725 30.613 1.00 20.91 C ANISOU 1521 CA LYS A 224 3307 2456 2183 205 892 -144 C ATOM 1522 C LYS A 224 17.427 -32.258 29.172 1.00 21.17 C ANISOU 1522 C LYS A 224 3186 2526 2332 205 823 -115 C ATOM 1523 O LYS A 224 17.920 -33.342 28.867 1.00 20.74 O ANISOU 1523 O LYS A 224 3133 2477 2271 173 754 -80 O ATOM 1524 CB LYS A 224 18.273 -32.655 31.513 1.00 23.34 C ANISOU 1524 CB LYS A 224 3764 2736 2368 163 844 -119 C ATOM 1525 CG LYS A 224 18.573 -32.018 32.886 1.00 23.44 C ANISOU 1525 CG LYS A 224 3953 2707 2247 166 877 -152 C ATOM 1526 CD LYS A 224 19.507 -30.825 32.774 1.00 23.34 C ANISOU 1526 CD LYS A 224 3964 2673 2230 203 780 -192 C ATOM 1527 CE LYS A 224 20.022 -30.372 34.157 1.00 22.02 C ANISOU 1527 CE LYS A 224 3993 2457 1915 198 774 -225 C ATOM 1528 NZ LYS A 224 21.115 -29.414 33.999 1.00 23.09 N ANISOU 1528 NZ LYS A 224 4149 2569 2056 220 650 -257 N ATOM 1529 N PRO A 225 16.860 -31.469 28.259 1.00 20.03 N ANISOU 1529 N PRO A 225 2917 2402 2292 245 834 -130 N ATOM 1530 CA PRO A 225 16.874 -31.860 26.854 1.00 19.39 C ANISOU 1530 CA PRO A 225 2707 2353 2306 248 758 -106 C ATOM 1531 C PRO A 225 18.307 -31.877 26.348 1.00 19.24 C ANISOU 1531 C PRO A 225 2721 2330 2261 248 624 -96 C ATOM 1532 O PRO A 225 19.185 -31.242 26.907 1.00 20.63 O ANISOU 1532 O PRO A 225 2986 2478 2375 256 585 -114 O ATOM 1533 CB PRO A 225 16.086 -30.722 26.200 1.00 21.05 C ANISOU 1533 CB PRO A 225 2815 2573 2609 301 791 -129 C ATOM 1534 CG PRO A 225 16.391 -29.510 27.092 1.00 20.60 C ANISOU 1534 CG PRO A 225 2857 2477 2493 332 824 -168 C ATOM 1535 CD PRO A 225 16.289 -30.113 28.466 1.00 19.60 C ANISOU 1535 CD PRO A 225 2848 2334 2265 295 904 -173 C ATOM 1536 N GLY A 226 18.567 -32.594 25.288 1.00 19.44 N ANISOU 1536 N GLY A 226 2672 2380 2336 238 553 -72 N ATOM 1537 CA GLY A 226 19.893 -32.596 24.697 1.00 18.28 C ANISOU 1537 CA GLY A 226 2536 2232 2178 241 440 -66 C ATOM 1538 C GLY A 226 20.280 -31.239 24.136 1.00 19.11 C ANISOU 1538 C GLY A 226 2614 2332 2314 276 410 -84 C ATOM 1539 O GLY A 226 19.438 -30.413 23.740 1.00 18.30 O ANISOU 1539 O GLY A 226 2453 2233 2266 307 454 -93 O ATOM 1540 N VAL A 227 21.596 -31.016 24.127 1.00 16.19 N ANISOU 1540 N VAL A 227 2287 1948 1914 271 329 -88 N ATOM 1541 CA VAL A 227 22.217 -29.838 23.583 1.00 16.27 C ANISOU 1541 CA VAL A 227 2282 1948 1952 290 290 -99 C ATOM 1542 C VAL A 227 22.932 -30.228 22.290 1.00 16.21 C ANISOU 1542 C VAL A 227 2205 1968 1987 285 221 -79 C ATOM 1543 O VAL A 227 23.573 -31.303 22.213 1.00 18.46 O ANISOU 1543 O VAL A 227 2491 2265 2257 265 176 -69 O ATOM 1544 CB VAL A 227 23.217 -29.222 24.595 1.00 17.30 C ANISOU 1544 CB VAL A 227 2513 2038 2022 280 253 -125 C ATOM 1545 CG1 VAL A 227 23.770 -27.903 24.054 1.00 17.45 C ANISOU 1545 CG1 VAL A 227 2516 2037 2078 292 222 -137 C ATOM 1546 CG2 VAL A 227 22.595 -29.061 25.921 1.00 18.29 C ANISOU 1546 CG2 VAL A 227 2729 2137 2083 281 321 -146 C ATOM 1547 N TYR A 228 22.796 -29.374 21.280 1.00 15.57 N ANISOU 1547 N TYR A 228 2068 1892 1955 305 217 -73 N ATOM 1548 CA TYR A 228 23.203 -29.638 19.912 1.00 15.72 C ANISOU 1548 CA TYR A 228 2023 1939 2010 304 173 -53 C ATOM 1549 C TYR A 228 24.076 -28.495 19.388 1.00 14.92 C ANISOU 1549 C TYR A 228 1925 1819 1923 304 144 -53 C ATOM 1550 O TYR A 228 23.825 -27.332 19.693 1.00 16.57 O ANISOU 1550 O TYR A 228 2162 1995 2139 319 165 -62 O ATOM 1551 CB TYR A 228 21.975 -29.860 19.013 1.00 15.59 C ANISOU 1551 CB TYR A 228 1937 1949 2037 324 197 -36 C ATOM 1552 CG TYR A 228 21.164 -31.050 19.479 1.00 15.64 C ANISOU 1552 CG TYR A 228 1931 1971 2040 311 227 -35 C ATOM 1553 CD1 TYR A 228 20.199 -30.926 20.461 1.00 16.66 C ANISOU 1553 CD1 TYR A 228 2076 2088 2167 316 296 -47 C ATOM 1554 CD2 TYR A 228 21.461 -32.306 19.016 1.00 16.16 C ANISOU 1554 CD2 TYR A 228 1978 2059 2103 291 192 -26 C ATOM 1555 CE1 TYR A 228 19.483 -32.031 20.944 1.00 17.07 C ANISOU 1555 CE1 TYR A 228 2121 2149 2216 293 335 -42 C ATOM 1556 CE2 TYR A 228 20.762 -33.397 19.482 1.00 15.90 C ANISOU 1556 CE2 TYR A 228 1943 2030 2068 271 219 -22 C ATOM 1557 CZ TYR A 228 19.799 -33.269 20.421 1.00 16.76 C ANISOU 1557 CZ TYR A 228 2065 2128 2177 268 290 -27 C ATOM 1558 OH TYR A 228 19.164 -34.425 20.872 1.00 19.02 O ANISOU 1558 OH TYR A 228 2351 2415 2462 237 322 -19 O ATOM 1559 N THR A 229 25.094 -28.789 18.603 1.00 13.95 N ANISOU 1559 N THR A 229 1777 1714 1809 287 101 -44 N ATOM 1560 CA THR A 229 25.912 -27.762 17.976 1.00 14.29 C ANISOU 1560 CA THR A 229 1817 1741 1871 277 85 -38 C ATOM 1561 C THR A 229 25.097 -27.098 16.874 1.00 17.14 C ANISOU 1561 C THR A 229 2151 2105 2257 302 104 -13 C ATOM 1562 O THR A 229 24.463 -27.774 16.071 1.00 15.84 O ANISOU 1562 O THR A 229 1947 1972 2098 315 104 3 O ATOM 1563 CB THR A 229 27.143 -28.373 17.374 1.00 17.51 C ANISOU 1563 CB THR A 229 2193 2172 2286 253 50 -36 C ATOM 1564 OG1 THR A 229 27.791 -29.136 18.401 1.00 18.36 O ANISOU 1564 OG1 THR A 229 2323 2276 2376 240 18 -58 O ATOM 1565 CG2 THR A 229 28.082 -27.317 16.864 1.00 17.77 C ANISOU 1565 CG2 THR A 229 2222 2187 2344 231 44 -31 C ATOM 1566 N LYS A 230 25.101 -25.746 16.841 1.00 15.64 N ANISOU 1566 N LYS A 230 1989 1873 2082 308 113 -9 N ATOM 1567 CA LYS A 230 24.296 -24.970 15.922 1.00 16.85 C ANISOU 1567 CA LYS A 230 2131 2014 2258 338 122 18 C ATOM 1568 C LYS A 230 25.025 -24.827 14.590 1.00 16.77 C ANISOU 1568 C LYS A 230 2110 2016 2247 318 104 49 C ATOM 1569 O LYS A 230 25.882 -23.932 14.411 1.00 16.92 O ANISOU 1569 O LYS A 230 2156 2002 2272 291 103 57 O ATOM 1570 CB LYS A 230 24.014 -23.607 16.584 1.00 18.65 C ANISOU 1570 CB LYS A 230 2407 2180 2501 356 139 6 C ATOM 1571 CG LYS A 230 23.000 -22.777 15.848 1.00 17.64 C ANISOU 1571 CG LYS A 230 2272 2028 2405 402 144 30 C ATOM 1572 CD LYS A 230 22.758 -21.396 16.477 1.00 18.50 C ANISOU 1572 CD LYS A 230 2432 2064 2533 425 160 14 C ATOM 1573 CE LYS A 230 22.169 -21.419 17.823 1.00 20.03 C ANISOU 1573 CE LYS A 230 2644 2243 2722 447 200 -30 C ATOM 1574 NZ LYS A 230 22.003 -20.042 18.495 1.00 22.73 N ANISOU 1574 NZ LYS A 230 3049 2507 3080 473 219 -56 N ATOM 1575 N VAL A 231 24.742 -25.742 13.663 1.00 15.30 N ANISOU 1575 N VAL A 231 1888 1876 2050 325 93 64 N ATOM 1576 CA VAL A 231 25.478 -25.836 12.419 1.00 17.10 C ANISOU 1576 CA VAL A 231 2112 2123 2261 304 87 88 C ATOM 1577 C VAL A 231 25.439 -24.526 11.628 1.00 16.25 C ANISOU 1577 C VAL A 231 2043 1976 2154 307 90 124 C ATOM 1578 O VAL A 231 26.401 -24.210 10.963 1.00 16.17 O ANISOU 1578 O VAL A 231 2048 1963 2133 273 102 142 O ATOM 1579 CB VAL A 231 24.950 -27.057 11.568 1.00 15.71 C ANISOU 1579 CB VAL A 231 1906 1999 2066 318 70 92 C ATOM 1580 CG1 VAL A 231 25.563 -27.112 10.185 1.00 17.00 C ANISOU 1580 CG1 VAL A 231 2080 2180 2197 303 71 115 C ATOM 1581 CG2 VAL A 231 25.205 -28.366 12.304 1.00 18.00 C ANISOU 1581 CG2 VAL A 231 2168 2317 2355 307 67 60 C ATOM 1582 N TYR A 232 24.327 -23.810 11.660 1.00 16.68 N ANISOU 1582 N TYR A 232 2111 1998 2226 350 80 137 N ATOM 1583 CA TYR A 232 24.194 -22.552 10.907 1.00 17.96 C ANISOU 1583 CA TYR A 232 2321 2111 2390 361 73 177 C ATOM 1584 C TYR A 232 25.376 -21.605 11.174 1.00 17.83 C ANISOU 1584 C TYR A 232 2345 2049 2380 313 95 180 C ATOM 1585 O TYR A 232 25.840 -20.915 10.265 1.00 19.16 O ANISOU 1585 O TYR A 232 2554 2191 2535 291 101 220 O ATOM 1586 CB TYR A 232 22.874 -21.848 11.220 1.00 18.78 C ANISOU 1586 CB TYR A 232 2428 2177 2531 421 58 178 C ATOM 1587 CG TYR A 232 22.685 -20.589 10.408 1.00 18.99 C ANISOU 1587 CG TYR A 232 2511 2145 2561 441 38 223 C ATOM 1588 CD1 TYR A 232 22.366 -20.648 9.065 1.00 18.51 C ANISOU 1588 CD1 TYR A 232 2468 2095 2470 456 2 268 C ATOM 1589 CD2 TYR A 232 22.852 -19.355 10.991 1.00 21.94 C ANISOU 1589 CD2 TYR A 232 2931 2444 2962 444 51 221 C ATOM 1590 CE1 TYR A 232 22.209 -19.455 8.296 1.00 20.72 C ANISOU 1590 CE1 TYR A 232 2817 2311 2745 474 -22 318 C ATOM 1591 CE2 TYR A 232 22.691 -18.185 10.250 1.00 22.67 C ANISOU 1591 CE2 TYR A 232 3085 2469 3058 462 30 267 C ATOM 1592 CZ TYR A 232 22.389 -18.256 8.925 1.00 24.03 C ANISOU 1592 CZ TYR A 232 3279 2654 3199 476 -6 318 C ATOM 1593 OH TYR A 232 22.217 -17.101 8.191 1.00 29.51 O ANISOU 1593 OH TYR A 232 4048 3275 3890 496 -33 370 O ATOM 1594 N ASN A 233 25.888 -21.618 12.401 1.00 17.12 N ANISOU 1594 N ASN A 233 2249 1947 2309 292 106 140 N ATOM 1595 CA ASN A 233 26.985 -20.692 12.767 1.00 18.12 C ANISOU 1595 CA ASN A 233 2408 2024 2453 242 116 136 C ATOM 1596 C ASN A 233 28.342 -21.099 12.175 1.00 20.07 C ANISOU 1596 C ASN A 233 2629 2302 2695 181 130 143 C ATOM 1597 O ASN A 233 29.311 -20.306 12.220 1.00 23.62 O ANISOU 1597 O ASN A 233 3095 2711 3167 129 142 148 O ATOM 1598 CB ASN A 233 27.115 -20.615 14.271 1.00 19.93 C ANISOU 1598 CB ASN A 233 2645 2230 2697 239 110 86 C ATOM 1599 CG ASN A 233 26.006 -19.840 14.914 1.00 20.31 C ANISOU 1599 CG ASN A 233 2731 2228 2758 290 114 73 C ATOM 1600 OD1 ASN A 233 25.124 -19.329 14.237 1.00 23.17 O ANISOU 1600 OD1 ASN A 233 3105 2569 3131 333 113 103 O ATOM 1601 ND2 ASN A 233 26.080 -19.700 16.237 1.00 22.41 N ANISOU 1601 ND2 ASN A 233 3022 2468 3024 289 115 26 N ATOM 1602 N TYR A 234 28.383 -22.287 11.556 1.00 17.78 N ANISOU 1602 N TYR A 234 2297 2079 2379 187 134 145 N ATOM 1603 CA TYR A 234 29.582 -22.873 11.019 1.00 18.04 C ANISOU 1603 CA TYR A 234 2294 2151 2411 142 156 142 C ATOM 1604 C TYR A 234 29.559 -23.012 9.503 1.00 18.34 C ANISOU 1604 C TYR A 234 2347 2214 2407 140 182 182 C ATOM 1605 O TYR A 234 30.485 -23.578 8.940 1.00 19.73 O ANISOU 1605 O TYR A 234 2492 2426 2577 109 214 177 O ATOM 1606 CB TYR A 234 29.910 -24.221 11.658 1.00 18.01 C ANISOU 1606 CB TYR A 234 2234 2197 2411 147 140 99 C ATOM 1607 CG TYR A 234 30.097 -24.071 13.136 1.00 16.73 C ANISOU 1607 CG TYR A 234 2074 2007 2275 142 111 62 C ATOM 1608 CD1 TYR A 234 31.322 -23.653 13.665 1.00 18.36 C ANISOU 1608 CD1 TYR A 234 2265 2191 2519 93 103 41 C ATOM 1609 CD2 TYR A 234 29.036 -24.254 14.019 1.00 17.49 C ANISOU 1609 CD2 TYR A 234 2192 2095 2358 183 94 46 C ATOM 1610 CE1 TYR A 234 31.480 -23.427 15.018 1.00 18.56 C ANISOU 1610 CE1 TYR A 234 2309 2184 2559 88 66 6 C ATOM 1611 CE2 TYR A 234 29.165 -24.024 15.379 1.00 17.03 C ANISOU 1611 CE2 TYR A 234 2157 2006 2307 178 73 12 C ATOM 1612 CZ TYR A 234 30.395 -23.582 15.869 1.00 18.09 C ANISOU 1612 CZ TYR A 234 2289 2114 2469 131 53 -8 C ATOM 1613 OH TYR A 234 30.540 -23.371 17.224 1.00 19.61 O ANISOU 1613 OH TYR A 234 2518 2274 2659 126 21 -44 O ATOM 1614 N VAL A 235 28.545 -22.468 8.839 1.00 18.28 N ANISOU 1614 N VAL A 235 2391 2184 2372 174 169 221 N ATOM 1615 CA VAL A 235 28.422 -22.612 7.393 1.00 18.36 C ANISOU 1615 CA VAL A 235 2436 2215 2326 176 182 260 C ATOM 1616 C VAL A 235 29.643 -22.030 6.699 1.00 20.54 C ANISOU 1616 C VAL A 235 2735 2476 2593 113 241 287 C ATOM 1617 O VAL A 235 30.217 -22.682 5.827 1.00 21.69 O ANISOU 1617 O VAL A 235 2873 2666 2701 93 280 289 O ATOM 1618 CB VAL A 235 27.063 -22.054 6.878 1.00 23.52 C ANISOU 1618 CB VAL A 235 3142 2838 2956 231 138 298 C ATOM 1619 CG1 VAL A 235 27.041 -21.951 5.379 1.00 24.77 C ANISOU 1619 CG1 VAL A 235 3363 3003 3046 227 143 347 C ATOM 1620 CG2 VAL A 235 25.964 -22.963 7.328 1.00 24.41 C ANISOU 1620 CG2 VAL A 235 3208 2986 3079 284 94 267 C ATOM 1621 N LYS A 236 30.056 -20.811 7.062 1.00 22.56 N ANISOU 1621 N LYS A 236 3020 2667 2885 77 254 305 N ATOM 1622 CA LYS A 236 31.222 -20.211 6.401 1.00 24.85 C ANISOU 1622 CA LYS A 236 3329 2939 3176 5 319 333 C ATOM 1623 C LYS A 236 32.503 -21.041 6.679 1.00 21.52 C ANISOU 1623 C LYS A 236 2815 2569 2792 -40 360 287 C ATOM 1624 O LYS A 236 33.309 -21.319 5.768 1.00 23.66 O ANISOU 1624 O LYS A 236 3076 2872 3043 -79 427 299 O ATOM 1625 CB LYS A 236 31.412 -18.742 6.819 1.00 26.84 C ANISOU 1625 CB LYS A 236 3628 3100 3469 -31 319 358 C ATOM 1626 CG LYS A 236 32.528 -18.012 6.073 1.00 33.91 C ANISOU 1626 CG LYS A 236 4550 3965 4368 -116 392 397 C ATOM 1627 CD LYS A 236 32.699 -16.585 6.626 1.00 41.11 C ANISOU 1627 CD LYS A 236 5510 4778 5333 -155 382 415 C ATOM 1628 CE LYS A 236 33.721 -16.566 7.747 1.00 45.73 C ANISOU 1628 CE LYS A 236 6013 5358 6004 -208 381 359 C ATOM 1629 NZ LYS A 236 33.848 -15.222 8.374 0.00 46.31 N ANISOU 1629 NZ LYS A 236 6137 5329 6129 -246 361 365 N ATOM 1630 N TRP A 237 32.657 -21.487 7.919 1.00 21.66 N ANISOU 1630 N TRP A 237 2770 2597 2863 -30 321 234 N ATOM 1631 CA TRP A 237 33.814 -22.300 8.286 1.00 20.36 C ANISOU 1631 CA TRP A 237 2515 2476 2745 -60 339 188 C ATOM 1632 C TRP A 237 33.853 -23.608 7.470 1.00 19.29 C ANISOU 1632 C TRP A 237 2349 2412 2566 -32 365 175 C ATOM 1633 O TRP A 237 34.925 -24.020 7.018 1.00 22.17 O ANISOU 1633 O TRP A 237 2660 2810 2953 -66 420 160 O ATOM 1634 CB TRP A 237 33.830 -22.612 9.798 1.00 20.35 C ANISOU 1634 CB TRP A 237 2472 2468 2791 -43 274 137 C ATOM 1635 CG TRP A 237 34.987 -23.520 10.181 1.00 20.94 C ANISOU 1635 CG TRP A 237 2454 2585 2918 -63 273 90 C ATOM 1636 CD1 TRP A 237 36.306 -23.173 10.273 1.00 23.41 C ANISOU 1636 CD1 TRP A 237 2705 2889 3301 -125 297 75 C ATOM 1637 CD2 TRP A 237 34.918 -24.910 10.514 1.00 20.52 C ANISOU 1637 CD2 TRP A 237 2356 2583 2858 -19 243 53 C ATOM 1638 NE1 TRP A 237 37.056 -24.259 10.604 1.00 25.04 N ANISOU 1638 NE1 TRP A 237 2827 3142 3548 -115 281 29 N ATOM 1639 CE2 TRP A 237 36.232 -25.345 10.757 1.00 21.06 C ANISOU 1639 CE2 TRP A 237 2337 2670 2993 -49 247 17 C ATOM 1640 CE3 TRP A 237 33.876 -25.834 10.605 1.00 19.67 C ANISOU 1640 CE3 TRP A 237 2271 2502 2701 40 212 47 C ATOM 1641 CZ2 TRP A 237 36.529 -26.655 11.100 1.00 22.61 C ANISOU 1641 CZ2 TRP A 237 2479 2908 3204 -14 215 -23 C ATOM 1642 CZ3 TRP A 237 34.170 -27.127 10.942 1.00 20.86 C ANISOU 1642 CZ3 TRP A 237 2372 2691 2863 66 187 10 C ATOM 1643 CH2 TRP A 237 35.492 -27.532 11.176 1.00 21.18 C ANISOU 1643 CH2 TRP A 237 2336 2746 2966 43 187 -24 C ATOM 1644 N ILE A 238 32.698 -24.263 7.310 1.00 18.54 N ANISOU 1644 N ILE A 238 2286 2340 2419 29 325 177 N ATOM 1645 CA ILE A 238 32.597 -25.507 6.538 1.00 17.68 C ANISOU 1645 CA ILE A 238 2162 2290 2264 58 339 162 C ATOM 1646 C ILE A 238 32.966 -25.241 5.082 1.00 20.75 C ANISOU 1646 C ILE A 238 2598 2690 2595 31 410 197 C ATOM 1647 O ILE A 238 33.822 -25.939 4.532 1.00 22.35 O ANISOU 1647 O ILE A 238 2763 2933 2795 16 466 174 O ATOM 1648 CB ILE A 238 31.193 -26.127 6.684 1.00 17.24 C ANISOU 1648 CB ILE A 238 2133 2246 2173 119 275 159 C ATOM 1649 CG1 ILE A 238 30.982 -26.642 8.118 1.00 16.99 C ANISOU 1649 CG1 ILE A 238 2054 2213 2190 139 225 118 C ATOM 1650 CG2 ILE A 238 30.971 -27.237 5.680 1.00 20.32 C ANISOU 1650 CG2 ILE A 238 2531 2684 2505 144 283 149 C ATOM 1651 CD1 ILE A 238 29.553 -26.998 8.467 1.00 19.36 C ANISOU 1651 CD1 ILE A 238 2373 2512 2471 188 173 119 C ATOM 1652 N LYS A 239 32.384 -24.201 4.473 1.00 23.28 N ANISOU 1652 N LYS A 239 3005 2968 2871 25 411 254 N ATOM 1653 CA LYS A 239 32.648 -23.956 3.069 1.00 25.08 C ANISOU 1653 CA LYS A 239 3301 3202 3024 1 476 295 C ATOM 1654 C LYS A 239 34.095 -23.569 2.857 1.00 23.57 C ANISOU 1654 C LYS A 239 3073 3011 2872 -72 574 295 C ATOM 1655 O LYS A 239 34.720 -24.015 1.875 1.00 28.09 O ANISOU 1655 O LYS A 239 3652 3620 3399 -92 654 293 O ATOM 1656 CB LYS A 239 31.706 -22.889 2.514 1.00 31.01 C ANISOU 1656 CB LYS A 239 4162 3900 3720 13 444 361 C ATOM 1657 CG LYS A 239 30.249 -23.309 2.531 1.00 37.29 C ANISOU 1657 CG LYS A 239 4984 4702 4483 87 351 360 C ATOM 1658 CD LYS A 239 29.382 -22.247 1.852 1.00 41.76 C ANISOU 1658 CD LYS A 239 5658 5212 4998 106 313 428 C ATOM 1659 CE LYS A 239 27.927 -22.675 1.735 1.00 46.24 C ANISOU 1659 CE LYS A 239 6240 5788 5542 179 216 426 C ATOM 1660 NZ LYS A 239 27.070 -21.505 1.335 1.00 52.23 N ANISOU 1660 NZ LYS A 239 7086 6480 6280 207 162 488 N ATOM 1661 N ASN A 240 34.660 -22.781 3.767 1.00 24.38 N ANISOU 1661 N ASN A 240 3131 3072 3060 -114 571 291 N ATOM 1662 CA ASN A 240 36.053 -22.374 3.649 1.00 27.55 C ANISOU 1662 CA ASN A 240 3478 3469 3520 -192 658 288 C ATOM 1663 C ASN A 240 36.974 -23.575 3.824 1.00 27.45 C ANISOU 1663 C ASN A 240 3351 3522 3558 -188 689 223 C ATOM 1664 O ASN A 240 37.967 -23.716 3.112 1.00 29.10 O ANISOU 1664 O ASN A 240 3523 3758 3777 -231 789 217 O ATOM 1665 CB ASN A 240 36.423 -21.299 4.673 1.00 30.81 C ANISOU 1665 CB ASN A 240 3866 3818 4022 -239 630 290 C ATOM 1666 CG ASN A 240 35.857 -19.912 4.330 1.00 35.18 C ANISOU 1666 CG ASN A 240 4535 4293 4542 -262 627 358 C ATOM 1667 OD1 ASN A 240 35.859 -19.020 5.190 1.00 39.40 O ANISOU 1667 OD1 ASN A 240 5073 4764 5135 -284 586 359 O ATOM 1668 ND2 ASN A 240 35.377 -19.725 3.105 1.00 35.01 N ANISOU 1668 ND2 ASN A 240 4613 4267 4422 -254 664 415 N ATOM 1669 N THR A 241 36.674 -24.437 4.786 1.00 24.46 N ANISOU 1669 N THR A 241 2915 3164 3213 -136 609 173 N ATOM 1670 CA THR A 241 37.513 -25.595 5.044 1.00 23.64 C ANISOU 1670 CA THR A 241 2706 3112 3164 -122 621 111 C ATOM 1671 C THR A 241 37.505 -26.568 3.861 1.00 24.39 C ANISOU 1671 C THR A 241 2821 3260 3187 -92 683 100 C ATOM 1672 O THR A 241 38.550 -27.088 3.449 1.00 26.16 O ANISOU 1672 O THR A 241 2973 3519 3446 -108 759 67 O ATOM 1673 CB THR A 241 37.058 -26.330 6.308 1.00 24.15 C ANISOU 1673 CB THR A 241 2733 3180 3264 -69 515 69 C ATOM 1674 OG1 THR A 241 37.191 -25.456 7.434 1.00 26.00 O ANISOU 1674 OG1 THR A 241 2953 3365 3560 -99 462 70 O ATOM 1675 CG2 THR A 241 37.899 -27.565 6.538 1.00 27.00 C ANISOU 1675 CG2 THR A 241 2994 3585 3678 -47 516 9 C ATOM 1676 N ILE A 242 36.328 -26.807 3.289 1.00 24.18 N ANISOU 1676 N ILE A 242 2889 3237 3060 -48 650 125 N ATOM 1677 CA ILE A 242 36.212 -27.629 2.093 1.00 24.16 C ANISOU 1677 CA ILE A 242 2931 3276 2971 -22 700 117 C ATOM 1678 C ILE A 242 37.027 -27.046 0.931 1.00 29.58 C ANISOU 1678 C ILE A 242 3653 3967 3618 -79 828 146 C ATOM 1679 O ILE A 242 37.827 -27.750 0.328 1.00 31.77 O ANISOU 1679 O ILE A 242 3892 4287 3894 -81 912 109 O ATOM 1680 CB ILE A 242 34.744 -27.820 1.702 1.00 25.19 C ANISOU 1680 CB ILE A 242 3163 3402 3008 27 625 142 C ATOM 1681 CG1 ILE A 242 34.059 -28.737 2.726 1.00 23.79 C ANISOU 1681 CG1 ILE A 242 2937 3231 2869 81 525 102 C ATOM 1682 CG2 ILE A 242 34.644 -28.405 0.313 1.00 27.31 C ANISOU 1682 CG2 ILE A 242 3506 3703 3169 42 676 142 C ATOM 1683 CD1 ILE A 242 32.560 -28.798 2.589 1.00 26.16 C ANISOU 1683 CD1 ILE A 242 3310 3521 3108 123 442 125 C ATOM 1684 N ALA A 243 36.824 -25.766 0.615 1.00 28.92 N ANISOU 1684 N ALA A 243 3647 3838 3503 -124 847 212 N ATOM 1685 CA ALA A 243 37.587 -25.106 -0.448 1.00 30.33 C ANISOU 1685 CA ALA A 243 3873 4012 3641 -189 976 251 C ATOM 1686 C ALA A 243 39.092 -25.178 -0.210 1.00 31.29 C ANISOU 1686 C ALA A 243 3862 4154 3872 -244 1075 211 C ATOM 1687 O ALA A 243 39.880 -25.338 -1.160 1.00 37.24 O ANISOU 1687 O ALA A 243 4616 4937 4597 -278 1205 207 O ATOM 1688 CB ALA A 243 37.120 -23.636 -0.593 1.00 36.53 C ANISOU 1688 CB ALA A 243 4760 4727 4394 -231 963 332 C ATOM 1689 N ALA A 244 39.520 -25.064 1.040 1.00 29.48 N ANISOU 1689 N ALA A 244 3521 3911 3771 -254 1017 179 N ATOM 1690 CA ALA A 244 40.948 -25.049 1.344 1.00 29.66 C ANISOU 1690 CA ALA A 244 3405 3948 3918 -308 1091 141 C ATOM 1691 C ALA A 244 41.592 -26.426 1.269 1.00 33.14 C ANISOU 1691 C ALA A 244 3742 4452 4398 -262 1122 65 C ATOM 1692 O ALA A 244 42.820 -26.548 1.321 1.00 35.93 O ANISOU 1692 O ALA A 244 3971 4826 4855 -297 1198 27 O ATOM 1693 CB ALA A 244 41.195 -24.455 2.675 1.00 32.11 C ANISOU 1693 CB ALA A 244 3640 4217 4344 -335 1005 130 C ATOM 1694 N ASN A 245 40.759 -27.462 1.175 1.00 30.89 N ANISOU 1694 N ASN A 245 3503 4192 4040 -181 1059 41 N ATOM 1695 CA ASN A 245 41.230 -28.828 1.273 1.00 30.08 C ANISOU 1695 CA ASN A 245 3313 4137 3980 -124 1060 -34 C ATOM 1696 C ASN A 245 40.703 -29.661 0.115 1.00 36.60 C ANISOU 1696 C ASN A 245 4233 4995 4677 -77 1105 -44 C ATOM 1697 O ASN A 245 40.496 -30.850 0.253 1.00 34.61 O ANISOU 1697 O ASN A 245 3961 4766 4423 -10 1058 -96 O ATOM 1698 CB ASN A 245 40.775 -29.452 2.597 1.00 28.49 C ANISOU 1698 CB ASN A 245 3064 3925 3837 -69 912 -67 C ATOM 1699 CG ASN A 245 41.569 -28.957 3.761 1.00 30.31 C ANISOU 1699 CG ASN A 245 3181 4131 4203 -105 868 -82 C ATOM 1700 OD1 ASN A 245 42.677 -29.454 4.029 1.00 33.22 O ANISOU 1700 OD1 ASN A 245 3422 4522 4679 -104 892 -135 O ATOM 1701 ND2 ASN A 245 41.049 -27.942 4.441 1.00 29.14 N ANISOU 1701 ND2 ASN A 245 3079 3936 4056 -136 801 -40 N ATOM 1702 N SER A 246 40.492 -29.024 -1.031 1.00 45.11 N ANISOU 1702 N SER A 246 5425 6069 5644 -113 1192 7 N ATOM 1703 CA SER A 246 40.002 -29.717 -2.216 1.00 52.12 C ANISOU 1703 CA SER A 246 6425 6985 6395 -75 1233 -1 C ATOM 1704 C SER A 246 41.107 -29.875 -3.246 1.00 61.41 C ANISOU 1704 C SER A 246 7583 8195 7554 -106 1410 -25 C ATOM 1705 O SER A 246 42.282 -29.653 -2.952 1.00 65.49 O ANISOU 1705 O SER A 246 7971 8722 8190 -148 1494 -48 O ATOM 1706 CB SER A 246 38.830 -28.961 -2.846 1.00 53.21 C ANISOU 1706 CB SER A 246 6730 7090 6395 -83 1190 75 C ATOM 1707 OG SER A 246 37.638 -29.145 -2.098 1.00 51.50 O ANISOU 1707 OG SER A 246 6537 6854 6177 -34 1034 83 O ATOM 1708 OXT SER A 246 40.840 -30.227 -4.397 1.00 63.33 O ANISOU 1708 OXT SER A 246 7941 8458 7665 -91 1473 -25 O TER 1709 SER A 246 ATOM 1710 N ILE B 16 4.216 -25.221 3.292 1.00 17.54 N ANISOU 1710 N ILE B 16 2565 1897 2201 49 -141 68 N ATOM 1711 CA ILE B 16 4.420 -24.446 4.531 1.00 16.74 C ANISOU 1711 CA ILE B 16 2498 1805 2058 44 -182 95 C ATOM 1712 C ILE B 16 5.559 -25.105 5.295 1.00 17.23 C ANISOU 1712 C ILE B 16 2582 1798 2166 66 -267 119 C ATOM 1713 O ILE B 16 5.458 -26.279 5.706 1.00 17.77 O ANISOU 1713 O ILE B 16 2697 1817 2239 54 -302 147 O ATOM 1714 CB ILE B 16 3.210 -24.391 5.471 1.00 16.48 C ANISOU 1714 CB ILE B 16 2530 1800 1932 -2 -164 122 C ATOM 1715 CG1 ILE B 16 1.994 -23.872 4.698 1.00 16.83 C ANISOU 1715 CG1 ILE B 16 2547 1904 1944 -23 -85 96 C ATOM 1716 CG2 ILE B 16 3.378 -23.646 6.774 1.00 17.16 C ANISOU 1716 CG2 ILE B 16 2661 1896 1964 -11 -201 144 C ATOM 1717 CD1 ILE B 16 1.939 -22.348 4.457 1.00 18.53 C ANISOU 1717 CD1 ILE B 16 2721 2172 2148 -11 -59 71 C ATOM 1718 N VAL B 17 6.648 -24.349 5.456 1.00 17.81 N ANISOU 1718 N VAL B 17 2620 1866 2282 98 -306 108 N ATOM 1719 CA VAL B 17 7.812 -24.804 6.215 1.00 17.12 C ANISOU 1719 CA VAL B 17 2544 1712 2247 123 -400 128 C ATOM 1720 C VAL B 17 7.685 -24.319 7.654 1.00 18.02 C ANISOU 1720 C VAL B 17 2730 1832 2285 101 -453 167 C ATOM 1721 O VAL B 17 7.446 -23.127 7.870 1.00 18.14 O ANISOU 1721 O VAL B 17 2740 1899 2254 94 -427 156 O ATOM 1722 CB VAL B 17 9.111 -24.232 5.589 1.00 18.46 C ANISOU 1722 CB VAL B 17 2629 1870 2514 168 -414 91 C ATOM 1723 CG1 VAL B 17 10.319 -24.614 6.413 1.00 21.34 C ANISOU 1723 CG1 VAL B 17 2997 2165 2944 196 -520 108 C ATOM 1724 CG2 VAL B 17 9.300 -24.774 4.181 1.00 21.66 C ANISOU 1724 CG2 VAL B 17 2970 2270 2991 186 -358 48 C ATOM 1725 N GLY B 18 7.870 -25.224 8.628 1.00 19.95 N ANISOU 1725 N GLY B 18 3044 2019 2516 89 -528 211 N ATOM 1726 CA GLY B 18 7.852 -24.815 10.024 1.00 18.61 C ANISOU 1726 CA GLY B 18 2952 1851 2267 65 -586 248 C ATOM 1727 C GLY B 18 6.504 -24.522 10.615 1.00 20.63 C ANISOU 1727 C GLY B 18 3276 2163 2400 9 -526 264 C ATOM 1728 O GLY B 18 6.436 -23.880 11.656 1.00 22.22 O ANISOU 1728 O GLY B 18 3531 2384 2527 -12 -552 279 O ATOM 1729 N GLY B 19 5.437 -25.057 10.026 1.00 18.60 N ANISOU 1729 N GLY B 19 3019 1927 2120 -17 -451 259 N ATOM 1730 CA GLY B 19 4.097 -24.844 10.524 1.00 18.67 C ANISOU 1730 CA GLY B 19 3081 1987 2024 -71 -386 268 C ATOM 1731 C GLY B 19 3.589 -26.077 11.239 1.00 20.21 C ANISOU 1731 C GLY B 19 3365 2143 2171 -118 -407 318 C ATOM 1732 O GLY B 19 4.369 -26.846 11.813 1.00 22.53 O ANISOU 1732 O GLY B 19 3705 2369 2486 -112 -497 358 O ATOM 1733 N TYR B 20 2.278 -26.266 11.211 1.00 19.63 N ANISOU 1733 N TYR B 20 3314 2107 2037 -166 -327 317 N ATOM 1734 CA TYR B 20 1.641 -27.340 11.965 1.00 19.93 C ANISOU 1734 CA TYR B 20 3443 2116 2015 -223 -333 367 C ATOM 1735 C TYR B 20 0.420 -27.810 11.204 1.00 19.91 C ANISOU 1735 C TYR B 20 3413 2139 2012 -252 -243 349 C ATOM 1736 O TYR B 20 -0.121 -27.116 10.348 1.00 20.17 O ANISOU 1736 O TYR B 20 3374 2226 2065 -239 -173 301 O ATOM 1737 CB TYR B 20 1.266 -26.846 13.383 1.00 20.38 C ANISOU 1737 CB TYR B 20 3590 2202 1953 -275 -335 392 C ATOM 1738 CG TYR B 20 0.353 -25.657 13.447 1.00 21.06 C ANISOU 1738 CG TYR B 20 3650 2372 1981 -294 -244 346 C ATOM 1739 CD1 TYR B 20 0.866 -24.359 13.367 1.00 20.91 C ANISOU 1739 CD1 TYR B 20 3582 2388 1977 -254 -250 307 C ATOM 1740 CD2 TYR B 20 -1.006 -25.801 13.536 1.00 23.24 C ANISOU 1740 CD2 TYR B 20 3941 2689 2200 -350 -152 338 C ATOM 1741 CE1 TYR B 20 0.038 -23.265 13.429 1.00 21.02 C ANISOU 1741 CE1 TYR B 20 3569 2471 1947 -269 -172 263 C ATOM 1742 CE2 TYR B 20 -1.849 -24.719 13.571 1.00 23.99 C ANISOU 1742 CE2 TYR B 20 4002 2855 2258 -363 -71 290 C ATOM 1743 CZ TYR B 20 -1.334 -23.447 13.512 1.00 23.45 C ANISOU 1743 CZ TYR B 20 3890 2818 2204 -321 -82 252 C ATOM 1744 OH TYR B 20 -2.215 -22.377 13.555 1.00 26.26 O ANISOU 1744 OH TYR B 20 4210 3238 2529 -333 -4 202 O ATOM 1745 N ASN B 21 -0.006 -29.018 11.497 1.00 21.13 N ANISOU 1745 N ASN B 21 3627 2250 2151 -294 -251 390 N ATOM 1746 CA ASN B 21 -1.173 -29.580 10.852 1.00 20.24 C ANISOU 1746 CA ASN B 21 3494 2154 2041 -328 -173 377 C ATOM 1747 C ASN B 21 -2.416 -28.759 11.192 1.00 21.83 C ANISOU 1747 C ASN B 21 3695 2435 2164 -375 -80 352 C ATOM 1748 O ASN B 21 -2.722 -28.545 12.369 1.00 23.61 O ANISOU 1748 O ASN B 21 3994 2677 2299 -423 -73 377 O ATOM 1749 CB ASN B 21 -1.337 -31.048 11.304 1.00 22.50 C ANISOU 1749 CB ASN B 21 3858 2370 2320 -372 -209 434 C ATOM 1750 CG ASN B 21 -2.315 -31.836 10.462 1.00 25.70 C ANISOU 1750 CG ASN B 21 4233 2774 2758 -397 -147 419 C ATOM 1751 OD1 ASN B 21 -3.430 -31.409 10.227 1.00 26.69 O ANISOU 1751 OD1 ASN B 21 4330 2961 2852 -429 -61 389 O ATOM 1752 ND2 ASN B 21 -1.909 -33.053 10.041 1.00 27.50 N ANISOU 1752 ND2 ASN B 21 4469 2924 3055 -385 -197 439 N ATOM 1753 N CYS B 22 -3.148 -28.317 10.175 1.00 19.31 N ANISOU 1753 N CYS B 22 3295 2162 1879 -363 -9 302 N ATOM 1754 CA CYS B 22 -4.351 -27.510 10.373 1.00 22.13 C ANISOU 1754 CA CYS B 22 3635 2591 2184 -399 78 269 C ATOM 1755 C CYS B 22 -5.535 -28.275 10.976 1.00 23.54 C ANISOU 1755 C CYS B 22 3865 2772 2306 -478 134 291 C ATOM 1756 O CYS B 22 -6.596 -27.690 11.176 1.00 29.18 O ANISOU 1756 O CYS B 22 4561 3543 2985 -513 212 260 O ATOM 1757 CB CYS B 22 -4.860 -26.916 9.048 1.00 21.99 C ANISOU 1757 CB CYS B 22 3515 2614 2227 -367 127 213 C ATOM 1758 SG CYS B 22 -3.807 -25.742 8.231 1.00 22.46 S ANISOU 1758 SG CYS B 22 3501 2690 2343 -288 93 177 S ATOM 1759 N GLU B 23 -5.380 -29.562 11.240 1.00 22.27 N ANISOU 1759 N GLU B 23 3767 2550 2145 -508 97 342 N ATOM 1760 CA GLU B 23 -6.493 -30.323 11.835 1.00 27.36 C ANISOU 1760 CA GLU B 23 4466 3194 2735 -591 152 368 C ATOM 1761 C GLU B 23 -7.002 -29.721 13.174 1.00 32.52 C ANISOU 1761 C GLU B 23 5186 3893 3279 -651 198 375 C ATOM 1762 O GLU B 23 -8.118 -30.011 13.620 1.00 30.50 O ANISOU 1762 O GLU B 23 4955 3661 2974 -723 275 376 O ATOM 1763 CB GLU B 23 -6.097 -31.791 12.043 1.00 28.99 C ANISOU 1763 CB GLU B 23 4743 3315 2955 -614 90 431 C ATOM 1764 CG GLU B 23 -4.982 -31.990 13.010 1.00 30.46 C ANISOU 1764 CG GLU B 23 5017 3452 3104 -608 -4 486 C ATOM 1765 CD GLU B 23 -4.549 -33.448 13.123 1.00 37.82 C ANISOU 1765 CD GLU B 23 6013 4290 4068 -624 -78 548 C ATOM 1766 OE1 GLU B 23 -3.519 -33.689 13.787 1.00 43.42 O ANISOU 1766 OE1 GLU B 23 6786 4945 4767 -608 -175 595 O ATOM 1767 OE2 GLU B 23 -5.237 -34.327 12.532 1.00 36.27 O ANISOU 1767 OE2 GLU B 23 5799 4070 3911 -649 -44 548 O ATOM 1768 N GLU B 24 -6.181 -28.914 13.830 1.00 29.75 N ANISOU 1768 N GLU B 24 4865 3553 2887 -625 154 378 N ATOM 1769 CA GLU B 24 -6.594 -28.294 15.091 1.00 30.57 C ANISOU 1769 CA GLU B 24 5034 3701 2881 -680 196 377 C ATOM 1770 C GLU B 24 -7.283 -26.948 14.885 1.00 28.21 C ANISOU 1770 C GLU B 24 4656 3480 2582 -665 278 302 C ATOM 1771 O GLU B 24 -7.664 -26.275 15.861 1.00 28.19 O ANISOU 1771 O GLU B 24 4694 3522 2496 -705 324 284 O ATOM 1772 CB GLU B 24 -5.368 -28.111 16.009 1.00 36.74 C ANISOU 1772 CB GLU B 24 5898 4451 3612 -664 99 418 C ATOM 1773 CG GLU B 24 -4.177 -27.338 15.373 1.00 49.01 C ANISOU 1773 CG GLU B 24 7384 5996 5240 -571 26 393 C ATOM 1774 CD GLU B 24 -3.089 -26.974 16.404 1.00 47.87 C ANISOU 1774 CD GLU B 24 7317 5830 5041 -562 -63 423 C ATOM 1775 OE1 GLU B 24 -3.205 -25.887 17.036 1.00 50.48 O ANISOU 1775 OE1 GLU B 24 7657 6213 5310 -570 -35 390 O ATOM 1776 OE2 GLU B 24 -2.119 -27.763 16.566 1.00 42.90 O ANISOU 1776 OE2 GLU B 24 6733 5129 4436 -545 -166 477 O ATOM 1777 N ASN B 25 -7.413 -26.536 13.620 1.00 26.55 N ANISOU 1777 N ASN B 25 4337 3286 2466 -608 291 256 N ATOM 1778 CA ASN B 25 -7.961 -25.246 13.244 1.00 24.64 C ANISOU 1778 CA ASN B 25 4009 3106 2245 -582 349 187 C ATOM 1779 C ASN B 25 -9.163 -25.470 12.292 1.00 30.16 C ANISOU 1779 C ASN B 25 4628 3827 3005 -595 420 151 C ATOM 1780 O ASN B 25 -9.413 -26.580 11.825 1.00 33.26 O ANISOU 1780 O ASN B 25 5026 4184 3428 -615 416 177 O ATOM 1781 CB ASN B 25 -6.902 -24.431 12.462 1.00 26.90 C ANISOU 1781 CB ASN B 25 4235 3387 2597 -496 285 167 C ATOM 1782 CG ASN B 25 -5.971 -23.635 13.349 1.00 37.69 C ANISOU 1782 CG ASN B 25 5647 4757 3915 -478 235 172 C ATOM 1783 OD1 ASN B 25 -5.090 -22.932 12.850 1.00 41.07 O ANISOU 1783 OD1 ASN B 25 6031 5181 4392 -416 186 158 O ATOM 1784 ND2 ASN B 25 -6.171 -23.692 14.641 1.00 42.17 N ANISOU 1784 ND2 ASN B 25 6303 5334 4385 -535 251 190 N ATOM 1785 N SER B 26 -9.918 -24.403 12.067 1.00 29.32 N ANISOU 1785 N SER B 26 4448 3774 2917 -585 480 89 N ATOM 1786 CA SER B 26 -10.967 -24.371 11.046 1.00 29.01 C ANISOU 1786 CA SER B 26 4318 3756 2950 -583 530 47 C ATOM 1787 C SER B 26 -10.436 -23.553 9.874 1.00 20.71 C ANISOU 1787 C SER B 26 3187 2708 1973 -504 485 19 C ATOM 1788 O SER B 26 -10.223 -22.370 10.090 1.00 24.49 O ANISOU 1788 O SER B 26 3642 3215 2446 -474 485 -12 O ATOM 1789 CB SER B 26 -12.179 -23.610 11.614 1.00 35.67 C ANISOU 1789 CB SER B 26 5127 4654 3771 -622 623 -9 C ATOM 1790 OG SER B 26 -13.259 -23.580 10.698 1.00 38.06 O ANISOU 1790 OG SER B 26 5338 4974 4149 -623 667 -51 O ATOM 1791 N VAL B 27 -10.229 -24.157 8.671 1.00 20.29 N ANISOU 1791 N VAL B 27 3098 2627 1985 -474 450 29 N ATOM 1792 CA VAL B 27 -9.785 -23.377 7.494 1.00 17.66 C ANISOU 1792 CA VAL B 27 2694 2301 1715 -408 415 3 C ATOM 1793 C VAL B 27 -10.690 -23.649 6.276 1.00 17.35 C ANISOU 1793 C VAL B 27 2586 2267 1739 -409 436 -23 C ATOM 1794 O VAL B 27 -10.235 -24.167 5.252 1.00 19.60 O ANISOU 1794 O VAL B 27 2856 2526 2064 -382 397 -13 O ATOM 1795 CB VAL B 27 -8.285 -23.601 7.149 1.00 21.70 C ANISOU 1795 CB VAL B 27 3231 2773 2241 -360 338 36 C ATOM 1796 CG1 VAL B 27 -7.791 -22.536 6.229 1.00 21.67 C ANISOU 1796 CG1 VAL B 27 3164 2785 2284 -302 313 8 C ATOM 1797 CG2 VAL B 27 -7.436 -23.657 8.433 1.00 27.11 C ANISOU 1797 CG2 VAL B 27 3996 3441 2865 -370 305 71 C ATOM 1798 N PRO B 28 -11.981 -23.281 6.372 1.00 15.94 N ANISOU 1798 N PRO B 28 2361 2122 1571 -439 496 -62 N ATOM 1799 CA PRO B 28 -12.973 -23.767 5.403 1.00 16.71 C ANISOU 1799 CA PRO B 28 2404 2221 1726 -454 514 -82 C ATOM 1800 C PRO B 28 -12.939 -23.001 4.094 1.00 15.80 C ANISOU 1800 C PRO B 28 2219 2115 1669 -402 479 -110 C ATOM 1801 O PRO B 28 -13.616 -23.413 3.143 1.00 15.42 O ANISOU 1801 O PRO B 28 2129 2062 1666 -408 477 -125 O ATOM 1802 CB PRO B 28 -14.300 -23.557 6.127 1.00 17.16 C ANISOU 1802 CB PRO B 28 2434 2309 1777 -506 591 -117 C ATOM 1803 CG PRO B 28 -14.039 -22.364 6.940 1.00 19.48 C ANISOU 1803 CG PRO B 28 2731 2633 2038 -489 604 -138 C ATOM 1804 CD PRO B 28 -12.655 -22.627 7.498 1.00 17.72 C ANISOU 1804 CD PRO B 28 2592 2384 1758 -473 555 -89 C ATOM 1805 N TYR B 29 -12.176 -21.919 4.052 1.00 14.40 N ANISOU 1805 N TYR B 29 2033 1950 1489 -355 449 -116 N ATOM 1806 CA TYR B 29 -12.079 -21.056 2.858 1.00 14.13 C ANISOU 1806 CA TYR B 29 1941 1925 1504 -309 414 -137 C ATOM 1807 C TYR B 29 -10.893 -21.468 2.003 1.00 14.77 C ANISOU 1807 C TYR B 29 2045 1978 1588 -276 362 -109 C ATOM 1808 O TYR B 29 -10.716 -20.947 0.904 1.00 14.58 O ANISOU 1808 O TYR B 29 1986 1958 1595 -246 333 -119 O ATOM 1809 CB TYR B 29 -11.935 -19.565 3.272 1.00 13.50 C ANISOU 1809 CB TYR B 29 1836 1870 1425 -280 413 -161 C ATOM 1810 CG TYR B 29 -10.862 -19.356 4.304 1.00 13.45 C ANISOU 1810 CG TYR B 29 1887 1857 1366 -271 402 -139 C ATOM 1811 CD1 TYR B 29 -9.532 -19.259 3.945 1.00 14.73 C ANISOU 1811 CD1 TYR B 29 2072 2000 1526 -233 350 -112 C ATOM 1812 CD2 TYR B 29 -11.179 -19.321 5.638 1.00 14.79 C ANISOU 1812 CD2 TYR B 29 2090 2040 1489 -305 444 -145 C ATOM 1813 CE1 TYR B 29 -8.515 -19.121 4.925 1.00 14.62 C ANISOU 1813 CE1 TYR B 29 2111 1976 1470 -226 331 -91 C ATOM 1814 CE2 TYR B 29 -10.208 -19.218 6.608 1.00 16.33 C ANISOU 1814 CE2 TYR B 29 2347 2228 1630 -302 426 -122 C ATOM 1815 CZ TYR B 29 -8.877 -19.068 6.249 1.00 16.93 C ANISOU 1815 CZ TYR B 29 2440 2281 1711 -259 365 -96 C ATOM 1816 OH TYR B 29 -7.933 -18.993 7.253 1.00 18.95 O ANISOU 1816 OH TYR B 29 2756 2525 1919 -257 339 -73 O ATOM 1817 N GLN B 30 -10.060 -22.381 2.482 1.00 13.61 N ANISOU 1817 N GLN B 30 1958 1802 1413 -283 349 -74 N ATOM 1818 CA GLN B 30 -8.924 -22.852 1.702 1.00 13.54 C ANISOU 1818 CA GLN B 30 1963 1763 1417 -252 306 -56 C ATOM 1819 C GLN B 30 -9.368 -23.757 0.595 1.00 13.96 C ANISOU 1819 C GLN B 30 2002 1802 1501 -263 304 -63 C ATOM 1820 O GLN B 30 -10.142 -24.704 0.853 1.00 15.21 O ANISOU 1820 O GLN B 30 2173 1948 1658 -304 327 -59 O ATOM 1821 CB GLN B 30 -7.961 -23.595 2.610 1.00 14.70 C ANISOU 1821 CB GLN B 30 2174 1875 1535 -255 286 -19 C ATOM 1822 CG GLN B 30 -6.808 -24.293 1.868 1.00 13.68 C ANISOU 1822 CG GLN B 30 2057 1708 1434 -225 245 -6 C ATOM 1823 CD GLN B 30 -5.646 -23.418 1.506 1.00 13.81 C ANISOU 1823 CD GLN B 30 2055 1728 1466 -178 214 -10 C ATOM 1824 OE1 GLN B 30 -5.180 -23.362 0.301 1.00 17.44 O ANISOU 1824 OE1 GLN B 30 2484 2185 1958 -153 203 -25 O ATOM 1825 NE2 GLN B 30 -5.107 -22.782 2.481 1.00 13.54 N ANISOU 1825 NE2 GLN B 30 2040 1697 1408 -168 200 2 N ATOM 1826 N VAL B 31 -8.878 -23.546 -0.619 1.00 14.40 N ANISOU 1826 N VAL B 31 2034 1856 1580 -233 278 -74 N ATOM 1827 CA VAL B 31 -9.125 -24.487 -1.692 1.00 14.77 C ANISOU 1827 CA VAL B 31 2077 1885 1649 -243 272 -84 C ATOM 1828 C VAL B 31 -7.806 -24.993 -2.242 1.00 14.49 C ANISOU 1828 C VAL B 31 2063 1820 1623 -214 246 -76 C ATOM 1829 O VAL B 31 -6.742 -24.377 -2.079 1.00 13.62 O ANISOU 1829 O VAL B 31 1956 1709 1509 -183 230 -68 O ATOM 1830 CB VAL B 31 -10.041 -23.981 -2.790 1.00 16.58 C ANISOU 1830 CB VAL B 31 2260 2140 1899 -246 270 -112 C ATOM 1831 CG1 VAL B 31 -11.373 -23.392 -2.207 1.00 17.52 C ANISOU 1831 CG1 VAL B 31 2343 2286 2026 -270 295 -127 C ATOM 1832 CG2 VAL B 31 -9.324 -22.958 -3.600 1.00 15.38 C ANISOU 1832 CG2 VAL B 31 2091 2003 1748 -210 245 -117 C ATOM 1833 N SER B 32 -7.883 -26.153 -2.891 1.00 13.61 N ANISOU 1833 N SER B 32 1963 1680 1528 -227 244 -84 N ATOM 1834 CA SER B 32 -6.779 -26.709 -3.665 1.00 14.52 C ANISOU 1834 CA SER B 32 2089 1767 1662 -202 226 -92 C ATOM 1835 C SER B 32 -7.126 -26.560 -5.130 1.00 14.89 C ANISOU 1835 C SER B 32 2112 1833 1714 -203 227 -124 C ATOM 1836 O SER B 32 -8.212 -26.938 -5.542 1.00 16.79 O ANISOU 1836 O SER B 32 2343 2079 1957 -231 233 -137 O ATOM 1837 CB SER B 32 -6.600 -28.188 -3.337 1.00 16.08 C ANISOU 1837 CB SER B 32 2321 1911 1878 -217 220 -82 C ATOM 1838 OG SER B 32 -5.726 -28.877 -4.237 1.00 16.94 O ANISOU 1838 OG SER B 32 2432 1989 2016 -196 209 -103 O ATOM 1839 N LEU B 33 -6.209 -26.050 -5.930 1.00 13.06 N ANISOU 1839 N LEU B 33 1870 1609 1481 -176 221 -137 N ATOM 1840 CA LEU B 33 -6.336 -25.984 -7.375 1.00 13.06 C ANISOU 1840 CA LEU B 33 1861 1625 1476 -180 222 -166 C ATOM 1841 C LEU B 33 -5.635 -27.208 -7.968 1.00 14.43 C ANISOU 1841 C LEU B 33 2054 1761 1669 -176 227 -189 C ATOM 1842 O LEU B 33 -4.467 -27.478 -7.672 1.00 14.86 O ANISOU 1842 O LEU B 33 2114 1789 1745 -151 228 -188 O ATOM 1843 CB LEU B 33 -5.733 -24.697 -7.948 1.00 14.14 C ANISOU 1843 CB LEU B 33 1983 1794 1596 -160 219 -166 C ATOM 1844 CG LEU B 33 -6.247 -23.381 -7.327 1.00 14.88 C ANISOU 1844 CG LEU B 33 2056 1918 1680 -156 210 -146 C ATOM 1845 CD1 LEU B 33 -5.704 -22.231 -8.123 1.00 15.33 C ANISOU 1845 CD1 LEU B 33 2102 1999 1723 -142 202 -146 C ATOM 1846 CD2 LEU B 33 -7.743 -23.328 -7.252 1.00 16.13 C ANISOU 1846 CD2 LEU B 33 2199 2091 1839 -181 205 -149 C ATOM 1847 N ASN B 34 -6.387 -27.929 -8.791 1.00 15.05 N ANISOU 1847 N ASN B 34 2138 1834 1745 -202 227 -214 N ATOM 1848 CA ASN B 34 -5.989 -29.236 -9.270 1.00 14.03 C ANISOU 1848 CA ASN B 34 2026 1663 1640 -204 232 -242 C ATOM 1849 C ASN B 34 -5.991 -29.286 -10.787 1.00 16.88 C ANISOU 1849 C ASN B 34 2392 2042 1981 -213 238 -285 C ATOM 1850 O ASN B 34 -6.937 -28.873 -11.450 1.00 17.73 O ANISOU 1850 O ASN B 34 2496 2180 2060 -237 227 -291 O ATOM 1851 CB ASN B 34 -6.941 -30.278 -8.648 1.00 14.64 C ANISOU 1851 CB ASN B 34 2115 1709 1737 -233 225 -232 C ATOM 1852 CG ASN B 34 -6.542 -31.710 -8.966 1.00 17.65 C ANISOU 1852 CG ASN B 34 2518 2035 2154 -235 224 -258 C ATOM 1853 OD1 ASN B 34 -6.737 -32.162 -10.094 1.00 18.80 O ANISOU 1853 OD1 ASN B 34 2666 2180 2297 -246 227 -299 O ATOM 1854 ND2 ASN B 34 -6.012 -32.435 -7.977 1.00 18.45 N ANISOU 1854 ND2 ASN B 34 2635 2087 2287 -225 215 -235 N ATOM 1855 N SER B 37 -4.900 -29.834 -11.313 1.00 16.20 N ANISOU 1855 N SER B 37 2313 1932 1911 -196 255 -317 N ATOM 1856 CA ASER B 37 -4.764 -30.085 -12.751 0.50 16.77 C ANISOU 1856 CA ASER B 37 2397 2015 1960 -209 270 -366 C ATOM 1857 CA BSER B 37 -4.688 -30.063 -12.741 0.50 17.21 C ANISOU 1857 CA BSER B 37 2453 2071 2017 -207 271 -366 C ATOM 1858 C SER B 37 -4.253 -31.518 -12.940 1.00 19.31 C ANISOU 1858 C SER B 37 2729 2281 2326 -203 281 -407 C ATOM 1859 O SER B 37 -3.297 -31.778 -13.658 1.00 22.63 O ANISOU 1859 O SER B 37 3150 2694 2755 -191 308 -451 O ATOM 1860 CB ASER B 37 -3.822 -29.066 -13.398 0.50 18.92 C ANISOU 1860 CB ASER B 37 2663 2322 2203 -196 292 -374 C ATOM 1861 CB BSER B 37 -3.587 -29.128 -13.268 0.50 20.46 C ANISOU 1861 CB BSER B 37 2856 2511 2408 -189 296 -375 C ATOM 1862 OG ASER B 37 -3.730 -29.274 -14.788 0.50 20.43 O ANISOU 1862 OG ASER B 37 2875 2528 2358 -216 312 -421 O ATOM 1863 OG BSER B 37 -2.382 -29.271 -12.510 0.50 22.60 O ANISOU 1863 OG BSER B 37 3109 2751 2727 -154 307 -370 O ATOM 1864 N GLY B 38 -4.926 -32.446 -12.289 1.00 19.06 N ANISOU 1864 N GLY B 38 2706 2212 2326 -216 262 -395 N ATOM 1865 CA GLY B 38 -4.461 -33.816 -12.191 1.00 20.23 C ANISOU 1865 CA GLY B 38 2862 2294 2529 -207 262 -423 C ATOM 1866 C GLY B 38 -3.630 -34.105 -10.954 1.00 20.69 C ANISOU 1866 C GLY B 38 2915 2306 2639 -177 249 -389 C ATOM 1867 O GLY B 38 -3.238 -35.272 -10.683 1.00 23.76 O ANISOU 1867 O GLY B 38 3312 2629 3086 -167 237 -403 O ATOM 1868 N TYR B 39 -3.360 -33.036 -10.190 1.00 16.09 N ANISOU 1868 N TYR B 39 2320 1754 2039 -162 245 -346 N ATOM 1869 CA TYR B 39 -2.578 -33.044 -8.971 1.00 17.47 C ANISOU 1869 CA TYR B 39 2493 1896 2250 -134 225 -308 C ATOM 1870 C TYR B 39 -2.740 -31.619 -8.432 1.00 16.66 C ANISOU 1870 C TYR B 39 2379 1848 2102 -132 225 -268 C ATOM 1871 O TYR B 39 -3.077 -30.684 -9.166 1.00 14.86 O ANISOU 1871 O TYR B 39 2140 1675 1831 -141 242 -278 O ATOM 1872 CB TYR B 39 -1.097 -33.383 -9.242 1.00 17.43 C ANISOU 1872 CB TYR B 39 2470 1854 2301 -94 231 -344 C ATOM 1873 CG TYR B 39 -0.413 -32.379 -10.151 1.00 16.12 C ANISOU 1873 CG TYR B 39 2278 1738 2110 -82 266 -375 C ATOM 1874 CD1 TYR B 39 -0.502 -32.492 -11.548 1.00 18.53 C ANISOU 1874 CD1 TYR B 39 2584 2066 2390 -97 302 -431 C ATOM 1875 CD2 TYR B 39 0.298 -31.319 -9.628 1.00 16.11 C ANISOU 1875 CD2 TYR B 39 2255 1759 2105 -59 264 -348 C ATOM 1876 CE1 TYR B 39 0.083 -31.545 -12.366 1.00 19.83 C ANISOU 1876 CE1 TYR B 39 2733 2278 2523 -95 337 -454 C ATOM 1877 CE2 TYR B 39 0.909 -30.360 -10.443 1.00 15.68 C ANISOU 1877 CE2 TYR B 39 2179 1750 2028 -54 298 -372 C ATOM 1878 CZ TYR B 39 0.791 -30.488 -11.811 1.00 18.96 C ANISOU 1878 CZ TYR B 39 2600 2189 2415 -74 336 -422 C ATOM 1879 OH TYR B 39 1.417 -29.534 -12.574 1.00 21.53 O ANISOU 1879 OH TYR B 39 2910 2558 2712 -75 372 -440 O ATOM 1880 N HIS B 40 -2.414 -31.453 -7.161 1.00 15.14 N ANISOU 1880 N HIS B 40 2193 1638 1922 -119 202 -224 N ATOM 1881 CA HIS B 40 -2.434 -30.133 -6.520 1.00 13.38 C ANISOU 1881 CA HIS B 40 1960 1460 1664 -113 200 -190 C ATOM 1882 C HIS B 40 -1.272 -29.281 -7.002 1.00 14.38 C ANISOU 1882 C HIS B 40 2059 1607 1799 -81 211 -208 C ATOM 1883 O HIS B 40 -0.116 -29.678 -6.863 1.00 15.52 O ANISOU 1883 O HIS B 40 2193 1712 1991 -52 202 -220 O ATOM 1884 CB HIS B 40 -2.328 -30.317 -5.016 1.00 14.57 C ANISOU 1884 CB HIS B 40 2134 1581 1822 -111 171 -142 C ATOM 1885 CG HIS B 40 -2.079 -29.042 -4.271 1.00 14.90 C ANISOU 1885 CG HIS B 40 2167 1659 1835 -99 166 -114 C ATOM 1886 ND1 HIS B 40 -3.104 -28.193 -3.861 1.00 15.47 N ANISOU 1886 ND1 HIS B 40 2239 1778 1861 -122 177 -95 N ATOM 1887 CD2 HIS B 40 -0.917 -28.412 -3.971 1.00 15.82 C ANISOU 1887 CD2 HIS B 40 2269 1773 1970 -65 151 -110 C ATOM 1888 CE1 HIS B 40 -2.568 -27.122 -3.300 1.00 16.42 C ANISOU 1888 CE1 HIS B 40 2350 1920 1969 -102 169 -80 C ATOM 1889 NE2 HIS B 40 -1.249 -27.235 -3.342 1.00 15.41 N ANISOU 1889 NE2 HIS B 40 2215 1764 1878 -69 151 -86 N ATOM 1890 N PHE B 41 -1.574 -28.089 -7.529 1.00 14.86 N ANISOU 1890 N PHE B 41 2105 1724 1818 -87 227 -209 N ATOM 1891 CA PHE B 41 -0.503 -27.209 -7.971 1.00 14.48 C ANISOU 1891 CA PHE B 41 2031 1695 1774 -64 241 -222 C ATOM 1892 C PHE B 41 -0.482 -25.822 -7.342 1.00 13.98 C ANISOU 1892 C PHE B 41 1956 1666 1687 -57 230 -189 C ATOM 1893 O PHE B 41 0.522 -25.133 -7.420 1.00 15.42 O ANISOU 1893 O PHE B 41 2118 1855 1884 -37 235 -192 O ATOM 1894 CB PHE B 41 -0.461 -27.064 -9.494 1.00 14.53 C ANISOU 1894 CB PHE B 41 2032 1729 1759 -77 274 -264 C ATOM 1895 CG PHE B 41 -1.612 -26.254 -10.070 1.00 13.55 C ANISOU 1895 CG PHE B 41 1916 1654 1577 -106 274 -253 C ATOM 1896 CD1 PHE B 41 -1.450 -24.894 -10.302 1.00 14.83 C ANISOU 1896 CD1 PHE B 41 2067 1856 1711 -105 276 -238 C ATOM 1897 CD2 PHE B 41 -2.831 -26.848 -10.358 1.00 15.82 C ANISOU 1897 CD2 PHE B 41 2221 1943 1847 -134 265 -259 C ATOM 1898 CE1 PHE B 41 -2.518 -24.150 -10.806 1.00 13.53 C ANISOU 1898 CE1 PHE B 41 1909 1729 1504 -128 264 -227 C ATOM 1899 CE2 PHE B 41 -3.877 -26.091 -10.890 1.00 18.16 C ANISOU 1899 CE2 PHE B 41 2519 2280 2101 -157 256 -251 C ATOM 1900 CZ PHE B 41 -3.717 -24.743 -11.076 1.00 15.87 C ANISOU 1900 CZ PHE B 41 2218 2025 1786 -153 252 -233 C ATOM 1901 N CYS B 42 -1.573 -25.404 -6.691 1.00 14.17 N ANISOU 1901 N CYS B 42 1992 1712 1681 -75 218 -160 N ATOM 1902 CA CYS B 42 -1.664 -24.069 -6.093 1.00 14.98 C ANISOU 1902 CA CYS B 42 2083 1847 1763 -68 209 -135 C ATOM 1903 C CYS B 42 -2.823 -24.117 -5.125 1.00 12.14 C ANISOU 1903 C CYS B 42 1737 1492 1383 -88 201 -112 C ATOM 1904 O CYS B 42 -3.670 -25.025 -5.164 1.00 13.97 O ANISOU 1904 O CYS B 42 1984 1712 1613 -112 206 -116 O ATOM 1905 CB CYS B 42 -1.949 -23.017 -7.174 1.00 14.87 C ANISOU 1905 CB CYS B 42 2053 1875 1722 -77 221 -146 C ATOM 1906 SG CYS B 42 -0.422 -22.286 -7.901 1.00 15.75 S ANISOU 1906 SG CYS B 42 2144 1993 1849 -56 237 -159 S ATOM 1907 N GLY B 43 -2.828 -23.162 -4.200 1.00 12.74 N ANISOU 1907 N GLY B 43 1809 1585 1447 -81 191 -92 N ATOM 1908 CA GLY B 43 -3.968 -22.885 -3.354 1.00 12.79 C ANISOU 1908 CA GLY B 43 1822 1609 1430 -101 195 -78 C ATOM 1909 C GLY B 43 -4.864 -21.766 -3.884 1.00 13.43 C ANISOU 1909 C GLY B 43 1874 1730 1498 -109 201 -88 C ATOM 1910 O GLY B 43 -4.586 -21.147 -4.905 1.00 13.00 O ANISOU 1910 O GLY B 43 1803 1691 1445 -99 197 -98 O ATOM 1911 N GLY B 44 -5.892 -21.468 -3.122 1.00 12.23 N ANISOU 1911 N GLY B 44 1719 1594 1335 -126 209 -85 N ATOM 1912 CA GLY B 44 -6.789 -20.351 -3.378 1.00 13.18 C ANISOU 1912 CA GLY B 44 1807 1746 1457 -128 209 -96 C ATOM 1913 C GLY B 44 -7.675 -20.154 -2.169 1.00 12.38 C ANISOU 1913 C GLY B 44 1701 1654 1347 -145 227 -98 C ATOM 1914 O GLY B 44 -7.652 -20.955 -1.198 1.00 12.63 O ANISOU 1914 O GLY B 44 1765 1671 1364 -162 241 -86 O ATOM 1915 N SER B 45 -8.485 -19.103 -2.230 1.00 13.42 N ANISOU 1915 N SER B 45 1797 1810 1491 -144 227 -113 N ATOM 1916 CA SER B 45 -9.399 -18.692 -1.151 1.00 14.33 C ANISOU 1916 CA SER B 45 1898 1941 1606 -159 252 -127 C ATOM 1917 C SER B 45 -10.795 -18.456 -1.681 1.00 13.73 C ANISOU 1917 C SER B 45 1776 1880 1562 -174 258 -153 C ATOM 1918 O SER B 45 -10.970 -17.716 -2.627 1.00 14.39 O ANISOU 1918 O SER B 45 1829 1969 1669 -159 228 -161 O ATOM 1919 CB SER B 45 -8.918 -17.436 -0.481 1.00 16.29 C ANISOU 1919 CB SER B 45 2139 2199 1851 -135 245 -130 C ATOM 1920 OG SER B 45 -7.676 -17.624 0.098 1.00 15.94 O ANISOU 1920 OG SER B 45 2134 2140 1782 -122 235 -108 O ATOM 1921 N LEU B 46 -11.784 -19.132 -1.095 1.00 13.41 N ANISOU 1921 N LEU B 46 1729 1843 1525 -208 293 -166 N ATOM 1922 CA LEU B 46 -13.177 -18.919 -1.451 1.00 14.27 C ANISOU 1922 CA LEU B 46 1783 1962 1675 -225 300 -197 C ATOM 1923 C LEU B 46 -13.658 -17.575 -0.871 1.00 14.72 C ANISOU 1923 C LEU B 46 1796 2038 1757 -210 308 -224 C ATOM 1924 O LEU B 46 -13.726 -17.437 0.357 1.00 14.63 O ANISOU 1924 O LEU B 46 1795 2036 1726 -221 349 -234 O ATOM 1925 CB LEU B 46 -14.047 -20.062 -0.944 1.00 14.60 C ANISOU 1925 CB LEU B 46 1828 2001 1718 -271 343 -204 C ATOM 1926 CG LEU B 46 -15.476 -20.081 -1.471 1.00 13.88 C ANISOU 1926 CG LEU B 46 1675 1916 1681 -291 346 -237 C ATOM 1927 CD1 LEU B 46 -15.511 -20.420 -2.954 1.00 14.78 C ANISOU 1927 CD1 LEU B 46 1783 2018 1814 -284 295 -233 C ATOM 1928 CD2 LEU B 46 -16.284 -21.050 -0.697 1.00 15.66 C ANISOU 1928 CD2 LEU B 46 1903 2141 1907 -341 400 -245 C ATOM 1929 N ILE B 47 -14.014 -16.632 -1.752 1.00 14.26 N ANISOU 1929 N ILE B 47 1694 1981 1742 -187 267 -238 N ATOM 1930 CA ILE B 47 -14.477 -15.287 -1.307 1.00 15.70 C ANISOU 1930 CA ILE B 47 1828 2173 1962 -167 266 -268 C ATOM 1931 C ILE B 47 -15.957 -15.063 -1.562 1.00 18.49 C ANISOU 1931 C ILE B 47 2111 2530 2385 -178 267 -308 C ATOM 1932 O ILE B 47 -16.556 -14.112 -1.033 1.00 21.28 O ANISOU 1932 O ILE B 47 2415 2888 2782 -166 278 -346 O ATOM 1933 CB ILE B 47 -13.625 -14.169 -1.921 1.00 14.34 C ANISOU 1933 CB ILE B 47 1661 1994 1795 -128 213 -251 C ATOM 1934 CG1 ILE B 47 -13.699 -14.252 -3.467 1.00 17.60 C ANISOU 1934 CG1 ILE B 47 2070 2396 2222 -124 158 -233 C ATOM 1935 CG2 ILE B 47 -12.229 -14.247 -1.399 1.00 15.62 C ANISOU 1935 CG2 ILE B 47 1879 2153 1903 -117 220 -222 C ATOM 1936 CD1 ILE B 47 -13.383 -12.927 -4.161 1.00 19.65 C ANISOU 1936 CD1 ILE B 47 2315 2646 2505 -94 102 -223 C ATOM 1937 N ASN B 48 -16.584 -15.921 -2.332 1.00 16.51 N ANISOU 1937 N ASN B 48 1849 2273 2151 -200 255 -307 N ATOM 1938 CA ASN B 48 -17.996 -15.839 -2.628 1.00 19.16 C ANISOU 1938 CA ASN B 48 2113 2608 2559 -213 250 -346 C ATOM 1939 C ASN B 48 -18.427 -17.263 -2.971 1.00 18.31 C ANISOU 1939 C ASN B 48 2019 2497 2443 -253 265 -339 C ATOM 1940 O ASN B 48 -17.576 -18.097 -3.316 1.00 18.61 O ANISOU 1940 O ASN B 48 2120 2527 2425 -259 259 -303 O ATOM 1941 CB ASN B 48 -18.078 -14.930 -3.871 1.00 22.96 C ANISOU 1941 CB ASN B 48 2568 3075 3080 -182 166 -339 C ATOM 1942 CG ASN B 48 -19.433 -14.701 -4.370 1.00 27.40 C ANISOU 1942 CG ASN B 48 3055 3629 3727 -187 134 -375 C ATOM 1943 OD1 ASN B 48 -20.086 -13.689 -4.061 1.00 36.86 O ANISOU 1943 OD1 ASN B 48 4189 4822 4993 -167 125 -411 O ATOM 1944 ND2 ASN B 48 -19.846 -15.531 -5.239 1.00 22.06 N ANISOU 1944 ND2 ASN B 48 2381 2945 3055 -208 106 -367 N ATOM 1945 N GLU B 49 -19.707 -17.580 -2.878 1.00 20.97 N ANISOU 1945 N GLU B 49 2297 2835 2838 -280 286 -376 N ATOM 1946 CA GLU B 49 -20.188 -18.920 -3.212 1.00 19.40 C ANISOU 1946 CA GLU B 49 2105 2627 2638 -321 298 -372 C ATOM 1947 C GLU B 49 -19.738 -19.361 -4.601 1.00 17.64 C ANISOU 1947 C GLU B 49 1918 2389 2396 -312 229 -343 C ATOM 1948 O GLU B 49 -19.676 -20.544 -4.894 1.00 20.98 O ANISOU 1948 O GLU B 49 2374 2802 2795 -340 236 -331 O ATOM 1949 CB GLU B 49 -21.708 -19.022 -3.159 1.00 23.16 C ANISOU 1949 CB GLU B 49 2497 3104 3199 -349 314 -420 C ATOM 1950 CG GLU B 49 -22.258 -18.762 -1.790 1.00 32.84 C ANISOU 1950 CG GLU B 49 3686 4348 4444 -369 399 -457 C ATOM 1951 CD GLU B 49 -23.777 -18.925 -1.705 1.00 40.58 C ANISOU 1951 CD GLU B 49 4573 5328 5516 -401 426 -512 C ATOM 1952 OE1 GLU B 49 -24.313 -18.654 -0.592 1.00 48.37 O ANISOU 1952 OE1 GLU B 49 5523 6333 6525 -422 505 -552 O ATOM 1953 OE2 GLU B 49 -24.415 -19.294 -2.726 1.00 36.11 O ANISOU 1953 OE2 GLU B 49 3970 4746 5003 -407 371 -518 O ATOM 1954 N GLN B 50 -19.448 -18.420 -5.516 1.00 17.28 N ANISOU 1954 N GLN B 50 1868 2340 2358 -277 160 -334 N ATOM 1955 CA AGLN B 50 -19.026 -18.866 -6.852 0.50 15.01 C ANISOU 1955 CA AGLN B 50 1621 2041 2040 -276 102 -310 C ATOM 1956 CA BGLN B 50 -19.119 -18.678 -6.911 0.34 16.09 C ANISOU 1956 CA BGLN B 50 1751 2178 2186 -273 94 -312 C ATOM 1957 C GLN B 50 -17.682 -18.294 -7.299 1.00 15.75 C ANISOU 1957 C GLN B 50 1773 2137 2076 -246 75 -275 C ATOM 1958 O GLN B 50 -17.319 -18.412 -8.486 1.00 17.03 O ANISOU 1958 O GLN B 50 1967 2292 2210 -244 26 -258 O ATOM 1959 CB AGLN B 50 -20.108 -18.572 -7.902 0.66 21.24 C ANISOU 1959 CB AGLN B 50 2360 2821 2891 -279 31 -330 C ATOM 1960 CB BGLN B 50 -20.077 -17.870 -7.810 0.34 18.79 C ANISOU 1960 CB BGLN B 50 2034 2511 2593 -262 19 -331 C ATOM 1961 CG AGLN B 50 -20.100 -19.477 -9.107 0.66 25.44 C ANISOU 1961 CG AGLN B 50 2929 3342 3397 -300 -13 -320 C ATOM 1962 CG BGLN B 50 -21.514 -18.410 -7.866 0.34 20.90 C ANISOU 1962 CG BGLN B 50 2235 2772 2936 -291 16 -369 C ATOM 1963 CD AGLN B 50 -21.394 -19.415 -9.952 0.66 27.25 C ANISOU 1963 CD AGLN B 50 3101 3558 3694 -313 -81 -346 C ATOM 1964 CD BGLN B 50 -22.393 -17.597 -8.817 0.34 24.08 C ANISOU 1964 CD BGLN B 50 2581 3158 3408 -277 -75 -385 C ATOM 1965 OE1AGLN B 50 -21.582 -20.188 -10.916 0.66 25.64 O ANISOU 1965 OE1AGLN B 50 2923 3346 3475 -335 -121 -345 O ATOM 1966 OE1BGLN B 50 -22.791 -16.468 -8.514 0.34 25.00 O ANISOU 1966 OE1BGLN B 50 2644 3272 3585 -250 -94 -403 O ATOM 1967 NE2AGLN B 50 -22.286 -18.493 -9.592 0.66 22.96 N ANISOU 1967 NE2AGLN B 50 2480 3012 3231 -299 -98 -372 N ATOM 1968 NE2BGLN B 50 -22.673 -18.162 -9.981 0.34 23.52 N ANISOU 1968 NE2BGLN B 50 2529 3077 3332 -294 -138 -378 N ATOM 1969 N TRP B 51 -16.888 -17.735 -6.372 1.00 16.00 N ANISOU 1969 N TRP B 51 1820 2176 2084 -225 110 -264 N ATOM 1970 CA TRP B 51 -15.596 -17.152 -6.759 1.00 14.19 C ANISOU 1970 CA TRP B 51 1637 1947 1808 -198 88 -233 C ATOM 1971 C TRP B 51 -14.449 -17.453 -5.791 1.00 14.40 C ANISOU 1971 C TRP B 51 1708 1976 1787 -191 137 -215 C ATOM 1972 O TRP B 51 -14.637 -17.383 -4.562 1.00 13.93 O ANISOU 1972 O TRP B 51 1636 1922 1733 -195 181 -227 O ATOM 1973 CB TRP B 51 -15.664 -15.628 -6.922 1.00 14.77 C ANISOU 1973 CB TRP B 51 1681 2020 1913 -168 46 -233 C ATOM 1974 CG TRP B 51 -16.539 -15.179 -8.064 1.00 16.03 C ANISOU 1974 CG TRP B 51 1808 2168 2113 -169 -25 -239 C ATOM 1975 CD1 TRP B 51 -17.879 -15.019 -8.039 1.00 18.82 C ANISOU 1975 CD1 TRP B 51 2096 2516 2539 -175 -45 -271 C ATOM 1976 CD2 TRP B 51 -16.106 -14.822 -9.365 1.00 16.30 C ANISOU 1976 CD2 TRP B 51 1877 2195 2119 -166 -88 -210 C ATOM 1977 NE1 TRP B 51 -18.335 -14.589 -9.280 1.00 19.05 N ANISOU 1977 NE1 TRP B 51 2118 2531 2591 -174 -129 -263 N ATOM 1978 CE2 TRP B 51 -17.248 -14.448 -10.099 1.00 17.16 C ANISOU 1978 CE2 TRP B 51 1946 2292 2283 -170 -155 -223 C ATOM 1979 CE3 TRP B 51 -14.854 -14.770 -9.982 1.00 16.40 C ANISOU 1979 CE3 TRP B 51 1953 2211 2066 -163 -93 -177 C ATOM 1980 CZ2 TRP B 51 -17.174 -14.037 -11.419 1.00 19.61 C ANISOU 1980 CZ2 TRP B 51 2287 2593 2573 -174 -231 -198 C ATOM 1981 CZ3 TRP B 51 -14.781 -14.339 -11.295 1.00 17.78 C ANISOU 1981 CZ3 TRP B 51 2156 2380 2221 -169 -157 -155 C ATOM 1982 CH2 TRP B 51 -15.942 -13.982 -11.992 1.00 18.72 C ANISOU 1982 CH2 TRP B 51 2242 2485 2384 -175 -228 -163 C ATOM 1983 N VAL B 52 -13.287 -17.739 -6.377 1.00 14.62 N ANISOU 1983 N VAL B 52 1786 1999 1771 -183 127 -189 N ATOM 1984 CA VAL B 52 -12.038 -18.015 -5.697 1.00 13.31 C ANISOU 1984 CA VAL B 52 1661 1829 1566 -172 156 -170 C ATOM 1985 C VAL B 52 -10.983 -16.987 -6.100 1.00 14.62 C ANISOU 1985 C VAL B 52 1840 1997 1718 -144 131 -152 C ATOM 1986 O VAL B 52 -10.878 -16.623 -7.279 1.00 14.19 O ANISOU 1986 O VAL B 52 1791 1943 1659 -142 95 -145 O ATOM 1987 CB VAL B 52 -11.585 -19.442 -6.060 1.00 13.35 C ANISOU 1987 CB VAL B 52 1706 1820 1546 -189 170 -164 C ATOM 1988 CG1 VAL B 52 -10.130 -19.664 -5.677 1.00 13.93 C ANISOU 1988 CG1 VAL B 52 1819 1883 1590 -172 184 -144 C ATOM 1989 CG2 VAL B 52 -12.492 -20.465 -5.436 1.00 15.38 C ANISOU 1989 CG2 VAL B 52 1956 2071 1817 -220 200 -176 C ATOM 1990 N VAL B 53 -10.203 -16.526 -5.136 1.00 13.21 N ANISOU 1990 N VAL B 53 1670 1818 1530 -126 148 -144 N ATOM 1991 CA AVAL B 53 -9.010 -15.703 -5.360 0.50 13.21 C ANISOU 1991 CA AVAL B 53 1685 1816 1518 -103 132 -126 C ATOM 1992 CA BVAL B 53 -9.026 -15.737 -5.472 0.50 13.73 C ANISOU 1992 CA BVAL B 53 1751 1882 1583 -104 130 -125 C ATOM 1993 C VAL B 53 -7.754 -16.574 -5.297 1.00 13.77 C ANISOU 1993 C VAL B 53 1794 1876 1561 -100 150 -112 C ATOM 1994 O VAL B 53 -7.614 -17.391 -4.373 1.00 13.31 O ANISOU 1994 O VAL B 53 1753 1810 1496 -105 174 -111 O ATOM 1995 CB AVAL B 53 -8.861 -14.619 -4.270 0.50 11.85 C ANISOU 1995 CB AVAL B 53 1496 1647 1359 -83 134 -130 C ATOM 1996 CB BVAL B 53 -8.965 -14.420 -4.678 0.50 14.56 C ANISOU 1996 CB BVAL B 53 1834 1991 1708 -82 123 -128 C ATOM 1997 CG1AVAL B 53 -7.449 -14.010 -4.298 0.50 10.79 C ANISOU 1997 CG1AVAL B 53 1380 1506 1212 -62 123 -110 C ATOM 1998 CG1BVAL B 53 -8.830 -14.682 -3.229 0.50 15.07 C ANISOU 1998 CG1BVAL B 53 1907 2056 1762 -82 156 -136 C ATOM 1999 CG2AVAL B 53 -9.967 -13.544 -4.443 0.50 11.23 C ANISOU 1999 CG2AVAL B 53 1372 1574 1323 -78 110 -148 C ATOM 2000 CG2BVAL B 53 -7.854 -13.449 -5.222 0.50 15.24 C ANISOU 2000 CG2BVAL B 53 1929 2072 1789 -63 97 -108 C ATOM 2001 N SER B 54 -6.845 -16.378 -6.218 1.00 12.15 N ANISOU 2001 N SER B 54 1603 1669 1346 -93 138 -101 N ATOM 2002 CA SER B 54 -5.588 -17.076 -6.223 1.00 10.75 C ANISOU 2002 CA SER B 54 1450 1478 1156 -86 154 -95 C ATOM 2003 C SER B 54 -4.486 -16.161 -6.796 1.00 12.89 C ANISOU 2003 C SER B 54 1720 1750 1426 -73 145 -84 C ATOM 2004 O SER B 54 -4.711 -14.949 -6.922 1.00 13.20 O ANISOU 2004 O SER B 54 1744 1798 1472 -67 124 -76 O ATOM 2005 CB SER B 54 -5.736 -18.394 -6.996 1.00 14.50 C ANISOU 2005 CB SER B 54 1944 1945 1621 -104 166 -106 C ATOM 2006 OG SER B 54 -4.556 -19.189 -6.936 1.00 14.14 O ANISOU 2006 OG SER B 54 1917 1880 1577 -95 182 -107 O ATOM 2007 N ALA B 55 -3.330 -16.721 -7.104 1.00 13.48 N ANISOU 2007 N ALA B 55 1809 1815 1499 -68 161 -85 N ATOM 2008 CA ALA B 55 -2.227 -15.944 -7.659 1.00 12.63 C ANISOU 2008 CA ALA B 55 1698 1709 1393 -61 162 -77 C ATOM 2009 C ALA B 55 -2.251 -15.979 -9.180 1.00 12.91 C ANISOU 2009 C ALA B 55 1747 1756 1403 -84 169 -82 C ATOM 2010 O ALA B 55 -2.612 -16.979 -9.780 1.00 14.11 O ANISOU 2010 O ALA B 55 1915 1908 1539 -99 181 -98 O ATOM 2011 CB ALA B 55 -0.912 -16.497 -7.184 1.00 14.53 C ANISOU 2011 CB ALA B 55 1938 1930 1655 -44 179 -82 C ATOM 2012 N GLY B 56 -1.808 -14.895 -9.812 1.00 13.24 N ANISOU 2012 N GLY B 56 1788 1806 1437 -90 162 -67 N ATOM 2013 CA GLY B 56 -1.734 -14.875 -11.246 1.00 14.59 C ANISOU 2013 CA GLY B 56 1983 1989 1571 -119 171 -68 C ATOM 2014 C GLY B 56 -0.759 -15.855 -11.844 1.00 14.01 C ANISOU 2014 C GLY B 56 1922 1914 1489 -127 216 -93 C ATOM 2015 O GLY B 56 -0.984 -16.352 -12.958 1.00 15.40 O ANISOU 2015 O GLY B 56 2124 2100 1627 -154 229 -107 O ATOM 2016 N HIS B 57 0.317 -16.139 -11.143 1.00 14.33 N ANISOU 2016 N HIS B 57 1940 1937 1565 -104 238 -103 N ATOM 2017 CA HIS B 57 1.261 -17.141 -11.664 1.00 14.71 C ANISOU 2017 CA HIS B 57 1990 1976 1621 -107 282 -135 C ATOM 2018 C HIS B 57 0.752 -18.572 -11.575 1.00 16.72 C ANISOU 2018 C HIS B 57 2256 2217 1879 -105 287 -160 C ATOM 2019 O HIS B 57 1.374 -19.453 -12.181 1.00 19.10 O ANISOU 2019 O HIS B 57 2561 2510 2186 -110 322 -194 O ATOM 2020 CB HIS B 57 2.638 -17.000 -11.057 1.00 16.49 C ANISOU 2020 CB HIS B 57 2184 2185 1898 -84 299 -141 C ATOM 2021 CG HIS B 57 2.737 -17.509 -9.667 1.00 15.70 C ANISOU 2021 CG HIS B 57 2068 2058 1840 -51 275 -138 C ATOM 2022 ND1 HIS B 57 2.666 -16.694 -8.553 1.00 16.81 N ANISOU 2022 ND1 HIS B 57 2196 2195 1996 -33 241 -112 N ATOM 2023 CD2 HIS B 57 2.962 -18.772 -9.215 1.00 17.82 C ANISOU 2023 CD2 HIS B 57 2335 2300 2138 -35 278 -158 C ATOM 2024 CE1 HIS B 57 2.782 -17.465 -7.462 1.00 16.90 C ANISOU 2024 CE1 HIS B 57 2206 2181 2035 -11 224 -114 C ATOM 2025 NE2 HIS B 57 3.010 -18.722 -7.846 1.00 17.72 N ANISOU 2025 NE2 HIS B 57 2315 2268 2151 -11 244 -139 N ATOM 2026 N CYS B 58 -0.387 -18.770 -10.939 1.00 15.34 N ANISOU 2026 N CYS B 58 2086 2041 1702 -102 256 -147 N ATOM 2027 CA CYS B 58 -1.117 -20.046 -10.943 1.00 15.63 C ANISOU 2027 CA CYS B 58 2137 2065 1737 -109 256 -166 C ATOM 2028 C CYS B 58 -2.051 -20.240 -12.111 1.00 16.66 C ANISOU 2028 C CYS B 58 2292 2213 1824 -140 252 -177 C ATOM 2029 O CYS B 58 -2.774 -21.229 -12.153 1.00 16.84 O ANISOU 2029 O CYS B 58 2326 2226 1848 -149 247 -193 O ATOM 2030 CB CYS B 58 -1.918 -20.173 -9.659 1.00 15.87 C ANISOU 2030 CB CYS B 58 2160 2085 1785 -97 230 -147 C ATOM 2031 SG CYS B 58 -0.888 -20.305 -8.111 1.00 16.28 S ANISOU 2031 SG CYS B 58 2198 2108 1881 -63 225 -135 S ATOM 2032 N TYR B 59 -2.055 -19.307 -13.047 1.00 15.07 N ANISOU 2032 N TYR B 59 2103 2036 1586 -160 247 -167 N ATOM 2033 CA TYR B 59 -2.937 -19.422 -14.157 1.00 15.62 C ANISOU 2033 CA TYR B 59 2203 2122 1611 -192 231 -174 C ATOM 2034 C TYR B 59 -2.679 -20.686 -14.970 1.00 17.05 C ANISOU 2034 C TYR B 59 2407 2296 1775 -208 264 -217 C ATOM 2035 O TYR B 59 -1.540 -21.004 -15.293 1.00 19.36 O ANISOU 2035 O TYR B 59 2700 2584 2071 -206 309 -242 O ATOM 2036 CB TYR B 59 -2.771 -18.196 -15.085 1.00 16.20 C ANISOU 2036 CB TYR B 59 2296 2218 1642 -214 220 -152 C ATOM 2037 CG TYR B 59 -3.708 -18.305 -16.271 1.00 19.23 C ANISOU 2037 CG TYR B 59 2719 2616 1973 -250 192 -156 C ATOM 2038 CD1 TYR B 59 -5.022 -17.849 -16.192 1.00 21.79 C ANISOU 2038 CD1 TYR B 59 3038 2941 2300 -254 132 -135 C ATOM 2039 CD2 TYR B 59 -3.283 -18.859 -17.436 1.00 22.67 C ANISOU 2039 CD2 TYR B 59 3194 3063 2359 -281 223 -184 C ATOM 2040 CE1 TYR B 59 -5.905 -17.978 -17.242 1.00 24.45 C ANISOU 2040 CE1 TYR B 59 3409 3288 2595 -286 94 -138 C ATOM 2041 CE2 TYR B 59 -4.170 -19.038 -18.500 1.00 22.34 C ANISOU 2041 CE2 TYR B 59 3194 3033 2263 -317 190 -189 C ATOM 2042 CZ TYR B 59 -5.465 -18.591 -18.394 1.00 24.46 C ANISOU 2042 CZ TYR B 59 3457 3300 2538 -318 121 -164 C ATOM 2043 OH TYR B 59 -6.347 -18.745 -19.479 1.00 29.65 O ANISOU 2043 OH TYR B 59 4157 3965 3145 -354 77 -168 O ATOM 2044 N LYS B 60 -3.787 -21.371 -15.270 1.00 17.49 N ANISOU 2044 N LYS B 60 2478 2350 1818 -225 240 -229 N ATOM 2045 CA LYS B 60 -3.849 -22.462 -16.254 1.00 17.77 C ANISOU 2045 CA LYS B 60 2543 2381 1826 -248 259 -272 C ATOM 2046 C LYS B 60 -5.193 -22.236 -16.955 1.00 19.99 C ANISOU 2046 C LYS B 60 2847 2678 2069 -278 208 -263 C ATOM 2047 O LYS B 60 -6.107 -21.605 -16.399 1.00 22.29 O ANISOU 2047 O LYS B 60 3117 2972 2379 -272 164 -232 O ATOM 2048 CB LYS B 60 -3.778 -23.838 -15.575 1.00 18.88 C ANISOU 2048 CB LYS B 60 2670 2487 2015 -231 275 -299 C ATOM 2049 CG LYS B 60 -2.397 -24.205 -14.989 1.00 19.36 C ANISOU 2049 CG LYS B 60 2710 2525 2122 -201 316 -313 C ATOM 2050 CD LYS B 60 -2.372 -25.642 -14.356 1.00 24.11 C ANISOU 2050 CD LYS B 60 3305 3082 2775 -186 321 -336 C ATOM 2051 CE LYS B 60 -0.969 -26.167 -14.052 1.00 25.37 C ANISOU 2051 CE LYS B 60 3444 3210 2985 -157 355 -362 C ATOM 2052 NZ LYS B 60 -0.212 -26.445 -15.301 1.00 25.87 N ANISOU 2052 NZ LYS B 60 3519 3282 3029 -171 402 -414 N ATOM 2053 N SER B 61 -5.334 -22.704 -18.201 1.00 22.64 N ANISOU 2053 N SER B 61 3226 3025 2354 -312 211 -293 N ATOM 2054 CA SER B 61 -6.570 -22.408 -18.930 1.00 22.92 C ANISOU 2054 CA SER B 61 3285 3073 2352 -341 150 -282 C ATOM 2055 C SER B 61 -7.793 -23.210 -18.413 1.00 21.35 C ANISOU 2055 C SER B 61 3062 2854 2196 -339 116 -291 C ATOM 2056 O SER B 61 -8.915 -22.768 -18.597 1.00 26.39 O ANISOU 2056 O SER B 61 3696 3498 2833 -352 57 -274 O ATOM 2057 CB SER B 61 -6.430 -22.728 -20.423 1.00 30.56 C ANISOU 2057 CB SER B 61 4313 4056 3242 -384 157 -313 C ATOM 2058 OG SER B 61 -5.873 -24.003 -20.608 1.00 33.54 O ANISOU 2058 OG SER B 61 4699 4419 3626 -385 209 -367 O ATOM 2059 N ARG B 62 -7.548 -24.313 -17.748 1.00 23.69 N ANISOU 2059 N ARG B 62 3341 3125 2535 -324 150 -316 N ATOM 2060 CA ARG B 62 -8.626 -25.038 -17.039 1.00 22.11 C ANISOU 2060 CA ARG B 62 3114 2904 2384 -323 126 -319 C ATOM 2061 C ARG B 62 -8.086 -25.472 -15.670 1.00 19.47 C ANISOU 2061 C ARG B 62 2749 2544 2104 -292 161 -309 C ATOM 2062 O ARG B 62 -6.919 -25.850 -15.495 1.00 21.32 O ANISOU 2062 O ARG B 62 2988 2765 2347 -274 202 -322 O ATOM 2063 CB ARG B 62 -9.164 -26.209 -17.924 1.00 24.42 C ANISOU 2063 CB ARG B 62 3436 3183 2660 -354 116 -363 C ATOM 2064 CG ARG B 62 -9.882 -25.752 -19.293 1.00 20.35 C ANISOU 2064 CG ARG B 62 2958 2692 2082 -391 64 -368 C ATOM 2065 CD ARG B 62 -11.440 -25.586 -19.216 1.00 28.19 C ANISOU 2065 CD ARG B 62 3925 3682 3102 -406 -5 -355 C ATOM 2066 NE ARG B 62 -12.011 -24.470 -18.399 1.00 24.42 N ANISOU 2066 NE ARG B 62 3401 3213 2665 -386 -35 -312 N ATOM 2067 CZ ARG B 62 -12.258 -23.220 -18.813 1.00 32.14 C ANISOU 2067 CZ ARG B 62 4382 4210 3622 -388 -82 -282 C ATOM 2068 NH1 ARG B 62 -11.923 -22.764 -20.021 1.00 30.19 N ANISOU 2068 NH1 ARG B 62 4189 3979 3302 -411 -105 -279 N ATOM 2069 NH2 ARG B 62 -12.819 -22.370 -17.961 1.00 32.24 N ANISOU 2069 NH2 ARG B 62 4344 4221 3685 -367 -104 -254 N ATOM 2070 N ILE B 63 -8.946 -25.356 -14.649 1.00 18.74 N ANISOU 2070 N ILE B 63 2624 2446 2052 -287 143 -287 N ATOM 2071 CA ILE B 63 -8.592 -25.635 -13.265 1.00 16.71 C ANISOU 2071 CA ILE B 63 2344 2167 1836 -264 167 -270 C ATOM 2072 C ILE B 63 -9.797 -26.280 -12.593 1.00 16.28 C ANISOU 2072 C ILE B 63 2272 2097 1817 -281 156 -268 C ATOM 2073 O ILE B 63 -10.922 -25.786 -12.702 1.00 18.79 O ANISOU 2073 O ILE B 63 2567 2431 2140 -296 126 -264 O ATOM 2074 CB ILE B 63 -8.231 -24.328 -12.537 1.00 15.73 C ANISOU 2074 CB ILE B 63 2200 2063 1715 -240 166 -235 C ATOM 2075 CG1 ILE B 63 -6.993 -23.678 -13.151 1.00 16.78 C ANISOU 2075 CG1 ILE B 63 2348 2208 1819 -226 182 -235 C ATOM 2076 CG2 ILE B 63 -8.005 -24.576 -11.073 1.00 19.34 C ANISOU 2076 CG2 ILE B 63 2642 2501 2207 -222 185 -217 C ATOM 2077 CD1 ILE B 63 -6.564 -22.334 -12.506 1.00 17.89 C ANISOU 2077 CD1 ILE B 63 2469 2365 1965 -204 178 -202 C ATOM 2078 N GLN B 64 -9.551 -27.353 -11.865 1.00 15.92 N ANISOU 2078 N GLN B 64 2232 2018 1799 -280 178 -271 N ATOM 2079 CA GLN B 64 -10.578 -27.942 -11.020 1.00 16.52 C ANISOU 2079 CA GLN B 64 2292 2078 1908 -301 177 -263 C ATOM 2080 C GLN B 64 -10.324 -27.452 -9.610 1.00 15.93 C ANISOU 2080 C GLN B 64 2205 2004 1844 -284 195 -229 C ATOM 2081 O GLN B 64 -9.223 -27.583 -9.085 1.00 16.74 O ANISOU 2081 O GLN B 64 2324 2090 1947 -261 209 -217 O ATOM 2082 CB GLN B 64 -10.515 -29.448 -11.035 1.00 17.17 C ANISOU 2082 CB GLN B 64 2395 2116 2011 -316 187 -282 C ATOM 2083 CG GLN B 64 -11.603 -30.058 -10.202 1.00 18.69 C ANISOU 2083 CG GLN B 64 2574 2291 2236 -346 190 -271 C ATOM 2084 CD GLN B 64 -11.615 -31.537 -10.321 1.00 21.84 C ANISOU 2084 CD GLN B 64 2996 2642 2659 -366 193 -289 C ATOM 2085 OE1 GLN B 64 -10.949 -32.229 -9.583 1.00 23.48 O ANISOU 2085 OE1 GLN B 64 3224 2812 2884 -357 206 -273 O ATOM 2086 NE2 GLN B 64 -12.328 -32.038 -11.314 1.00 27.74 N ANISOU 2086 NE2 GLN B 64 3743 3386 3411 -391 174 -322 N ATOM 2087 N VAL B 65 -11.307 -26.809 -9.002 1.00 14.81 N ANISOU 2087 N VAL B 65 2033 1882 1713 -295 192 -217 N ATOM 2088 CA VAL B 65 -11.225 -26.328 -7.650 1.00 13.98 C ANISOU 2088 CA VAL B 65 1918 1781 1611 -286 212 -191 C ATOM 2089 C VAL B 65 -11.753 -27.380 -6.692 1.00 16.21 C ANISOU 2089 C VAL B 65 2210 2037 1912 -316 234 -183 C ATOM 2090 O VAL B 65 -12.861 -27.919 -6.860 1.00 16.08 O ANISOU 2090 O VAL B 65 2178 2016 1917 -350 235 -197 O ATOM 2091 CB VAL B 65 -12.037 -25.050 -7.494 1.00 15.73 C ANISOU 2091 CB VAL B 65 2099 2038 1840 -284 203 -191 C ATOM 2092 CG1 VAL B 65 -11.916 -24.540 -6.076 1.00 17.05 C ANISOU 2092 CG1 VAL B 65 2261 2211 2005 -277 228 -172 C ATOM 2093 CG2 VAL B 65 -11.558 -24.010 -8.496 1.00 15.58 C ANISOU 2093 CG2 VAL B 65 2078 2041 1803 -260 174 -193 C ATOM 2094 N ARG B 66 -10.946 -27.720 -5.707 1.00 13.87 N ANISOU 2094 N ARG B 66 1943 1719 1608 -307 248 -158 N ATOM 2095 CA ARG B 66 -11.326 -28.695 -4.708 1.00 15.06 C ANISOU 2095 CA ARG B 66 2115 1840 1766 -339 267 -140 C ATOM 2096 C ARG B 66 -11.499 -28.032 -3.354 1.00 16.17 C ANISOU 2096 C ARG B 66 2256 1999 1888 -345 290 -117 C ATOM 2097 O ARG B 66 -10.552 -27.471 -2.767 1.00 15.87 O ANISOU 2097 O ARG B 66 2236 1964 1830 -316 284 -98 O ATOM 2098 CB ARG B 66 -10.297 -29.810 -4.676 1.00 15.33 C ANISOU 2098 CB ARG B 66 2193 1824 1808 -329 256 -130 C ATOM 2099 CG ARG B 66 -10.205 -30.548 -6.037 1.00 16.36 C ANISOU 2099 CG ARG B 66 2322 1935 1957 -327 241 -164 C ATOM 2100 CD ARG B 66 -9.365 -31.793 -5.943 1.00 17.58 C ANISOU 2100 CD ARG B 66 2514 2032 2135 -321 232 -161 C ATOM 2101 NE ARG B 66 -9.532 -32.573 -7.183 1.00 18.71 N ANISOU 2101 NE ARG B 66 2656 2156 2296 -329 224 -202 N ATOM 2102 CZ ARG B 66 -9.083 -33.815 -7.326 1.00 21.11 C ANISOU 2102 CZ ARG B 66 2986 2404 2632 -330 215 -213 C ATOM 2103 NH1 ARG B 66 -8.411 -34.419 -6.348 1.00 22.05 N ANISOU 2103 NH1 ARG B 66 3132 2476 2770 -322 207 -182 N ATOM 2104 NH2 ARG B 66 -9.329 -34.493 -8.447 1.00 21.45 N ANISOU 2104 NH2 ARG B 66 3027 2432 2688 -341 210 -256 N ATOM 2105 N LEU B 67 -12.732 -28.062 -2.877 1.00 15.37 N ANISOU 2105 N LEU B 67 2133 1911 1795 -384 317 -123 N ATOM 2106 CA LEU B 67 -13.128 -27.411 -1.638 1.00 14.74 C ANISOU 2106 CA LEU B 67 2049 1855 1697 -398 350 -112 C ATOM 2107 C LEU B 67 -13.399 -28.460 -0.584 1.00 17.05 C ANISOU 2107 C LEU B 67 2384 2120 1976 -445 379 -86 C ATOM 2108 O LEU B 67 -13.664 -29.632 -0.904 1.00 17.69 O ANISOU 2108 O LEU B 67 2481 2166 2076 -473 375 -83 O ATOM 2109 CB LEU B 67 -14.389 -26.561 -1.839 1.00 15.37 C ANISOU 2109 CB LEU B 67 2065 1974 1803 -410 367 -145 C ATOM 2110 CG LEU B 67 -14.342 -25.600 -3.039 1.00 17.52 C ANISOU 2110 CG LEU B 67 2297 2267 2094 -372 328 -167 C ATOM 2111 CD1 LEU B 67 -14.990 -26.139 -4.299 1.00 19.24 C ANISOU 2111 CD1 LEU B 67 2492 2476 2342 -385 302 -190 C ATOM 2112 CD2 LEU B 67 -14.914 -24.266 -2.616 1.00 23.80 C ANISOU 2112 CD2 LEU B 67 3045 3098 2900 -362 340 -185 C ATOM 2113 N GLY B 69 -13.300 -28.084 0.684 1.00 16.20 N ANISOU 2113 N GLY B 69 2301 2022 1830 -458 405 -67 N ATOM 2114 CA GLY B 69 -13.633 -28.991 1.751 1.00 16.98 C ANISOU 2114 CA GLY B 69 2448 2099 1906 -512 436 -38 C ATOM 2115 C GLY B 69 -12.533 -30.027 2.033 1.00 19.03 C ANISOU 2115 C GLY B 69 2778 2303 2150 -507 399 5 C ATOM 2116 O GLY B 69 -12.799 -31.062 2.651 1.00 22.04 O ANISOU 2116 O GLY B 69 3205 2649 2521 -555 411 34 O ATOM 2117 N GLU B 70 -11.337 -29.794 1.528 1.00 16.09 N ANISOU 2117 N GLU B 70 2412 1917 1784 -452 353 8 N ATOM 2118 CA GLU B 70 -10.231 -30.736 1.651 1.00 17.05 C ANISOU 2118 CA GLU B 70 2587 1981 1911 -437 310 40 C ATOM 2119 C GLU B 70 -9.447 -30.519 2.935 1.00 18.61 C ANISOU 2119 C GLU B 70 2840 2168 2063 -434 294 80 C ATOM 2120 O GLU B 70 -9.140 -29.371 3.316 1.00 18.73 O ANISOU 2120 O GLU B 70 2844 2221 2052 -410 297 74 O ATOM 2121 CB GLU B 70 -9.242 -30.514 0.488 1.00 17.90 C ANISOU 2121 CB GLU B 70 2667 2081 2053 -377 272 16 C ATOM 2122 CG GLU B 70 -9.717 -30.992 -0.857 1.00 19.53 C ANISOU 2122 CG GLU B 70 2838 2283 2298 -377 272 -20 C ATOM 2123 CD GLU B 70 -9.638 -32.474 -1.007 1.00 21.36 C ANISOU 2123 CD GLU B 70 3103 2453 2559 -398 257 -10 C ATOM 2124 OE1 GLU B 70 -9.608 -32.937 -2.171 1.00 22.02 O ANISOU 2124 OE1 GLU B 70 3167 2523 2677 -386 246 -43 O ATOM 2125 OE2 GLU B 70 -9.544 -33.183 0.021 1.00 19.28 O ANISOU 2125 OE2 GLU B 70 2889 2150 2284 -425 251 30 O ATOM 2126 N HIS B 71 -9.026 -31.620 3.536 1.00 19.78 N ANISOU 2126 N HIS B 71 3051 2258 2207 -455 267 121 N ATOM 2127 CA HIS B 71 -7.967 -31.599 4.529 1.00 19.34 C ANISOU 2127 CA HIS B 71 3054 2175 2121 -441 224 163 C ATOM 2128 C HIS B 71 -6.791 -32.453 4.051 1.00 18.86 C ANISOU 2128 C HIS B 71 3006 2046 2112 -401 160 174 C ATOM 2129 O HIS B 71 -5.703 -31.952 3.819 1.00 18.56 O ANISOU 2129 O HIS B 71 2952 2005 2095 -346 124 165 O ATOM 2130 CB HIS B 71 -8.406 -32.087 5.916 1.00 22.18 C ANISOU 2130 CB HIS B 71 3489 2519 2420 -505 238 211 C ATOM 2131 CG HIS B 71 -7.323 -31.905 6.915 1.00 22.80 C ANISOU 2131 CG HIS B 71 3628 2574 2461 -489 185 251 C ATOM 2132 ND1 HIS B 71 -6.695 -32.947 7.563 1.00 31.33 N ANISOU 2132 ND1 HIS B 71 4784 3583 3537 -504 128 306 N ATOM 2133 CD2 HIS B 71 -6.635 -30.794 7.241 1.00 21.50 C ANISOU 2133 CD2 HIS B 71 3455 2441 2274 -451 168 242 C ATOM 2134 CE1 HIS B 71 -5.721 -32.458 8.312 1.00 23.69 C ANISOU 2134 CE1 HIS B 71 3853 2608 2540 -479 78 329 C ATOM 2135 NE2 HIS B 71 -5.666 -31.161 8.134 1.00 27.29 N ANISOU 2135 NE2 HIS B 71 4258 3127 2984 -447 103 290 N ATOM 2136 N ASN B 72 -7.039 -33.741 3.847 1.00 19.23 N ANISOU 2136 N ASN B 72 3078 2038 2190 -427 149 188 N ATOM 2137 CA ASN B 72 -6.112 -34.654 3.210 1.00 17.74 C ANISOU 2137 CA ASN B 72 2891 1782 2068 -390 97 184 C ATOM 2138 C ASN B 72 -6.439 -34.714 1.722 1.00 18.30 C ANISOU 2138 C ASN B 72 2897 1870 2186 -370 122 125 C ATOM 2139 O ASN B 72 -7.520 -35.203 1.346 1.00 19.52 O ANISOU 2139 O ASN B 72 3043 2030 2346 -411 155 113 O ATOM 2140 CB ASN B 72 -6.247 -36.009 3.886 1.00 20.57 C ANISOU 2140 CB ASN B 72 3318 2066 2433 -434 68 232 C ATOM 2141 CG ASN B 72 -5.242 -36.942 3.434 1.00 20.86 C ANISOU 2141 CG ASN B 72 3359 2024 2542 -395 7 231 C ATOM 2142 OD1 ASN B 72 -4.950 -37.001 2.241 1.00 19.96 O ANISOU 2142 OD1 ASN B 72 3190 1910 2484 -355 11 178 O ATOM 2143 ND2 ASN B 72 -4.702 -37.738 4.367 1.00 26.97 N ANISOU 2143 ND2 ASN B 72 4202 2725 3319 -407 -53 287 N ATOM 2144 N ILE B 73 -5.547 -34.161 0.887 1.00 19.91 N ANISOU 2144 N ILE B 73 3057 2086 2421 -312 108 89 N ATOM 2145 CA ILE B 73 -5.794 -34.105 -0.555 1.00 19.40 C ANISOU 2145 CA ILE B 73 2939 2044 2387 -295 131 33 C ATOM 2146 C ILE B 73 -5.578 -35.416 -1.270 1.00 19.97 C ANISOU 2146 C ILE B 73 3018 2053 2519 -293 112 12 C ATOM 2147 O ILE B 73 -5.923 -35.508 -2.453 1.00 21.05 O ANISOU 2147 O ILE B 73 3119 2205 2673 -290 132 -35 O ATOM 2148 CB ILE B 73 -4.996 -32.996 -1.267 1.00 20.57 C ANISOU 2148 CB ILE B 73 3041 2235 2539 -244 133 -1 C ATOM 2149 CG1 ILE B 73 -3.514 -33.106 -0.918 1.00 18.48 C ANISOU 2149 CG1 ILE B 73 2786 1927 2309 -199 88 10 C ATOM 2150 CG2 ILE B 73 -5.630 -31.626 -0.956 1.00 22.04 C ANISOU 2150 CG2 ILE B 73 3207 2495 2674 -253 164 2 C ATOM 2151 CD1 ILE B 73 -2.629 -32.167 -1.820 1.00 21.42 C ANISOU 2151 CD1 ILE B 73 3107 2333 2698 -151 96 -30 C ATOM 2152 N GLU B 74 -5.069 -36.449 -0.557 1.00 19.11 N ANISOU 2152 N GLU B 74 2955 1868 2439 -297 69 48 N ATOM 2153 CA GLU B 74 -4.809 -37.766 -1.174 1.00 21.12 C ANISOU 2153 CA GLU B 74 3215 2048 2760 -292 45 27 C ATOM 2154 C GLU B 74 -5.976 -38.633 -0.925 1.00 23.15 C ANISOU 2154 C GLU B 74 3504 2282 3011 -353 58 48 C ATOM 2155 O GLU B 74 -6.361 -39.735 -1.788 1.00 28.96 O ANISOU 2155 O GLU B 74 4233 2971 3797 -368 58 13 O ATOM 2156 CB GLU B 74 -3.598 -38.464 -0.570 1.00 21.20 C ANISOU 2156 CB GLU B 74 3256 1976 2822 -260 -19 53 C ATOM 2157 CG GLU B 74 -3.145 -39.670 -1.415 1.00 35.18 C ANISOU 2157 CG GLU B 74 5016 3672 4678 -239 -42 12 C ATOM 2158 CD GLU B 74 -3.509 -41.012 -0.823 1.00 43.19 C ANISOU 2158 CD GLU B 74 6085 4601 5723 -277 -79 53 C ATOM 2159 OE1 GLU B 74 -3.745 -41.960 -1.637 1.00 41.58 O ANISOU 2159 OE1 GLU B 74 5872 4353 5572 -282 -77 13 O ATOM 2160 OE2 GLU B 74 -3.531 -41.136 0.434 1.00 49.03 O ANISOU 2160 OE2 GLU B 74 6882 5314 6433 -304 -113 123 O ATOM 2161 N VAL B 75 -6.955 -38.521 0.235 1.00 22.03 N ANISOU 2161 N VAL B 75 3402 2159 2809 -416 79 103 N ATOM 2162 CA VAL B 75 -7.964 -39.470 0.704 1.00 23.70 C ANISOU 2162 CA VAL B 75 3653 2336 3017 -484 90 134 C ATOM 2163 C VAL B 75 -9.341 -38.774 0.572 1.00 23.30 C ANISOU 2163 C VAL B 75 3567 2362 2922 -528 156 116 C ATOM 2164 O VAL B 75 -9.472 -37.606 0.929 1.00 21.47 O ANISOU 2164 O VAL B 75 3316 2198 2642 -521 183 117 O ATOM 2165 CB VAL B 75 -7.686 -39.757 2.192 1.00 25.28 C ANISOU 2165 CB VAL B 75 3929 2497 3181 -514 60 210 C ATOM 2166 CG1 VAL B 75 -8.752 -40.656 2.739 1.00 31.01 C ANISOU 2166 CG1 VAL B 75 4699 3191 3893 -593 81 247 C ATOM 2167 CG2 VAL B 75 -6.305 -40.388 2.384 1.00 30.37 C ANISOU 2167 CG2 VAL B 75 4604 3058 3876 -466 -17 230 C ATOM 2168 N LEU B 76 -10.357 -39.411 0.020 1.00 23.68 N ANISOU 2168 N LEU B 76 3599 2403 2996 -569 180 95 N ATOM 2169 CA LEU B 76 -11.727 -38.903 0.119 1.00 25.71 C ANISOU 2169 CA LEU B 76 3825 2721 3223 -620 237 85 C ATOM 2170 C LEU B 76 -12.169 -39.042 1.558 1.00 27.71 C ANISOU 2170 C LEU B 76 4131 2968 3428 -681 261 145 C ATOM 2171 O LEU B 76 -12.168 -40.159 2.118 1.00 29.46 O ANISOU 2171 O LEU B 76 4412 3122 3661 -721 242 188 O ATOM 2172 CB LEU B 76 -12.690 -39.739 -0.720 1.00 26.45 C ANISOU 2172 CB LEU B 76 3893 2794 3363 -657 248 52 C ATOM 2173 CG LEU B 76 -12.698 -39.485 -2.198 1.00 27.03 C ANISOU 2173 CG LEU B 76 3911 2892 3468 -618 240 -15 C ATOM 2174 CD1 LEU B 76 -13.668 -40.495 -2.855 1.00 31.13 C ANISOU 2174 CD1 LEU B 76 4416 3377 4033 -664 243 -42 C ATOM 2175 CD2 LEU B 76 -13.061 -38.075 -2.553 1.00 27.96 C ANISOU 2175 CD2 LEU B 76 3974 3096 3554 -597 266 -43 C ATOM 2176 N GLU B 77 -12.580 -37.945 2.154 1.00 22.57 N ANISOU 2176 N GLU B 77 3464 2386 2724 -691 303 147 N ATOM 2177 CA GLU B 77 -12.966 -37.918 3.559 1.00 23.72 C ANISOU 2177 CA GLU B 77 3664 2538 2811 -750 336 197 C ATOM 2178 C GLU B 77 -14.467 -37.650 3.751 1.00 26.21 C ANISOU 2178 C GLU B 77 3941 2904 3115 -815 413 177 C ATOM 2179 O GLU B 77 -15.011 -37.849 4.846 1.00 31.15 O ANISOU 2179 O GLU B 77 4610 3531 3695 -883 455 213 O ATOM 2180 CB GLU B 77 -12.183 -36.821 4.272 1.00 29.78 C ANISOU 2180 CB GLU B 77 4448 3344 3522 -713 328 212 C ATOM 2181 CG GLU B 77 -10.692 -36.848 3.983 1.00 30.78 C ANISOU 2181 CG GLU B 77 4592 3433 3672 -641 255 219 C ATOM 2182 CD GLU B 77 -10.043 -35.417 3.982 1.00 29.83 C ANISOU 2182 CD GLU B 77 4439 3372 3524 -583 252 197 C ATOM 2183 OE1 GLU B 77 -9.453 -35.150 5.057 1.00 30.51 O ANISOU 2183 OE1 GLU B 77 4579 3453 3561 -585 233 238 O ATOM 2184 OE2 GLU B 77 -10.092 -34.581 2.964 1.00 22.38 O ANISOU 2184 OE2 GLU B 77 3424 2476 2604 -539 265 144 O ATOM 2185 N GLY B 78 -15.108 -37.202 2.689 1.00 23.92 N ANISOU 2185 N GLY B 78 3569 2653 2867 -796 429 118 N ATOM 2186 CA GLY B 78 -16.538 -37.096 2.612 1.00 26.23 C ANISOU 2186 CA GLY B 78 3808 2981 3177 -851 489 89 C ATOM 2187 C GLY B 78 -17.142 -35.701 2.598 1.00 22.45 C ANISOU 2187 C GLY B 78 3261 2583 2688 -837 532 46 C ATOM 2188 O GLY B 78 -18.376 -35.580 2.496 1.00 27.56 O ANISOU 2188 O GLY B 78 3851 3258 3363 -879 580 15 O ATOM 2189 N ASN B 79 -16.306 -34.676 2.705 1.00 20.60 N ANISOU 2189 N ASN B 79 3028 2380 2421 -778 513 44 N ATOM 2190 CA ASN B 79 -16.765 -33.281 2.710 1.00 20.79 C ANISOU 2190 CA ASN B 79 2988 2473 2437 -757 545 5 C ATOM 2191 C ASN B 79 -16.296 -32.491 1.497 1.00 21.11 C ANISOU 2191 C ASN B 79 2978 2536 2508 -683 499 -32 C ATOM 2192 O ASN B 79 -16.530 -31.284 1.396 1.00 20.94 O ANISOU 2192 O ASN B 79 2906 2564 2485 -657 511 -61 O ATOM 2193 CB ASN B 79 -16.321 -32.561 3.976 1.00 23.90 C ANISOU 2193 CB ASN B 79 3425 2893 2762 -759 570 30 C ATOM 2194 CG ASN B 79 -16.867 -33.230 5.220 1.00 28.59 C ANISOU 2194 CG ASN B 79 4076 3475 3313 -842 624 66 C ATOM 2195 OD1 ASN B 79 -18.060 -33.550 5.318 1.00 29.22 O ANISOU 2195 OD1 ASN B 79 4122 3565 3416 -902 681 47 O ATOM 2196 ND2 ASN B 79 -15.990 -33.470 6.168 1.00 35.09 N ANISOU 2196 ND2 ASN B 79 4987 4273 4074 -848 604 118 N ATOM 2197 N GLU B 80 -15.658 -33.185 0.560 1.00 20.36 N ANISOU 2197 N GLU B 80 2896 2400 2439 -654 448 -31 N ATOM 2198 CA GLU B 80 -15.109 -32.542 -0.627 1.00 17.32 C ANISOU 2198 CA GLU B 80 2475 2032 2072 -591 406 -63 C ATOM 2199 C GLU B 80 -16.209 -32.082 -1.577 1.00 18.14 C ANISOU 2199 C GLU B 80 2506 2171 2217 -597 411 -110 C ATOM 2200 O GLU B 80 -17.246 -32.760 -1.758 1.00 20.08 O ANISOU 2200 O GLU B 80 2729 2404 2497 -644 428 -125 O ATOM 2201 CB GLU B 80 -14.178 -33.485 -1.391 1.00 21.16 C ANISOU 2201 CB GLU B 80 2995 2466 2577 -565 359 -58 C ATOM 2202 CG GLU B 80 -12.927 -33.949 -0.651 1.00 21.74 C ANISOU 2202 CG GLU B 80 3135 2496 2628 -547 335 -15 C ATOM 2203 CD GLU B 80 -13.122 -35.176 0.198 1.00 21.59 C ANISOU 2203 CD GLU B 80 3172 2422 2609 -599 340 25 C ATOM 2204 OE1 GLU B 80 -14.238 -35.719 0.355 1.00 21.30 O ANISOU 2204 OE1 GLU B 80 3127 2381 2585 -658 373 24 O ATOM 2205 OE2 GLU B 80 -12.097 -35.620 0.720 1.00 23.25 O ANISOU 2205 OE2 GLU B 80 3437 2589 2810 -582 307 61 O ATOM 2206 N GLN B 81 -15.927 -30.969 -2.225 1.00 17.92 N ANISOU 2206 N GLN B 81 2443 2178 2186 -549 389 -133 N ATOM 2207 CA GLN B 81 -16.664 -30.529 -3.416 1.00 17.10 C ANISOU 2207 CA GLN B 81 2280 2097 2119 -540 367 -174 C ATOM 2208 C GLN B 81 -15.623 -30.288 -4.492 1.00 16.55 C ANISOU 2208 C GLN B 81 2226 2025 2037 -488 320 -181 C ATOM 2209 O GLN B 81 -14.661 -29.554 -4.273 1.00 18.58 O ANISOU 2209 O GLN B 81 2499 2295 2264 -449 313 -166 O ATOM 2210 CB GLN B 81 -17.492 -29.269 -3.158 1.00 16.03 C ANISOU 2210 CB GLN B 81 2083 2009 1996 -537 386 -196 C ATOM 2211 CG GLN B 81 -18.546 -29.487 -2.081 1.00 18.06 C ANISOU 2211 CG GLN B 81 2319 2273 2268 -592 445 -198 C ATOM 2212 CD GLN B 81 -19.284 -28.220 -1.729 1.00 20.74 C ANISOU 2212 CD GLN B 81 2595 2658 2627 -586 470 -227 C ATOM 2213 OE1 GLN B 81 -19.691 -27.467 -2.608 1.00 20.83 O ANISOU 2213 OE1 GLN B 81 2552 2687 2676 -559 434 -257 O ATOM 2214 NE2 GLN B 81 -19.433 -27.955 -0.448 1.00 21.41 N ANISOU 2214 NE2 GLN B 81 2690 2759 2687 -610 528 -220 N ATOM 2215 N PHE B 82 -15.817 -30.892 -5.648 1.00 17.32 N ANISOU 2215 N PHE B 82 2319 2106 2155 -492 290 -205 N ATOM 2216 CA PHE B 82 -14.901 -30.676 -6.750 1.00 17.20 C ANISOU 2216 CA PHE B 82 2320 2092 2123 -452 254 -218 C ATOM 2217 C PHE B 82 -15.708 -29.937 -7.819 1.00 17.06 C ANISOU 2217 C PHE B 82 2259 2107 2118 -450 224 -249 C ATOM 2218 O PHE B 82 -16.703 -30.465 -8.325 1.00 19.28 O ANISOU 2218 O PHE B 82 2517 2379 2430 -483 211 -272 O ATOM 2219 CB PHE B 82 -14.400 -31.977 -7.335 1.00 18.11 C ANISOU 2219 CB PHE B 82 2473 2160 2247 -458 241 -228 C ATOM 2220 CG PHE B 82 -13.522 -32.827 -6.429 1.00 17.97 C ANISOU 2220 CG PHE B 82 2503 2098 2228 -456 254 -197 C ATOM 2221 CD1 PHE B 82 -13.071 -32.402 -5.189 1.00 19.18 C ANISOU 2221 CD1 PHE B 82 2672 2256 2360 -447 273 -160 C ATOM 2222 CD2 PHE B 82 -13.073 -34.051 -6.891 1.00 21.11 C ANISOU 2222 CD2 PHE B 82 2932 2444 2645 -459 240 -209 C ATOM 2223 CE1 PHE B 82 -12.263 -33.210 -4.420 1.00 20.19 C ANISOU 2223 CE1 PHE B 82 2847 2336 2487 -446 272 -129 C ATOM 2224 CE2 PHE B 82 -12.295 -34.886 -6.086 1.00 22.28 C ANISOU 2224 CE2 PHE B 82 3123 2541 2802 -456 241 -180 C ATOM 2225 CZ PHE B 82 -11.884 -34.461 -4.862 1.00 21.47 C ANISOU 2225 CZ PHE B 82 3037 2442 2677 -450 253 -137 C ATOM 2226 N ILE B 83 -15.288 -28.727 -8.147 1.00 16.39 N ANISOU 2226 N ILE B 83 2162 2054 2011 -415 208 -247 N ATOM 2227 CA ILE B 83 -16.028 -27.827 -9.011 1.00 16.02 C ANISOU 2227 CA ILE B 83 2075 2035 1975 -412 171 -267 C ATOM 2228 C ILE B 83 -15.058 -27.260 -10.011 1.00 14.88 C ANISOU 2228 C ILE B 83 1960 1904 1791 -379 142 -267 C ATOM 2229 O ILE B 83 -14.069 -26.620 -9.684 1.00 17.29 O ANISOU 2229 O ILE B 83 2280 2218 2070 -349 154 -248 O ATOM 2230 CB ILE B 83 -16.754 -26.721 -8.257 1.00 17.43 C ANISOU 2230 CB ILE B 83 2203 2242 2177 -408 182 -264 C ATOM 2231 CG1 ILE B 83 -17.695 -27.291 -7.192 1.00 18.29 C ANISOU 2231 CG1 ILE B 83 2285 2342 2321 -447 225 -267 C ATOM 2232 CG2 ILE B 83 -17.536 -25.833 -9.226 1.00 19.74 C ANISOU 2232 CG2 ILE B 83 2454 2555 2493 -402 130 -283 C ATOM 2233 CD1 ILE B 83 -18.289 -26.208 -6.283 1.00 19.25 C ANISOU 2233 CD1 ILE B 83 2357 2492 2464 -443 251 -271 C ATOM 2234 N ASN B 84 -15.349 -27.489 -11.288 1.00 17.65 N ANISOU 2234 N ASN B 84 2318 2254 2134 -391 104 -290 N ATOM 2235 CA ASN B 84 -14.506 -26.955 -12.343 1.00 18.03 C ANISOU 2235 CA ASN B 84 2398 2316 2136 -370 80 -293 C ATOM 2236 C ASN B 84 -14.729 -25.460 -12.555 1.00 18.82 C ANISOU 2236 C ASN B 84 2474 2447 2231 -353 49 -278 C ATOM 2237 O ASN B 84 -15.810 -24.917 -12.311 1.00 21.69 O ANISOU 2237 O ASN B 84 2790 2819 2632 -360 26 -280 O ATOM 2238 CB ASN B 84 -14.722 -27.792 -13.607 1.00 19.71 C ANISOU 2238 CB ASN B 84 2638 2516 2333 -394 52 -325 C ATOM 2239 CG ASN B 84 -14.115 -29.186 -13.475 1.00 19.13 C ANISOU 2239 CG ASN B 84 2598 2407 2263 -402 85 -340 C ATOM 2240 OD1 ASN B 84 -12.907 -29.331 -13.294 1.00 23.38 O ANISOU 2240 OD1 ASN B 84 3163 2937 2783 -378 114 -334 O ATOM 2241 ND2 ASN B 84 -14.958 -30.216 -13.529 1.00 22.80 N ANISOU 2241 ND2 ASN B 84 3056 2847 2761 -434 77 -360 N ATOM 2242 N ALA B 85 -13.686 -24.762 -12.962 1.00 17.75 N ANISOU 2242 N ALA B 85 2366 2325 2054 -330 48 -265 N ATOM 2243 CA ALA B 85 -13.819 -23.371 -13.293 1.00 19.06 C ANISOU 2243 CA ALA B 85 2518 2514 2212 -316 12 -249 C ATOM 2244 C ALA B 85 -14.613 -23.126 -14.568 1.00 20.17 C ANISOU 2244 C ALA B 85 2663 2659 2340 -337 -52 -260 C ATOM 2245 O ALA B 85 -14.418 -23.784 -15.574 1.00 20.79 O ANISOU 2245 O ALA B 85 2783 2734 2380 -356 -64 -277 O ATOM 2246 CB ALA B 85 -12.450 -22.749 -13.417 1.00 19.50 C ANISOU 2246 CB ALA B 85 2605 2579 2226 -292 31 -230 C ATOM 2247 N ALA B 86 -15.511 -22.151 -14.508 1.00 18.58 N ANISOU 2247 N ALA B 86 2420 2465 2175 -332 -97 -251 N ATOM 2248 CA ALA B 86 -16.189 -21.602 -15.675 1.00 18.24 C ANISOU 2248 CA ALA B 86 2383 2425 2123 -347 -175 -251 C ATOM 2249 C ALA B 86 -15.427 -20.477 -16.322 1.00 19.83 C ANISOU 2249 C ALA B 86 2620 2639 2274 -335 -202 -222 C ATOM 2250 O ALA B 86 -15.487 -20.329 -17.549 1.00 22.66 O ANISOU 2250 O ALA B 86 3023 3001 2587 -355 -254 -218 O ATOM 2251 CB ALA B 86 -17.577 -21.091 -15.269 1.00 23.19 C ANISOU 2251 CB ALA B 86 2937 3045 2828 -345 -218 -259 C ATOM 2252 N LYS B 87 -14.789 -19.639 -15.515 1.00 17.48 N ANISOU 2252 N LYS B 87 2308 2348 1987 -306 -171 -200 N ATOM 2253 CA ALYS B 87 -14.033 -18.485 -15.994 0.50 18.59 C ANISOU 2253 CA ALYS B 87 2477 2496 2089 -295 -192 -169 C ATOM 2254 CA BLYS B 87 -13.996 -18.552 -16.045 0.50 17.90 C ANISOU 2254 CA BLYS B 87 2394 2409 1998 -297 -190 -170 C ATOM 2255 C LYS B 87 -12.751 -18.406 -15.170 1.00 16.97 C ANISOU 2255 C LYS B 87 2281 2297 1871 -272 -121 -159 C ATOM 2256 O LYS B 87 -12.773 -18.672 -13.972 1.00 17.76 O ANISOU 2256 O LYS B 87 2345 2392 2009 -255 -80 -167 O ATOM 2257 CB ALYS B 87 -14.834 -17.178 -15.784 0.50 20.64 C ANISOU 2257 CB ALYS B 87 2691 2748 2402 -278 -252 -152 C ATOM 2258 CB BLYS B 87 -14.817 -17.250 -16.074 0.50 20.94 C ANISOU 2258 CB BLYS B 87 2741 2787 2427 -285 -261 -151 C ATOM 2259 CG ALYS B 87 -16.222 -17.202 -16.393 0.50 21.83 C ANISOU 2259 CG ALYS B 87 2816 2888 2592 -295 -330 -165 C ATOM 2260 CG BLYS B 87 -15.818 -17.147 -17.223 0.50 24.60 C ANISOU 2260 CG BLYS B 87 3215 3242 2889 -309 -351 -152 C ATOM 2261 CD ALYS B 87 -16.932 -15.877 -16.338 0.50 25.07 C ANISOU 2261 CD ALYS B 87 3182 3284 3060 -276 -400 -149 C ATOM 2262 CD BLYS B 87 -16.446 -15.762 -17.276 0.50 28.56 C ANISOU 2262 CD BLYS B 87 3682 3729 3439 -293 -427 -129 C ATOM 2263 CE ALYS B 87 -18.367 -15.984 -16.852 0.50 27.17 C ANISOU 2263 CE ALYS B 87 3408 3532 3382 -290 -481 -168 C ATOM 2264 CE BLYS B 87 -17.578 -15.715 -18.299 0.50 31.14 C ANISOU 2264 CE BLYS B 87 4010 4040 3781 -315 -529 -131 C ATOM 2265 NZ ALYS B 87 -18.870 -14.725 -17.504 0.50 27.01 N ANISOU 2265 NZ ALYS B 87 3382 3492 3390 -282 -585 -142 N ATOM 2266 NZ BLYS B 87 -18.322 -16.995 -18.319 0.50 33.37 N ANISOU 2266 NZ BLYS B 87 4273 4323 4084 -335 -518 -171 N ATOM 2267 N ILE B 88 -11.644 -18.012 -15.774 1.00 17.81 N ANISOU 2267 N ILE B 88 2432 2412 1922 -274 -109 -142 N ATOM 2268 CA ILE B 88 -10.387 -17.843 -15.080 1.00 16.88 C ANISOU 2268 CA ILE B 88 2317 2297 1799 -252 -51 -133 C ATOM 2269 C ILE B 88 -9.780 -16.518 -15.563 1.00 19.04 C ANISOU 2269 C ILE B 88 2609 2577 2047 -250 -74 -100 C ATOM 2270 O ILE B 88 -9.500 -16.346 -16.754 1.00 21.34 O ANISOU 2270 O ILE B 88 2949 2877 2282 -277 -93 -90 O ATOM 2271 CB ILE B 88 -9.393 -19.019 -15.323 1.00 17.33 C ANISOU 2271 CB ILE B 88 2409 2355 1822 -261 6 -155 C ATOM 2272 CG1 ILE B 88 -9.984 -20.388 -14.910 1.00 16.96 C ANISOU 2272 CG1 ILE B 88 2349 2294 1800 -267 24 -185 C ATOM 2273 CG2 ILE B 88 -8.109 -18.802 -14.550 1.00 20.16 C ANISOU 2273 CG2 ILE B 88 2760 2711 2187 -235 57 -146 C ATOM 2274 CD1 ILE B 88 -9.184 -21.537 -15.377 1.00 22.46 C ANISOU 2274 CD1 ILE B 88 3081 2984 2470 -277 65 -211 C ATOM 2275 N ILE B 89 -9.673 -15.559 -14.653 1.00 17.16 N ANISOU 2275 N ILE B 89 2336 2334 1849 -223 -76 -83 N ATOM 2276 CA ILE B 89 -9.378 -14.177 -15.031 1.00 16.24 C ANISOU 2276 CA ILE B 89 2228 2216 1725 -221 -113 -49 C ATOM 2277 C ILE B 89 -8.141 -13.723 -14.256 1.00 17.64 C ANISOU 2277 C ILE B 89 2399 2394 1910 -199 -65 -39 C ATOM 2278 O ILE B 89 -8.231 -13.360 -13.079 1.00 17.35 O ANISOU 2278 O ILE B 89 2321 2350 1920 -171 -56 -43 O ATOM 2279 CB ILE B 89 -10.570 -13.223 -14.760 1.00 19.29 C ANISOU 2279 CB ILE B 89 2572 2588 2167 -207 -180 -40 C ATOM 2280 CG1 ILE B 89 -11.845 -13.806 -15.421 1.00 21.19 C ANISOU 2280 CG1 ILE B 89 2810 2825 2416 -227 -229 -56 C ATOM 2281 CG2 ILE B 89 -10.253 -11.814 -15.206 1.00 21.28 C ANISOU 2281 CG2 ILE B 89 2839 2830 2415 -207 -225 -2 C ATOM 2282 CD1 ILE B 89 -13.080 -13.084 -15.107 1.00 24.71 C ANISOU 2282 CD1 ILE B 89 3202 3254 2934 -212 -290 -59 C ATOM 2283 N ARG B 90 -6.986 -13.794 -14.905 1.00 19.17 N ANISOU 2283 N ARG B 90 2631 2596 2055 -214 -32 -32 N ATOM 2284 CA ARG B 90 -5.764 -13.239 -14.367 1.00 18.06 C ANISOU 2284 CA ARG B 90 2483 2454 1924 -199 4 -21 C ATOM 2285 C ARG B 90 -5.832 -11.713 -14.410 1.00 18.15 C ANISOU 2285 C ARG B 90 2488 2456 1951 -195 -41 14 C ATOM 2286 O ARG B 90 -6.452 -11.086 -15.291 1.00 19.33 O ANISOU 2286 O ARG B 90 2661 2602 2082 -216 -97 37 O ATOM 2287 CB ARG B 90 -4.570 -13.754 -15.146 1.00 18.03 C ANISOU 2287 CB ARG B 90 2515 2461 1873 -220 56 -29 C ATOM 2288 CG ARG B 90 -3.173 -13.490 -14.495 1.00 18.89 C ANISOU 2288 CG ARG B 90 2606 2566 2004 -202 104 -28 C ATOM 2289 CD ARG B 90 -2.044 -14.151 -15.320 1.00 23.20 C ANISOU 2289 CD ARG B 90 3179 3122 2514 -225 163 -49 C ATOM 2290 NE ARG B 90 -2.010 -13.730 -16.699 1.00 28.88 N ANISOU 2290 NE ARG B 90 3946 3856 3169 -269 158 -35 N ATOM 2291 CZ ARG B 90 -1.243 -14.224 -17.684 1.00 39.48 C ANISOU 2291 CZ ARG B 90 5323 5213 4464 -301 210 -56 C ATOM 2292 NH1 ARG B 90 -0.373 -15.184 -17.478 1.00 40.21 N ANISOU 2292 NH1 ARG B 90 5398 5303 4576 -290 271 -97 N ATOM 2293 NH2 ARG B 90 -1.344 -13.716 -18.912 1.00 45.55 N ANISOU 2293 NH2 ARG B 90 6146 5996 5164 -348 198 -36 N ATOM 2294 N HIS B 91 -5.233 -11.070 -13.423 1.00 17.03 N ANISOU 2294 N HIS B 91 2317 2305 1847 -168 -27 20 N ATOM 2295 CA HIS B 91 -5.228 -9.613 -13.415 1.00 17.23 C ANISOU 2295 CA HIS B 91 2335 2317 1895 -163 -70 50 C ATOM 2296 C HIS B 91 -4.659 -9.112 -14.730 1.00 16.34 C ANISOU 2296 C HIS B 91 2273 2207 1730 -202 -79 82 C ATOM 2297 O HIS B 91 -3.610 -9.624 -15.184 1.00 18.06 O ANISOU 2297 O HIS B 91 2515 2438 1907 -222 -24 76 O ATOM 2298 CB HIS B 91 -4.384 -9.050 -12.282 1.00 16.36 C ANISOU 2298 CB HIS B 91 2195 2198 1824 -135 -46 49 C ATOM 2299 CG HIS B 91 -4.640 -7.599 -12.058 1.00 16.81 C ANISOU 2299 CG HIS B 91 2235 2234 1920 -124 -96 71 C ATOM 2300 ND1 HIS B 91 -4.107 -6.589 -12.855 1.00 17.46 N ANISOU 2300 ND1 HIS B 91 2343 2304 1987 -146 -120 109 N ATOM 2301 CD2 HIS B 91 -5.469 -6.981 -11.184 1.00 17.62 C ANISOU 2301 CD2 HIS B 91 2297 2321 2077 -95 -129 60 C ATOM 2302 CE1 HIS B 91 -4.585 -5.423 -12.448 1.00 18.30 C ANISOU 2302 CE1 HIS B 91 2426 2385 2143 -128 -172 121 C ATOM 2303 NE2 HIS B 91 -5.429 -5.631 -11.453 1.00 20.54 N ANISOU 2303 NE2 HIS B 91 2666 2666 2470 -96 -178 88 N ATOM 2304 N PRO B 92 -5.333 -8.145 -15.365 1.00 18.18 N ANISOU 2304 N PRO B 92 2521 2424 1961 -216 -148 114 N ATOM 2305 CA PRO B 92 -4.911 -7.756 -16.717 1.00 19.18 C ANISOU 2305 CA PRO B 92 2711 2555 2023 -263 -160 149 C ATOM 2306 C PRO B 92 -3.524 -7.120 -16.798 1.00 19.74 C ANISOU 2306 C PRO B 92 2795 2626 2080 -279 -117 170 C ATOM 2307 O PRO B 92 -2.936 -7.072 -17.890 1.00 23.17 O ANISOU 2307 O PRO B 92 3284 3072 2449 -326 -97 190 O ATOM 2308 CB PRO B 92 -5.977 -6.743 -17.154 1.00 22.15 C ANISOU 2308 CB PRO B 92 3094 2904 2416 -268 -258 184 C ATOM 2309 CG PRO B 92 -6.739 -6.385 -15.973 1.00 21.28 C ANISOU 2309 CG PRO B 92 2917 2775 2393 -220 -286 165 C ATOM 2310 CD PRO B 92 -6.559 -7.450 -14.947 1.00 21.26 C ANISOU 2310 CD PRO B 92 2877 2792 2409 -192 -218 118 C ATOM 2311 N GLN B 93 -3.004 -6.652 -15.675 1.00 18.50 N ANISOU 2311 N GLN B 93 2590 2457 1982 -244 -99 163 N ATOM 2312 CA GLN B 93 -1.695 -6.024 -15.613 1.00 17.83 C ANISOU 2312 CA GLN B 93 2506 2368 1901 -255 -61 179 C ATOM 2313 C GLN B 93 -0.669 -6.887 -14.875 1.00 16.06 C ANISOU 2313 C GLN B 93 2251 2158 1694 -235 14 140 C ATOM 2314 O GLN B 93 0.392 -6.392 -14.458 1.00 17.56 O ANISOU 2314 O GLN B 93 2420 2341 1912 -231 42 144 O ATOM 2315 CB GLN B 93 -1.784 -4.625 -14.997 1.00 19.94 C ANISOU 2315 CB GLN B 93 2747 2603 2226 -235 -112 205 C ATOM 2316 CG GLN B 93 -2.358 -3.594 -15.948 1.00 23.41 C ANISOU 2316 CG GLN B 93 3227 3019 2647 -266 -185 255 C ATOM 2317 CD GLN B 93 -3.827 -3.554 -15.990 1.00 31.82 C ANISOU 2317 CD GLN B 93 4285 4071 3733 -249 -259 254 C ATOM 2318 OE1 GLN B 93 -4.483 -3.365 -14.955 1.00 37.62 O ANISOU 2318 OE1 GLN B 93 4966 4791 4537 -203 -283 229 O ATOM 2319 NE2 GLN B 93 -4.389 -3.660 -17.211 1.00 34.26 N ANISOU 2319 NE2 GLN B 93 4649 4382 3985 -288 -301 281 N ATOM 2320 N TYR B 94 -0.974 -8.181 -14.760 1.00 16.96 N ANISOU 2320 N TYR B 94 2360 2288 1794 -225 42 104 N ATOM 2321 CA TYR B 94 -0.012 -9.156 -14.256 1.00 15.50 C ANISOU 2321 CA TYR B 94 2154 2113 1623 -210 107 69 C ATOM 2322 C TYR B 94 1.288 -9.019 -15.049 1.00 15.78 C ANISOU 2322 C TYR B 94 2207 2157 1633 -245 162 72 C ATOM 2323 O TYR B 94 1.262 -8.985 -16.270 1.00 18.50 O ANISOU 2323 O TYR B 94 2598 2514 1917 -289 172 84 O ATOM 2324 CB TYR B 94 -0.578 -10.585 -14.401 1.00 15.98 C ANISOU 2324 CB TYR B 94 2224 2186 1662 -208 125 35 C ATOM 2325 CG TYR B 94 0.442 -11.645 -14.037 1.00 15.69 C ANISOU 2325 CG TYR B 94 2168 2151 1641 -195 187 -1 C ATOM 2326 CD1 TYR B 94 0.828 -11.825 -12.745 1.00 17.14 C ANISOU 2326 CD1 TYR B 94 2313 2321 1880 -156 191 -13 C ATOM 2327 CD2 TYR B 94 1.055 -12.438 -15.013 1.00 17.13 C ANISOU 2327 CD2 TYR B 94 2375 2347 1786 -223 240 -25 C ATOM 2328 CE1 TYR B 94 1.817 -12.797 -12.398 1.00 19.23 C ANISOU 2328 CE1 TYR B 94 2558 2579 2168 -142 237 -44 C ATOM 2329 CE2 TYR B 94 2.001 -13.380 -14.667 1.00 18.68 C ANISOU 2329 CE2 TYR B 94 2547 2537 2012 -207 291 -62 C ATOM 2330 CZ TYR B 94 2.352 -13.578 -13.359 1.00 20.54 C ANISOU 2330 CZ TYR B 94 2741 2755 2309 -165 285 -70 C ATOM 2331 OH TYR B 94 3.324 -14.497 -12.936 1.00 23.28 O ANISOU 2331 OH TYR B 94 3062 3088 2698 -144 323 -103 O ATOM 2332 N ASP B 95 2.408 -8.969 -14.360 1.00 17.41 N ANISOU 2332 N ASP B 95 2376 2356 1885 -226 198 59 N ATOM 2333 CA ASP B 95 3.723 -8.852 -14.999 1.00 18.06 C ANISOU 2333 CA ASP B 95 2459 2444 1959 -258 258 54 C ATOM 2334 C ASP B 95 4.552 -10.091 -14.670 1.00 17.66 C ANISOU 2334 C ASP B 95 2378 2396 1936 -238 316 4 C ATOM 2335 O ASP B 95 4.905 -10.314 -13.511 1.00 17.10 O ANISOU 2335 O ASP B 95 2264 2309 1926 -196 307 -11 O ATOM 2336 CB ASP B 95 4.455 -7.604 -14.503 1.00 19.37 C ANISOU 2336 CB ASP B 95 2598 2591 2170 -255 246 80 C ATOM 2337 CG ASP B 95 5.707 -7.300 -15.306 1.00 23.23 C ANISOU 2337 CG ASP B 95 3091 3087 2649 -299 308 81 C ATOM 2338 OD1 ASP B 95 6.592 -8.180 -15.457 1.00 20.45 O ANISOU 2338 OD1 ASP B 95 2717 2744 2308 -301 373 40 O ATOM 2339 OD2 ASP B 95 5.845 -6.134 -15.783 1.00 27.65 O ANISOU 2339 OD2 ASP B 95 3671 3639 3195 -333 292 122 O ATOM 2340 N ARG B 96 4.829 -10.889 -15.698 1.00 19.90 N ANISOU 2340 N ARG B 96 2686 2697 2176 -270 369 -23 N ATOM 2341 CA ARG B 96 5.512 -12.181 -15.461 1.00 19.80 C ANISOU 2341 CA ARG B 96 2644 2681 2197 -249 420 -76 C ATOM 2342 C ARG B 96 6.983 -12.092 -15.106 1.00 22.00 C ANISOU 2342 C ARG B 96 2871 2948 2540 -239 466 -98 C ATOM 2343 O ARG B 96 7.560 -13.141 -14.736 1.00 23.87 O ANISOU 2343 O ARG B 96 3074 3173 2824 -212 495 -142 O ATOM 2344 CB ARG B 96 5.325 -13.140 -16.647 1.00 22.57 C ANISOU 2344 CB ARG B 96 3036 3054 2488 -283 465 -109 C ATOM 2345 CG ARG B 96 5.921 -12.679 -17.855 1.00 29.36 C ANISOU 2345 CG ARG B 96 3927 3934 3295 -339 517 -108 C ATOM 2346 CD ARG B 96 5.541 -13.613 -18.990 1.00 43.96 C ANISOU 2346 CD ARG B 96 5826 5805 5072 -373 552 -142 C ATOM 2347 NE ARG B 96 6.725 -14.274 -19.493 1.00 57.15 N ANISOU 2347 NE ARG B 96 7475 7482 6756 -389 644 -199 N ATOM 2348 CZ ARG B 96 7.544 -13.724 -20.380 1.00 65.34 C ANISOU 2348 CZ ARG B 96 8529 8539 7758 -442 708 -202 C ATOM 2349 NH1 ARG B 96 8.618 -14.387 -20.800 1.00 68.23 N ANISOU 2349 NH1 ARG B 96 8867 8910 8147 -455 800 -265 N ATOM 2350 NH2 ARG B 96 7.274 -12.510 -20.859 1.00 68.23 N ANISOU 2350 NH2 ARG B 96 8940 8916 8068 -485 682 -143 N ATOM 2351 N LYS B 97 7.590 -10.902 -15.172 1.00 20.72 N ANISOU 2351 N LYS B 97 2698 2784 2390 -259 469 -70 N ATOM 2352 CA LYS B 97 8.966 -10.688 -14.756 1.00 22.73 C ANISOU 2352 CA LYS B 97 2895 3023 2717 -250 505 -89 C ATOM 2353 C LYS B 97 9.043 -10.074 -13.377 1.00 22.22 C ANISOU 2353 C LYS B 97 2793 2933 2718 -206 444 -69 C ATOM 2354 O LYS B 97 9.742 -10.563 -12.522 1.00 21.89 O ANISOU 2354 O LYS B 97 2703 2871 2744 -169 442 -95 O ATOM 2355 CB LYS B 97 9.690 -9.802 -15.732 1.00 28.46 C ANISOU 2355 CB LYS B 97 3632 3763 3419 -307 555 -75 C ATOM 2356 CG LYS B 97 11.183 -9.681 -15.426 1.00 41.61 C ANISOU 2356 CG LYS B 97 5228 5414 5167 -304 604 -104 C ATOM 2357 CD LYS B 97 11.978 -9.082 -16.589 1.00 53.19 C ANISOU 2357 CD LYS B 97 6706 6900 6605 -372 681 -103 C ATOM 2358 CE LYS B 97 13.485 -9.178 -16.324 1.00 61.97 C ANISOU 2358 CE LYS B 97 7737 7997 7813 -368 739 -147 C ATOM 2359 NZ LYS B 97 14.284 -9.202 -17.595 1.00 68.23 N ANISOU 2359 NZ LYS B 97 8535 8816 8575 -435 847 -176 N ATOM 2360 N THR B 98 8.320 -8.985 -13.148 1.00 19.40 N ANISOU 2360 N THR B 98 2458 2573 2340 -210 389 -23 N ATOM 2361 CA THR B 98 8.377 -8.320 -11.845 1.00 17.82 C ANISOU 2361 CA THR B 98 2226 2349 2197 -171 333 -9 C ATOM 2362 C THR B 98 7.437 -8.921 -10.823 1.00 16.69 C ANISOU 2362 C THR B 98 2086 2199 2055 -127 284 -14 C ATOM 2363 O THR B 98 7.591 -8.657 -9.622 1.00 18.13 O ANISOU 2363 O THR B 98 2243 2363 2282 -92 245 -14 O ATOM 2364 CB THR B 98 7.980 -6.834 -11.954 1.00 18.32 C ANISOU 2364 CB THR B 98 2308 2406 2248 -191 292 38 C ATOM 2365 OG1 THR B 98 6.601 -6.732 -12.345 1.00 18.30 O ANISOU 2365 OG1 THR B 98 2352 2415 2188 -198 255 61 O ATOM 2366 CG2 THR B 98 8.900 -6.105 -12.937 1.00 20.96 C ANISOU 2366 CG2 THR B 98 2643 2744 2576 -243 338 53 C ATOM 2367 N LEU B 99 6.443 -9.664 -11.282 1.00 15.71 N ANISOU 2367 N LEU B 99 1998 2091 1881 -132 284 -18 N ATOM 2368 CA LEU B 99 5.447 -10.306 -10.477 1.00 14.51 C ANISOU 2368 CA LEU B 99 1854 1937 1724 -101 249 -24 C ATOM 2369 C LEU B 99 4.440 -9.317 -9.872 1.00 14.51 C ANISOU 2369 C LEU B 99 1861 1932 1719 -90 191 4 C ATOM 2370 O LEU B 99 3.648 -9.666 -9.008 1.00 14.65 O ANISOU 2370 O LEU B 99 1880 1948 1741 -65 164 -2 O ATOM 2371 CB LEU B 99 6.042 -11.206 -9.379 1.00 16.28 C ANISOU 2371 CB LEU B 99 2048 2142 1997 -63 248 -50 C ATOM 2372 CG LEU B 99 7.186 -12.083 -9.914 1.00 18.95 C ANISOU 2372 CG LEU B 99 2364 2474 2361 -68 301 -84 C ATOM 2373 CD1 LEU B 99 7.747 -12.971 -8.796 1.00 22.34 C ANISOU 2373 CD1 LEU B 99 2765 2876 2847 -28 284 -105 C ATOM 2374 CD2 LEU B 99 6.725 -12.931 -11.065 1.00 20.64 C ANISOU 2374 CD2 LEU B 99 2609 2707 2526 -94 340 -102 C ATOM 2375 N ASN B 100 4.413 -8.110 -10.391 1.00 14.52 N ANISOU 2375 N ASN B 100 1871 1933 1713 -112 176 33 N ATOM 2376 CA ASN B 100 3.372 -7.142 -10.007 1.00 14.06 C ANISOU 2376 CA ASN B 100 1819 1867 1656 -103 120 55 C ATOM 2377 C ASN B 100 2.006 -7.597 -10.429 1.00 13.74 C ANISOU 2377 C ASN B 100 1805 1839 1577 -108 101 56 C ATOM 2378 O ASN B 100 1.818 -8.276 -11.452 1.00 15.10 O ANISOU 2378 O ASN B 100 2005 2027 1706 -134 124 54 O ATOM 2379 CB ASN B 100 3.716 -5.742 -10.574 1.00 15.05 C ANISOU 2379 CB ASN B 100 1951 1980 1788 -129 103 89 C ATOM 2380 CG ASN B 100 2.987 -4.634 -9.884 1.00 15.66 C ANISOU 2380 CG ASN B 100 2018 2037 1894 -109 44 103 C ATOM 2381 OD1 ASN B 100 2.721 -3.554 -10.558 1.00 22.33 O ANISOU 2381 OD1 ASN B 100 2880 2868 2735 -132 12 137 O ATOM 2382 ND2 ASN B 100 2.701 -4.772 -8.664 1.00 11.35 N ANISOU 2382 ND2 ASN B 100 1450 1486 1378 -72 27 81 N ATOM 2383 N ASN B 101 1.020 -7.321 -9.581 1.00 13.89 N ANISOU 2383 N ASN B 101 1812 1851 1615 -83 61 53 N ATOM 2384 CA ASN B 101 -0.370 -7.688 -9.820 1.00 12.98 C ANISOU 2384 CA ASN B 101 1710 1744 1479 -84 38 49 C ATOM 2385 C ASN B 101 -0.549 -9.184 -9.878 1.00 12.73 C ANISOU 2385 C ASN B 101 1686 1727 1423 -85 72 25 C ATOM 2386 O ASN B 101 -1.242 -9.733 -10.768 1.00 13.85 O ANISOU 2386 O ASN B 101 1852 1880 1531 -105 70 24 O ATOM 2387 CB ASN B 101 -0.886 -7.026 -11.085 1.00 13.54 C ANISOU 2387 CB ASN B 101 1808 1814 1521 -115 8 79 C ATOM 2388 CG ASN B 101 -0.794 -5.506 -11.002 1.00 15.23 C ANISOU 2388 CG ASN B 101 2014 2005 1767 -114 -34 106 C ATOM 2389 OD1 ASN B 101 -1.353 -4.845 -10.082 1.00 15.49 O ANISOU 2389 OD1 ASN B 101 2019 2022 1845 -85 -68 98 O ATOM 2390 ND2 ASN B 101 -0.076 -4.926 -11.963 1.00 17.28 N ANISOU 2390 ND2 ASN B 101 2299 2260 2004 -149 -28 137 N ATOM 2391 N ASP B 102 0.104 -9.867 -8.935 1.00 13.62 N ANISOU 2391 N ASP B 102 1784 1836 1556 -63 97 5 N ATOM 2392 CA ASP B 102 0.056 -11.333 -8.904 1.00 14.17 C ANISOU 2392 CA ASP B 102 1862 1910 1611 -62 126 -17 C ATOM 2393 C ASP B 102 -1.248 -11.829 -8.220 1.00 14.12 C ANISOU 2393 C ASP B 102 1855 1907 1604 -53 109 -28 C ATOM 2394 O ASP B 102 -1.263 -12.250 -7.033 1.00 13.71 O ANISOU 2394 O ASP B 102 1794 1848 1567 -34 112 -38 O ATOM 2395 CB ASP B 102 1.278 -11.926 -8.213 1.00 14.39 C ANISOU 2395 CB ASP B 102 1876 1926 1665 -45 150 -31 C ATOM 2396 CG ASP B 102 1.373 -13.450 -8.389 1.00 16.15 C ANISOU 2396 CG ASP B 102 2110 2147 1881 -46 179 -53 C ATOM 2397 OD1 ASP B 102 0.683 -13.994 -9.281 1.00 14.28 O ANISOU 2397 OD1 ASP B 102 1893 1922 1612 -66 188 -60 O ATOM 2398 OD2 ASP B 102 2.208 -14.060 -7.652 1.00 16.38 O ANISOU 2398 OD2 ASP B 102 2126 2158 1939 -26 187 -65 O ATOM 2399 N ILE B 103 -2.355 -11.747 -8.960 1.00 13.11 N ANISOU 2399 N ILE B 103 1736 1788 1457 -70 90 -24 N ATOM 2400 CA ILE B 103 -3.672 -12.117 -8.458 1.00 13.07 C ANISOU 2400 CA ILE B 103 1722 1786 1459 -66 76 -37 C ATOM 2401 C ILE B 103 -4.538 -12.566 -9.614 1.00 13.50 C ANISOU 2401 C ILE B 103 1792 1849 1489 -91 64 -38 C ATOM 2402 O ILE B 103 -4.326 -12.147 -10.743 1.00 14.19 O ANISOU 2402 O ILE B 103 1899 1940 1551 -110 51 -23 O ATOM 2403 CB ILE B 103 -4.308 -10.930 -7.655 1.00 13.08 C ANISOU 2403 CB ILE B 103 1695 1781 1493 -49 46 -35 C ATOM 2404 CG1 ILE B 103 -5.529 -11.402 -6.854 1.00 13.92 C ANISOU 2404 CG1 ILE B 103 1783 1892 1612 -45 48 -57 C ATOM 2405 CG2 ILE B 103 -4.616 -9.727 -8.567 1.00 15.44 C ANISOU 2405 CG2 ILE B 103 1993 2076 1798 -57 4 -14 C ATOM 2406 CD1 ILE B 103 -5.926 -10.405 -5.761 1.00 15.46 C ANISOU 2406 CD1 ILE B 103 1950 2082 1841 -25 36 -69 C ATOM 2407 N MET B 104 -5.492 -13.452 -9.332 1.00 13.50 N ANISOU 2407 N MET B 104 1786 1851 1491 -94 67 -56 N ATOM 2408 CA MET B 104 -6.346 -14.052 -10.308 1.00 13.09 C ANISOU 2408 CA MET B 104 1748 1806 1421 -118 53 -63 C ATOM 2409 C MET B 104 -7.662 -14.371 -9.641 1.00 14.56 C ANISOU 2409 C MET B 104 1906 1991 1635 -116 44 -80 C ATOM 2410 O MET B 104 -7.706 -14.707 -8.448 1.00 14.73 O ANISOU 2410 O MET B 104 1913 2010 1675 -104 69 -90 O ATOM 2411 CB MET B 104 -5.648 -15.334 -10.850 1.00 20.57 C ANISOU 2411 CB MET B 104 2725 2754 2338 -131 90 -76 C ATOM 2412 CG MET B 104 -6.483 -16.228 -11.697 1.00 21.02 C ANISOU 2412 CG MET B 104 2798 2814 2375 -156 82 -91 C ATOM 2413 SD MET B 104 -5.454 -17.587 -12.296 1.00 18.37 S ANISOU 2413 SD MET B 104 2494 2474 2011 -167 129 -114 S ATOM 2414 CE MET B 104 -5.310 -18.657 -10.949 1.00 19.82 C ANISOU 2414 CE MET B 104 2663 2638 2230 -148 157 -127 C ATOM 2415 N LEU B 105 -8.751 -14.326 -10.407 1.00 13.48 N ANISOU 2415 N LEU B 105 1764 1856 1503 -132 7 -83 N ATOM 2416 CA LEU B 105 -10.046 -14.777 -9.973 1.00 14.62 C ANISOU 2416 CA LEU B 105 1876 1998 1679 -137 1 -105 C ATOM 2417 C LEU B 105 -10.524 -15.978 -10.781 1.00 13.95 C ANISOU 2417 C LEU B 105 1811 1915 1574 -164 0 -118 C ATOM 2418 O LEU B 105 -10.311 -16.029 -11.992 1.00 15.25 O ANISOU 2418 O LEU B 105 2008 2082 1703 -180 -23 -110 O ATOM 2419 CB LEU B 105 -11.058 -13.639 -10.159 1.00 15.68 C ANISOU 2419 CB LEU B 105 1975 2128 1855 -131 -53 -104 C ATOM 2420 CG LEU B 105 -11.014 -12.543 -9.113 1.00 15.13 C ANISOU 2420 CG LEU B 105 1871 2053 1824 -104 -51 -106 C ATOM 2421 CD1 LEU B 105 -11.782 -11.317 -9.563 1.00 17.11 C ANISOU 2421 CD1 LEU B 105 2092 2290 2119 -95 -115 -102 C ATOM 2422 CD2 LEU B 105 -11.593 -13.063 -7.781 1.00 16.19 C ANISOU 2422 CD2 LEU B 105 1974 2193 1986 -100 -6 -136 C ATOM 2423 N ILE B 106 -11.180 -16.915 -10.094 1.00 14.22 N ANISOU 2423 N ILE B 106 1828 1947 1629 -171 26 -138 N ATOM 2424 CA ILE B 106 -11.745 -18.104 -10.707 1.00 14.07 C ANISOU 2424 CA ILE B 106 1821 1924 1602 -197 25 -155 C ATOM 2425 C ILE B 106 -13.211 -18.098 -10.403 1.00 16.45 C ANISOU 2425 C ILE B 106 2075 2224 1953 -208 6 -174 C ATOM 2426 O ILE B 106 -13.601 -18.024 -9.257 1.00 17.48 O ANISOU 2426 O ILE B 106 2172 2354 2114 -202 35 -183 O ATOM 2427 CB ILE B 106 -11.118 -19.383 -10.141 1.00 16.40 C ANISOU 2427 CB ILE B 106 2139 2210 1882 -202 75 -162 C ATOM 2428 CG1 ILE B 106 -9.647 -19.448 -10.525 1.00 16.70 C ANISOU 2428 CG1 ILE B 106 2216 2247 1884 -191 94 -151 C ATOM 2429 CG2 ILE B 106 -11.807 -20.625 -10.697 1.00 16.85 C ANISOU 2429 CG2 ILE B 106 2205 2258 1940 -230 73 -183 C ATOM 2430 CD1 ILE B 106 -8.919 -20.484 -9.733 1.00 18.93 C ANISOU 2430 CD1 ILE B 106 2513 2512 2168 -185 135 -155 C ATOM 2431 N LYS B 107 -14.052 -18.139 -11.428 1.00 16.48 N ANISOU 2431 N LYS B 107 2073 2225 1964 -225 -44 -182 N ATOM 2432 CA LYS B 107 -15.462 -18.326 -11.243 1.00 15.62 C ANISOU 2432 CA LYS B 107 1913 2111 1912 -238 -63 -205 C ATOM 2433 C LYS B 107 -15.812 -19.795 -11.327 1.00 17.61 C ANISOU 2433 C LYS B 107 2175 2356 2159 -267 -39 -224 C ATOM 2434 O LYS B 107 -15.448 -20.455 -12.313 1.00 17.52 O ANISOU 2434 O LYS B 107 2208 2341 2105 -282 -54 -224 O ATOM 2435 CB LYS B 107 -16.267 -17.555 -12.295 1.00 16.96 C ANISOU 2435 CB LYS B 107 2065 2275 2103 -241 -145 -204 C ATOM 2436 CG LYS B 107 -17.748 -17.637 -12.047 1.00 18.41 C ANISOU 2436 CG LYS B 107 2181 2450 2363 -251 -168 -234 C ATOM 2437 CD LYS B 107 -18.579 -16.969 -13.129 1.00 21.82 C ANISOU 2437 CD LYS B 107 2595 2870 2825 -254 -264 -232 C ATOM 2438 CE LYS B 107 -20.060 -16.954 -12.753 1.00 24.80 C ANISOU 2438 CE LYS B 107 2887 3236 3299 -258 -285 -268 C ATOM 2439 NZ LYS B 107 -20.919 -16.539 -13.926 1.00 26.57 N ANISOU 2439 NZ LYS B 107 3098 3443 3556 -265 -393 -268 N ATOM 2440 N LEU B 108 -16.470 -20.335 -10.304 1.00 16.69 N ANISOU 2440 N LEU B 108 2023 2236 2082 -278 2 -242 N ATOM 2441 CA LEU B 108 -16.881 -21.713 -10.300 1.00 17.60 C ANISOU 2441 CA LEU B 108 2146 2340 2202 -310 25 -258 C ATOM 2442 C LEU B 108 -18.049 -21.954 -11.230 1.00 19.06 C ANISOU 2442 C LEU B 108 2302 2518 2421 -333 -30 -280 C ATOM 2443 O LEU B 108 -18.934 -21.088 -11.369 1.00 18.82 O ANISOU 2443 O LEU B 108 2220 2491 2441 -327 -72 -290 O ATOM 2444 CB LEU B 108 -17.272 -22.111 -8.874 1.00 18.37 C ANISOU 2444 CB LEU B 108 2216 2436 2329 -321 86 -265 C ATOM 2445 CG LEU B 108 -16.214 -21.856 -7.779 1.00 18.87 C ANISOU 2445 CG LEU B 108 2307 2505 2360 -301 135 -244 C ATOM 2446 CD1 LEU B 108 -16.699 -22.287 -6.372 1.00 19.87 C ANISOU 2446 CD1 LEU B 108 2416 2631 2504 -322 195 -250 C ATOM 2447 CD2 LEU B 108 -14.957 -22.597 -8.162 1.00 19.92 C ANISOU 2447 CD2 LEU B 108 2502 2625 2441 -295 141 -225 C ATOM 2448 N SER B 109 -18.083 -23.139 -11.826 1.00 18.20 N ANISOU 2448 N SER B 109 2224 2396 2295 -359 -32 -291 N ATOM 2449 CA ASER B 109 -19.158 -23.436 -12.753 0.50 17.74 C ANISOU 2449 CA ASER B 109 2144 2330 2268 -384 -90 -313 C ATOM 2450 CA BSER B 109 -19.156 -23.493 -12.750 0.50 18.04 C ANISOU 2450 CA BSER B 109 2182 2366 2304 -385 -89 -314 C ATOM 2451 C SER B 109 -20.500 -23.621 -12.043 1.00 20.57 C ANISOU 2451 C SER B 109 2427 2682 2709 -404 -79 -338 C ATOM 2452 O SER B 109 -21.591 -23.405 -12.654 1.00 24.61 O ANISOU 2452 O SER B 109 2892 3187 3271 -416 -140 -359 O ATOM 2453 CB ASER B 109 -18.775 -24.646 -13.580 0.50 19.33 C ANISOU 2453 CB ASER B 109 2401 2518 2426 -407 -94 -324 C ATOM 2454 CB BSER B 109 -18.766 -24.756 -13.531 0.50 20.11 C ANISOU 2454 CB BSER B 109 2501 2616 2526 -409 -89 -325 C ATOM 2455 OG ASER B 109 -18.836 -25.810 -12.779 0.50 20.65 O ANISOU 2455 OG ASER B 109 2567 2668 2612 -427 -37 -333 O ATOM 2456 OG BSER B 109 -19.852 -25.354 -14.244 0.50 22.98 O ANISOU 2456 OG BSER B 109 2844 2966 2922 -441 -137 -352 O ATOM 2457 N SER B 110 -20.458 -23.993 -10.768 1.00 20.95 N ANISOU 2457 N SER B 110 2460 2730 2771 -411 -5 -338 N ATOM 2458 CA SER B 110 -21.644 -24.000 -9.924 1.00 23.84 C ANISOU 2458 CA SER B 110 2751 3095 3211 -431 24 -362 C ATOM 2459 C SER B 110 -21.311 -23.478 -8.549 1.00 21.81 C ANISOU 2459 C SER B 110 2483 2853 2951 -418 93 -353 C ATOM 2460 O SER B 110 -20.145 -23.370 -8.168 1.00 21.50 O ANISOU 2460 O SER B 110 2498 2819 2852 -397 119 -326 O ATOM 2461 CB SER B 110 -22.217 -25.391 -9.783 1.00 27.08 C ANISOU 2461 CB SER B 110 3159 3487 3644 -478 52 -378 C ATOM 2462 OG SER B 110 -21.203 -26.278 -9.379 1.00 30.37 O ANISOU 2462 OG SER B 110 3644 3894 4003 -483 99 -355 O ATOM 2463 N ARG B 111 -22.337 -23.036 -7.821 1.00 23.99 N ANISOU 2463 N ARG B 111 2685 3136 3294 -428 119 -381 N ATOM 2464 CA ARG B 111 -22.130 -22.497 -6.489 1.00 21.67 C ANISOU 2464 CA ARG B 111 2380 2859 2995 -420 187 -381 C ATOM 2465 C ARG B 111 -21.641 -23.577 -5.520 1.00 19.04 C ANISOU 2465 C ARG B 111 2099 2521 2614 -451 261 -361 C ATOM 2466 O ARG B 111 -22.205 -24.658 -5.449 1.00 22.48 O ANISOU 2466 O ARG B 111 2532 2943 3068 -495 284 -369 O ATOM 2467 CB ARG B 111 -23.448 -21.939 -5.964 1.00 24.67 C ANISOU 2467 CB ARG B 111 2664 3246 3465 -432 207 -426 C ATOM 2468 CG ARG B 111 -23.919 -20.727 -6.725 1.00 31.58 C ANISOU 2468 CG ARG B 111 3483 4119 4398 -395 130 -444 C ATOM 2469 CD ARG B 111 -25.277 -20.198 -6.230 1.00 39.86 C ANISOU 2469 CD ARG B 111 4422 5169 5554 -404 148 -498 C ATOM 2470 NE ARG B 111 -25.492 -18.862 -6.761 1.00 49.69 N ANISOU 2470 NE ARG B 111 5622 6407 6850 -359 74 -510 N ATOM 2471 CZ ARG B 111 -25.119 -17.737 -6.146 1.00 56.74 C ANISOU 2471 CZ ARG B 111 6504 7308 7745 -324 89 -514 C ATOM 2472 NH1 ARG B 111 -24.540 -17.776 -4.942 1.00 56.06 N ANISOU 2472 NH1 ARG B 111 6450 7243 7609 -330 179 -511 N ATOM 2473 NH2 ARG B 111 -25.336 -16.564 -6.735 1.00 59.96 N ANISOU 2473 NH2 ARG B 111 6874 7702 8207 -284 10 -521 N ATOM 2474 N ALA B 112 -20.656 -23.235 -4.709 1.00 18.35 N ANISOU 2474 N ALA B 112 2058 2444 2472 -432 295 -337 N ATOM 2475 CA ALA B 112 -20.208 -24.094 -3.624 1.00 19.19 C ANISOU 2475 CA ALA B 112 2215 2544 2533 -461 360 -315 C ATOM 2476 C ALA B 112 -21.354 -24.166 -2.629 1.00 17.49 C ANISOU 2476 C ALA B 112 1948 2340 2359 -504 426 -345 C ATOM 2477 O ALA B 112 -22.070 -23.176 -2.416 1.00 20.10 O ANISOU 2477 O ALA B 112 2210 2689 2739 -493 434 -381 O ATOM 2478 CB ALA B 112 -18.974 -23.509 -2.979 1.00 20.97 C ANISOU 2478 CB ALA B 112 2492 2778 2698 -428 370 -287 C ATOM 2479 N VAL B 113 -21.529 -25.325 -1.994 1.00 20.12 N ANISOU 2479 N VAL B 113 2311 2658 2674 -554 476 -332 N ATOM 2480 CA VAL B 113 -22.503 -25.488 -0.917 1.00 21.62 C ANISOU 2480 CA VAL B 113 2465 2861 2890 -606 556 -356 C ATOM 2481 C VAL B 113 -21.788 -25.098 0.370 1.00 19.90 C ANISOU 2481 C VAL B 113 2299 2659 2602 -605 608 -336 C ATOM 2482 O VAL B 113 -20.715 -25.599 0.652 1.00 20.26 O ANISOU 2482 O VAL B 113 2427 2689 2581 -599 599 -291 O ATOM 2483 CB VAL B 113 -22.983 -26.938 -0.855 1.00 21.67 C ANISOU 2483 CB VAL B 113 2490 2841 2903 -668 583 -345 C ATOM 2484 CG1 VAL B 113 -23.813 -27.196 0.362 1.00 23.97 C ANISOU 2484 CG1 VAL B 113 2762 3145 3202 -730 676 -360 C ATOM 2485 CG2 VAL B 113 -23.759 -27.298 -2.115 1.00 25.72 C ANISOU 2485 CG2 VAL B 113 2947 3337 3486 -671 528 -371 C ATOM 2486 N ILE B 114 -22.352 -24.158 1.108 1.00 19.72 N ANISOU 2486 N ILE B 114 2227 2666 2601 -606 655 -373 N ATOM 2487 CA ILE B 114 -21.723 -23.587 2.281 1.00 19.69 C ANISOU 2487 CA ILE B 114 2268 2681 2532 -602 698 -364 C ATOM 2488 C ILE B 114 -22.100 -24.394 3.537 1.00 20.84 C ANISOU 2488 C ILE B 114 2453 2831 2636 -675 788 -356 C ATOM 2489 O ILE B 114 -23.278 -24.644 3.814 1.00 22.67 O ANISOU 2489 O ILE B 114 2626 3071 2914 -725 848 -394 O ATOM 2490 CB ILE B 114 -22.121 -22.107 2.425 1.00 19.03 C ANISOU 2490 CB ILE B 114 2113 2625 2493 -565 704 -415 C ATOM 2491 CG1 ILE B 114 -21.755 -21.299 1.184 1.00 21.65 C ANISOU 2491 CG1 ILE B 114 2414 2948 2863 -499 611 -415 C ATOM 2492 CG2 ILE B 114 -21.479 -21.506 3.663 1.00 20.64 C ANISOU 2492 CG2 ILE B 114 2366 2849 2627 -562 749 -412 C ATOM 2493 CD1 ILE B 114 -20.258 -21.368 0.846 1.00 21.93 C ANISOU 2493 CD1 ILE B 114 2534 2971 2829 -461 557 -360 C ATOM 2494 N ASN B 115 -21.084 -24.788 4.306 1.00 18.71 N ANISOU 2494 N ASN B 115 2280 2552 2276 -683 795 -307 N ATOM 2495 CA ASN B 115 -21.280 -25.619 5.507 1.00 20.69 C ANISOU 2495 CA ASN B 115 2591 2802 2467 -757 869 -285 C ATOM 2496 C ASN B 115 -20.046 -25.415 6.392 1.00 19.27 C ANISOU 2496 C ASN B 115 2509 2622 2192 -743 858 -242 C ATOM 2497 O ASN B 115 -19.280 -24.479 6.185 1.00 21.30 O ANISOU 2497 O ASN B 115 2764 2887 2440 -681 813 -245 O ATOM 2498 CB ASN B 115 -21.551 -27.087 5.100 1.00 21.21 C ANISOU 2498 CB ASN B 115 2682 2830 2548 -804 862 -252 C ATOM 2499 CG ASN B 115 -20.423 -27.691 4.320 1.00 19.24 C ANISOU 2499 CG ASN B 115 2490 2541 2280 -763 777 -203 C ATOM 2500 OD1 ASN B 115 -19.271 -27.359 4.505 1.00 21.39 O ANISOU 2500 OD1 ASN B 115 2817 2809 2502 -721 738 -174 O ATOM 2501 ND2 ASN B 115 -20.763 -28.532 3.343 1.00 21.91 N ANISOU 2501 ND2 ASN B 115 2806 2849 2669 -770 744 -202 N ATOM 2502 N ALA B 116 -19.874 -26.200 7.436 1.00 20.13 N ANISOU 2502 N ALA B 116 2701 2721 2228 -802 900 -203 N ATOM 2503 CA ALA B 116 -18.735 -26.030 8.327 1.00 21.11 C ANISOU 2503 CA ALA B 116 2920 2841 2260 -792 882 -162 C ATOM 2504 C ALA B 116 -17.405 -26.246 7.654 1.00 18.99 C ANISOU 2504 C ALA B 116 2693 2536 1985 -730 784 -116 C ATOM 2505 O ALA B 116 -16.376 -25.706 8.121 1.00 22.43 O ANISOU 2505 O ALA B 116 3178 2973 2370 -696 750 -96 O ATOM 2506 CB ALA B 116 -18.871 -26.996 9.503 1.00 24.58 C ANISOU 2506 CB ALA B 116 3449 3269 2622 -876 936 -121 C ATOM 2507 N HIS B 117 -17.401 -27.009 6.549 1.00 19.12 N ANISOU 2507 N HIS B 117 2689 2520 2055 -716 739 -104 N ATOM 2508 CA HIS B 117 -16.150 -27.418 5.886 1.00 17.17 C ANISOU 2508 CA HIS B 117 2483 2235 1806 -665 656 -63 C ATOM 2509 C HIS B 117 -15.721 -26.546 4.716 1.00 15.77 C ANISOU 2509 C HIS B 117 2247 2068 1677 -591 602 -90 C ATOM 2510 O HIS B 117 -14.541 -26.555 4.212 1.00 17.08 O ANISOU 2510 O HIS B 117 2440 2212 1839 -541 540 -67 O ATOM 2511 CB HIS B 117 -16.288 -28.862 5.379 1.00 19.75 C ANISOU 2511 CB HIS B 117 2832 2513 2157 -696 639 -35 C ATOM 2512 CG HIS B 117 -16.800 -29.789 6.423 1.00 22.44 C ANISOU 2512 CG HIS B 117 3232 2838 2458 -777 690 -4 C ATOM 2513 ND1 HIS B 117 -16.082 -30.077 7.562 1.00 28.31 N ANISOU 2513 ND1 HIS B 117 4070 3564 3123 -801 687 46 N ATOM 2514 CD2 HIS B 117 -17.986 -30.428 6.542 1.00 24.81 C ANISOU 2514 CD2 HIS B 117 3508 3137 2781 -845 749 -16 C ATOM 2515 CE1 HIS B 117 -16.793 -30.899 8.325 1.00 29.33 C ANISOU 2515 CE1 HIS B 117 4241 3681 3223 -883 741 68 C ATOM 2516 NE2 HIS B 117 -17.952 -31.136 7.728 1.00 28.10 N ANISOU 2516 NE2 HIS B 117 4011 3535 3129 -912 783 30 N ATOM 2517 N VAL B 118 -16.873 -25.728 4.182 1.00 17.42 N ANISOU 2517 N VAL B 118 2361 2314 1945 -587 630 -148 N ATOM 2518 CA VAL B 118 -16.653 -24.946 2.980 1.00 15.19 C ANISOU 2518 CA VAL B 118 2023 2038 1710 -527 577 -171 C ATOM 2519 C VAL B 118 -17.374 -23.661 3.243 1.00 15.32 C ANISOU 2519 C VAL B 118 1974 2094 1752 -516 607 -219 C ATOM 2520 O VAL B 118 -18.607 -23.627 3.364 1.00 17.23 O ANISOU 2520 O VAL B 118 2158 2352 2036 -551 654 -257 O ATOM 2521 CB VAL B 118 -17.292 -25.651 1.751 1.00 15.20 C ANISOU 2521 CB VAL B 118 1984 2022 1770 -534 553 -183 C ATOM 2522 CG1 VAL B 118 -17.194 -24.770 0.536 1.00 16.55 C ANISOU 2522 CG1 VAL B 118 2104 2205 1981 -481 499 -207 C ATOM 2523 CG2 VAL B 118 -16.613 -26.978 1.481 1.00 16.46 C ANISOU 2523 CG2 VAL B 118 2206 2137 1910 -545 525 -143 C ATOM 2524 N SER B 119 -16.630 -22.556 3.325 1.00 16.44 N ANISOU 2524 N SER B 119 2116 2249 1879 -467 580 -222 N ATOM 2525 CA SER B 119 -17.285 -21.256 3.537 1.00 17.06 C ANISOU 2525 CA SER B 119 2130 2360 1993 -451 602 -272 C ATOM 2526 C SER B 119 -16.325 -20.152 3.102 1.00 16.49 C ANISOU 2526 C SER B 119 2056 2289 1921 -387 545 -267 C ATOM 2527 O SER B 119 -15.152 -20.403 2.806 1.00 17.00 O ANISOU 2527 O SER B 119 2171 2335 1952 -362 500 -227 O ATOM 2528 CB SER B 119 -17.764 -21.038 4.958 1.00 23.92 C ANISOU 2528 CB SER B 119 3010 3252 2827 -492 680 -295 C ATOM 2529 OG SER B 119 -16.680 -21.104 5.813 1.00 25.07 O ANISOU 2529 OG SER B 119 3239 3393 2893 -490 674 -258 O ATOM 2530 N THR B 120 -16.871 -18.946 2.992 1.00 15.99 N ANISOU 2530 N THR B 120 1927 2243 1904 -363 545 -311 N ATOM 2531 CA THR B 120 -16.125 -17.836 2.413 1.00 15.82 C ANISOU 2531 CA THR B 120 1894 2220 1897 -306 486 -308 C ATOM 2532 C THR B 120 -15.322 -17.068 3.462 1.00 15.86 C ANISOU 2532 C THR B 120 1936 2234 1855 -290 498 -307 C ATOM 2533 O THR B 120 -15.656 -17.087 4.667 1.00 17.00 O ANISOU 2533 O THR B 120 2097 2395 1967 -322 558 -327 O ATOM 2534 CB THR B 120 -17.069 -16.870 1.709 1.00 16.40 C ANISOU 2534 CB THR B 120 1880 2298 2052 -283 465 -351 C ATOM 2535 OG1 THR B 120 -17.918 -16.252 2.680 1.00 19.65 O ANISOU 2535 OG1 THR B 120 2247 2729 2489 -298 523 -403 O ATOM 2536 CG2 THR B 120 -17.926 -17.563 0.635 1.00 20.55 C ANISOU 2536 CG2 THR B 120 2365 2813 2628 -299 443 -355 C ATOM 2537 N ILE B 121 -14.269 -16.412 2.989 1.00 14.88 N ANISOU 2537 N ILE B 121 1827 2101 1726 -245 442 -285 N ATOM 2538 CA ILE B 121 -13.455 -15.501 3.812 1.00 13.30 C ANISOU 2538 CA ILE B 121 1653 1906 1494 -222 438 -288 C ATOM 2539 C ILE B 121 -13.718 -14.058 3.383 1.00 14.95 C ANISOU 2539 C ILE B 121 1800 2118 1763 -183 411 -322 C ATOM 2540 O ILE B 121 -13.780 -13.791 2.180 1.00 15.52 O ANISOU 2540 O ILE B 121 1839 2178 1879 -160 363 -313 O ATOM 2541 CB ILE B 121 -11.942 -15.867 3.779 1.00 14.29 C ANISOU 2541 CB ILE B 121 1845 2013 1571 -204 397 -237 C ATOM 2542 CG1 ILE B 121 -11.127 -14.991 4.740 1.00 16.94 C ANISOU 2542 CG1 ILE B 121 2209 2353 1874 -186 391 -241 C ATOM 2543 CG2 ILE B 121 -11.379 -15.798 2.365 1.00 14.91 C ANISOU 2543 CG2 ILE B 121 1908 2076 1681 -172 341 -214 C ATOM 2544 CD1 ILE B 121 -11.400 -15.223 6.142 1.00 20.64 C ANISOU 2544 CD1 ILE B 121 2718 2836 2290 -223 441 -255 C ATOM 2545 N SER B 122 -13.939 -13.173 4.366 1.00 16.78 N ANISOU 2545 N SER B 122 2019 2363 1995 -181 441 -362 N ATOM 2546 CA SER B 122 -14.203 -11.760 4.072 1.00 16.21 C ANISOU 2546 CA SER B 122 1886 2286 1985 -143 414 -399 C ATOM 2547 C SER B 122 -13.064 -11.050 3.358 1.00 16.45 C ANISOU 2547 C SER B 122 1933 2298 2021 -101 343 -364 C ATOM 2548 O SER B 122 -11.910 -11.297 3.634 1.00 15.64 O ANISOU 2548 O SER B 122 1887 2190 1864 -97 329 -328 O ATOM 2549 CB SER B 122 -14.398 -11.045 5.388 1.00 19.58 C ANISOU 2549 CB SER B 122 2313 2729 2398 -149 462 -448 C ATOM 2550 OG SER B 122 -15.605 -11.423 5.983 1.00 24.43 O ANISOU 2550 OG SER B 122 2895 3362 3024 -187 535 -494 O ATOM 2551 N LEU B 123 -13.399 -10.208 2.393 1.00 16.85 N ANISOU 2551 N LEU B 123 1930 2334 2138 -72 297 -372 N ATOM 2552 CA LEU B 123 -12.422 -9.302 1.803 1.00 15.26 C ANISOU 2552 CA LEU B 123 1738 2114 1947 -37 236 -345 C ATOM 2553 C LEU B 123 -12.007 -8.271 2.844 1.00 15.84 C ANISOU 2553 C LEU B 123 1816 2187 2017 -20 245 -374 C ATOM 2554 O LEU B 123 -12.755 -7.958 3.780 1.00 18.63 O ANISOU 2554 O LEU B 123 2144 2552 2383 -29 290 -427 O ATOM 2555 CB LEU B 123 -12.999 -8.627 0.544 1.00 16.51 C ANISOU 2555 CB LEU B 123 1845 2254 2176 -17 180 -344 C ATOM 2556 CG LEU B 123 -13.187 -9.575 -0.671 1.00 19.94 C ANISOU 2556 CG LEU B 123 2287 2686 2603 -33 156 -310 C ATOM 2557 CD1 LEU B 123 -13.805 -8.764 -1.806 1.00 24.66 C ANISOU 2557 CD1 LEU B 123 2839 3264 3268 -15 92 -310 C ATOM 2558 CD2 LEU B 123 -11.895 -10.227 -1.064 1.00 20.39 C ANISOU 2558 CD2 LEU B 123 2407 2743 2598 -36 146 -259 C ATOM 2559 N PRO B 124 -10.791 -7.744 2.692 1.00 14.36 N ANISOU 2559 N PRO B 124 1659 1986 1813 1 204 -343 N ATOM 2560 CA PRO B 124 -10.247 -6.792 3.673 1.00 15.85 C ANISOU 2560 CA PRO B 124 1857 2170 1994 17 205 -368 C ATOM 2561 C PRO B 124 -10.848 -5.402 3.517 1.00 16.94 C ANISOU 2561 C PRO B 124 1936 2290 2211 44 180 -409 C ATOM 2562 O PRO B 124 -11.088 -4.988 2.383 1.00 16.78 O ANISOU 2562 O PRO B 124 1883 2250 2243 60 132 -391 O ATOM 2563 CB PRO B 124 -8.778 -6.756 3.324 1.00 16.96 C ANISOU 2563 CB PRO B 124 2041 2298 2107 29 162 -317 C ATOM 2564 CG PRO B 124 -8.725 -7.030 1.867 1.00 15.15 C ANISOU 2564 CG PRO B 124 1800 2058 1900 33 128 -277 C ATOM 2565 CD PRO B 124 -9.840 -8.040 1.604 1.00 14.59 C ANISOU 2565 CD PRO B 124 1714 2002 1828 9 160 -286 C ATOM 2566 N THR B 125 -11.099 -4.727 4.636 1.00 15.27 N ANISOU 2566 N THR B 125 1714 2083 2004 48 210 -465 N ATOM 2567 CA THR B 125 -11.654 -3.395 4.620 1.00 18.01 C ANISOU 2567 CA THR B 125 2002 2407 2432 76 188 -513 C ATOM 2568 C THR B 125 -10.594 -2.336 4.926 1.00 18.75 C ANISOU 2568 C THR B 125 2117 2479 2529 101 148 -509 C ATOM 2569 O THR B 125 -10.908 -1.119 4.881 1.00 19.05 O ANISOU 2569 O THR B 125 2109 2489 2640 128 119 -546 O ATOM 2570 CB THR B 125 -12.779 -3.274 5.613 1.00 19.85 C ANISOU 2570 CB THR B 125 2198 2658 2686 65 255 -592 C ATOM 2571 OG1 THR B 125 -12.328 -3.715 6.895 1.00 21.97 O ANISOU 2571 OG1 THR B 125 2526 2955 2868 38 309 -607 O ATOM 2572 CG2 THR B 125 -13.934 -4.131 5.175 1.00 23.58 C ANISOU 2572 CG2 THR B 125 2632 3144 3182 43 287 -601 C ATOM 2573 N ALA B 127 -9.402 -2.772 5.248 1.00 15.54 N ANISOU 2573 N ALA B 127 1773 2081 2052 91 143 -470 N ATOM 2574 CA ALA B 127 -8.208 -1.904 5.440 1.00 15.83 C ANISOU 2574 CA ALA B 127 1832 2095 2088 111 99 -456 C ATOM 2575 C ALA B 127 -6.953 -2.725 5.239 1.00 17.55 C ANISOU 2575 C ALA B 127 2106 2318 2246 100 83 -393 C ATOM 2576 O ALA B 127 -7.045 -3.955 5.208 1.00 19.51 O ANISOU 2576 O ALA B 127 2380 2587 2445 77 112 -370 O ATOM 2577 CB ALA B 127 -8.218 -1.318 6.827 1.00 19.17 C ANISOU 2577 CB ALA B 127 2267 2524 2493 111 127 -517 C ATOM 2578 N APRO B 128 -5.809 -2.094 4.900 0.50 14.91 N ANISOU 2578 N APRO B 128 1781 1959 1925 115 33 -362 N ATOM 2579 N BPRO B 128 -5.767 -2.091 5.190 0.50 15.48 N ANISOU 2579 N BPRO B 128 1859 2034 1988 114 39 -370 N ATOM 2580 CA APRO B 128 -4.565 -2.769 4.459 0.50 13.81 C ANISOU 2580 CA APRO B 128 1678 1819 1751 109 13 -304 C ATOM 2581 CA BPRO B 128 -4.636 -3.013 5.289 0.50 15.49 C ANISOU 2581 CA BPRO B 128 1909 2043 1932 102 34 -325 C ATOM 2582 C APRO B 128 -3.877 -3.605 5.572 0.50 12.48 C ANISOU 2582 C APRO B 128 1563 1666 1513 94 31 -302 C ATOM 2583 C BPRO B 128 -4.466 -3.454 6.738 0.50 15.00 C ANISOU 2583 C BPRO B 128 1894 1999 1805 86 61 -351 C ATOM 2584 O APRO B 128 -4.206 -3.432 6.767 0.50 15.61 O ANISOU 2584 O APRO B 128 1978 2074 1880 87 54 -345 O ATOM 2585 O BPRO B 128 -5.000 -2.799 7.648 0.50 16.79 O ANISOU 2585 O BPRO B 128 2117 2231 2031 86 81 -406 O ATOM 2586 CB APRO B 128 -3.644 -1.617 4.029 0.50 16.38 C ANISOU 2586 CB APRO B 128 1991 2112 2122 127 -38 -288 C ATOM 2587 CB BPRO B 128 -3.435 -2.166 4.859 0.50 16.73 C ANISOU 2587 CB BPRO B 128 2064 2171 2122 118 -19 -298 C ATOM 2588 CG APRO B 128 -4.391 -0.385 4.204 0.50 17.15 C ANISOU 2588 CG APRO B 128 2049 2190 2276 144 -51 -332 C ATOM 2589 CG BPRO B 128 -4.013 -0.814 4.442 0.50 16.02 C ANISOU 2589 CG BPRO B 128 1927 2057 2105 137 -44 -322 C ATOM 2590 CD APRO B 128 -5.684 -0.624 4.934 0.50 13.83 C ANISOU 2590 CD APRO B 128 1615 1792 1850 139 -4 -387 C ATOM 2591 CD BPRO B 128 -5.331 -0.680 5.140 0.50 15.82 C ANISOU 2591 CD BPRO B 128 1880 2045 2087 137 -6 -383 C ATOM 2592 N APRO B 129 -2.888 -4.448 5.204 0.50 14.61 N ANISOU 2592 N APRO B 129 1860 1933 1757 89 17 -255 N ATOM 2593 N BPRO B 129 -3.715 -4.551 6.945 0.50 17.93 N ANISOU 2593 N BPRO B 129 2313 2377 2122 71 61 -312 N ATOM 2594 CA APRO B 129 -2.142 -5.210 6.210 0.50 15.03 C ANISOU 2594 CA APRO B 129 1965 1992 1754 78 17 -246 C ATOM 2595 CA BPRO B 129 -3.347 -5.068 8.262 0.50 18.06 C ANISOU 2595 CA BPRO B 129 2388 2405 2069 53 71 -321 C ATOM 2596 C APRO B 129 -1.505 -4.274 7.238 0.50 16.99 C ANISOU 2596 C APRO B 129 2228 2228 1999 87 -12 -273 C ATOM 2597 C BPRO B 129 -2.223 -4.205 8.815 0.50 17.87 C ANISOU 2597 C BPRO B 129 2378 2361 2051 69 22 -327 C ATOM 2598 O APRO B 129 -1.043 -3.187 6.895 0.50 17.60 O ANISOU 2598 O APRO B 129 2277 2285 2127 105 -45 -277 O ATOM 2599 O BPRO B 129 -1.357 -3.769 8.071 0.50 20.81 O ANISOU 2599 O BPRO B 129 2727 2709 2469 88 -20 -299 O ATOM 2600 CB APRO B 129 -1.063 -5.912 5.385 0.50 15.95 C ANISOU 2600 CB APRO B 129 2088 2096 1879 81 -7 -196 C ATOM 2601 CB BPRO B 129 -2.829 -6.475 7.939 0.50 21.08 C ANISOU 2601 CB BPRO B 129 2804 2789 2418 39 68 -268 C ATOM 2602 CG APRO B 129 -1.609 -5.992 4.009 0.50 18.86 C ANISOU 2602 CG APRO B 129 2421 2466 2279 81 5 -180 C ATOM 2603 CG BPRO B 129 -2.284 -6.351 6.566 0.50 15.44 C ANISOU 2603 CG BPRO B 129 2051 2056 1758 59 39 -234 C ATOM 2604 CD APRO B 129 -2.357 -4.683 3.857 0.50 15.93 C ANISOU 2604 CD APRO B 129 2013 2090 1951 92 -2 -210 C ATOM 2605 CD BPRO B 129 -3.264 -5.444 5.867 0.50 14.44 C ANISOU 2605 CD BPRO B 129 1871 1932 1685 69 50 -259 C ATOM 2606 N AALA B 130 -1.508 -4.674 8.498 0.50 15.23 N ANISOU 2606 N AALA B 130 2055 2018 1715 71 -1 -291 N ATOM 2607 N BALA B 130 -2.246 -3.951 10.114 0.50 18.60 N ANISOU 2607 N BALA B 130 2510 2462 2095 57 29 -364 N ATOM 2608 CA AALA B 130 -1.083 -3.802 9.599 0.50 14.65 C ANISOU 2608 CA AALA B 130 2002 1937 1626 75 -24 -327 C ATOM 2609 CA BALA B 130 -1.155 -3.192 10.689 0.50 17.67 C ANISOU 2609 CA BALA B 130 2410 2323 1981 70 -24 -370 C ATOM 2610 C AALA B 130 0.184 -4.399 10.231 0.50 16.39 C ANISOU 2610 C AALA B 130 2274 2145 1808 70 -69 -296 C ATOM 2611 C BALA B 130 0.059 -4.133 10.782 0.50 18.80 C ANISOU 2611 C BALA B 130 2594 2454 2095 65 -67 -317 C ATOM 2612 O AALA B 130 0.178 -5.562 10.580 0.50 16.82 O ANISOU 2612 O AALA B 130 2373 2209 1810 50 -58 -271 O ATOM 2613 O BALA B 130 -0.080 -5.326 11.049 0.50 18.74 O ANISOU 2613 O BALA B 130 2628 2459 2034 44 -50 -292 O ATOM 2614 CB AALA B 130 -2.209 -3.716 10.664 0.50 17.30 C ANISOU 2614 CB AALA B 130 2361 2299 1914 54 28 -383 C ATOM 2615 CB BALA B 130 -1.550 -2.667 12.063 0.50 20.72 C ANISOU 2615 CB BALA B 130 2833 2723 2317 55 -6 -431 C ATOM 2616 N THR B 132 1.230 -3.610 10.467 1.00 21.10 N ANISOU 2616 N THR B 132 2868 2718 2433 86 -123 -298 N ATOM 2617 CA THR B 132 2.487 -4.217 10.868 1.00 18.55 C ANISOU 2617 CA THR B 132 2579 2376 2092 85 -175 -265 C ATOM 2618 C THR B 132 2.342 -4.845 12.242 1.00 17.06 C ANISOU 2618 C THR B 132 2468 2201 1814 59 -176 -275 C ATOM 2619 O THR B 132 1.838 -4.191 13.175 1.00 19.43 O ANISOU 2619 O THR B 132 2795 2514 2073 48 -162 -322 O ATOM 2620 CB THR B 132 3.592 -3.181 10.880 1.00 19.66 C ANISOU 2620 CB THR B 132 2695 2487 2287 105 -233 -271 C ATOM 2621 OG1 THR B 132 3.731 -2.676 9.521 1.00 21.82 O ANISOU 2621 OG1 THR B 132 2903 2748 2639 121 -227 -254 O ATOM 2622 CG2 THR B 132 4.890 -3.756 11.353 1.00 21.94 C ANISOU 2622 CG2 THR B 132 3012 2753 2569 106 -294 -242 C ATOM 2623 N GLY B 133 2.872 -6.043 12.371 1.00 16.22 N ANISOU 2623 N GLY B 133 2399 2086 1677 50 -199 -231 N ATOM 2624 CA GLY B 133 2.862 -6.805 13.598 1.00 16.70 C ANISOU 2624 CA GLY B 133 2544 2153 1650 21 -212 -224 C ATOM 2625 C GLY B 133 1.638 -7.678 13.796 1.00 18.15 C ANISOU 2625 C GLY B 133 2761 2365 1769 -12 -143 -224 C ATOM 2626 O GLY B 133 1.618 -8.491 14.738 1.00 21.58 O ANISOU 2626 O GLY B 133 3272 2802 2124 -44 -151 -206 O ATOM 2627 N THR B 134 0.605 -7.499 12.983 1.00 17.93 N ANISOU 2627 N THR B 134 2681 2359 1775 -10 -79 -242 N ATOM 2628 CA THR B 134 -0.576 -8.335 13.111 1.00 18.34 C ANISOU 2628 CA THR B 134 2755 2437 1778 -43 -11 -243 C ATOM 2629 C THR B 134 -0.209 -9.772 12.819 1.00 18.19 C ANISOU 2629 C THR B 134 2765 2402 1746 -53 -28 -185 C ATOM 2630 O THR B 134 0.482 -10.056 11.837 1.00 18.35 O ANISOU 2630 O THR B 134 2745 2399 1828 -26 -59 -154 O ATOM 2631 CB THR B 134 -1.703 -7.873 12.129 1.00 21.13 C ANISOU 2631 CB THR B 134 3033 2808 2187 -33 48 -272 C ATOM 2632 OG1 THR B 134 -2.006 -6.473 12.332 1.00 24.79 O ANISOU 2632 OG1 THR B 134 3462 3277 2680 -17 56 -328 O ATOM 2633 CG2 THR B 134 -2.951 -8.658 12.327 1.00 21.33 C ANISOU 2633 CG2 THR B 134 3074 2861 2170 -69 119 -281 C ATOM 2634 N LYS B 135 -0.731 -10.693 13.636 1.00 20.33 N ANISOU 2634 N LYS B 135 3104 2683 1936 -95 -2 -173 N ATOM 2635 CA LYS B 135 -0.497 -12.134 13.411 1.00 21.11 C ANISOU 2635 CA LYS B 135 3235 2762 2024 -109 -18 -117 C ATOM 2636 C LYS B 135 -1.553 -12.642 12.455 1.00 21.20 C ANISOU 2636 C LYS B 135 3201 2790 2066 -116 48 -119 C ATOM 2637 O LYS B 135 -2.757 -12.370 12.624 1.00 24.93 O ANISOU 2637 O LYS B 135 3660 3294 2517 -140 117 -156 O ATOM 2638 CB LYS B 135 -0.570 -12.920 14.703 1.00 27.70 C ANISOU 2638 CB LYS B 135 4171 3594 2758 -156 -25 -96 C ATOM 2639 CG LYS B 135 0.262 -12.301 15.829 1.00 34.24 C ANISOU 2639 CG LYS B 135 5056 4414 3538 -158 -87 -103 C ATOM 2640 CD LYS B 135 -0.633 -11.640 16.895 1.00 37.31 C ANISOU 2640 CD LYS B 135 5490 4844 3844 -198 -28 -155 C ATOM 2641 CE LYS B 135 -0.922 -10.158 16.624 1.00 41.78 C ANISOU 2641 CE LYS B 135 5985 5430 4460 -168 0 -221 C ATOM 2642 NZ LYS B 135 -2.270 -9.834 16.051 1.00 32.47 N ANISOU 2642 NZ LYS B 135 4742 4284 3313 -173 93 -265 N ATOM 2643 N CYS B 136 -1.080 -13.402 11.465 1.00 18.92 N ANISOU 2643 N CYS B 136 2884 2476 1829 -96 25 -83 N ATOM 2644 CA CYS B 136 -1.922 -13.878 10.394 1.00 17.00 C ANISOU 2644 CA CYS B 136 2594 2243 1621 -99 73 -84 C ATOM 2645 C CYS B 136 -1.757 -15.372 10.266 1.00 17.53 C ANISOU 2645 C CYS B 136 2698 2285 1677 -116 62 -39 C ATOM 2646 O CYS B 136 -0.786 -15.923 10.746 1.00 20.73 O ANISOU 2646 O CYS B 136 3148 2657 2070 -112 5 -6 O ATOM 2647 CB CYS B 136 -1.523 -13.293 9.107 1.00 16.59 C ANISOU 2647 CB CYS B 136 2470 2185 1650 -58 59 -89 C ATOM 2648 SG CYS B 136 -1.550 -11.450 9.089 1.00 24.74 S ANISOU 2648 SG CYS B 136 3452 3233 2714 -32 57 -136 S ATOM 2649 N LEU B 137 -2.744 -16.017 9.639 1.00 16.96 N ANISOU 2649 N LEU B 137 2606 2224 1614 -134 112 -41 N ATOM 2650 CA LEU B 137 -2.694 -17.455 9.406 1.00 16.62 C ANISOU 2650 CA LEU B 137 2592 2154 1569 -151 105 -2 C ATOM 2651 C LEU B 137 -2.514 -17.696 7.941 1.00 15.33 C ANISOU 2651 C LEU B 137 2367 1979 1477 -121 103 -2 C ATOM 2652 O LEU B 137 -3.334 -17.273 7.102 1.00 15.33 O ANISOU 2652 O LEU B 137 2315 2005 1506 -118 142 -28 O ATOM 2653 CB LEU B 137 -4.016 -18.099 9.837 1.00 16.13 C ANISOU 2653 CB LEU B 137 2557 2111 1460 -204 169 -6 C ATOM 2654 CG LEU B 137 -4.093 -19.620 9.752 1.00 17.27 C ANISOU 2654 CG LEU B 137 2742 2224 1596 -231 164 35 C ATOM 2655 CD1 LEU B 137 -3.184 -20.266 10.736 1.00 19.67 C ANISOU 2655 CD1 LEU B 137 3127 2490 1857 -242 106 79 C ATOM 2656 CD2 LEU B 137 -5.529 -20.121 9.964 1.00 20.53 C ANISOU 2656 CD2 LEU B 137 3162 2660 1977 -285 238 24 C ATOM 2657 N ILE B 138 -1.417 -18.367 7.629 1.00 13.87 N ANISOU 2657 N ILE B 138 2191 1755 1324 -100 53 26 N ATOM 2658 CA ILE B 138 -1.063 -18.768 6.281 1.00 13.66 C ANISOU 2658 CA ILE B 138 2117 1714 1360 -74 50 26 C ATOM 2659 C ILE B 138 -1.275 -20.271 6.181 1.00 14.20 C ANISOU 2659 C ILE B 138 2218 1753 1427 -96 51 50 C ATOM 2660 O ILE B 138 -0.885 -20.985 7.093 1.00 15.30 O ANISOU 2660 O ILE B 138 2415 1861 1539 -110 17 80 O ATOM 2661 CB ILE B 138 0.370 -18.442 5.937 1.00 14.53 C ANISOU 2661 CB ILE B 138 2202 1798 1520 -34 -1 30 C ATOM 2662 CG1 ILE B 138 0.677 -16.979 6.360 1.00 17.33 C ANISOU 2662 CG1 ILE B 138 2540 2174 1870 -18 -13 11 C ATOM 2663 CG2 ILE B 138 0.622 -18.658 4.442 1.00 15.63 C ANISOU 2663 CG2 ILE B 138 2288 1934 1718 -13 14 19 C ATOM 2664 CD1 ILE B 138 2.190 -16.612 6.285 1.00 22.11 C ANISOU 2664 CD1 ILE B 138 3125 2752 2525 17 -69 16 C ATOM 2665 N SER B 139 -1.847 -20.784 5.086 1.00 13.63 N ANISOU 2665 N SER B 139 2112 1683 1383 -99 83 40 N ATOM 2666 CA SER B 139 -2.085 -22.217 5.010 1.00 14.14 C ANISOU 2666 CA SER B 139 2208 1716 1449 -121 84 60 C ATOM 2667 C SER B 139 -1.899 -22.734 3.595 1.00 14.01 C ANISOU 2667 C SER B 139 2149 1687 1488 -102 90 46 C ATOM 2668 O SER B 139 -1.963 -21.971 2.602 1.00 14.87 O ANISOU 2668 O SER B 139 2207 1823 1621 -84 108 19 O ATOM 2669 CB SER B 139 -3.505 -22.500 5.519 1.00 15.47 C ANISOU 2669 CB SER B 139 2400 1908 1571 -171 133 60 C ATOM 2670 OG SER B 139 -4.488 -21.712 4.870 1.00 15.63 O ANISOU 2670 OG SER B 139 2367 1972 1599 -174 179 25 O ATOM 2671 N GLY B 140 -1.619 -24.020 3.488 1.00 12.93 N ANISOU 2671 N GLY B 140 2036 1504 1371 -107 71 62 N ATOM 2672 CA GLY B 140 -1.453 -24.656 2.209 1.00 12.95 C ANISOU 2672 CA GLY B 140 2006 1491 1423 -93 80 43 C ATOM 2673 C GLY B 140 -0.867 -26.045 2.250 1.00 12.98 C ANISOU 2673 C GLY B 140 2037 1434 1462 -90 47 58 C ATOM 2674 O GLY B 140 -0.489 -26.563 3.327 1.00 14.16 O ANISOU 2674 O GLY B 140 2236 1545 1599 -97 7 93 O ATOM 2675 N TRP B 141 -0.859 -26.673 1.077 1.00 12.93 N ANISOU 2675 N TRP B 141 2002 1414 1495 -82 63 33 N ATOM 2676 CA TRP B 141 -0.283 -27.994 0.884 1.00 13.74 C ANISOU 2676 CA TRP B 141 2119 1454 1647 -73 35 35 C ATOM 2677 C TRP B 141 1.106 -27.987 0.242 1.00 15.69 C ANISOU 2677 C TRP B 141 2327 1674 1961 -26 13 10 C ATOM 2678 O TRP B 141 1.560 -28.977 -0.401 1.00 16.85 O ANISOU 2678 O TRP B 141 2462 1776 2163 -13 7 -11 O ATOM 2679 CB TRP B 141 -1.222 -28.911 0.078 1.00 13.90 C ANISOU 2679 CB TRP B 141 2140 1469 1673 -100 67 18 C ATOM 2680 CG TRP B 141 -2.503 -29.292 0.759 1.00 14.70 C ANISOU 2680 CG TRP B 141 2279 1578 1728 -150 86 44 C ATOM 2681 CD1 TRP B 141 -2.708 -30.363 1.565 1.00 16.51 C ANISOU 2681 CD1 TRP B 141 2561 1758 1952 -178 64 79 C ATOM 2682 CD2 TRP B 141 -3.774 -28.619 0.658 1.00 13.34 C ANISOU 2682 CD2 TRP B 141 2092 1463 1512 -181 132 34 C ATOM 2683 NE1 TRP B 141 -4.023 -30.411 2.002 1.00 16.13 N ANISOU 2683 NE1 TRP B 141 2534 1737 1857 -230 101 91 N ATOM 2684 CE2 TRP B 141 -4.705 -29.363 1.443 1.00 15.15 C ANISOU 2684 CE2 TRP B 141 2363 1677 1714 -230 144 60 C ATOM 2685 CE3 TRP B 141 -4.221 -27.476 -0.015 1.00 13.57 C ANISOU 2685 CE3 TRP B 141 2077 1550 1530 -173 161 6 C ATOM 2686 CZ2 TRP B 141 -6.039 -28.977 1.558 1.00 15.26 C ANISOU 2686 CZ2 TRP B 141 2367 1737 1696 -269 189 52 C ATOM 2687 CZ3 TRP B 141 -5.546 -27.133 0.098 1.00 14.99 C ANISOU 2687 CZ3 TRP B 141 2247 1767 1680 -208 196 0 C ATOM 2688 CH2 TRP B 141 -6.444 -27.875 0.865 1.00 15.02 C ANISOU 2688 CH2 TRP B 141 2284 1759 1663 -254 213 20 C ATOM 2689 N GLY B 142 1.816 -26.876 0.400 1.00 15.03 N ANISOU 2689 N GLY B 142 2217 1615 1878 -2 4 6 N ATOM 2690 CA GLY B 142 3.130 -26.751 -0.177 1.00 15.39 C ANISOU 2690 CA GLY B 142 2218 1640 1990 38 -9 -21 C ATOM 2691 C GLY B 142 4.211 -27.531 0.569 1.00 16.01 C ANISOU 2691 C GLY B 142 2309 1648 2126 63 -75 -4 C ATOM 2692 O GLY B 142 3.957 -28.167 1.625 1.00 17.22 O ANISOU 2692 O GLY B 142 2517 1765 2259 47 -118 37 O ATOM 2693 N ASN B 143 5.413 -27.447 0.036 1.00 16.04 N ANISOU 2693 N ASN B 143 2261 1630 2203 100 -84 -36 N ATOM 2694 CA ASN B 143 6.593 -28.130 0.565 1.00 16.96 C ANISOU 2694 CA ASN B 143 2371 1675 2399 133 -150 -31 C ATOM 2695 C ASN B 143 6.762 -27.726 2.023 1.00 16.57 C ANISOU 2695 C ASN B 143 2366 1613 2316 130 -217 20 C ATOM 2696 O ASN B 143 6.613 -26.556 2.394 1.00 17.39 O ANISOU 2696 O ASN B 143 2471 1767 2370 123 -207 29 O ATOM 2697 CB ASN B 143 7.826 -27.694 -0.213 1.00 16.19 C ANISOU 2697 CB ASN B 143 2197 1574 2380 170 -137 -79 C ATOM 2698 CG ASN B 143 8.996 -28.677 -0.113 1.00 15.53 C ANISOU 2698 CG ASN B 143 2084 1408 2407 208 -190 -97 C ATOM 2699 OD1 ASN B 143 9.017 -29.572 0.694 1.00 18.74 O ANISOU 2699 OD1 ASN B 143 2533 1755 2833 211 -255 -65 O ATOM 2700 ND2 ASN B 143 9.994 -28.431 -0.955 1.00 21.02 N ANISOU 2700 ND2 ASN B 143 2706 2102 3178 236 -161 -151 N ATOM 2701 N THR B 144 7.112 -28.730 2.860 1.00 17.25 N ANISOU 2701 N THR B 144 2492 1628 2433 135 -289 52 N ATOM 2702 CA THR B 144 7.404 -28.463 4.248 1.00 19.59 C ANISOU 2702 CA THR B 144 2840 1905 2699 131 -364 101 C ATOM 2703 C THR B 144 8.922 -28.452 4.532 1.00 18.97 C ANISOU 2703 C THR B 144 2721 1770 2716 178 -441 93 C ATOM 2704 O THR B 144 9.328 -28.245 5.693 1.00 23.36 O ANISOU 2704 O THR B 144 3319 2302 3255 178 -519 132 O ATOM 2705 CB THR B 144 6.693 -29.437 5.212 1.00 20.15 C ANISOU 2705 CB THR B 144 3000 1937 2717 94 -404 156 C ATOM 2706 OG1 THR B 144 7.267 -30.730 5.109 1.00 24.24 O ANISOU 2706 OG1 THR B 144 3519 2369 3320 114 -458 159 O ATOM 2707 CG2 THR B 144 5.177 -29.506 4.926 1.00 21.12 C ANISOU 2707 CG2 THR B 144 3155 2113 2758 45 -325 160 C ATOM 2708 N ALA B 145 9.735 -28.670 3.490 1.00 20.28 N ANISOU 2708 N ALA B 145 2807 1916 2983 215 -420 39 N ATOM 2709 CA ALA B 145 11.185 -28.579 3.574 1.00 21.04 C ANISOU 2709 CA ALA B 145 2843 1964 3187 261 -478 17 C ATOM 2710 C ALA B 145 11.784 -27.356 2.868 1.00 20.67 C ANISOU 2710 C ALA B 145 2718 1970 3165 277 -426 -28 C ATOM 2711 O ALA B 145 11.289 -26.927 1.826 1.00 21.64 O ANISOU 2711 O ALA B 145 2813 2150 3258 263 -334 -61 O ATOM 2712 CB ALA B 145 11.833 -29.825 3.041 1.00 23.36 C ANISOU 2712 CB ALA B 145 3099 2181 3597 293 -501 -15 C ATOM 2713 N SER B 146 12.842 -26.779 3.435 1.00 19.82 N ANISOU 2713 N SER B 146 2578 1841 3112 303 -488 -27 N ATOM 2714 CA SER B 146 13.591 -25.684 2.836 1.00 19.40 C ANISOU 2714 CA SER B 146 2445 1823 3101 319 -448 -68 C ATOM 2715 C SER B 146 14.640 -26.124 1.833 1.00 21.49 C ANISOU 2715 C SER B 146 2616 2054 3496 353 -420 -132 C ATOM 2716 O SER B 146 15.116 -25.305 1.049 1.00 22.74 O ANISOU 2716 O SER B 146 2708 2251 3682 355 -358 -173 O ATOM 2717 CB SER B 146 14.331 -24.945 3.965 1.00 25.81 C ANISOU 2717 CB SER B 146 3261 2618 3926 331 -536 -41 C ATOM 2718 OG SER B 146 13.399 -24.414 4.834 1.00 38.84 O ANISOU 2718 OG SER B 146 4994 4308 5454 298 -549 7 O ATOM 2719 N SER B 147 15.033 -27.391 1.924 1.00 19.75 N ANISOU 2719 N SER B 147 2390 1757 3357 377 -470 -140 N ATOM 2720 CA SER B 147 15.882 -28.090 0.951 1.00 20.82 C ANISOU 2720 CA SER B 147 2440 1850 3619 409 -438 -209 C ATOM 2721 C SER B 147 15.216 -29.427 0.658 1.00 22.51 C ANISOU 2721 C SER B 147 2694 2027 3831 404 -430 -211 C ATOM 2722 O SER B 147 14.663 -30.086 1.532 1.00 24.03 O ANISOU 2722 O SER B 147 2965 2182 3984 394 -499 -155 O ATOM 2723 CB SER B 147 17.304 -28.319 1.487 1.00 21.87 C ANISOU 2723 CB SER B 147 2509 1905 3896 456 -531 -226 C ATOM 2724 OG SER B 147 17.973 -27.071 1.615 1.00 23.56 O ANISOU 2724 OG SER B 147 2674 2154 4124 459 -528 -234 O ATOM 2725 N GLY B 148 15.246 -29.839 -0.599 1.00 26.06 N ANISOU 2725 N GLY B 148 3096 2487 4320 407 -343 -276 N ATOM 2726 CA GLY B 148 14.615 -31.095 -0.939 1.00 25.44 C ANISOU 2726 CA GLY B 148 3053 2371 4243 401 -334 -284 C ATOM 2727 C GLY B 148 13.099 -30.987 -0.912 1.00 25.04 C ANISOU 2727 C GLY B 148 3089 2379 4047 352 -295 -238 C ATOM 2728 O GLY B 148 12.551 -29.886 -1.009 1.00 24.79 O ANISOU 2728 O GLY B 148 3073 2427 3919 324 -248 -221 O ATOM 2729 N ALA B 149 12.453 -32.155 -0.716 1.00 29.58 N ANISOU 2729 N ALA B 149 3717 2906 4615 342 -323 -218 N ATOM 2730 CA ALA B 149 10.994 -32.338 -0.868 1.00 30.82 C ANISOU 2730 CA ALA B 149 3947 3108 4657 295 -279 -189 C ATOM 2731 C ALA B 149 10.410 -33.075 0.289 1.00 34.94 C ANISOU 2731 C ALA B 149 4552 3579 5145 277 -359 -118 C ATOM 2732 O ALA B 149 10.810 -34.199 0.617 1.00 35.34 O ANISOU 2732 O ALA B 149 4611 3541 5275 297 -425 -113 O ATOM 2733 CB ALA B 149 10.691 -33.180 -2.078 1.00 33.89 C ANISOU 2733 CB ALA B 149 4314 3488 5073 292 -213 -249 C ATOM 2734 N ASP B 150 9.366 -32.498 0.816 1.00 25.38 N ANISOU 2734 N ASP B 150 3404 2427 3814 235 -344 -67 N ATOM 2735 CA ASP B 150 8.606 -33.070 1.862 1.00 26.01 C ANISOU 2735 CA ASP B 150 3571 2478 3835 202 -396 0 C ATOM 2736 C ASP B 150 7.189 -32.481 1.707 1.00 26.04 C ANISOU 2736 C ASP B 150 3613 2567 3714 151 -321 17 C ATOM 2737 O ASP B 150 6.826 -31.551 2.407 1.00 26.12 O ANISOU 2737 O ASP B 150 3652 2626 3645 131 -321 51 O ATOM 2738 CB ASP B 150 9.195 -32.734 3.219 1.00 34.85 C ANISOU 2738 CB ASP B 150 4727 3567 4948 210 -490 56 C ATOM 2739 CG ASP B 150 8.671 -33.647 4.315 1.00 42.84 C ANISOU 2739 CG ASP B 150 5834 4522 5921 179 -561 127 C ATOM 2740 OD1 ASP B 150 7.637 -34.314 4.064 1.00 38.66 O ANISOU 2740 OD1 ASP B 150 5344 3996 5349 142 -520 136 O ATOM 2741 OD2 ASP B 150 9.285 -33.676 5.420 1.00 49.17 O ANISOU 2741 OD2 ASP B 150 6675 5277 6733 187 -658 174 O ATOM 2742 N TYR B 151 6.426 -33.019 0.752 1.00 22.44 N ANISOU 2742 N TYR B 151 3151 2124 3249 133 -259 -15 N ATOM 2743 CA TYR B 151 5.082 -32.503 0.463 1.00 22.07 C ANISOU 2743 CA TYR B 151 3129 2155 3103 87 -190 -8 C ATOM 2744 C TYR B 151 4.053 -33.297 1.235 1.00 23.95 C ANISOU 2744 C TYR B 151 3442 2368 3290 42 -210 43 C ATOM 2745 O TYR B 151 4.063 -34.552 1.193 1.00 23.55 O ANISOU 2745 O TYR B 151 3411 2247 3289 41 -239 46 O ATOM 2746 CB TYR B 151 4.772 -32.546 -1.035 1.00 19.54 C ANISOU 2746 CB TYR B 151 2762 1869 2794 87 -114 -71 C ATOM 2747 CG TYR B 151 5.544 -31.520 -1.808 1.00 20.45 C ANISOU 2747 CG TYR B 151 2813 2029 2928 114 -76 -116 C ATOM 2748 CD1 TYR B 151 5.011 -30.287 -2.099 1.00 18.34 C ANISOU 2748 CD1 TYR B 151 2537 1843 2589 97 -29 -115 C ATOM 2749 CD2 TYR B 151 6.867 -31.743 -2.142 1.00 21.34 C ANISOU 2749 CD2 TYR B 151 2872 2099 3137 158 -93 -156 C ATOM 2750 CE1 TYR B 151 5.731 -29.305 -2.775 1.00 18.37 C ANISOU 2750 CE1 TYR B 151 2487 1885 2607 116 3 -149 C ATOM 2751 CE2 TYR B 151 7.590 -30.792 -2.799 1.00 22.24 C ANISOU 2751 CE2 TYR B 151 2928 2254 3268 176 -54 -194 C ATOM 2752 CZ TYR B 151 7.038 -29.589 -3.135 1.00 21.94 C ANISOU 2752 CZ TYR B 151 2888 2296 3152 154 -6 -189 C ATOM 2753 OH TYR B 151 7.713 -28.549 -3.774 1.00 27.94 O ANISOU 2753 OH TYR B 151 3597 3098 3921 165 33 -219 O ATOM 2754 N PRO B 152 3.188 -32.583 1.965 1.00 19.95 N ANISOU 2754 N PRO B 152 2976 1915 2688 5 -193 82 N ATOM 2755 CA PRO B 152 2.211 -33.172 2.886 1.00 20.39 C ANISOU 2755 CA PRO B 152 3107 1956 2684 -47 -204 136 C ATOM 2756 C PRO B 152 0.921 -33.589 2.217 1.00 21.52 C ANISOU 2756 C PRO B 152 3253 2127 2798 -88 -141 120 C ATOM 2757 O PRO B 152 0.452 -32.898 1.292 1.00 22.18 O ANISOU 2757 O PRO B 152 3291 2273 2864 -87 -80 79 O ATOM 2758 CB PRO B 152 1.931 -32.025 3.862 1.00 22.31 C ANISOU 2758 CB PRO B 152 3378 2255 2842 -67 -201 168 C ATOM 2759 CG PRO B 152 2.074 -30.765 2.969 1.00 20.57 C ANISOU 2759 CG PRO B 152 3087 2106 2622 -40 -149 119 C ATOM 2760 CD PRO B 152 3.157 -31.098 1.982 1.00 21.53 C ANISOU 2760 CD PRO B 152 3150 2193 2839 9 -160 74 C ATOM 2761 N ASP B 153 0.286 -34.624 2.735 1.00 21.28 N ANISOU 2761 N ASP B 153 3280 2052 2756 -128 -157 157 N ATOM 2762 CA ASP B 153 -1.060 -34.941 2.305 1.00 20.16 C ANISOU 2762 CA ASP B 153 3144 1939 2579 -176 -98 148 C ATOM 2763 C ASP B 153 -2.060 -33.999 3.014 1.00 19.41 C ANISOU 2763 C ASP B 153 3069 1916 2389 -219 -55 172 C ATOM 2764 O ASP B 153 -3.116 -33.693 2.464 1.00 19.98 O ANISOU 2764 O ASP B 153 3116 2041 2436 -245 5 147 O ATOM 2765 CB ASP B 153 -1.398 -36.388 2.622 1.00 19.77 C ANISOU 2765 CB ASP B 153 3146 1812 2554 -209 -128 180 C ATOM 2766 CG ASP B 153 -0.605 -37.395 1.789 1.00 24.58 C ANISOU 2766 CG ASP B 153 3728 2347 3265 -168 -162 144 C ATOM 2767 OD1 ASP B 153 -0.052 -37.056 0.722 1.00 26.00 O ANISOU 2767 OD1 ASP B 153 3843 2546 3488 -125 -140 83 O ATOM 2768 OD2 ASP B 153 -0.667 -38.574 2.187 1.00 27.92 O ANISOU 2768 OD2 ASP B 153 4198 2693 3720 -189 -204 175 O ATOM 2769 N GLU B 154 -1.739 -33.595 4.243 1.00 18.47 N ANISOU 2769 N GLU B 154 2996 1795 2224 -227 -88 217 N ATOM 2770 CA GLU B 154 -2.661 -32.818 5.086 1.00 18.62 C ANISOU 2770 CA GLU B 154 3045 1876 2155 -273 -46 237 C ATOM 2771 C GLU B 154 -2.295 -31.336 5.136 1.00 17.80 C ANISOU 2771 C GLU B 154 2903 1834 2025 -242 -33 215 C ATOM 2772 O GLU B 154 -1.136 -30.967 5.202 1.00 18.61 O ANISOU 2772 O GLU B 154 2993 1920 2158 -196 -81 213 O ATOM 2773 CB GLU B 154 -2.701 -33.414 6.473 1.00 21.50 C ANISOU 2773 CB GLU B 154 3500 2198 2470 -317 -85 303 C ATOM 2774 CG GLU B 154 -3.262 -34.839 6.430 1.00 26.00 C ANISOU 2774 CG GLU B 154 4110 2708 3060 -360 -89 328 C ATOM 2775 CD GLU B 154 -3.761 -35.434 7.708 1.00 33.03 C ANISOU 2775 CD GLU B 154 5095 3570 3884 -428 -101 394 C ATOM 2776 OE1 GLU B 154 -4.207 -36.612 7.614 1.00 40.00 O ANISOU 2776 OE1 GLU B 154 6009 4399 4791 -464 -105 416 O ATOM 2777 OE2 GLU B 154 -3.733 -34.806 8.782 1.00 28.46 O ANISOU 2777 OE2 GLU B 154 4566 3020 3229 -451 -105 424 O ATOM 2778 N LEU B 155 -3.328 -30.495 5.119 1.00 16.46 N ANISOU 2778 N LEU B 155 2714 1734 1806 -268 30 196 N ATOM 2779 CA LEU B 155 -3.171 -29.054 5.075 1.00 15.47 C ANISOU 2779 CA LEU B 155 2549 1669 1660 -242 48 170 C ATOM 2780 C LEU B 155 -2.353 -28.569 6.265 1.00 15.13 C ANISOU 2780 C LEU B 155 2551 1616 1582 -234 0 201 C ATOM 2781 O LEU B 155 -2.605 -29.001 7.415 1.00 18.23 O ANISOU 2781 O LEU B 155 3016 1991 1919 -276 -13 243 O ATOM 2782 CB LEU B 155 -4.549 -28.400 5.107 1.00 16.26 C ANISOU 2782 CB LEU B 155 2631 1833 1716 -280 118 150 C ATOM 2783 CG LEU B 155 -4.605 -26.870 4.966 1.00 16.27 C ANISOU 2783 CG LEU B 155 2584 1894 1702 -256 141 118 C ATOM 2784 CD1 LEU B 155 -4.066 -26.405 3.642 1.00 15.06 C ANISOU 2784 CD1 LEU B 155 2366 1751 1604 -208 135 84 C ATOM 2785 CD2 LEU B 155 -6.042 -26.320 5.143 1.00 19.50 C ANISOU 2785 CD2 LEU B 155 2975 2358 2076 -296 207 97 C ATOM 2786 N GLN B 156 -1.390 -27.686 5.974 1.00 15.44 N ANISOU 2786 N GLN B 156 2549 1667 1650 -183 -25 181 N ATOM 2787 CA GLN B 156 -0.518 -27.069 6.983 1.00 16.39 C ANISOU 2787 CA GLN B 156 2700 1781 1746 -168 -77 202 C ATOM 2788 C GLN B 156 -0.863 -25.621 7.212 1.00 14.51 C ANISOU 2788 C GLN B 156 2439 1609 1466 -167 -41 177 C ATOM 2789 O GLN B 156 -1.359 -24.942 6.318 1.00 14.68 O ANISOU 2789 O GLN B 156 2400 1674 1505 -156 8 139 O ATOM 2790 CB GLN B 156 0.949 -27.205 6.563 1.00 17.75 C ANISOU 2790 CB GLN B 156 2841 1907 1996 -112 -140 197 C ATOM 2791 CG GLN B 156 1.355 -28.612 6.292 1.00 17.61 C ANISOU 2791 CG GLN B 156 2838 1817 2035 -106 -179 213 C ATOM 2792 CD GLN B 156 1.558 -29.453 7.532 1.00 20.34 C ANISOU 2792 CD GLN B 156 3271 2106 2353 -133 -245 271 C ATOM 2793 OE1 GLN B 156 2.400 -29.142 8.380 1.00 22.74 O ANISOU 2793 OE1 GLN B 156 3604 2389 2649 -118 -310 294 O ATOM 2794 NE2 GLN B 156 0.797 -30.511 7.622 1.00 23.72 N ANISOU 2794 NE2 GLN B 156 3741 2506 2764 -174 -231 295 N ATOM 2795 N CYS B 157 -0.511 -25.129 8.406 1.00 16.08 N ANISOU 2795 N CYS B 157 2687 1810 1614 -177 -74 198 N ATOM 2796 CA CYS B 157 -0.887 -23.819 8.932 1.00 16.69 C ANISOU 2796 CA CYS B 157 2758 1943 1640 -184 -43 176 C ATOM 2797 C CYS B 157 0.376 -23.203 9.525 1.00 16.71 C ANISOU 2797 C CYS B 157 2773 1928 1650 -151 -114 184 C ATOM 2798 O CYS B 157 1.238 -23.905 10.082 1.00 18.14 O ANISOU 2798 O CYS B 157 3000 2055 1839 -145 -186 220 O ATOM 2799 CB CYS B 157 -1.982 -24.033 10.072 1.00 18.49 C ANISOU 2799 CB CYS B 157 3059 2193 1776 -250 -3 193 C ATOM 2800 SG CYS B 157 -3.702 -24.062 9.388 1.00 22.73 S ANISOU 2800 SG CYS B 157 3549 2778 2308 -287 101 159 S ATOM 2801 N LEU B 158 0.456 -21.881 9.457 1.00 15.65 N ANISOU 2801 N LEU B 158 2598 1834 1513 -131 -98 151 N ATOM 2802 CA LEU B 158 1.566 -21.125 10.051 1.00 14.63 C ANISOU 2802 CA LEU B 158 2476 1694 1390 -103 -161 153 C ATOM 2803 C LEU B 158 1.012 -19.806 10.564 1.00 15.44 C ANISOU 2803 C LEU B 158 2575 1850 1441 -114 -125 122 C ATOM 2804 O LEU B 158 0.301 -19.093 9.852 1.00 15.68 O ANISOU 2804 O LEU B 158 2550 1921 1488 -109 -65 86 O ATOM 2805 CB LEU B 158 2.647 -20.880 9.029 1.00 17.17 C ANISOU 2805 CB LEU B 158 2723 1995 1804 -49 -191 136 C ATOM 2806 CG LEU B 158 3.758 -19.928 9.443 1.00 18.31 C ANISOU 2806 CG LEU B 158 2853 2132 1971 -18 -248 129 C ATOM 2807 CD1 LEU B 158 4.577 -20.510 10.586 1.00 21.92 C ANISOU 2807 CD1 LEU B 158 3378 2540 2411 -22 -336 167 C ATOM 2808 CD2 LEU B 158 4.632 -19.645 8.220 1.00 20.04 C ANISOU 2808 CD2 LEU B 158 2988 2342 2287 27 -250 105 C ATOM 2809 N ASP B 159 1.326 -19.470 11.812 1.00 17.73 N ANISOU 2809 N ASP B 159 2928 2137 1671 -131 -163 133 N ATOM 2810 CA ASP B 159 1.005 -18.140 12.344 1.00 18.38 C ANISOU 2810 CA ASP B 159 3006 2264 1714 -135 -138 96 C ATOM 2811 C ASP B 159 2.237 -17.256 12.229 1.00 18.00 C ANISOU 2811 C ASP B 159 2920 2200 1718 -89 -200 85 C ATOM 2812 O ASP B 159 3.302 -17.605 12.703 1.00 21.31 O ANISOU 2812 O ASP B 159 3370 2578 2149 -76 -280 112 O ATOM 2813 CB ASP B 159 0.508 -18.246 13.777 1.00 20.54 C ANISOU 2813 CB ASP B 159 3375 2551 1880 -188 -132 107 C ATOM 2814 CG ASP B 159 -0.841 -18.981 13.836 1.00 28.12 C ANISOU 2814 CG ASP B 159 4360 3533 2793 -240 -52 111 C ATOM 2815 OD1 ASP B 159 -1.887 -18.436 13.401 1.00 32.79 O ANISOU 2815 OD1 ASP B 159 4901 4168 3390 -248 27 69 O ATOM 2816 OD2 ASP B 159 -0.854 -20.117 14.273 1.00 32.41 O ANISOU 2816 OD2 ASP B 159 4969 4045 3300 -273 -72 156 O ATOM 2817 N ALA B 160 2.101 -16.156 11.482 1.00 17.63 N ANISOU 2817 N ALA B 160 2799 2182 1715 -63 -166 46 N ATOM 2818 CA ALA B 160 3.239 -15.283 11.201 1.00 16.47 C ANISOU 2818 CA ALA B 160 2606 2021 1630 -22 -216 33 C ATOM 2819 C ALA B 160 2.786 -13.835 11.142 1.00 16.27 C ANISOU 2819 C ALA B 160 2544 2034 1604 -16 -181 -10 C ATOM 2820 O ALA B 160 1.655 -13.547 10.767 1.00 18.23 O ANISOU 2820 O ALA B 160 2770 2317 1841 -29 -113 -34 O ATOM 2821 CB ALA B 160 3.838 -15.654 9.892 1.00 18.67 C ANISOU 2821 CB ALA B 160 2818 2279 1997 11 -219 39 C ATOM 2822 N PRO B 161 3.691 -12.898 11.480 1.00 16.78 N ANISOU 2822 N PRO B 161 2596 2088 1691 6 -231 -23 N ATOM 2823 CA PRO B 161 3.287 -11.502 11.548 1.00 15.98 C ANISOU 2823 CA PRO B 161 2465 2015 1591 11 -205 -66 C ATOM 2824 C PRO B 161 3.611 -10.731 10.285 1.00 15.64 C ANISOU 2824 C PRO B 161 2337 1971 1633 43 -195 -78 C ATOM 2825 O PRO B 161 4.568 -11.000 9.588 1.00 16.80 O ANISOU 2825 O PRO B 161 2449 2092 1841 65 -226 -60 O ATOM 2826 CB PRO B 161 4.141 -10.966 12.688 1.00 17.04 C ANISOU 2826 CB PRO B 161 2642 2133 1699 12 -273 -71 C ATOM 2827 CG PRO B 161 5.413 -11.772 12.544 1.00 18.48 C ANISOU 2827 CG PRO B 161 2824 2270 1928 32 -346 -32 C ATOM 2828 CD PRO B 161 4.977 -13.133 12.113 1.00 15.95 C ANISOU 2828 CD PRO B 161 2518 1942 1599 19 -319 -1 C ATOM 2829 N VAL B 162 2.788 -9.734 10.019 1.00 14.74 N ANISOU 2829 N VAL B 162 2192 1885 1524 43 -152 -112 N ATOM 2830 CA VAL B 162 3.061 -8.770 8.975 1.00 13.96 C ANISOU 2830 CA VAL B 162 2024 1784 1497 68 -150 -123 C ATOM 2831 C VAL B 162 4.323 -7.999 9.334 1.00 16.56 C ANISOU 2831 C VAL B 162 2343 2087 1861 87 -212 -126 C ATOM 2832 O VAL B 162 4.474 -7.477 10.444 1.00 15.42 O ANISOU 2832 O VAL B 162 2234 1941 1683 81 -241 -146 O ATOM 2833 CB VAL B 162 1.885 -7.790 8.851 1.00 13.89 C ANISOU 2833 CB VAL B 162 1991 1802 1486 64 -104 -160 C ATOM 2834 CG1 VAL B 162 2.219 -6.708 7.792 1.00 15.26 C ANISOU 2834 CG1 VAL B 162 2101 1966 1733 86 -113 -165 C ATOM 2835 CG2 VAL B 162 0.617 -8.508 8.458 1.00 15.89 C ANISOU 2835 CG2 VAL B 162 2244 2078 1715 45 -45 -161 C ATOM 2836 N LEU B 163 5.242 -7.913 8.379 1.00 16.60 N ANISOU 2836 N LEU B 163 2299 2072 1937 106 -229 -110 N ATOM 2837 CA LEU B 163 6.480 -7.142 8.559 1.00 15.68 C ANISOU 2837 CA LEU B 163 2157 1928 1871 122 -285 -114 C ATOM 2838 C LEU B 163 6.399 -5.721 7.997 1.00 15.58 C ANISOU 2838 C LEU B 163 2097 1919 1904 130 -274 -135 C ATOM 2839 O LEU B 163 5.615 -5.446 7.122 1.00 16.05 O ANISOU 2839 O LEU B 163 2131 1995 1973 127 -229 -136 O ATOM 2840 CB LEU B 163 7.644 -7.891 7.918 1.00 18.70 C ANISOU 2840 CB LEU B 163 2509 2283 2312 135 -309 -89 C ATOM 2841 CG LEU B 163 7.991 -9.243 8.513 1.00 17.76 C ANISOU 2841 CG LEU B 163 2433 2145 2169 134 -341 -67 C ATOM 2842 CD1 LEU B 163 8.938 -10.028 7.601 1.00 19.33 C ANISOU 2842 CD1 LEU B 163 2586 2318 2439 149 -347 -50 C ATOM 2843 CD2 LEU B 163 8.599 -9.087 9.866 1.00 21.43 C ANISOU 2843 CD2 LEU B 163 2943 2591 2610 133 -413 -69 C ATOM 2844 N SER B 164 7.227 -4.830 8.534 1.00 17.00 N ANISOU 2844 N SER B 164 2269 2079 2113 138 -323 -149 N ATOM 2845 CA SER B 164 7.243 -3.463 8.048 1.00 15.69 C ANISOU 2845 CA SER B 164 2059 1906 1996 144 -321 -165 C ATOM 2846 C SER B 164 7.725 -3.365 6.633 1.00 14.75 C ANISOU 2846 C SER B 164 1885 1779 1941 146 -301 -142 C ATOM 2847 O SER B 164 8.507 -4.206 6.182 1.00 17.13 O ANISOU 2847 O SER B 164 2172 2071 2267 148 -303 -120 O ATOM 2848 CB SER B 164 8.150 -2.617 8.925 1.00 18.78 C ANISOU 2848 CB SER B 164 2452 2272 2410 150 -383 -185 C ATOM 2849 OG SER B 164 9.507 -2.988 8.769 1.00 18.69 O ANISOU 2849 OG SER B 164 2416 2233 2451 157 -426 -165 O ATOM 2850 N GLN B 165 7.324 -2.293 5.941 1.00 17.03 N ANISOU 2850 N GLN B 165 2143 2068 2260 144 -283 -147 N ATOM 2851 CA GLN B 165 7.777 -2.066 4.599 1.00 17.01 C ANISOU 2851 CA GLN B 165 2096 2057 2308 138 -263 -123 C ATOM 2852 C GLN B 165 9.309 -1.962 4.564 1.00 16.50 C ANISOU 2852 C GLN B 165 2000 1965 2304 140 -296 -115 C ATOM 2853 O GLN B 165 9.935 -2.510 3.652 1.00 16.91 O ANISOU 2853 O GLN B 165 2023 2014 2386 134 -273 -96 O ATOM 2854 CB GLN B 165 7.093 -0.838 4.016 1.00 19.10 C ANISOU 2854 CB GLN B 165 2343 2318 2594 133 -254 -126 C ATOM 2855 CG GLN B 165 7.435 -0.624 2.576 1.00 20.51 C ANISOU 2855 CG GLN B 165 2490 2493 2811 119 -230 -95 C ATOM 2856 CD GLN B 165 6.465 0.294 1.860 1.00 27.35 C ANISOU 2856 CD GLN B 165 3350 3357 3684 112 -222 -89 C ATOM 2857 OE1 GLN B 165 5.226 0.078 1.868 1.00 34.18 O ANISOU 2857 OE1 GLN B 165 4231 4240 4514 116 -205 -99 O ATOM 2858 NE2 GLN B 165 7.016 1.268 1.174 1.00 26.94 N ANISOU 2858 NE2 GLN B 165 3274 3281 3680 99 -233 -71 N ATOM 2859 N ALA B 166 9.921 -1.314 5.549 1.00 15.93 N ANISOU 2859 N ALA B 166 1930 1871 2252 147 -349 -134 N ATOM 2860 CA ALA B 166 11.360 -1.156 5.573 1.00 16.51 C ANISOU 2860 CA ALA B 166 1965 1915 2392 149 -386 -131 C ATOM 2861 C ALA B 166 12.051 -2.520 5.574 1.00 18.82 C ANISOU 2861 C ALA B 166 2255 2204 2691 156 -390 -119 C ATOM 2862 O ALA B 166 13.040 -2.699 4.878 1.00 18.24 O ANISOU 2862 O ALA B 166 2133 2115 2681 153 -383 -111 O ATOM 2863 CB ALA B 166 11.803 -0.341 6.780 1.00 17.66 C ANISOU 2863 CB ALA B 166 2123 2038 2549 156 -451 -158 C ATOM 2864 N LYS B 167 11.523 -3.488 6.340 1.00 16.93 N ANISOU 2864 N LYS B 167 2067 1978 2389 163 -400 -120 N ATOM 2865 CA LYS B 167 12.159 -4.800 6.411 1.00 16.81 C ANISOU 2865 CA LYS B 167 2052 1951 2385 171 -414 -108 C ATOM 2866 C LYS B 167 11.975 -5.570 5.094 1.00 17.29 C ANISOU 2866 C LYS B 167 2087 2025 2457 166 -349 -92 C ATOM 2867 O LYS B 167 12.889 -6.280 4.641 1.00 17.42 O ANISOU 2867 O LYS B 167 2067 2023 2527 172 -348 -89 O ATOM 2868 CB LYS B 167 11.605 -5.604 7.594 1.00 17.63 C ANISOU 2868 CB LYS B 167 2226 2059 2413 174 -445 -107 C ATOM 2869 CG LYS B 167 12.053 -5.104 8.933 1.00 19.23 C ANISOU 2869 CG LYS B 167 2460 2243 2602 177 -520 -122 C ATOM 2870 CD LYS B 167 11.299 -5.857 10.040 1.00 20.75 C ANISOU 2870 CD LYS B 167 2736 2449 2699 169 -535 -118 C ATOM 2871 CE LYS B 167 11.704 -5.412 11.406 1.00 21.37 C ANISOU 2871 CE LYS B 167 2860 2511 2748 167 -611 -134 C ATOM 2872 NZ LYS B 167 10.828 -6.059 12.447 1.00 25.52 N ANISOU 2872 NZ LYS B 167 3476 3056 3164 148 -612 -131 N ATOM 2873 N CYS B 168 10.795 -5.443 4.513 1.00 17.00 N ANISOU 2873 N CYS B 168 2068 2018 2372 154 -296 -87 N ATOM 2874 CA CYS B 168 10.465 -6.074 3.246 1.00 16.08 C ANISOU 2874 CA CYS B 168 1936 1919 2254 145 -235 -75 C ATOM 2875 C CYS B 168 11.440 -5.553 2.149 1.00 17.55 C ANISOU 2875 C CYS B 168 2063 2094 2510 135 -212 -72 C ATOM 2876 O CYS B 168 12.073 -6.327 1.413 1.00 17.62 O ANISOU 2876 O CYS B 168 2043 2098 2552 134 -183 -72 O ATOM 2877 CB CYS B 168 8.969 -5.928 2.926 1.00 18.48 C ANISOU 2877 CB CYS B 168 2271 2255 2496 134 -196 -72 C ATOM 2878 SG CYS B 168 8.357 -7.042 1.659 1.00 23.47 S ANISOU 2878 SG CYS B 168 2905 2908 3105 123 -134 -59 S ATOM 2879 N GLU B 169 11.599 -4.236 2.083 1.00 16.33 N ANISOU 2879 N GLU B 169 1891 1933 2381 127 -223 -73 N ATOM 2880 CA AGLU B 169 12.502 -3.639 1.114 0.50 16.28 C ANISOU 2880 CA AGLU B 169 1833 1915 2436 109 -199 -68 C ATOM 2881 CA BGLU B 169 12.511 -3.599 1.138 0.50 16.69 C ANISOU 2881 CA BGLU B 169 1885 1967 2490 109 -201 -68 C ATOM 2882 C GLU B 169 13.963 -4.001 1.341 1.00 19.52 C ANISOU 2882 C GLU B 169 2195 2297 2923 118 -222 -81 C ATOM 2883 O GLU B 169 14.681 -4.251 0.388 1.00 20.45 O ANISOU 2883 O GLU B 169 2271 2414 3086 104 -179 -82 O ATOM 2884 CB AGLU B 169 12.357 -2.107 1.114 0.50 18.57 C ANISOU 2884 CB AGLU B 169 2117 2196 2742 97 -216 -64 C ATOM 2885 CB BGLU B 169 12.395 -2.055 1.232 0.50 18.95 C ANISOU 2885 CB BGLU B 169 2165 2242 2792 99 -222 -66 C ATOM 2886 CG AGLU B 169 13.424 -1.438 0.271 0.50 17.68 C ANISOU 2886 CG AGLU B 169 1953 2067 2699 73 -196 -57 C ATOM 2887 CG BGLU B 169 11.003 -1.487 0.968 0.50 19.63 C ANISOU 2887 CG BGLU B 169 2286 2347 2824 92 -207 -57 C ATOM 2888 CD AGLU B 169 13.150 -1.530 -1.251 0.50 17.41 C ANISOU 2888 CD AGLU B 169 1916 2053 2645 42 -127 -35 C ATOM 2889 CD BGLU B 169 10.596 -1.464 -0.489 0.50 22.73 C ANISOU 2889 CD BGLU B 169 2677 2757 3204 67 -153 -33 C ATOM 2890 OE1AGLU B 169 14.064 -1.264 -2.099 0.50 13.00 O ANISOU 2890 OE1AGLU B 169 1319 1488 2134 15 -92 -29 O ATOM 2891 OE1BGLU B 169 11.463 -1.670 -1.367 0.50 22.76 O ANISOU 2891 OE1BGLU B 169 2651 2758 3239 47 -119 -24 O ATOM 2892 OE2AGLU B 169 12.012 -1.891 -1.566 0.50 20.06 O ANISOU 2892 OE2AGLU B 169 2292 2413 2918 43 -108 -26 O ATOM 2893 OE2BGLU B 169 9.404 -1.229 -0.748 0.50 23.53 O ANISOU 2893 OE2BGLU B 169 2806 2873 3262 64 -146 -25 O ATOM 2894 N ALA B 170 14.415 -4.054 2.594 1.00 17.10 N ANISOU 2894 N ALA B 170 1896 1969 2633 139 -290 -93 N ATOM 2895 CA ALA B 170 15.788 -4.417 2.910 1.00 18.54 C ANISOU 2895 CA ALA B 170 2029 2117 2896 151 -328 -107 C ATOM 2896 C ALA B 170 16.078 -5.865 2.506 1.00 18.40 C ANISOU 2896 C ALA B 170 2000 2098 2894 162 -303 -110 C ATOM 2897 O ALA B 170 17.179 -6.193 2.085 1.00 20.55 O ANISOU 2897 O ALA B 170 2211 2349 3249 165 -295 -124 O ATOM 2898 CB ALA B 170 16.037 -4.232 4.376 1.00 20.99 C ANISOU 2898 CB ALA B 170 2365 2405 3205 170 -416 -116 C ATOM 2899 N SER B 171 15.051 -6.714 2.605 1.00 17.15 N ANISOU 2899 N SER B 171 1897 1960 2660 168 -288 -100 N ATOM 2900 CA SER B 171 15.165 -8.123 2.229 1.00 17.25 C ANISOU 2900 CA SER B 171 1905 1968 2681 178 -266 -103 C ATOM 2901 C SER B 171 15.247 -8.304 0.715 1.00 17.70 C ANISOU 2901 C SER B 171 1926 2044 2756 158 -180 -109 C ATOM 2902 O SER B 171 15.938 -9.230 0.219 1.00 18.85 O ANISOU 2902 O SER B 171 2034 2174 2954 166 -157 -126 O ATOM 2903 CB SER B 171 13.958 -8.893 2.774 1.00 17.49 C ANISOU 2903 CB SER B 171 2009 2015 2622 183 -272 -88 C ATOM 2904 OG SER B 171 13.924 -8.958 4.192 1.00 19.15 O ANISOU 2904 OG SER B 171 2262 2208 2807 196 -348 -83 O ATOM 2905 N TYR B 172 14.557 -7.461 -0.045 1.00 15.77 N ANISOU 2905 N TYR B 172 1694 1829 2469 132 -133 -97 N ATOM 2906 CA TYR B 172 14.442 -7.625 -1.488 1.00 17.36 C ANISOU 2906 CA TYR B 172 1880 2053 2661 107 -52 -98 C ATOM 2907 C TYR B 172 14.610 -6.291 -2.216 1.00 16.58 C ANISOU 2907 C TYR B 172 1763 1964 2574 74 -24 -87 C ATOM 2908 O TYR B 172 13.658 -5.749 -2.751 1.00 15.89 O ANISOU 2908 O TYR B 172 1711 1900 2427 55 -1 -66 O ATOM 2909 CB TYR B 172 13.076 -8.208 -1.806 1.00 16.82 C ANISOU 2909 CB TYR B 172 1869 2014 2507 102 -26 -85 C ATOM 2910 CG TYR B 172 12.815 -9.601 -1.229 1.00 14.55 C ANISOU 2910 CG TYR B 172 1606 1717 2204 126 -46 -91 C ATOM 2911 CD1 TYR B 172 13.333 -10.711 -1.862 1.00 16.25 C ANISOU 2911 CD1 TYR B 172 1797 1922 2454 130 -12 -111 C ATOM 2912 CD2 TYR B 172 12.032 -9.758 -0.125 1.00 15.30 C ANISOU 2912 CD2 TYR B 172 1751 1812 2251 139 -93 -80 C ATOM 2913 CE1 TYR B 172 13.085 -11.967 -1.408 1.00 17.64 C ANISOU 2913 CE1 TYR B 172 1998 2084 2621 149 -32 -114 C ATOM 2914 CE2 TYR B 172 11.734 -11.052 0.355 1.00 15.87 C ANISOU 2914 CE2 TYR B 172 1853 1874 2304 154 -109 -79 C ATOM 2915 CZ TYR B 172 12.291 -12.141 -0.309 1.00 16.30 C ANISOU 2915 CZ TYR B 172 1882 1913 2400 160 -82 -95 C ATOM 2916 OH TYR B 172 12.068 -13.460 0.111 1.00 17.41 O ANISOU 2916 OH TYR B 172 2050 2035 2531 174 -101 -93 O ATOM 2917 N PRO B 173 15.803 -5.705 -2.151 1.00 17.19 N ANISOU 2917 N PRO B 173 1784 2018 2730 69 -33 -98 N ATOM 2918 CA PRO B 173 15.977 -4.326 -2.636 1.00 16.96 C ANISOU 2918 CA PRO B 173 1741 1990 2715 37 -19 -83 C ATOM 2919 C PRO B 173 15.537 -4.140 -4.072 1.00 16.62 C ANISOU 2919 C PRO B 173 1714 1974 2626 -4 57 -66 C ATOM 2920 O PRO B 173 15.958 -4.875 -4.977 1.00 20.26 O ANISOU 2920 O PRO B 173 2154 2447 3095 -20 120 -81 O ATOM 2921 CB PRO B 173 17.453 -4.064 -2.437 1.00 19.65 C ANISOU 2921 CB PRO B 173 2009 2298 3158 36 -30 -104 C ATOM 2922 CG PRO B 173 17.908 -5.045 -1.368 1.00 23.61 C ANISOU 2922 CG PRO B 173 2497 2776 3698 79 -89 -126 C ATOM 2923 CD PRO B 173 17.003 -6.242 -1.503 1.00 20.10 C ANISOU 2923 CD PRO B 173 2101 2352 3185 94 -70 -124 C ATOM 2924 N GLY B 174 14.661 -3.149 -4.257 1.00 16.70 N ANISOU 2924 N GLY B 174 1763 1994 2587 -21 46 -36 N ATOM 2925 CA GLY B 174 14.168 -2.796 -5.558 1.00 17.80 C ANISOU 2925 CA GLY B 174 1929 2155 2678 -63 99 -12 C ATOM 2926 C GLY B 174 13.113 -3.692 -6.172 1.00 17.13 C ANISOU 2926 C GLY B 174 1891 2101 2516 -64 129 -7 C ATOM 2927 O GLY B 174 12.612 -3.404 -7.261 1.00 20.13 O ANISOU 2927 O GLY B 174 2302 2499 2847 -100 164 15 O ATOM 2928 N LYS B 175 12.754 -4.782 -5.481 1.00 16.29 N ANISOU 2928 N LYS B 175 1795 1998 2397 -27 110 -27 N ATOM 2929 CA LYS B 175 11.845 -5.776 -6.037 1.00 16.77 C ANISOU 2929 CA LYS B 175 1893 2084 2394 -28 139 -28 C ATOM 2930 C LYS B 175 10.443 -5.805 -5.488 1.00 18.02 C ANISOU 2930 C LYS B 175 2098 2253 2497 -10 100 -15 C ATOM 2931 O LYS B 175 9.578 -6.542 -5.947 1.00 18.49 O ANISOU 2931 O LYS B 175 2189 2333 2505 -13 120 -15 O ATOM 2932 CB LYS B 175 12.416 -7.190 -5.807 1.00 17.21 C ANISOU 2932 CB LYS B 175 1927 2134 2478 -5 155 -61 C ATOM 2933 CG LYS B 175 13.716 -7.432 -6.506 1.00 20.83 C ANISOU 2933 CG LYS B 175 2334 2585 2995 -22 208 -85 C ATOM 2934 CD LYS B 175 14.211 -8.814 -6.189 1.00 29.90 C ANISOU 2934 CD LYS B 175 3458 3719 4183 8 212 -120 C ATOM 2935 CE LYS B 175 15.481 -9.114 -6.988 1.00 38.97 C ANISOU 2935 CE LYS B 175 4546 4861 5399 -9 276 -156 C ATOM 2936 NZ LYS B 175 15.258 -10.099 -8.094 1.00 47.01 N ANISOU 2936 NZ LYS B 175 5579 5900 6381 -27 347 -180 N ATOM 2937 N ILE B 176 10.193 -5.004 -4.481 1.00 16.25 N ANISOU 2937 N ILE B 176 1876 2015 2284 8 47 -10 N ATOM 2938 CA ILE B 176 8.904 -4.941 -3.823 1.00 15.57 C ANISOU 2938 CA ILE B 176 1825 1936 2154 26 15 -7 C ATOM 2939 C ILE B 176 8.070 -3.815 -4.421 1.00 18.83 C ANISOU 2939 C ILE B 176 2255 2354 2546 6 7 16 C ATOM 2940 O ILE B 176 8.467 -2.641 -4.407 1.00 20.42 O ANISOU 2940 O ILE B 176 2442 2536 2780 -3 -14 28 O ATOM 2941 CB ILE B 176 9.058 -4.711 -2.323 1.00 17.83 C ANISOU 2941 CB ILE B 176 2108 2205 2461 55 -37 -21 C ATOM 2942 CG1 ILE B 176 9.924 -5.815 -1.701 1.00 17.28 C ANISOU 2942 CG1 ILE B 176 2025 2124 2417 75 -44 -38 C ATOM 2943 CG2 ILE B 176 7.709 -4.650 -1.667 1.00 19.19 C ANISOU 2943 CG2 ILE B 176 2315 2390 2587 68 -58 -24 C ATOM 2944 CD1 ILE B 176 9.408 -7.228 -1.927 1.00 19.98 C ANISOU 2944 CD1 ILE B 176 2390 2480 2722 79 -18 -43 C ATOM 2945 N THR B 177 6.977 -4.164 -5.050 1.00 14.79 N ANISOU 2945 N THR B 177 1772 1861 1985 -3 20 25 N ATOM 2946 CA THR B 177 6.072 -3.165 -5.596 1.00 15.16 C ANISOU 2946 CA THR B 177 1836 1906 2017 -17 0 48 C ATOM 2947 C THR B 177 5.078 -2.729 -4.520 1.00 14.46 C ANISOU 2947 C THR B 177 1751 1811 1931 11 -42 33 C ATOM 2948 O THR B 177 4.931 -3.369 -3.443 1.00 15.03 O ANISOU 2948 O THR B 177 1825 1889 1998 36 -47 9 O ATOM 2949 CB THR B 177 5.342 -3.640 -6.837 1.00 17.25 C ANISOU 2949 CB THR B 177 2129 2192 2233 -43 24 64 C ATOM 2950 OG1 THR B 177 4.346 -4.585 -6.446 1.00 16.11 O ANISOU 2950 OG1 THR B 177 1999 2064 2059 -24 24 46 O ATOM 2951 CG2 THR B 177 6.283 -4.310 -7.786 1.00 21.91 C ANISOU 2951 CG2 THR B 177 2718 2794 2812 -70 77 65 C ATOM 2952 N SER B 178 4.263 -1.722 -4.852 1.00 16.52 N ANISOU 2952 N SER B 178 2018 2062 2196 5 -71 48 N ATOM 2953 CA SER B 178 3.254 -1.250 -3.953 1.00 18.00 C ANISOU 2953 CA SER B 178 2203 2242 2393 30 -104 27 C ATOM 2954 C SER B 178 2.137 -2.237 -3.700 1.00 15.23 C ANISOU 2954 C SER B 178 1864 1916 2006 41 -89 8 C ATOM 2955 O SER B 178 1.340 -2.056 -2.786 1.00 17.89 O ANISOU 2955 O SER B 178 2196 2253 2348 61 -103 -19 O ATOM 2956 CB SER B 178 2.645 0.052 -4.453 1.00 20.64 C ANISOU 2956 CB SER B 178 2536 2552 2754 24 -142 44 C ATOM 2957 OG SER B 178 2.080 -0.149 -5.718 1.00 23.24 O ANISOU 2957 OG SER B 178 2885 2891 3056 -1 -138 73 O ATOM 2958 N ASN B 179 2.095 -3.317 -4.479 1.00 13.91 N ANISOU 2958 N ASN B 179 1712 1770 1803 26 -57 18 N ATOM 2959 CA ASN B 179 1.090 -4.351 -4.322 1.00 13.97 C ANISOU 2959 CA ASN B 179 1731 1798 1779 31 -42 2 C ATOM 2960 C ASN B 179 1.569 -5.593 -3.577 1.00 13.90 C ANISOU 2960 C ASN B 179 1729 1800 1752 40 -15 -14 C ATOM 2961 O ASN B 179 0.867 -6.593 -3.542 1.00 15.16 O ANISOU 2961 O ASN B 179 1901 1976 1885 39 3 -23 O ATOM 2962 CB ASN B 179 0.581 -4.733 -5.697 1.00 14.39 C ANISOU 2962 CB ASN B 179 1801 1864 1805 6 -32 23 C ATOM 2963 CG ASN B 179 -0.086 -3.579 -6.371 1.00 13.88 C ANISOU 2963 CG ASN B 179 1735 1784 1756 -3 -71 43 C ATOM 2964 OD1 ASN B 179 -1.008 -2.954 -5.801 1.00 15.62 O ANISOU 2964 OD1 ASN B 179 1939 1993 2003 16 -102 27 O ATOM 2965 ND2 ASN B 179 0.424 -3.182 -7.519 1.00 14.66 N ANISOU 2965 ND2 ASN B 179 1851 1877 1844 -31 -73 76 N ATOM 2966 N MET B 180 2.735 -5.505 -2.966 1.00 12.30 N ANISOU 2966 N MET B 180 1518 1585 1570 49 -19 -18 N ATOM 2967 CA MET B 180 3.399 -6.600 -2.284 1.00 12.44 C ANISOU 2967 CA MET B 180 1543 1604 1582 59 -7 -28 C ATOM 2968 C MET B 180 3.664 -6.271 -0.847 1.00 14.58 C ANISOU 2968 C MET B 180 1814 1863 1862 78 -35 -44 C ATOM 2969 O MET B 180 3.951 -5.112 -0.490 1.00 15.14 O ANISOU 2969 O MET B 180 1872 1920 1960 84 -61 -48 O ATOM 2970 CB MET B 180 4.720 -6.961 -2.948 1.00 14.08 C ANISOU 2970 CB MET B 180 1735 1802 1811 51 11 -20 C ATOM 2971 CG MET B 180 4.592 -7.469 -4.350 1.00 14.15 C ANISOU 2971 CG MET B 180 1751 1826 1801 28 46 -10 C ATOM 2972 SD MET B 180 6.200 -7.625 -5.145 1.00 14.88 S ANISOU 2972 SD MET B 180 1817 1908 1927 15 78 -10 S ATOM 2973 CE MET B 180 5.727 -7.955 -6.835 1.00 17.98 C ANISOU 2973 CE MET B 180 2232 2324 2276 -21 121 0 C ATOM 2974 N PHE B 181 3.625 -7.293 0.006 1.00 12.00 N ANISOU 2974 N PHE B 181 1509 1539 1512 85 -33 -53 N ATOM 2975 CA PHE B 181 4.018 -7.120 1.377 1.00 12.46 C ANISOU 2975 CA PHE B 181 1580 1586 1569 98 -63 -66 C ATOM 2976 C PHE B 181 4.623 -8.408 1.930 1.00 14.42 C ANISOU 2976 C PHE B 181 1848 1824 1805 102 -69 -62 C ATOM 2977 O PHE B 181 4.426 -9.487 1.328 1.00 13.93 O ANISOU 2977 O PHE B 181 1793 1768 1733 96 -43 -54 O ATOM 2978 CB PHE B 181 2.904 -6.628 2.311 1.00 12.59 C ANISOU 2978 CB PHE B 181 1613 1614 1556 99 -66 -88 C ATOM 2979 CG PHE B 181 1.809 -7.622 2.608 1.00 12.05 C ANISOU 2979 CG PHE B 181 1571 1565 1441 89 -38 -93 C ATOM 2980 CD1 PHE B 181 0.939 -8.064 1.639 1.00 12.05 C ANISOU 2980 CD1 PHE B 181 1563 1579 1435 78 -8 -88 C ATOM 2981 CD2 PHE B 181 1.563 -8.070 3.947 1.00 14.23 C ANISOU 2981 CD2 PHE B 181 1885 1846 1677 85 -41 -106 C ATOM 2982 CE1 PHE B 181 -0.106 -8.923 1.917 1.00 13.58 C ANISOU 2982 CE1 PHE B 181 1775 1789 1595 65 18 -95 C ATOM 2983 CE2 PHE B 181 0.517 -8.947 4.209 1.00 15.34 C ANISOU 2983 CE2 PHE B 181 2048 2003 1776 68 -9 -111 C ATOM 2984 CZ PHE B 181 -0.316 -9.373 3.199 1.00 15.30 C ANISOU 2984 CZ PHE B 181 2027 2011 1776 59 21 -106 C ATOM 2985 N CYS B 182 5.399 -8.328 2.997 1.00 14.82 N ANISOU 2985 N CYS B 182 1909 1857 1863 113 -108 -66 N ATOM 2986 CA CYS B 182 6.068 -9.496 3.565 1.00 14.33 C ANISOU 2986 CA CYS B 182 1868 1777 1799 119 -129 -58 C ATOM 2987 C CYS B 182 5.417 -9.868 4.879 1.00 14.43 C ANISOU 2987 C CYS B 182 1935 1795 1753 112 -145 -61 C ATOM 2988 O CYS B 182 5.005 -9.001 5.665 1.00 14.70 O ANISOU 2988 O CYS B 182 1983 1838 1762 110 -155 -77 O ATOM 2989 CB CYS B 182 7.541 -9.251 3.837 1.00 17.93 C ANISOU 2989 CB CYS B 182 2300 2203 2310 134 -174 -58 C ATOM 2990 SG CYS B 182 8.616 -8.995 2.363 1.00 17.85 S ANISOU 2990 SG CYS B 182 2223 2182 2375 136 -149 -57 S ATOM 2991 N VAL B 183 5.355 -11.170 5.108 1.00 13.66 N ANISOU 2991 N VAL B 183 1868 1689 1634 107 -145 -47 N ATOM 2992 CA VAL B 183 4.819 -11.763 6.319 1.00 14.63 C ANISOU 2992 CA VAL B 183 2052 1813 1695 93 -158 -42 C ATOM 2993 C VAL B 183 5.788 -12.874 6.650 1.00 15.17 C ANISOU 2993 C VAL B 183 2139 1844 1782 101 -203 -20 C ATOM 2994 O VAL B 183 6.250 -13.618 5.784 1.00 16.59 O ANISOU 2994 O VAL B 183 2290 2007 2006 111 -195 -13 O ATOM 2995 CB VAL B 183 3.411 -12.363 6.083 1.00 15.61 C ANISOU 2995 CB VAL B 183 2195 1964 1774 70 -103 -43 C ATOM 2996 CG1 VAL B 183 2.841 -12.905 7.355 1.00 17.74 C ANISOU 2996 CG1 VAL B 183 2529 2236 1974 47 -107 -38 C ATOM 2997 CG2 VAL B 183 2.479 -11.295 5.525 1.00 15.29 C ANISOU 2997 CG2 VAL B 183 2121 1952 1735 67 -64 -66 C ATOM 2998 N GLY B 184A 6.119 -12.985 7.923 1.00 15.23 N ANISOU 2998 N GLY B 184A 2196 1836 1756 97 -254 -12 N ATOM 2999 CA GLY B 184A 7.088 -14.007 8.311 1.00 17.15 C ANISOU 2999 CA GLY B 184A 2458 2034 2023 107 -313 11 C ATOM 3000 C GLY B 184A 8.122 -13.518 9.303 1.00 15.31 C ANISOU 3000 C GLY B 184A 2241 1775 1803 118 -393 13 C ATOM 3001 O GLY B 184A 7.811 -12.717 10.180 1.00 16.42 O ANISOU 3001 O GLY B 184A 2416 1933 1891 106 -404 1 O ATOM 3002 N PHE B 184 9.346 -14.037 9.196 1.00 16.61 N ANISOU 3002 N PHE B 184 2378 1893 2038 142 -450 23 N ATOM 3003 CA PHE B 184 10.405 -13.908 10.202 1.00 16.50 C ANISOU 3003 CA PHE B 184 2384 1842 2044 153 -545 30 C ATOM 3004 C PHE B 184 11.709 -13.586 9.513 1.00 18.38 C ANISOU 3004 C PHE B 184 2537 2051 2397 185 -572 15 C ATOM 3005 O PHE B 184 12.148 -14.328 8.597 1.00 19.28 O ANISOU 3005 O PHE B 184 2601 2144 2580 201 -552 14 O ATOM 3006 CB PHE B 184 10.521 -15.215 10.980 1.00 19.36 C ANISOU 3006 CB PHE B 184 2813 2165 2379 146 -603 66 C ATOM 3007 CG PHE B 184 9.219 -15.658 11.574 1.00 17.68 C ANISOU 3007 CG PHE B 184 2683 1980 2054 107 -565 83 C ATOM 3008 CD1 PHE B 184 8.373 -16.498 10.896 1.00 18.73 C ANISOU 3008 CD1 PHE B 184 2817 2125 2175 95 -500 91 C ATOM 3009 CD2 PHE B 184 8.792 -15.123 12.793 1.00 18.82 C ANISOU 3009 CD2 PHE B 184 2902 2144 2107 79 -585 84 C ATOM 3010 CE1 PHE B 184 7.134 -16.857 11.430 1.00 18.92 C ANISOU 3010 CE1 PHE B 184 2910 2176 2102 54 -457 103 C ATOM 3011 CE2 PHE B 184 7.579 -15.523 13.338 1.00 19.30 C ANISOU 3011 CE2 PHE B 184 3035 2234 2066 38 -538 95 C ATOM 3012 CZ PHE B 184 6.751 -16.355 12.664 1.00 20.14 C ANISOU 3012 CZ PHE B 184 3135 2350 2166 25 -474 105 C ATOM 3013 N LEU B 185 12.379 -12.510 9.892 1.00 17.93 N ANISOU 3013 N LEU B 185 2457 1990 2367 193 -612 -1 N ATOM 3014 CA LEU B 185 13.676 -12.233 9.284 1.00 19.60 C ANISOU 3014 CA LEU B 185 2583 2171 2695 219 -637 -17 C ATOM 3015 C LEU B 185 14.697 -13.293 9.673 1.00 19.72 C ANISOU 3015 C LEU B 185 2593 2126 2774 240 -719 -3 C ATOM 3016 O LEU B 185 15.702 -13.457 8.996 1.00 20.21 O ANISOU 3016 O LEU B 185 2576 2159 2944 263 -726 -19 O ATOM 3017 CB LEU B 185 14.186 -10.842 9.625 1.00 21.79 C ANISOU 3017 CB LEU B 185 2834 2452 2994 221 -666 -38 C ATOM 3018 CG LEU B 185 13.340 -9.692 9.049 1.00 20.54 C ANISOU 3018 CG LEU B 185 2661 2341 2801 205 -589 -55 C ATOM 3019 CD1 LEU B 185 14.055 -8.392 9.377 1.00 23.79 C ANISOU 3019 CD1 LEU B 185 3041 2743 3255 209 -629 -75 C ATOM 3020 CD2 LEU B 185 13.104 -9.804 7.584 1.00 20.84 C ANISOU 3020 CD2 LEU B 185 2644 2398 2875 204 -503 -59 C ATOM 3021 N GLU B 186 14.471 -13.987 10.784 1.00 19.11 N ANISOU 3021 N GLU B 186 2599 2028 2633 231 -785 25 N ATOM 3022 CA GLU B 186 15.338 -15.094 11.169 1.00 20.24 C ANISOU 3022 CA GLU B 186 2747 2108 2837 251 -873 45 C ATOM 3023 C GLU B 186 15.112 -16.351 10.317 1.00 20.77 C ANISOU 3023 C GLU B 186 2795 2159 2938 260 -828 52 C ATOM 3024 O GLU B 186 15.808 -17.344 10.476 1.00 21.36 O ANISOU 3024 O GLU B 186 2863 2175 3078 280 -894 64 O ATOM 3025 CB GLU B 186 15.185 -15.427 12.668 1.00 21.52 C ANISOU 3025 CB GLU B 186 3017 2248 2912 233 -967 80 C ATOM 3026 CG GLU B 186 15.718 -14.331 13.589 1.00 24.11 C ANISOU 3026 CG GLU B 186 3361 2575 3226 230 -1039 68 C ATOM 3027 CD GLU B 186 17.204 -14.184 13.471 1.00 30.99 C ANISOU 3027 CD GLU B 186 4149 3392 4232 266 -1120 53 C ATOM 3028 OE1 GLU B 186 17.671 -13.105 13.044 1.00 38.17 O ANISOU 3028 OE1 GLU B 186 4986 4317 5199 274 -1098 19 O ATOM 3029 OE2 GLU B 186 17.908 -15.153 13.821 1.00 33.81 O ANISOU 3029 OE2 GLU B 186 4513 3689 4645 284 -1210 74 O ATOM 3030 N GLY B 187 14.162 -16.311 9.416 1.00 20.46 N ANISOU 3030 N GLY B 187 2747 2168 2861 245 -721 42 N ATOM 3031 CA GLY B 187 13.842 -17.480 8.606 1.00 19.26 C ANISOU 3031 CA GLY B 187 2583 2003 2730 249 -675 45 C ATOM 3032 C GLY B 187 13.174 -18.603 9.434 1.00 19.30 C ANISOU 3032 C GLY B 187 2683 1986 2663 230 -713 86 C ATOM 3033 O GLY B 187 12.558 -18.378 10.488 1.00 21.97 O ANISOU 3033 O GLY B 187 3105 2340 2902 202 -739 111 O ATOM 3034 N GLY B 188A 13.263 -19.835 8.932 1.00 18.61 N ANISOU 3034 N GLY B 188A 2585 1861 2624 241 -710 91 N ATOM 3035 CA GLY B 188A 12.779 -21.037 9.612 1.00 19.51 C ANISOU 3035 CA GLY B 188A 2783 1940 2691 224 -752 132 C ATOM 3036 C GLY B 188A 11.326 -21.439 9.443 1.00 19.33 C ANISOU 3036 C GLY B 188A 2816 1958 2570 186 -673 147 C ATOM 3037 O GLY B 188A 11.004 -22.591 9.604 1.00 19.74 O ANISOU 3037 O GLY B 188A 2913 1975 2612 175 -690 174 O ATOM 3038 N LYS B 188 10.466 -20.458 9.140 1.00 16.93 N ANISOU 3038 N LYS B 188 2508 1725 2202 165 -592 129 N ATOM 3039 CA LYS B 188 9.057 -20.694 8.951 1.00 17.59 C ANISOU 3039 CA LYS B 188 2631 1850 2201 129 -514 136 C ATOM 3040 C LYS B 188 8.609 -19.784 7.827 1.00 17.33 C ANISOU 3040 C LYS B 188 2533 1874 2176 132 -424 97 C ATOM 3041 O LYS B 188 8.930 -18.586 7.847 1.00 17.65 O ANISOU 3041 O LYS B 188 2542 1940 2224 141 -423 78 O ATOM 3042 CB LYS B 188 8.311 -20.296 10.225 1.00 18.52 C ANISOU 3042 CB LYS B 188 2837 1994 2205 91 -527 160 C ATOM 3043 CG LYS B 188 8.773 -21.036 11.467 1.00 20.35 C ANISOU 3043 CG LYS B 188 3150 2172 2409 79 -626 204 C ATOM 3044 CD LYS B 188 7.922 -20.750 12.672 1.00 24.28 C ANISOU 3044 CD LYS B 188 3744 2701 2779 31 -622 226 C ATOM 3045 CE LYS B 188 8.481 -21.442 13.855 1.00 26.56 C ANISOU 3045 CE LYS B 188 4119 2933 3038 17 -729 273 C ATOM 3046 NZ LYS B 188 7.587 -21.245 15.020 1.00 33.63 N ANISOU 3046 NZ LYS B 188 5120 3863 3796 -40 -714 294 N ATOM 3047 N ASP B 189 7.926 -20.342 6.841 1.00 16.21 N ANISOU 3047 N ASP B 189 2372 1747 2039 125 -358 87 N ATOM 3048 CA ASP B 189 7.583 -19.587 5.626 1.00 15.81 C ANISOU 3048 CA ASP B 189 2261 1744 2003 128 -281 53 C ATOM 3049 C ASP B 189 6.616 -20.424 4.793 1.00 14.85 C ANISOU 3049 C ASP B 189 2144 1634 1865 110 -221 50 C ATOM 3050 O ASP B 189 6.379 -21.602 5.040 1.00 17.09 O ANISOU 3050 O ASP B 189 2465 1885 2143 100 -236 68 O ATOM 3051 CB ASP B 189 8.891 -19.286 4.857 1.00 15.57 C ANISOU 3051 CB ASP B 189 2154 1693 2071 162 -292 27 C ATOM 3052 CG ASP B 189 8.849 -18.127 3.916 1.00 18.52 C ANISOU 3052 CG ASP B 189 2473 2110 2454 163 -236 1 C ATOM 3053 OD1 ASP B 189 7.812 -17.474 3.665 1.00 18.23 O ANISOU 3053 OD1 ASP B 189 2448 2120 2359 142 -187 -2 O ATOM 3054 OD2 ASP B 189 9.970 -17.896 3.389 1.00 18.27 O ANISOU 3054 OD2 ASP B 189 2381 2059 2500 185 -243 -20 O ATOM 3055 N SER B 190 6.040 -19.794 3.780 1.00 13.92 N ANISOU 3055 N SER B 190 1989 1561 1739 104 -156 26 N ATOM 3056 CA SER B 190 5.314 -20.529 2.764 1.00 14.54 C ANISOU 3056 CA SER B 190 2060 1649 1817 92 -103 15 C ATOM 3057 C SER B 190 6.303 -20.980 1.687 1.00 15.81 C ANISOU 3057 C SER B 190 2167 1784 2055 116 -94 -11 C ATOM 3058 O SER B 190 7.418 -20.463 1.566 1.00 16.78 O ANISOU 3058 O SER B 190 2248 1895 2233 140 -113 -24 O ATOM 3059 CB SER B 190 4.265 -19.623 2.158 1.00 16.70 C ANISOU 3059 CB SER B 190 2319 1979 2047 73 -47 2 C ATOM 3060 OG SER B 190 4.858 -18.432 1.615 1.00 15.79 O ANISOU 3060 OG SER B 190 2158 1883 1959 88 -39 -15 O ATOM 3061 N CYS B 191 5.903 -21.975 0.910 1.00 14.71 N ANISOU 3061 N CYS B 191 2029 1636 1926 109 -63 -23 N ATOM 3062 CA CYS B 191 6.813 -22.603 -0.019 1.00 16.11 C ANISOU 3062 CA CYS B 191 2161 1782 2177 130 -52 -54 C ATOM 3063 C CYS B 191 6.105 -23.078 -1.287 1.00 15.61 C ANISOU 3063 C CYS B 191 2090 1741 2100 113 9 -79 C ATOM 3064 O CYS B 191 4.893 -22.878 -1.462 1.00 14.88 O ANISOU 3064 O CYS B 191 2023 1686 1945 86 38 -71 O ATOM 3065 CB CYS B 191 7.547 -23.738 0.685 1.00 18.26 C ANISOU 3065 CB CYS B 191 2447 1986 2504 150 -113 -43 C ATOM 3066 SG CYS B 191 9.171 -24.212 -0.049 1.00 22.72 S ANISOU 3066 SG CYS B 191 2937 2501 3193 191 -122 -88 S ATOM 3067 N GLN B 192 6.857 -23.670 -2.212 1.00 16.14 N ANISOU 3067 N GLN B 192 2120 1785 2228 128 31 -116 N ATOM 3068 CA GLN B 192 6.252 -24.175 -3.445 1.00 14.21 C ANISOU 3068 CA GLN B 192 1873 1559 1967 110 87 -146 C ATOM 3069 C GLN B 192 5.078 -25.115 -3.150 1.00 13.92 C ANISOU 3069 C GLN B 192 1886 1512 1890 88 80 -128 C ATOM 3070 O GLN B 192 5.198 -26.093 -2.405 1.00 15.93 O ANISOU 3070 O GLN B 192 2165 1716 2171 95 39 -112 O ATOM 3071 CB GLN B 192 7.302 -24.931 -4.318 1.00 15.48 C ANISOU 3071 CB GLN B 192 1990 1685 2206 130 109 -195 C ATOM 3072 CG GLN B 192 8.156 -23.983 -5.137 1.00 16.70 C ANISOU 3072 CG GLN B 192 2094 1869 2383 134 150 -225 C ATOM 3073 CD GLN B 192 9.099 -23.143 -4.315 1.00 20.66 C ANISOU 3073 CD GLN B 192 2567 2360 2924 156 111 -209 C ATOM 3074 OE1 GLN B 192 9.708 -23.642 -3.362 1.00 21.84 O ANISOU 3074 OE1 GLN B 192 2713 2459 3126 182 51 -197 O ATOM 3075 NE2 GLN B 192 9.255 -21.860 -4.696 1.00 19.29 N ANISOU 3075 NE2 GLN B 192 2373 2231 2727 144 138 -208 N ATOM 3076 N GLY B 193 3.944 -24.856 -3.819 1.00 14.47 N ANISOU 3076 N GLY B 193 1969 1626 1903 59 120 -131 N ATOM 3077 CA GLY B 193 2.676 -25.511 -3.553 1.00 15.02 C ANISOU 3077 CA GLY B 193 2079 1696 1930 31 120 -114 C ATOM 3078 C GLY B 193 1.705 -24.676 -2.762 1.00 14.47 C ANISOU 3078 C GLY B 193 2032 1665 1802 11 115 -81 C ATOM 3079 O GLY B 193 0.533 -25.005 -2.715 1.00 15.25 O ANISOU 3079 O GLY B 193 2153 1776 1865 -17 128 -74 O ATOM 3080 N ASP B 194 2.205 -23.651 -2.083 1.00 14.06 N ANISOU 3080 N ASP B 194 1971 1625 1745 25 95 -66 N ATOM 3081 CA ASP B 194 1.359 -22.747 -1.305 1.00 13.41 C ANISOU 3081 CA ASP B 194 1906 1579 1612 9 94 -44 C ATOM 3082 C ASP B 194 0.801 -21.578 -2.096 1.00 13.76 C ANISOU 3082 C ASP B 194 1924 1673 1633 2 123 -57 C ATOM 3083 O ASP B 194 -0.158 -20.937 -1.629 1.00 13.69 O ANISOU 3083 O ASP B 194 1922 1693 1587 -14 129 -48 O ATOM 3084 CB ASP B 194 2.100 -22.229 -0.077 1.00 12.80 C ANISOU 3084 CB ASP B 194 1840 1488 1537 25 52 -22 C ATOM 3085 CG ASP B 194 2.404 -23.344 0.937 1.00 14.38 C ANISOU 3085 CG ASP B 194 2082 1636 1745 25 10 3 C ATOM 3086 OD1 ASP B 194 1.536 -24.225 1.127 1.00 14.87 O ANISOU 3086 OD1 ASP B 194 2178 1689 1784 -2 20 15 O ATOM 3087 OD2 ASP B 194 3.476 -23.290 1.540 1.00 16.12 O ANISOU 3087 OD2 ASP B 194 2302 1826 1997 48 -35 13 O ATOM 3088 N ALA B 195 1.432 -21.232 -3.223 1.00 13.14 N ANISOU 3088 N ALA B 195 1814 1604 1576 12 141 -78 N ATOM 3089 CA ALA B 195 1.018 -20.035 -3.975 1.00 14.49 C ANISOU 3089 CA ALA B 195 1965 1815 1724 4 159 -84 C ATOM 3090 C ALA B 195 -0.443 -19.986 -4.232 1.00 11.90 C ANISOU 3090 C ALA B 195 1648 1513 1360 -21 170 -83 C ATOM 3091 O ALA B 195 -1.089 -21.015 -4.509 1.00 13.75 O ANISOU 3091 O ALA B 195 1898 1739 1589 -38 180 -90 O ATOM 3092 CB ALA B 195 1.753 -19.946 -5.301 1.00 14.59 C ANISOU 3092 CB ALA B 195 1956 1834 1755 5 184 -106 C ATOM 3093 N GLY B 196 -1.007 -18.775 -4.163 1.00 11.32 N ANISOU 3093 N GLY B 196 1563 1470 1270 -25 166 -76 N ATOM 3094 CA GLY B 196 -2.412 -18.591 -4.415 1.00 12.77 C ANISOU 3094 CA GLY B 196 1745 1675 1431 -46 172 -79 C ATOM 3095 C GLY B 196 -3.248 -18.672 -3.145 1.00 12.53 C ANISOU 3095 C GLY B 196 1725 1647 1388 -54 171 -72 C ATOM 3096 O GLY B 196 -4.380 -18.210 -3.132 1.00 14.27 O ANISOU 3096 O GLY B 196 1934 1888 1602 -67 176 -79 O ATOM 3097 N GLY B 197 -2.708 -19.321 -2.097 1.00 13.24 N ANISOU 3097 N GLY B 197 1840 1713 1479 -49 164 -61 N ATOM 3098 CA GLY B 197 -3.432 -19.525 -0.884 1.00 13.75 C ANISOU 3098 CA GLY B 197 1925 1778 1520 -66 169 -53 C ATOM 3099 C GLY B 197 -3.512 -18.299 -0.001 1.00 14.31 C ANISOU 3099 C GLY B 197 1990 1868 1578 -59 163 -54 C ATOM 3100 O GLY B 197 -2.913 -17.247 -0.285 1.00 13.99 O ANISOU 3100 O GLY B 197 1928 1836 1553 -37 149 -57 O ATOM 3101 N PRO B 198 -4.225 -18.454 1.104 1.00 13.37 N ANISOU 3101 N PRO B 198 1893 1755 1432 -79 177 -52 N ATOM 3102 CA PRO B 198 -4.625 -17.329 1.944 1.00 12.72 C ANISOU 3102 CA PRO B 198 1803 1695 1335 -79 183 -65 C ATOM 3103 C PRO B 198 -3.595 -16.942 3.000 1.00 15.28 C ANISOU 3103 C PRO B 198 2156 2007 1643 -65 156 -53 C ATOM 3104 O PRO B 198 -2.892 -17.770 3.576 1.00 14.23 O ANISOU 3104 O PRO B 198 2063 1849 1496 -67 136 -31 O ATOM 3105 CB PRO B 198 -5.839 -17.874 2.667 1.00 15.20 C ANISOU 3105 CB PRO B 198 2132 2020 1622 -116 220 -72 C ATOM 3106 CG PRO B 198 -5.678 -19.356 2.726 1.00 15.83 C ANISOU 3106 CG PRO B 198 2251 2073 1690 -135 220 -49 C ATOM 3107 CD PRO B 198 -4.981 -19.698 1.453 1.00 14.17 C ANISOU 3107 CD PRO B 198 2023 1847 1516 -112 198 -45 C ATOM 3108 N VAL B 199 -3.536 -15.623 3.244 1.00 14.03 N ANISOU 3108 N VAL B 199 1975 1865 1490 -49 149 -70 N ATOM 3109 CA VAL B 199 -2.987 -15.012 4.439 1.00 12.78 C ANISOU 3109 CA VAL B 199 1843 1705 1308 -44 131 -71 C ATOM 3110 C VAL B 199 -4.155 -14.276 5.082 1.00 13.14 C ANISOU 3110 C VAL B 199 1880 1779 1335 -60 165 -103 C ATOM 3111 O VAL B 199 -4.651 -13.311 4.527 1.00 14.19 O ANISOU 3111 O VAL B 199 1966 1925 1500 -48 172 -126 O ATOM 3112 CB VAL B 199 -1.868 -14.015 4.141 1.00 14.56 C ANISOU 3112 CB VAL B 199 2045 1921 1567 -11 93 -71 C ATOM 3113 CG1 VAL B 199 -1.347 -13.469 5.460 1.00 17.54 C ANISOU 3113 CG1 VAL B 199 2453 2294 1917 -8 69 -75 C ATOM 3114 CG2 VAL B 199 -0.735 -14.634 3.317 1.00 18.35 C ANISOU 3114 CG2 VAL B 199 2518 2376 2080 6 69 -50 C ATOM 3115 N VAL B 200 -4.656 -14.801 6.180 1.00 13.41 N ANISOU 3115 N VAL B 200 1957 1820 1319 -92 190 -105 N ATOM 3116 CA VAL B 200 -5.810 -14.245 6.868 1.00 13.44 C ANISOU 3116 CA VAL B 200 1951 1851 1303 -114 237 -142 C ATOM 3117 C VAL B 200 -5.392 -13.590 8.192 1.00 16.27 C ANISOU 3117 C VAL B 200 2350 2215 1616 -118 229 -156 C ATOM 3118 O VAL B 200 -4.667 -14.191 8.998 1.00 16.85 O ANISOU 3118 O VAL B 200 2486 2273 1642 -131 204 -128 O ATOM 3119 CB VAL B 200 -6.902 -15.336 7.101 1.00 15.85 C ANISOU 3119 CB VAL B 200 2274 2167 1582 -159 287 -141 C ATOM 3120 CG1 VAL B 200 -8.034 -14.818 8.003 1.00 17.00 C ANISOU 3120 CG1 VAL B 200 2413 2342 1704 -188 346 -186 C ATOM 3121 CG2 VAL B 200 -7.420 -15.816 5.745 1.00 17.26 C ANISOU 3121 CG2 VAL B 200 2406 2341 1810 -154 291 -138 C ATOM 3122 N CYS B 201 -5.846 -12.350 8.388 1.00 17.33 N ANISOU 3122 N CYS B 201 2448 2367 1768 -106 244 -200 N ATOM 3123 CA CYS B 201 -5.468 -11.560 9.565 1.00 16.64 C ANISOU 3123 CA CYS B 201 2394 2285 1642 -107 236 -224 C ATOM 3124 C CYS B 201 -6.805 -11.071 10.125 1.00 20.09 C ANISOU 3124 C CYS B 201 2810 2753 2071 -132 304 -280 C ATOM 3125 O CYS B 201 -7.578 -10.421 9.412 1.00 18.26 O ANISOU 3125 O CYS B 201 2509 2528 1901 -115 321 -313 O ATOM 3126 CB CYS B 201 -4.567 -10.370 9.177 1.00 18.82 C ANISOU 3126 CB CYS B 201 2637 2546 1966 -64 184 -230 C ATOM 3127 SG CYS B 201 -3.215 -10.708 8.113 1.00 22.25 S ANISOU 3127 SG CYS B 201 3061 2950 2444 -32 123 -179 S ATOM 3128 N ASN B 202 -7.127 -11.442 11.359 1.00 22.50 N ANISOU 3128 N ASN B 202 3174 3075 2300 -174 343 -293 N ATOM 3129 CA ASN B 202 -8.359 -10.989 12.014 1.00 24.73 C ANISOU 3129 CA ASN B 202 3438 3389 2570 -202 418 -356 C ATOM 3130 C ASN B 202 -9.632 -11.175 11.158 1.00 21.77 C ANISOU 3130 C ASN B 202 2988 3025 2260 -207 466 -379 C ATOM 3131 O ASN B 202 -10.424 -10.227 10.987 1.00 24.32 O ANISOU 3131 O ASN B 202 3242 3358 2639 -192 493 -437 O ATOM 3132 CB ASN B 202 -8.191 -9.553 12.487 1.00 29.17 C ANISOU 3132 CB ASN B 202 3980 3955 3148 -177 410 -410 C ATOM 3133 CG ASN B 202 -7.095 -9.428 13.556 1.00 34.56 C ANISOU 3133 CG ASN B 202 4745 4631 3755 -184 369 -396 C ATOM 3134 OD1 ASN B 202 -6.861 -10.366 14.322 1.00 40.29 O ANISOU 3134 OD1 ASN B 202 5550 5359 4398 -224 373 -363 O ATOM 3135 ND2 ASN B 202 -6.412 -8.300 13.589 1.00 35.94 N ANISOU 3135 ND2 ASN B 202 4902 4792 3960 -147 323 -417 N ATOM 3136 N GLY B 203 -9.758 -12.363 10.573 1.00 20.67 N ANISOU 3136 N GLY B 203 2857 2877 2119 -224 466 -334 N ATOM 3137 CA GLY B 203 -10.931 -12.755 9.838 1.00 20.23 C ANISOU 3137 CA GLY B 203 2742 2829 2115 -237 507 -351 C ATOM 3138 C GLY B 203 -11.091 -12.164 8.446 1.00 17.96 C ANISOU 3138 C GLY B 203 2374 2529 1920 -192 467 -356 C ATOM 3139 O GLY B 203 -12.197 -12.220 7.895 1.00 21.01 O ANISOU 3139 O GLY B 203 2700 2923 2359 -199 497 -383 O ATOM 3140 N GLN B 204 -10.030 -11.536 7.920 1.00 16.97 N ANISOU 3140 N GLN B 204 2249 2385 1816 -148 402 -333 N ATOM 3141 CA GLN B 204 -10.045 -10.962 6.582 1.00 16.83 C ANISOU 3141 CA GLN B 204 2169 2352 1872 -110 359 -328 C ATOM 3142 C GLN B 204 -8.895 -11.464 5.756 1.00 14.81 C ANISOU 3142 C GLN B 204 1939 2075 1611 -92 305 -271 C ATOM 3143 O GLN B 204 -7.791 -11.624 6.254 1.00 16.05 O ANISOU 3143 O GLN B 204 2147 2223 1730 -87 280 -244 O ATOM 3144 CB GLN B 204 -10.009 -9.441 6.617 1.00 19.12 C ANISOU 3144 CB GLN B 204 2418 2638 2209 -76 337 -366 C ATOM 3145 CG GLN B 204 -11.217 -8.839 7.349 1.00 20.53 C ANISOU 3145 CG GLN B 204 2555 2834 2410 -88 394 -437 C ATOM 3146 CD GLN B 204 -11.333 -7.327 7.251 1.00 20.89 C ANISOU 3146 CD GLN B 204 2548 2868 2522 -50 368 -481 C ATOM 3147 OE1 GLN B 204 -10.384 -6.627 6.935 1.00 22.66 O ANISOU 3147 OE1 GLN B 204 2780 3071 2758 -20 312 -459 O ATOM 3148 NE2 GLN B 204 -12.510 -6.818 7.614 1.00 28.65 N ANISOU 3148 NE2 GLN B 204 3476 3861 3550 -55 414 -548 N ATOM 3149 N LEU B 209 -9.149 -11.678 4.481 1.00 14.10 N ANISOU 3149 N LEU B 209 1814 1978 1565 -82 285 -256 N ATOM 3150 CA LEU B 209 -8.132 -12.116 3.539 1.00 13.63 C ANISOU 3150 CA LEU B 209 1772 1901 1507 -66 243 -211 C ATOM 3151 C LEU B 209 -7.232 -10.955 3.159 1.00 15.55 C ANISOU 3151 C LEU B 209 2001 2131 1776 -31 198 -205 C ATOM 3152 O LEU B 209 -7.639 -10.103 2.370 1.00 19.27 O ANISOU 3152 O LEU B 209 2428 2599 2295 -15 179 -216 O ATOM 3153 CB LEU B 209 -8.778 -12.688 2.271 1.00 16.31 C ANISOU 3153 CB LEU B 209 2082 2238 1876 -72 239 -202 C ATOM 3154 CG LEU B 209 -7.800 -13.246 1.250 1.00 14.74 C ANISOU 3154 CG LEU B 209 1902 2023 1674 -62 207 -163 C ATOM 3155 CD1 LEU B 209 -7.104 -14.527 1.738 1.00 17.59 C ANISOU 3155 CD1 LEU B 209 2316 2374 1995 -77 217 -137 C ATOM 3156 CD2 LEU B 209 -8.499 -13.509 -0.095 1.00 14.47 C ANISOU 3156 CD2 LEU B 209 1839 1990 1670 -67 197 -162 C ATOM 3157 N GLN B 210 -6.041 -10.903 3.729 1.00 13.28 N ANISOU 3157 N GLN B 210 1750 1833 1462 -22 178 -187 N ATOM 3158 CA GLN B 210 -5.124 -9.807 3.454 1.00 13.06 C ANISOU 3158 CA GLN B 210 1709 1792 1463 7 137 -182 C ATOM 3159 C GLN B 210 -4.112 -10.126 2.368 1.00 13.84 C ANISOU 3159 C GLN B 210 1808 1875 1575 18 109 -145 C ATOM 3160 O GLN B 210 -3.576 -9.217 1.712 1.00 13.67 O ANISOU 3160 O GLN B 210 1765 1843 1586 35 81 -138 O ATOM 3161 CB GLN B 210 -4.401 -9.348 4.722 1.00 13.13 C ANISOU 3161 CB GLN B 210 1748 1797 1444 12 126 -192 C ATOM 3162 CG GLN B 210 -5.283 -8.716 5.753 1.00 13.78 C ANISOU 3162 CG GLN B 210 1826 1894 1514 3 156 -239 C ATOM 3163 CD GLN B 210 -5.716 -7.300 5.364 1.00 16.63 C ANISOU 3163 CD GLN B 210 2133 2250 1934 26 142 -271 C ATOM 3164 OE1 GLN B 210 -5.363 -6.786 4.285 1.00 18.36 O ANISOU 3164 OE1 GLN B 210 2324 2453 2198 45 107 -250 O ATOM 3165 NE2 GLN B 210 -6.497 -6.680 6.207 1.00 16.13 N ANISOU 3165 NE2 GLN B 210 2058 2198 1873 22 170 -321 N ATOM 3166 N GLY B 211 -3.710 -11.378 2.213 1.00 13.92 N ANISOU 3166 N GLY B 211 1846 1880 1562 7 116 -122 N ATOM 3167 CA GLY B 211 -2.638 -11.732 1.295 1.00 13.21 C ANISOU 3167 CA GLY B 211 1757 1775 1488 17 97 -96 C ATOM 3168 C GLY B 211 -2.936 -12.967 0.464 1.00 12.90 C ANISOU 3168 C GLY B 211 1724 1735 1442 2 114 -85 C ATOM 3169 O GLY B 211 -3.734 -13.826 0.869 1.00 13.72 O ANISOU 3169 O GLY B 211 1844 1845 1524 -17 137 -89 O ATOM 3170 N VAL B 212 -2.303 -13.007 -0.684 1.00 12.06 N ANISOU 3170 N VAL B 212 1606 1622 1354 9 106 -73 N ATOM 3171 CA VAL B 212 -2.216 -14.192 -1.552 1.00 12.80 C ANISOU 3171 CA VAL B 212 1709 1711 1444 -2 120 -66 C ATOM 3172 C VAL B 212 -0.735 -14.630 -1.562 1.00 13.16 C ANISOU 3172 C VAL B 212 1763 1735 1504 12 110 -56 C ATOM 3173 O VAL B 212 0.167 -13.822 -1.817 1.00 12.59 O ANISOU 3173 O VAL B 212 1674 1658 1453 25 97 -53 O ATOM 3174 CB VAL B 212 -2.626 -13.880 -2.974 1.00 13.32 C ANISOU 3174 CB VAL B 212 1757 1788 1517 -10 122 -67 C ATOM 3175 CG1 VAL B 212 -2.471 -15.096 -3.888 1.00 14.22 C ANISOU 3175 CG1 VAL B 212 1883 1895 1623 -22 137 -67 C ATOM 3176 CG2 VAL B 212 -4.083 -13.368 -3.049 1.00 15.61 C ANISOU 3176 CG2 VAL B 212 2029 2093 1808 -20 120 -79 C ATOM 3177 N VAL B 213 -0.437 -15.883 -1.244 1.00 13.44 N ANISOU 3177 N VAL B 213 1821 1751 1536 10 113 -52 N ATOM 3178 CA VAL B 213 0.931 -16.376 -1.284 1.00 12.96 C ANISOU 3178 CA VAL B 213 1759 1663 1502 26 100 -47 C ATOM 3179 C VAL B 213 1.488 -16.204 -2.700 1.00 12.31 C ANISOU 3179 C VAL B 213 1651 1586 1442 27 117 -56 C ATOM 3180 O VAL B 213 0.864 -16.611 -3.683 1.00 12.77 O ANISOU 3180 O VAL B 213 1710 1655 1487 11 139 -64 O ATOM 3181 CB VAL B 213 0.965 -17.866 -0.918 1.00 13.19 C ANISOU 3181 CB VAL B 213 1817 1666 1530 21 98 -43 C ATOM 3182 CG1 VAL B 213 2.378 -18.415 -1.019 1.00 13.69 C ANISOU 3182 CG1 VAL B 213 1870 1694 1637 42 80 -44 C ATOM 3183 CG2 VAL B 213 0.378 -18.146 0.437 1.00 13.80 C ANISOU 3183 CG2 VAL B 213 1930 1739 1575 9 86 -29 C ATOM 3184 N SER B 214 2.668 -15.570 -2.828 1.00 12.50 N ANISOU 3184 N SER B 214 1652 1601 1498 42 108 -57 N ATOM 3185 CA SER B 214 3.218 -15.193 -4.132 1.00 12.70 C ANISOU 3185 CA SER B 214 1654 1634 1536 36 132 -65 C ATOM 3186 C SER B 214 4.627 -15.732 -4.418 1.00 14.71 C ANISOU 3186 C SER B 214 1887 1865 1838 48 141 -79 C ATOM 3187 O SER B 214 4.790 -16.707 -5.175 1.00 15.76 O ANISOU 3187 O SER B 214 2020 1991 1978 43 168 -97 O ATOM 3188 CB SER B 214 3.121 -13.657 -4.281 1.00 14.88 C ANISOU 3188 CB SER B 214 1916 1928 1810 32 123 -55 C ATOM 3189 OG SER B 214 3.550 -13.207 -5.574 1.00 14.88 O ANISOU 3189 OG SER B 214 1904 1938 1813 16 147 -56 O ATOM 3190 N TRP B 215 5.652 -15.123 -3.823 1.00 16.38 N ANISOU 3190 N TRP B 215 2075 2061 2088 65 119 -77 N ATOM 3191 CA TRP B 215 7.029 -15.490 -4.179 1.00 13.73 C ANISOU 3191 CA TRP B 215 1704 1701 1810 76 130 -96 C ATOM 3192 C TRP B 215 7.968 -15.272 -3.031 1.00 15.58 C ANISOU 3192 C TRP B 215 1923 1907 2092 101 83 -91 C ATOM 3193 O TRP B 215 7.592 -14.746 -1.984 1.00 14.43 O ANISOU 3193 O TRP B 215 1797 1762 1924 106 44 -73 O ATOM 3194 CB TRP B 215 7.480 -14.738 -5.439 1.00 14.79 C ANISOU 3194 CB TRP B 215 1814 1856 1950 56 173 -105 C ATOM 3195 CG TRP B 215 7.624 -13.241 -5.264 1.00 14.03 C ANISOU 3195 CG TRP B 215 1706 1771 1854 51 158 -87 C ATOM 3196 CD1 TRP B 215 6.634 -12.324 -5.403 1.00 14.00 C ANISOU 3196 CD1 TRP B 215 1724 1791 1806 36 150 -66 C ATOM 3197 CD2 TRP B 215 8.828 -12.516 -5.046 1.00 13.37 C ANISOU 3197 CD2 TRP B 215 1583 1672 1824 58 149 -90 C ATOM 3198 NE1 TRP B 215 7.153 -11.063 -5.253 1.00 15.21 N ANISOU 3198 NE1 TRP B 215 1857 1941 1982 34 135 -55 N ATOM 3199 CE2 TRP B 215 8.486 -11.146 -5.014 1.00 12.91 C ANISOU 3199 CE2 TRP B 215 1529 1628 1748 46 135 -69 C ATOM 3200 CE3 TRP B 215 10.153 -12.883 -4.812 1.00 15.97 C ANISOU 3200 CE3 TRP B 215 1870 1973 2225 74 146 -110 C ATOM 3201 CZ2 TRP B 215 9.432 -10.151 -4.775 1.00 15.40 C ANISOU 3201 CZ2 TRP B 215 1811 1930 2110 47 120 -66 C ATOM 3202 CZ3 TRP B 215 11.085 -11.892 -4.586 1.00 17.80 C ANISOU 3202 CZ3 TRP B 215 2065 2195 2504 75 133 -109 C ATOM 3203 CH2 TRP B 215 10.704 -10.547 -4.536 1.00 16.15 C ANISOU 3203 CH2 TRP B 215 1865 2000 2270 61 120 -86 C ATOM 3204 N GLY B 216 9.190 -15.726 -3.193 1.00 14.52 N ANISOU 3204 N GLY B 216 1750 1743 2022 116 85 -111 N ATOM 3205 CA GLY B 216 10.251 -15.360 -2.290 1.00 15.65 C ANISOU 3205 CA GLY B 216 1866 1857 2223 138 37 -110 C ATOM 3206 C GLY B 216 11.583 -15.867 -2.774 1.00 16.85 C ANISOU 3206 C GLY B 216 1961 1979 2461 152 51 -142 C ATOM 3207 O GLY B 216 11.641 -16.551 -3.814 1.00 18.16 O ANISOU 3207 O GLY B 216 2114 2149 2636 143 104 -168 O ATOM 3208 N ASP B 217 12.665 -15.562 -2.070 1.00 17.10 N ANISOU 3208 N ASP B 217 1957 1980 2560 173 5 -146 N ATOM 3209 CA ASP B 217 13.955 -16.153 -2.449 1.00 19.31 C ANISOU 3209 CA ASP B 217 2173 2225 2939 190 14 -182 C ATOM 3210 C ASP B 217 14.072 -17.481 -1.723 1.00 19.13 C ANISOU 3210 C ASP B 217 2165 2154 2949 218 -39 -183 C ATOM 3211 O ASP B 217 14.468 -17.547 -0.568 1.00 20.08 O ANISOU 3211 O ASP B 217 2293 2240 3097 240 -118 -166 O ATOM 3212 CB ASP B 217 15.115 -15.231 -2.065 1.00 17.84 C ANISOU 3212 CB ASP B 217 1932 2022 2825 199 -15 -189 C ATOM 3213 CG ASP B 217 16.480 -15.787 -2.440 1.00 26.13 C ANISOU 3213 CG ASP B 217 2903 3034 3993 217 -4 -233 C ATOM 3214 OD1 ASP B 217 16.570 -16.892 -3.021 1.00 27.93 O ANISOU 3214 OD1 ASP B 217 3118 3246 4248 225 29 -262 O ATOM 3215 OD2 ASP B 217 17.473 -15.080 -2.116 1.00 28.97 O ANISOU 3215 OD2 ASP B 217 3209 3376 4423 224 -31 -242 O ATOM 3216 N GLY B 219 13.707 -18.564 -2.387 1.00 17.57 N ANISOU 3216 N GLY B 219 1978 1952 2746 217 -1 -201 N ATOM 3217 CA GLY B 219 13.576 -19.841 -1.711 1.00 20.28 C ANISOU 3217 CA GLY B 219 2351 2250 3107 238 -53 -194 C ATOM 3218 C GLY B 219 12.481 -19.724 -0.668 1.00 17.03 C ANISOU 3218 C GLY B 219 2015 1849 2604 227 -100 -144 C ATOM 3219 O GLY B 219 11.521 -18.945 -0.808 1.00 18.16 O ANISOU 3219 O GLY B 219 2192 2043 2666 202 -69 -126 O ATOM 3220 N CYS B 220 12.641 -20.522 0.383 1.00 18.76 N ANISOU 3220 N CYS B 220 2265 2021 2844 245 -174 -124 N ATOM 3221 CA CYS B 220 11.677 -20.581 1.450 1.00 20.08 C ANISOU 3221 CA CYS B 220 2509 2194 2926 231 -216 -79 C ATOM 3222 C CYS B 220 12.397 -20.716 2.777 1.00 18.17 C ANISOU 3222 C CYS B 220 2285 1903 2715 251 -315 -55 C ATOM 3223 O CYS B 220 13.343 -21.487 2.928 1.00 19.13 O ANISOU 3223 O CYS B 220 2378 1965 2925 278 -365 -65 O ATOM 3224 CB CYS B 220 10.734 -21.771 1.356 1.00 26.18 C ANISOU 3224 CB CYS B 220 3332 2957 3659 218 -202 -68 C ATOM 3225 SG CYS B 220 10.155 -22.327 -0.286 1.00 31.20 S ANISOU 3225 SG CYS B 220 3945 3619 4290 203 -106 -106 S ATOM 3226 N ALA B 221A 11.908 -19.971 3.764 1.00 18.11 N ANISOU 3226 N ALA B 221A 2329 1918 2635 235 -347 -24 N ATOM 3227 CA ALA B 221A 12.410 -20.037 5.114 1.00 18.26 C ANISOU 3227 CA ALA B 221A 2386 1898 2656 245 -445 4 C ATOM 3228 C ALA B 221A 13.892 -19.663 5.282 1.00 17.11 C ANISOU 3228 C ALA B 221A 2175 1712 2614 277 -504 -15 C ATOM 3229 O ALA B 221A 14.489 -20.006 6.305 1.00 18.29 O ANISOU 3229 O ALA B 221A 2350 1812 2788 291 -601 6 O ATOM 3230 CB ALA B 221A 12.101 -21.376 5.785 1.00 20.19 C ANISOU 3230 CB ALA B 221A 2694 2095 2882 241 -495 36 C ATOM 3231 N GLN B 221 14.476 -18.922 4.340 1.00 17.78 N ANISOU 3231 N GLN B 221 2180 1818 2757 285 -452 -52 N ATOM 3232 CA GLN B 221 15.856 -18.490 4.445 1.00 18.03 C ANISOU 3232 CA GLN B 221 2141 1815 2894 310 -499 -74 C ATOM 3233 C GLN B 221 15.939 -17.257 5.330 1.00 18.69 C ANISOU 3233 C GLN B 221 2245 1917 2938 302 -545 -58 C ATOM 3234 O GLN B 221 15.070 -16.370 5.302 1.00 16.95 O ANISOU 3234 O GLN B 221 2057 1751 2633 277 -500 -50 O ATOM 3235 CB GLN B 221 16.503 -18.213 3.077 1.00 20.08 C ANISOU 3235 CB GLN B 221 2307 2089 3234 315 -418 -122 C ATOM 3236 CG GLN B 221 16.457 -19.393 2.129 1.00 22.10 C ANISOU 3236 CG GLN B 221 2539 2328 3528 323 -366 -148 C ATOM 3237 CD GLN B 221 17.385 -19.208 0.931 1.00 32.98 C ANISOU 3237 CD GLN B 221 3820 3708 5001 329 -297 -203 C ATOM 3238 OE1 GLN B 221 17.087 -18.449 -0.007 1.00 35.28 O ANISOU 3238 OE1 GLN B 221 4096 4054 5257 302 -210 -217 O ATOM 3239 NE2 GLN B 221 18.526 -19.840 0.989 1.00 36.55 N ANISOU 3239 NE2 GLN B 221 4207 4101 5578 361 -337 -234 N ATOM 3240 N LYS B 222 17.032 -17.150 6.060 1.00 18.78 N ANISOU 3240 N LYS B 222 2231 1882 3024 324 -635 -60 N ATOM 3241 CA LYS B 222 17.310 -15.945 6.829 1.00 19.28 C ANISOU 3241 CA LYS B 222 2300 1956 3068 318 -682 -55 C ATOM 3242 C LYS B 222 17.263 -14.697 5.926 1.00 18.67 C ANISOU 3242 C LYS B 222 2169 1928 2995 303 -598 -80 C ATOM 3243 O LYS B 222 17.792 -14.692 4.825 1.00 20.64 O ANISOU 3243 O LYS B 222 2342 2180 3319 307 -537 -110 O ATOM 3244 CB LYS B 222 18.632 -16.057 7.556 1.00 23.06 C ANISOU 3244 CB LYS B 222 2742 2372 3648 346 -793 -60 C ATOM 3245 CG LYS B 222 18.862 -14.855 8.486 1.00 23.71 C ANISOU 3245 CG LYS B 222 2845 2463 3701 337 -854 -53 C ATOM 3246 CD LYS B 222 19.976 -15.031 9.461 1.00 27.88 C ANISOU 3246 CD LYS B 222 3363 2927 4304 361 -986 -49 C ATOM 3247 CE LYS B 222 20.294 -13.660 10.112 1.00 40.47 C ANISOU 3247 CE LYS B 222 4957 4535 5884 350 -1029 -56 C ATOM 3248 NZ LYS B 222 21.525 -13.754 10.945 1.00 44.97 N ANISOU 3248 NZ LYS B 222 5500 5039 6545 374 -1162 -59 N ATOM 3249 N ASN B 223 16.538 -13.677 6.393 1.00 17.68 N ANISOU 3249 N ASN B 223 2092 1844 2783 281 -592 -67 N ATOM 3250 CA ASN B 223 16.425 -12.380 5.750 1.00 18.93 C ANISOU 3250 CA ASN B 223 2214 2042 2938 265 -531 -82 C ATOM 3251 C ASN B 223 15.665 -12.433 4.424 1.00 18.99 C ANISOU 3251 C ASN B 223 2208 2092 2917 248 -423 -89 C ATOM 3252 O ASN B 223 15.730 -11.471 3.639 1.00 19.75 O ANISOU 3252 O ASN B 223 2264 2213 3027 233 -369 -101 O ATOM 3253 CB ASN B 223 17.789 -11.701 5.597 1.00 20.45 C ANISOU 3253 CB ASN B 223 2322 2207 3243 277 -560 -107 C ATOM 3254 CG ASN B 223 18.251 -11.075 6.924 1.00 30.21 C ANISOU 3254 CG ASN B 223 3582 3417 4479 283 -663 -100 C ATOM 3255 OD1 ASN B 223 17.498 -10.300 7.566 1.00 35.15 O ANISOU 3255 OD1 ASN B 223 4267 4071 5017 267 -672 -89 O ATOM 3256 ND2 ASN B 223 19.441 -11.421 7.347 1.00 33.94 N ANISOU 3256 ND2 ASN B 223 4010 3837 5048 307 -742 -110 N ATOM 3257 N LYS B 224 14.898 -13.503 4.215 1.00 16.55 N ANISOU 3257 N LYS B 224 1939 1788 2562 245 -395 -78 N ATOM 3258 CA LYS B 224 14.114 -13.673 2.998 1.00 16.64 C ANISOU 3258 CA LYS B 224 1946 1837 2539 228 -302 -85 C ATOM 3259 C LYS B 224 12.722 -14.205 3.329 1.00 16.27 C ANISOU 3259 C LYS B 224 1975 1813 2392 214 -288 -62 C ATOM 3260 O LYS B 224 12.340 -15.317 2.971 1.00 15.75 O ANISOU 3260 O LYS B 224 1926 1741 2317 214 -266 -60 O ATOM 3261 CB LYS B 224 14.841 -14.598 1.995 1.00 18.37 C ANISOU 3261 CB LYS B 224 2107 2034 2838 239 -264 -111 C ATOM 3262 CG LYS B 224 16.246 -14.138 1.618 1.00 17.02 C ANISOU 3262 CG LYS B 224 1851 1840 2777 250 -267 -140 C ATOM 3263 CD LYS B 224 16.233 -12.912 0.748 1.00 21.57 C ANISOU 3263 CD LYS B 224 2395 2455 3345 224 -201 -147 C ATOM 3264 CE LYS B 224 17.630 -12.320 0.738 1.00 28.66 C ANISOU 3264 CE LYS B 224 3215 3326 4350 231 -220 -171 C ATOM 3265 NZ LYS B 224 17.795 -11.177 -0.164 1.00 34.77 N ANISOU 3265 NZ LYS B 224 3952 4129 5129 201 -155 -178 N ATOM 3266 N PRO B 225 11.906 -13.375 4.007 1.00 14.62 N ANISOU 3266 N PRO B 225 1811 1632 2110 199 -297 -49 N ATOM 3267 CA PRO B 225 10.535 -13.769 4.281 1.00 16.52 C ANISOU 3267 CA PRO B 225 2115 1899 2260 181 -273 -34 C ATOM 3268 C PRO B 225 9.715 -13.810 2.990 1.00 14.89 C ANISOU 3268 C PRO B 225 1895 1729 2035 166 -193 -41 C ATOM 3269 O PRO B 225 10.092 -13.203 1.966 1.00 14.78 O ANISOU 3269 O PRO B 225 1831 1726 2057 164 -155 -55 O ATOM 3270 CB PRO B 225 10.048 -12.620 5.176 1.00 16.02 C ANISOU 3270 CB PRO B 225 2085 1859 2145 171 -294 -32 C ATOM 3271 CG PRO B 225 10.802 -11.431 4.655 1.00 16.30 C ANISOU 3271 CG PRO B 225 2060 1895 2237 177 -290 -47 C ATOM 3272 CD PRO B 225 12.182 -11.999 4.435 1.00 16.70 C ANISOU 3272 CD PRO B 225 2062 1905 2377 197 -321 -54 C ATOM 3273 N GLY B 226 8.632 -14.567 2.989 1.00 14.60 N ANISOU 3273 N GLY B 226 1900 1705 1941 152 -168 -31 N ATOM 3274 CA GLY B 226 7.758 -14.620 1.848 1.00 14.70 C ANISOU 3274 CA GLY B 226 1904 1750 1930 136 -102 -38 C ATOM 3275 C GLY B 226 7.127 -13.280 1.520 1.00 12.99 C ANISOU 3275 C GLY B 226 1678 1569 1688 124 -77 -41 C ATOM 3276 O GLY B 226 6.906 -12.405 2.371 1.00 13.04 O ANISOU 3276 O GLY B 226 1700 1583 1672 124 -103 -40 O ATOM 3277 N VAL B 227 6.905 -13.109 0.211 1.00 12.94 N ANISOU 3277 N VAL B 227 1647 1583 1688 113 -30 -48 N ATOM 3278 CA VAL B 227 6.247 -11.927 -0.367 1.00 13.59 C ANISOU 3278 CA VAL B 227 1719 1693 1750 100 -8 -47 C ATOM 3279 C VAL B 227 4.863 -12.340 -0.802 1.00 14.14 C ANISOU 3279 C VAL B 227 1814 1788 1771 83 23 -46 C ATOM 3280 O VAL B 227 4.638 -13.433 -1.365 1.00 14.08 O ANISOU 3280 O VAL B 227 1815 1780 1756 77 46 -48 O ATOM 3281 CB VAL B 227 7.056 -11.362 -1.499 1.00 15.00 C ANISOU 3281 CB VAL B 227 1858 1873 1968 94 16 -52 C ATOM 3282 CG1 VAL B 227 6.407 -10.040 -1.974 1.00 13.94 C ANISOU 3282 CG1 VAL B 227 1721 1760 1816 79 24 -43 C ATOM 3283 CG2 VAL B 227 8.491 -11.146 -1.109 1.00 16.55 C ANISOU 3283 CG2 VAL B 227 2021 2042 2226 109 -10 -58 C ATOM 3284 N TYR B 228 3.895 -11.466 -0.545 1.00 12.98 N ANISOU 3284 N TYR B 228 1675 1660 1597 76 20 -45 N ATOM 3285 CA TYR B 228 2.462 -11.744 -0.673 1.00 11.06 C ANISOU 3285 CA TYR B 228 1450 1438 1315 62 41 -47 C ATOM 3286 C TYR B 228 1.762 -10.600 -1.399 1.00 12.60 C ANISOU 3286 C TYR B 228 1627 1649 1510 55 45 -48 C ATOM 3287 O TYR B 228 2.178 -9.425 -1.268 1.00 13.46 O ANISOU 3287 O TYR B 228 1720 1754 1642 62 26 -47 O ATOM 3288 CB TYR B 228 1.839 -11.908 0.719 1.00 12.61 C ANISOU 3288 CB TYR B 228 1675 1635 1480 62 28 -52 C ATOM 3289 CG TYR B 228 2.441 -13.068 1.473 1.00 11.68 C ANISOU 3289 CG TYR B 228 1585 1496 1356 66 14 -44 C ATOM 3290 CD1 TYR B 228 3.609 -12.935 2.208 1.00 13.29 C ANISOU 3290 CD1 TYR B 228 1792 1677 1582 81 -25 -40 C ATOM 3291 CD2 TYR B 228 1.873 -14.313 1.379 1.00 14.48 C ANISOU 3291 CD2 TYR B 228 1963 1849 1690 53 32 -39 C ATOM 3292 CE1 TYR B 228 4.175 -14.019 2.855 1.00 13.62 C ANISOU 3292 CE1 TYR B 228 1860 1691 1624 86 -51 -29 C ATOM 3293 CE2 TYR B 228 2.423 -15.411 2.042 1.00 14.56 C ANISOU 3293 CE2 TYR B 228 2002 1832 1699 55 11 -27 C ATOM 3294 CZ TYR B 228 3.562 -15.272 2.736 1.00 13.79 C ANISOU 3294 CZ TYR B 228 1908 1709 1624 72 -32 -21 C ATOM 3295 OH TYR B 228 4.057 -16.413 3.324 1.00 16.08 O ANISOU 3295 OH TYR B 228 2228 1965 1918 75 -61 -6 O ATOM 3296 N THR B 229 0.766 -10.918 -2.210 1.00 12.28 N ANISOU 3296 N THR B 229 1589 1624 1451 40 65 -48 N ATOM 3297 CA THR B 229 -0.023 -9.882 -2.864 1.00 11.21 C ANISOU 3297 CA THR B 229 1440 1499 1320 33 57 -46 C ATOM 3298 C THR B 229 -0.974 -9.245 -1.885 1.00 12.68 C ANISOU 3298 C THR B 229 1621 1690 1506 40 46 -62 C ATOM 3299 O THR B 229 -1.651 -9.922 -1.138 1.00 12.75 O ANISOU 3299 O THR B 229 1643 1707 1495 37 59 -75 O ATOM 3300 CB THR B 229 -0.795 -10.467 -4.010 1.00 12.91 C ANISOU 3300 CB THR B 229 1661 1727 1518 15 72 -43 C ATOM 3301 OG1 THR B 229 0.135 -11.229 -4.798 1.00 15.77 O ANISOU 3301 OG1 THR B 229 2031 2085 1875 7 92 -38 O ATOM 3302 CG2 THR B 229 -1.501 -9.414 -4.845 1.00 13.46 C ANISOU 3302 CG2 THR B 229 1719 1801 1594 7 52 -34 C ATOM 3303 N LYS B 230 -1.007 -7.914 -1.878 1.00 12.61 N ANISOU 3303 N LYS B 230 1594 1675 1523 48 23 -64 N ATOM 3304 CA LYS B 230 -1.905 -7.123 -1.022 1.00 11.75 C ANISOU 3304 CA LYS B 230 1473 1567 1425 57 13 -88 C ATOM 3305 C LYS B 230 -3.332 -7.131 -1.548 1.00 11.78 C ANISOU 3305 C LYS B 230 1462 1581 1434 49 17 -98 C ATOM 3306 O LYS B 230 -3.667 -6.359 -2.425 1.00 12.49 O ANISOU 3306 O LYS B 230 1534 1662 1548 49 -7 -89 O ATOM 3307 CB LYS B 230 -1.421 -5.680 -0.964 1.00 14.58 C ANISOU 3307 CB LYS B 230 1814 1907 1820 69 -19 -88 C ATOM 3308 CG LYS B 230 -0.316 -5.341 -0.127 1.00 20.69 C ANISOU 3308 CG LYS B 230 2593 2668 2599 80 -31 -91 C ATOM 3309 CD LYS B 230 -0.176 -3.750 -0.115 1.00 18.03 C ANISOU 3309 CD LYS B 230 2234 2311 2307 90 -65 -96 C ATOM 3310 CE LYS B 230 1.134 -3.410 0.380 1.00 20.38 C ANISOU 3310 CE LYS B 230 2534 2592 2619 96 -82 -92 C ATOM 3311 NZ LYS B 230 1.327 -1.959 0.182 1.00 19.97 N ANISOU 3311 NZ LYS B 230 2460 2515 2612 101 -114 -91 N ATOM 3312 N VAL B 231 -4.183 -8.045 -1.050 1.00 12.43 N ANISOU 3312 N VAL B 231 1549 1678 1495 40 44 -116 N ATOM 3313 CA VAL B 231 -5.559 -8.179 -1.517 1.00 12.25 C ANISOU 3313 CA VAL B 231 1506 1664 1485 31 49 -129 C ATOM 3314 C VAL B 231 -6.314 -6.847 -1.424 1.00 12.32 C ANISOU 3314 C VAL B 231 1477 1662 1541 45 24 -152 C ATOM 3315 O VAL B 231 -7.149 -6.549 -2.294 1.00 13.73 O ANISOU 3315 O VAL B 231 1632 1837 1749 43 1 -151 O ATOM 3316 CB VAL B 231 -6.275 -9.304 -0.775 1.00 13.86 C ANISOU 3316 CB VAL B 231 1720 1883 1663 15 88 -148 C ATOM 3317 CG1 VAL B 231 -7.704 -9.392 -1.155 1.00 14.14 C ANISOU 3317 CG1 VAL B 231 1724 1927 1722 5 94 -168 C ATOM 3318 CG2 VAL B 231 -5.588 -10.648 -1.080 1.00 13.90 C ANISOU 3318 CG2 VAL B 231 1760 1889 1633 3 103 -123 C ATOM 3319 N TYR B 232 -6.063 -6.072 -0.359 1.00 11.90 N ANISOU 3319 N TYR B 232 1419 1604 1499 59 24 -175 N ATOM 3320 CA TYR B 232 -6.774 -4.812 -0.175 1.00 13.62 C ANISOU 3320 CA TYR B 232 1598 1807 1770 76 2 -205 C ATOM 3321 C TYR B 232 -6.619 -3.869 -1.387 1.00 12.31 C ANISOU 3321 C TYR B 232 1417 1616 1644 83 -51 -176 C ATOM 3322 O TYR B 232 -7.543 -3.111 -1.695 1.00 13.60 O ANISOU 3322 O TYR B 232 1545 1763 1860 93 -79 -192 O ATOM 3323 CB TYR B 232 -6.318 -4.151 1.127 1.00 13.95 C ANISOU 3323 CB TYR B 232 1644 1845 1810 89 10 -235 C ATOM 3324 CG TYR B 232 -6.996 -2.799 1.375 1.00 14.06 C ANISOU 3324 CG TYR B 232 1616 1838 1887 109 -12 -275 C ATOM 3325 CD1 TYR B 232 -8.345 -2.717 1.650 1.00 13.88 C ANISOU 3325 CD1 TYR B 232 1554 1822 1899 110 9 -321 C ATOM 3326 CD2 TYR B 232 -6.260 -1.601 1.305 1.00 14.68 C ANISOU 3326 CD2 TYR B 232 1690 1888 2000 126 -54 -268 C ATOM 3327 CE1 TYR B 232 -8.978 -1.481 1.869 1.00 15.54 C ANISOU 3327 CE1 TYR B 232 1717 2007 2179 132 -13 -365 C ATOM 3328 CE2 TYR B 232 -6.896 -0.394 1.503 1.00 14.41 C ANISOU 3328 CE2 TYR B 232 1615 1828 2031 146 -78 -306 C ATOM 3329 CZ TYR B 232 -8.205 -0.343 1.765 1.00 14.64 C ANISOU 3329 CZ TYR B 232 1605 1863 2096 151 -59 -354 C ATOM 3330 OH TYR B 232 -8.882 0.846 1.981 1.00 16.60 O ANISOU 3330 OH TYR B 232 1805 2080 2421 174 -83 -400 O ATOM 3331 N ASN B 233 -5.513 -3.955 -2.089 1.00 13.17 N ANISOU 3331 N ASN B 233 1553 1719 1730 76 -64 -134 N ATOM 3332 CA ASN B 233 -5.289 -3.096 -3.257 1.00 13.53 C ANISOU 3332 CA ASN B 233 1596 1742 1802 73 -110 -99 C ATOM 3333 C ASN B 233 -6.149 -3.458 -4.469 1.00 13.82 C ANISOU 3333 C ASN B 233 1632 1781 1837 58 -129 -81 C ATOM 3334 O ASN B 233 -6.199 -2.708 -5.444 1.00 15.64 O ANISOU 3334 O ASN B 233 1866 1991 2088 52 -175 -52 O ATOM 3335 CB ASN B 233 -3.823 -3.083 -3.645 1.00 13.07 C ANISOU 3335 CB ASN B 233 1566 1679 1719 63 -108 -64 C ATOM 3336 CG ASN B 233 -3.004 -2.255 -2.740 1.00 15.66 C ANISOU 3336 CG ASN B 233 1888 1992 2069 79 -116 -75 C ATOM 3337 OD1 ASN B 233 -3.493 -1.784 -1.715 1.00 17.16 O ANISOU 3337 OD1 ASN B 233 2060 2177 2282 96 -117 -113 O ATOM 3338 ND2 ASN B 233 -1.783 -2.010 -3.131 1.00 15.32 N ANISOU 3338 ND2 ASN B 233 1858 1939 2023 70 -120 -46 N ATOM 3339 N TYR B 234 -6.875 -4.573 -4.384 1.00 11.94 N ANISOU 3339 N TYR B 234 1393 1565 1577 49 -100 -98 N ATOM 3340 CA TYR B 234 -7.648 -5.134 -5.467 1.00 13.39 C ANISOU 3340 CA TYR B 234 1579 1755 1754 32 -116 -84 C ATOM 3341 C TYR B 234 -9.131 -5.293 -5.193 1.00 15.45 C ANISOU 3341 C TYR B 234 1799 2017 2053 37 -119 -121 C ATOM 3342 O TYR B 234 -9.862 -5.899 -5.995 1.00 14.14 O ANISOU 3342 O TYR B 234 1633 1857 1884 22 -133 -116 O ATOM 3343 CB TYR B 234 -7.041 -6.508 -5.887 1.00 12.71 C ANISOU 3343 CB TYR B 234 1531 1691 1606 11 -78 -68 C ATOM 3344 CG TYR B 234 -5.647 -6.352 -6.399 1.00 13.32 C ANISOU 3344 CG TYR B 234 1640 1765 1655 3 -74 -35 C ATOM 3345 CD1 TYR B 234 -5.370 -5.913 -7.695 1.00 13.74 C ANISOU 3345 CD1 TYR B 234 1715 1810 1696 -16 -104 0 C ATOM 3346 CD2 TYR B 234 -4.568 -6.587 -5.563 1.00 13.19 C ANISOU 3346 CD2 TYR B 234 1632 1752 1626 11 -42 -39 C ATOM 3347 CE1 TYR B 234 -4.050 -5.727 -8.104 1.00 14.88 C ANISOU 3347 CE1 TYR B 234 1883 1953 1818 -27 -90 26 C ATOM 3348 CE2 TYR B 234 -3.285 -6.383 -5.949 1.00 12.76 C ANISOU 3348 CE2 TYR B 234 1596 1693 1560 5 -37 -16 C ATOM 3349 CZ TYR B 234 -3.010 -5.946 -7.200 1.00 13.49 C ANISOU 3349 CZ TYR B 234 1703 1779 1642 -15 -56 15 C ATOM 3350 OH TYR B 234 -1.712 -5.752 -7.590 1.00 15.50 O ANISOU 3350 OH TYR B 234 1971 2030 1887 -26 -41 34 O ATOM 3351 N VAL B 235 -9.644 -4.723 -4.102 1.00 13.63 N ANISOU 3351 N VAL B 235 1531 1782 1866 56 -108 -164 N ATOM 3352 CA VAL B 235 -11.036 -4.949 -3.757 1.00 15.76 C ANISOU 3352 CA VAL B 235 1755 2056 2178 58 -97 -207 C ATOM 3353 C VAL B 235 -11.980 -4.420 -4.847 1.00 16.70 C ANISOU 3353 C VAL B 235 1843 2151 2353 61 -164 -200 C ATOM 3354 O VAL B 235 -12.918 -5.112 -5.184 1.00 15.85 O ANISOU 3354 O VAL B 235 1714 2050 2257 49 -164 -213 O ATOM 3355 CB VAL B 235 -11.339 -4.355 -2.378 1.00 19.50 C ANISOU 3355 CB VAL B 235 2195 2529 2685 76 -65 -261 C ATOM 3356 CG1 VAL B 235 -12.836 -4.285 -2.125 1.00 21.94 C ANISOU 3356 CG1 VAL B 235 2441 2836 3059 80 -58 -313 C ATOM 3357 CG2 VAL B 235 -10.573 -5.118 -1.261 1.00 20.87 C ANISOU 3357 CG2 VAL B 235 2407 2730 2793 65 -1 -267 C ATOM 3358 N LYS B 236 -11.714 -3.253 -5.440 1.00 15.21 N ANISOU 3358 N LYS B 236 1653 1928 2196 74 -227 -175 N ATOM 3359 CA LYS B 236 -12.593 -2.725 -6.496 1.00 17.26 C ANISOU 3359 CA LYS B 236 1891 2158 2509 76 -306 -161 C ATOM 3360 C LYS B 236 -12.484 -3.609 -7.745 1.00 16.41 C ANISOU 3360 C LYS B 236 1830 2065 2341 44 -324 -117 C ATOM 3361 O LYS B 236 -13.516 -3.967 -8.339 1.00 18.17 O ANISOU 3361 O LYS B 236 2030 2283 2590 37 -359 -124 O ATOM 3362 CB LYS B 236 -12.225 -1.280 -6.838 1.00 18.59 C ANISOU 3362 CB LYS B 236 2060 2283 2720 92 -372 -136 C ATOM 3363 CG LYS B 236 -13.008 -0.742 -8.072 1.00 25.16 C ANISOU 3363 CG LYS B 236 2885 3078 3598 89 -469 -107 C ATOM 3364 CD LYS B 236 -12.506 0.673 -8.496 1.00 31.45 C ANISOU 3364 CD LYS B 236 3696 3825 4428 99 -540 -68 C ATOM 3365 CE LYS B 236 -12.603 0.976 -10.006 1.00 36.99 C ANISOU 3365 CE LYS B 236 4442 4499 5114 74 -630 -3 C ATOM 3366 NZ LYS B 236 -14.005 1.073 -10.497 1.00 36.95 N ANISOU 3366 NZ LYS B 236 4393 4465 5181 84 -706 -18 N ATOM 3367 N TRP B 237 -11.272 -4.042 -8.092 1.00 15.80 N ANISOU 3367 N TRP B 237 1812 2005 2186 25 -296 -78 N ATOM 3368 CA TRP B 237 -11.097 -4.921 -9.259 1.00 16.06 C ANISOU 3368 CA TRP B 237 1893 2053 2156 -7 -304 -44 C ATOM 3369 C TRP B 237 -11.905 -6.201 -9.048 1.00 16.56 C ANISOU 3369 C TRP B 237 1939 2141 2212 -16 -268 -77 C ATOM 3370 O TRP B 237 -12.582 -6.698 -9.965 1.00 16.18 O ANISOU 3370 O TRP B 237 1898 2093 2157 -35 -302 -69 O ATOM 3371 CB TRP B 237 -9.619 -5.214 -9.497 1.00 16.46 C ANISOU 3371 CB TRP B 237 2000 2120 2135 -23 -264 -12 C ATOM 3372 CG TRP B 237 -9.438 -6.160 -10.636 1.00 17.50 C ANISOU 3372 CG TRP B 237 2179 2270 2202 -56 -260 11 C ATOM 3373 CD1 TRP B 237 -9.647 -5.877 -11.979 1.00 19.40 C ANISOU 3373 CD1 TRP B 237 2454 2499 2418 -81 -319 47 C ATOM 3374 CD2 TRP B 237 -9.054 -7.516 -10.557 1.00 16.27 C ANISOU 3374 CD2 TRP B 237 2044 2143 1997 -70 -200 -1 C ATOM 3375 NE1 TRP B 237 -9.417 -7.017 -12.720 1.00 18.84 N ANISOU 3375 NE1 TRP B 237 2425 2453 2282 -110 -291 51 N ATOM 3376 CE2 TRP B 237 -9.054 -8.034 -11.878 1.00 16.69 C ANISOU 3376 CE2 TRP B 237 2141 2202 1998 -102 -219 20 C ATOM 3377 CE3 TRP B 237 -8.732 -8.368 -9.499 1.00 16.65 C ANISOU 3377 CE3 TRP B 237 2081 2207 2038 -60 -136 -29 C ATOM 3378 CZ2 TRP B 237 -8.723 -9.353 -12.144 1.00 17.97 C ANISOU 3378 CZ2 TRP B 237 2330 2387 2111 -120 -171 9 C ATOM 3379 CZ3 TRP B 237 -8.400 -9.701 -9.784 1.00 16.48 C ANISOU 3379 CZ3 TRP B 237 2088 2205 1970 -78 -95 -33 C ATOM 3380 CH2 TRP B 237 -8.408 -10.173 -11.085 1.00 18.25 C ANISOU 3380 CH2 TRP B 237 2349 2434 2152 -106 -111 -18 C ATOM 3381 N ILE B 238 -11.808 -6.782 -7.852 1.00 14.76 N ANISOU 3381 N ILE B 238 1694 1933 1982 -8 -199 -111 N ATOM 3382 CA ILE B 238 -12.555 -8.007 -7.539 1.00 13.95 C ANISOU 3382 CA ILE B 238 1576 1851 1874 -22 -159 -140 C ATOM 3383 C ILE B 238 -14.050 -7.808 -7.637 1.00 16.24 C ANISOU 3383 C ILE B 238 1807 2128 2237 -19 -194 -172 C ATOM 3384 O ILE B 238 -14.759 -8.570 -8.329 1.00 17.71 O ANISOU 3384 O ILE B 238 1990 2318 2422 -38 -212 -174 O ATOM 3385 CB ILE B 238 -12.145 -8.526 -6.162 1.00 14.31 C ANISOU 3385 CB ILE B 238 1621 1915 1900 -18 -84 -165 C ATOM 3386 CG1 ILE B 238 -10.682 -8.979 -6.171 1.00 15.08 C ANISOU 3386 CG1 ILE B 238 1775 2022 1931 -24 -55 -134 C ATOM 3387 CG2 ILE B 238 -13.048 -9.658 -5.710 1.00 16.63 C ANISOU 3387 CG2 ILE B 238 1896 2225 2198 -36 -42 -196 C ATOM 3388 CD1 ILE B 238 -10.122 -9.258 -4.787 1.00 16.66 C ANISOU 3388 CD1 ILE B 238 1983 2234 2115 -16 0 -151 C ATOM 3389 N LYS B 239 -14.578 -6.762 -7.008 1.00 16.26 N ANISOU 3389 N LYS B 239 1756 2111 2310 7 -210 -202 N ATOM 3390 CA LYS B 239 -16.012 -6.488 -7.032 1.00 16.73 C ANISOU 3390 CA LYS B 239 1744 2154 2457 15 -244 -241 C ATOM 3391 C LYS B 239 -16.498 -6.204 -8.460 1.00 18.46 C ANISOU 3391 C LYS B 239 1969 2348 2698 9 -341 -209 C ATOM 3392 O LYS B 239 -17.511 -6.781 -8.891 1.00 19.68 O ANISOU 3392 O LYS B 239 2092 2501 2884 -3 -364 -226 O ATOM 3393 CB LYS B 239 -16.365 -5.381 -6.045 1.00 21.05 C ANISOU 3393 CB LYS B 239 2233 2684 3080 47 -237 -285 C ATOM 3394 CG LYS B 239 -16.131 -5.811 -4.597 1.00 25.37 C ANISOU 3394 CG LYS B 239 2777 3261 3601 44 -140 -325 C ATOM 3395 CD LYS B 239 -16.689 -4.783 -3.613 1.00 33.23 C ANISOU 3395 CD LYS B 239 3709 4241 4675 71 -126 -384 C ATOM 3396 CE LYS B 239 -16.435 -5.200 -2.156 1.00 40.26 C ANISOU 3396 CE LYS B 239 4608 5164 5524 61 -29 -423 C ATOM 3397 NZ LYS B 239 -17.029 -6.528 -1.837 1.00 47.80 N ANISOU 3397 NZ LYS B 239 5561 6150 6452 27 35 -439 N ATOM 3398 N ASN B 240 -15.750 -5.429 -9.224 1.00 17.93 N ANISOU 3398 N ASN B 240 1947 2262 2606 12 -396 -160 N ATOM 3399 CA ASN B 240 -16.095 -5.087 -10.608 1.00 19.44 C ANISOU 3399 CA ASN B 240 2159 2426 2800 0 -494 -120 C ATOM 3400 C ASN B 240 -16.075 -6.348 -11.493 1.00 20.50 C ANISOU 3400 C ASN B 240 2343 2586 2861 -37 -488 -101 C ATOM 3401 O ASN B 240 -16.958 -6.556 -12.349 1.00 23.28 O ANISOU 3401 O ASN B 240 2686 2924 3234 -50 -555 -98 O ATOM 3402 CB ASN B 240 -15.076 -4.088 -11.183 1.00 20.07 C ANISOU 3402 CB ASN B 240 2295 2485 2847 0 -536 -65 C ATOM 3403 CG ASN B 240 -15.266 -2.644 -10.680 1.00 25.35 C ANISOU 3403 CG ASN B 240 2917 3111 3603 35 -580 -76 C ATOM 3404 OD1 ASN B 240 -14.452 -1.790 -11.009 1.00 27.45 O ANISOU 3404 OD1 ASN B 240 3223 3357 3851 34 -610 -34 O ATOM 3405 ND2 ASN B 240 -16.299 -2.388 -9.902 1.00 24.70 N ANISOU 3405 ND2 ASN B 240 2753 3014 3616 63 -579 -135 N ATOM 3406 N THR B 241 -15.076 -7.178 -11.281 1.00 17.97 N ANISOU 3406 N THR B 241 2071 2298 2458 -53 -412 -91 N ATOM 3407 CA THR B 241 -14.936 -8.402 -12.086 1.00 17.46 C ANISOU 3407 CA THR B 241 2055 2255 2322 -86 -399 -79 C ATOM 3408 C THR B 241 -16.096 -9.347 -11.794 1.00 18.83 C ANISOU 3408 C THR B 241 2181 2438 2537 -93 -384 -122 C ATOM 3409 O THR B 241 -16.685 -9.936 -12.737 1.00 19.54 O ANISOU 3409 O THR B 241 2284 2525 2615 -117 -429 -119 O ATOM 3410 CB THR B 241 -13.594 -9.087 -11.852 1.00 18.40 C ANISOU 3410 CB THR B 241 2228 2402 2360 -97 -321 -66 C ATOM 3411 OG1 THR B 241 -12.526 -8.219 -12.238 1.00 19.56 O ANISOU 3411 OG1 THR B 241 2417 2541 2474 -96 -335 -26 O ATOM 3412 CG2 THR B 241 -13.488 -10.399 -12.668 1.00 18.54 C ANISOU 3412 CG2 THR B 241 2291 2439 2313 -130 -304 -63 C ATOM 3413 N ILE B 242 -16.431 -9.551 -10.525 1.00 18.33 N ANISOU 3413 N ILE B 242 2065 2383 2516 -79 -321 -164 N ATOM 3414 CA ILE B 242 -17.574 -10.377 -10.164 1.00 18.19 C ANISOU 3414 CA ILE B 242 1996 2372 2545 -90 -300 -207 C ATOM 3415 C ILE B 242 -18.884 -9.843 -10.758 1.00 20.95 C ANISOU 3415 C ILE B 242 2285 2692 2981 -84 -387 -224 C ATOM 3416 O ILE B 242 -19.670 -10.620 -11.323 1.00 22.35 O ANISOU 3416 O ILE B 242 2450 2870 3172 -106 -412 -236 O ATOM 3417 CB ILE B 242 -17.677 -10.493 -8.629 1.00 18.74 C ANISOU 3417 CB ILE B 242 2023 2456 2642 -79 -214 -248 C ATOM 3418 CG1 ILE B 242 -16.513 -11.344 -8.149 1.00 18.75 C ANISOU 3418 CG1 ILE B 242 2085 2481 2557 -92 -141 -229 C ATOM 3419 CG2 ILE B 242 -19.002 -11.083 -8.205 1.00 23.39 C ANISOU 3419 CG2 ILE B 242 2543 3047 3297 -92 -193 -297 C ATOM 3420 CD1 ILE B 242 -16.393 -11.409 -6.648 1.00 23.69 C ANISOU 3420 CD1 ILE B 242 2693 3121 3188 -85 -63 -258 C ATOM 3421 N ALA B 243 -19.095 -8.542 -10.723 1.00 22.20 N ANISOU 3421 N ALA B 243 2410 2823 3203 -56 -441 -223 N ATOM 3422 CA ALA B 243 -20.317 -7.926 -11.228 1.00 25.80 C ANISOU 3422 CA ALA B 243 2803 3243 3758 -44 -533 -241 C ATOM 3423 C ALA B 243 -20.383 -8.095 -12.736 1.00 26.50 C ANISOU 3423 C ALA B 243 2945 3317 3805 -67 -629 -195 C ATOM 3424 O ALA B 243 -21.445 -8.396 -13.275 1.00 30.45 O ANISOU 3424 O ALA B 243 3409 3803 4358 -76 -689 -212 O ATOM 3425 CB ALA B 243 -20.372 -6.455 -10.819 1.00 28.33 C ANISOU 3425 CB ALA B 243 3080 3529 4154 -5 -572 -248 C ATOM 3426 N ALA B 244 -19.252 -7.979 -13.419 1.00 24.37 N ANISOU 3426 N ALA B 244 2766 3055 3437 -81 -638 -140 N ATOM 3427 CA ALA B 244 -19.237 -8.043 -14.877 1.00 23.88 C ANISOU 3427 CA ALA B 244 2770 2982 3321 -109 -726 -95 C ATOM 3428 C ALA B 244 -19.405 -9.480 -15.400 1.00 25.37 C ANISOU 3428 C ALA B 244 2991 3198 3450 -145 -701 -105 C ATOM 3429 O ALA B 244 -19.685 -9.691 -16.589 1.00 27.88 O ANISOU 3429 O ALA B 244 3354 3508 3733 -172 -778 -82 O ATOM 3430 CB ALA B 244 -17.961 -7.457 -15.398 1.00 27.73 C ANISOU 3430 CB ALA B 244 3342 3472 3721 -119 -729 -39 C ATOM 3431 N ASN B 245 -19.234 -10.458 -14.513 1.00 22.94 N ANISOU 3431 N ASN B 245 2665 2921 3131 -148 -598 -140 N ATOM 3432 CA ASN B 245 -19.259 -11.864 -14.917 1.00 22.14 C ANISOU 3432 CA ASN B 245 2597 2841 2973 -182 -566 -150 C ATOM 3433 C ASN B 245 -20.284 -12.680 -14.162 1.00 25.85 C ANISOU 3433 C ASN B 245 2992 3315 3513 -185 -526 -203 C ATOM 3434 O ASN B 245 -20.060 -13.859 -13.873 1.00 30.01 O ANISOU 3434 O ASN B 245 3537 3863 4001 -205 -456 -218 O ATOM 3435 CB ASN B 245 -17.875 -12.472 -14.739 1.00 20.95 C ANISOU 3435 CB ASN B 245 2515 2719 2725 -192 -479 -133 C ATOM 3436 CG ASN B 245 -16.888 -11.972 -15.756 1.00 23.84 C ANISOU 3436 CG ASN B 245 2963 3086 3008 -205 -512 -85 C ATOM 3437 OD1 ASN B 245 -16.837 -12.470 -16.896 1.00 27.30 O ANISOU 3437 OD1 ASN B 245 3460 3529 3384 -237 -548 -71 O ATOM 3438 ND2 ASN B 245 -16.085 -10.995 -15.371 1.00 21.75 N ANISOU 3438 ND2 ASN B 245 2707 2818 2739 -185 -498 -61 N ATOM 3439 N SER B 246 -21.422 -12.075 -13.889 1.00 29.57 N ANISOU 3439 N SER B 246 3379 3763 4093 -167 -573 -232 N ATOM 3440 CA SER B 246 -22.454 -12.684 -13.060 1.00 40.84 C ANISOU 3440 CA SER B 246 4722 5194 5602 -172 -527 -287 C ATOM 3441 C SER B 246 -23.715 -12.936 -13.855 1.00 53.09 C ANISOU 3441 C SER B 246 6228 6722 7222 -186 -616 -307 C ATOM 3442 O SER B 246 -24.315 -14.004 -13.759 1.00 57.65 O ANISOU 3442 O SER B 246 6780 7308 7817 -213 -586 -337 O ATOM 3443 CB SER B 246 -22.815 -11.759 -11.906 1.00 44.97 C ANISOU 3443 CB SER B 246 5165 5708 6213 -138 -494 -321 C ATOM 3444 OG SER B 246 -21.984 -11.998 -10.787 1.00 42.74 O ANISOU 3444 OG SER B 246 4903 5453 5882 -135 -384 -325 O ATOM 3445 OXT SER B 246 -24.163 -12.053 -14.580 1.00 58.34 O ANISOU 3445 OXT SER B 246 6879 7356 7933 -172 -723 -293 O TER 3446 SER B 246 ATOM 3447 N ARG I 1 20.822 -31.315 -30.260 1.00 24.97 N ANISOU 3447 N ARG I 1 3502 3542 2443 575 479 -86 N ATOM 3448 CA ARG I 1 19.956 -30.765 -29.199 1.00 23.94 C ANISOU 3448 CA ARG I 1 3328 3375 2395 514 440 -89 C ATOM 3449 C ARG I 1 20.471 -29.388 -28.796 1.00 21.62 C ANISOU 3449 C ARG I 1 2969 3098 2147 468 488 -48 C ATOM 3450 O ARG I 1 21.681 -29.155 -28.776 1.00 23.02 O ANISOU 3450 O ARG I 1 3109 3320 2317 474 548 -26 O ATOM 3451 CB ARG I 1 19.822 -31.688 -27.963 1.00 28.48 C ANISOU 3451 CB ARG I 1 3874 3934 3013 503 410 -130 C ATOM 3452 CG ARG I 1 21.103 -31.813 -27.161 1.00 25.16 C ANISOU 3452 CG ARG I 1 3392 3553 2615 501 462 -130 C ATOM 3453 CD ARG I 1 20.980 -32.725 -25.898 1.00 21.48 C ANISOU 3453 CD ARG I 1 2899 3070 2191 487 429 -169 C ATOM 3454 NE ARG I 1 20.535 -34.070 -26.229 1.00 20.92 N ANISOU 3454 NE ARG I 1 2888 2981 2079 529 379 -207 N ATOM 3455 CZ ARG I 1 21.331 -35.039 -26.638 1.00 21.85 C ANISOU 3455 CZ ARG I 1 3032 3123 2146 583 394 -226 C ATOM 3456 NH1 ARG I 1 22.626 -34.847 -26.837 1.00 22.54 N ANISOU 3456 NH1 ARG I 1 3090 3258 2216 607 463 -207 N ATOM 3457 NH2 ARG I 1 20.810 -36.211 -26.935 1.00 21.50 N ANISOU 3457 NH2 ARG I 1 3050 3054 2065 618 338 -260 N ATOM 3458 N PRO I 2 19.532 -28.497 -28.491 1.00 20.01 N ANISOU 3458 N PRO I 2 2754 2858 1992 423 457 -36 N ATOM 3459 CA PRO I 2 19.929 -27.175 -27.971 1.00 21.12 C ANISOU 3459 CA PRO I 2 2837 3006 2183 375 491 -1 C ATOM 3460 C PRO I 2 20.771 -27.255 -26.712 1.00 22.16 C ANISOU 3460 C PRO I 2 2903 3154 2361 352 518 -8 C ATOM 3461 O PRO I 2 20.566 -28.129 -25.846 1.00 20.97 O ANISOU 3461 O PRO I 2 2743 2991 2233 353 494 -46 O ATOM 3462 CB PRO I 2 18.586 -26.526 -27.680 1.00 23.16 C ANISOU 3462 CB PRO I 2 3099 3213 2488 340 441 -2 C ATOM 3463 CG PRO I 2 17.627 -27.197 -28.642 1.00 24.75 C ANISOU 3463 CG PRO I 2 3369 3389 2645 372 391 -16 C ATOM 3464 CD PRO I 2 18.069 -28.605 -28.635 1.00 21.38 C ANISOU 3464 CD PRO I 2 2964 2980 2178 413 389 -51 C ATOM 3465 N ASP I 3 21.721 -26.326 -26.592 1.00 20.25 N ANISOU 3465 N ASP I 3 2618 2939 2136 328 565 31 N ATOM 3466 CA ASP I 3 22.569 -26.286 -25.406 1.00 21.23 C ANISOU 3466 CA ASP I 3 2682 3076 2307 301 587 31 C ATOM 3467 C ASP I 3 21.778 -26.062 -24.108 1.00 19.68 C ANISOU 3467 C ASP I 3 2466 2835 2178 258 549 6 C ATOM 3468 O ASP I 3 22.218 -26.462 -23.036 1.00 20.72 O ANISOU 3468 O ASP I 3 2564 2967 2342 242 551 -12 O ATOM 3469 CB ASP I 3 23.643 -25.197 -25.535 1.00 23.14 C ANISOU 3469 CB ASP I 3 2883 3349 2561 275 635 87 C ATOM 3470 CG ASP I 3 24.721 -25.528 -26.556 1.00 35.92 C ANISOU 3470 CG ASP I 3 4503 5025 4121 317 688 115 C ATOM 3471 OD1 ASP I 3 25.327 -24.559 -27.063 1.00 41.75 O ANISOU 3471 OD1 ASP I 3 5221 5787 4853 300 722 168 O ATOM 3472 OD2 ASP I 3 24.946 -26.730 -26.818 1.00 39.64 O ANISOU 3472 OD2 ASP I 3 4995 5515 4552 367 694 85 O ATOM 3473 N PHE I 4 20.627 -25.382 -24.171 1.00 19.04 N ANISOU 3473 N PHE I 4 2404 2714 2117 238 516 7 N ATOM 3474 CA PHE I 4 19.816 -25.180 -22.972 1.00 16.34 C ANISOU 3474 CA PHE I 4 2045 2331 1834 204 485 -17 C ATOM 3475 C PHE I 4 19.335 -26.476 -22.357 1.00 17.88 C ANISOU 3475 C PHE I 4 2247 2516 2031 219 455 -63 C ATOM 3476 O PHE I 4 18.975 -26.496 -21.189 1.00 19.39 O ANISOU 3476 O PHE I 4 2415 2683 2267 192 440 -84 O ATOM 3477 CB PHE I 4 18.682 -24.184 -23.224 1.00 18.27 C ANISOU 3477 CB PHE I 4 2305 2536 2100 186 459 -4 C ATOM 3478 CG PHE I 4 17.586 -24.655 -24.140 1.00 17.93 C ANISOU 3478 CG PHE I 4 2308 2475 2028 215 421 -14 C ATOM 3479 CD1 PHE I 4 16.698 -25.645 -23.747 1.00 17.97 C ANISOU 3479 CD1 PHE I 4 2326 2461 2043 226 381 -51 C ATOM 3480 CD2 PHE I 4 17.388 -24.061 -25.389 1.00 19.02 C ANISOU 3480 CD2 PHE I 4 2478 2614 2133 226 419 16 C ATOM 3481 CE1 PHE I 4 15.684 -26.013 -24.600 1.00 15.32 C ANISOU 3481 CE1 PHE I 4 2032 2104 1685 248 339 -54 C ATOM 3482 CE2 PHE I 4 16.324 -24.445 -26.216 1.00 17.85 C ANISOU 3482 CE2 PHE I 4 2378 2443 1963 248 376 9 C ATOM 3483 CZ PHE I 4 15.482 -25.418 -25.807 1.00 17.86 C ANISOU 3483 CZ PHE I 4 2388 2423 1976 258 334 -25 C ATOM 3484 N CYS I 5 19.357 -27.560 -23.138 1.00 17.93 N ANISOU 3484 N CYS I 5 2288 2539 1987 263 444 -80 N ATOM 3485 CA CYS I 5 19.015 -28.924 -22.688 1.00 17.40 C ANISOU 3485 CA CYS I 5 2234 2464 1915 281 411 -122 C ATOM 3486 C CYS I 5 19.975 -29.461 -21.627 1.00 17.70 C ANISOU 3486 C CYS I 5 2232 2519 1973 271 430 -138 C ATOM 3487 O CYS I 5 19.661 -30.430 -20.935 1.00 19.65 O ANISOU 3487 O CYS I 5 2481 2755 2231 271 400 -172 O ATOM 3488 CB CYS I 5 18.976 -29.917 -23.886 1.00 16.03 C ANISOU 3488 CB CYS I 5 2115 2303 1674 335 395 -133 C ATOM 3489 SG CYS I 5 17.711 -29.565 -25.130 1.00 19.75 S ANISOU 3489 SG CYS I 5 2644 2743 2116 347 354 -118 S ATOM 3490 N LEU I 6 21.159 -28.862 -21.552 1.00 19.76 N ANISOU 3490 N LEU I 6 2460 2809 2239 260 477 -110 N ATOM 3491 CA LEU I 6 22.225 -29.349 -20.662 1.00 19.60 C ANISOU 3491 CA LEU I 6 2402 2809 2238 252 496 -119 C ATOM 3492 C LEU I 6 22.245 -28.602 -19.330 1.00 21.47 C ANISOU 3492 C LEU I 6 2600 3021 2536 196 495 -115 C ATOM 3493 O LEU I 6 23.077 -28.900 -18.461 1.00 23.22 O ANISOU 3493 O LEU I 6 2790 3251 2780 180 504 -120 O ATOM 3494 CB LEU I 6 23.578 -29.180 -21.351 1.00 22.74 C ANISOU 3494 CB LEU I 6 2780 3254 2607 274 548 -85 C ATOM 3495 CG LEU I 6 23.696 -29.707 -22.785 1.00 27.86 C ANISOU 3495 CG LEU I 6 3471 3930 3186 333 562 -81 C ATOM 3496 CD1 LEU I 6 25.097 -29.455 -23.350 1.00 30.27 C ANISOU 3496 CD1 LEU I 6 3746 4286 3468 353 623 -41 C ATOM 3497 CD2 LEU I 6 23.340 -31.160 -22.860 1.00 27.62 C ANISOU 3497 CD2 LEU I 6 3477 3891 3124 374 528 -127 C ATOM 3498 N GLU I 7 21.328 -27.637 -19.159 1.00 18.34 N ANISOU 3498 N GLU I 7 2210 2592 2165 168 481 -107 N ATOM 3499 CA GLU I 7 21.273 -26.835 -17.940 1.00 19.67 C ANISOU 3499 CA GLU I 7 2354 2734 2388 120 480 -104 C ATOM 3500 C GLU I 7 20.417 -27.511 -16.898 1.00 20.19 C ANISOU 3500 C GLU I 7 2424 2771 2477 108 447 -145 C ATOM 3501 O GLU I 7 19.408 -28.170 -17.187 1.00 20.55 O ANISOU 3501 O GLU I 7 2493 2805 2510 129 417 -167 O ATOM 3502 CB GLU I 7 20.659 -25.458 -18.227 1.00 19.15 C ANISOU 3502 CB GLU I 7 2295 2643 2337 100 481 -78 C ATOM 3503 CG GLU I 7 21.372 -24.568 -19.194 1.00 23.46 C ANISOU 3503 CG GLU I 7 2838 3212 2866 101 509 -31 C ATOM 3504 CD GLU I 7 22.735 -24.128 -18.679 1.00 33.28 C ANISOU 3504 CD GLU I 7 4044 4474 4128 73 537 -2 C ATOM 3505 OE1 GLU I 7 23.675 -24.073 -19.480 1.00 41.66 O ANISOU 3505 OE1 GLU I 7 5093 5574 5163 87 567 32 O ATOM 3506 OE2 GLU I 7 22.872 -23.864 -17.473 1.00 35.02 O ANISOU 3506 OE2 GLU I 7 4248 4670 4388 37 528 -10 O ATOM 3507 N PRO I 8 20.779 -27.359 -15.622 1.00 20.18 N ANISOU 3507 N PRO I 8 2400 2755 2512 72 448 -153 N ATOM 3508 CA PRO I 8 19.937 -27.932 -14.577 1.00 18.39 C ANISOU 3508 CA PRO I 8 2179 2503 2307 58 420 -189 C ATOM 3509 C PRO I 8 18.575 -27.263 -14.503 1.00 16.34 C ANISOU 3509 C PRO I 8 1932 2210 2066 52 407 -191 C ATOM 3510 O PRO I 8 18.417 -26.086 -14.893 1.00 20.72 O ANISOU 3510 O PRO I 8 2490 2754 2630 46 420 -165 O ATOM 3511 CB PRO I 8 20.699 -27.648 -13.265 1.00 24.86 C ANISOU 3511 CB PRO I 8 2977 3311 3159 17 429 -190 C ATOM 3512 CG PRO I 8 21.795 -26.760 -13.610 1.00 28.72 C ANISOU 3512 CG PRO I 8 3449 3813 3650 6 456 -151 C ATOM 3513 CD PRO I 8 21.923 -26.601 -15.098 1.00 24.91 C ANISOU 3513 CD PRO I 8 2973 3359 3133 40 472 -126 C ATOM 3514 N PRO I 9 17.597 -28.006 -14.001 1.00 17.98 N ANISOU 3514 N PRO I 9 2146 2404 2283 54 380 -219 N ATOM 3515 CA PRO I 9 16.263 -27.414 -13.943 1.00 16.58 C ANISOU 3515 CA PRO I 9 1974 2198 2126 52 368 -217 C ATOM 3516 C PRO I 9 16.165 -26.261 -12.926 1.00 17.29 C ANISOU 3516 C PRO I 9 2057 2260 2253 21 388 -213 C ATOM 3517 O PRO I 9 16.870 -26.284 -11.920 1.00 19.62 O ANISOU 3517 O PRO I 9 2344 2551 2558 -4 397 -222 O ATOM 3518 CB PRO I 9 15.391 -28.579 -13.503 1.00 18.96 C ANISOU 3518 CB PRO I 9 2278 2496 2431 57 336 -244 C ATOM 3519 CG PRO I 9 16.310 -29.479 -12.801 1.00 18.43 C ANISOU 3519 CG PRO I 9 2204 2443 2356 47 335 -263 C ATOM 3520 CD PRO I 9 17.646 -29.341 -13.394 1.00 17.41 C ANISOU 3520 CD PRO I 9 2072 2339 2205 55 357 -248 C ATOM 3521 N TYR I 10 15.254 -25.343 -13.207 1.00 17.20 N ANISOU 3521 N TYR I 10 2051 2226 2258 26 388 -200 N ATOM 3522 CA TYR I 10 15.112 -24.085 -12.462 1.00 17.55 C ANISOU 3522 CA TYR I 10 2096 2239 2332 6 405 -194 C ATOM 3523 C TYR I 10 13.668 -23.939 -11.940 1.00 16.27 C ANISOU 3523 C TYR I 10 1933 2051 2197 13 398 -206 C ATOM 3524 O TYR I 10 12.727 -23.709 -12.691 1.00 16.15 O ANISOU 3524 O TYR I 10 1918 2029 2188 33 386 -195 O ATOM 3525 CB TYR I 10 15.512 -22.880 -13.332 1.00 16.55 C ANISOU 3525 CB TYR I 10 1978 2109 2203 6 416 -161 C ATOM 3526 CG TYR I 10 15.473 -21.560 -12.613 1.00 17.70 C ANISOU 3526 CG TYR I 10 2131 2218 2376 -15 428 -153 C ATOM 3527 CD1 TYR I 10 14.532 -20.620 -12.921 1.00 17.29 C ANISOU 3527 CD1 TYR I 10 2089 2139 2343 -3 425 -143 C ATOM 3528 CD2 TYR I 10 16.397 -21.278 -11.628 1.00 21.84 C ANISOU 3528 CD2 TYR I 10 2657 2733 2908 -45 438 -156 C ATOM 3529 CE1 TYR I 10 14.505 -19.400 -12.254 1.00 19.43 C ANISOU 3529 CE1 TYR I 10 2374 2373 2637 -19 433 -138 C ATOM 3530 CE2 TYR I 10 16.368 -20.053 -10.952 1.00 21.40 C ANISOU 3530 CE2 TYR I 10 2619 2637 2874 -64 443 -150 C ATOM 3531 CZ TYR I 10 15.428 -19.145 -11.291 1.00 21.23 C ANISOU 3531 CZ TYR I 10 2609 2590 2868 -48 441 -142 C ATOM 3532 OH TYR I 10 15.403 -17.907 -10.614 1.00 23.47 O ANISOU 3532 OH TYR I 10 2915 2829 3171 -63 443 -138 O ATOM 3533 N THR I 11 13.524 -24.019 -10.618 1.00 16.46 N ANISOU 3533 N THR I 11 1954 2060 2238 -5 407 -227 N ATOM 3534 CA THR I 11 12.236 -23.867 -9.952 1.00 16.01 C ANISOU 3534 CA THR I 11 1892 1982 2207 2 410 -238 C ATOM 3535 C THR I 11 11.752 -22.410 -9.986 1.00 16.18 C ANISOU 3535 C THR I 11 1924 1971 2252 9 425 -224 C ATOM 3536 O THR I 11 10.603 -22.128 -10.234 1.00 14.81 O ANISOU 3536 O THR I 11 1743 1786 2099 30 422 -217 O ATOM 3537 CB THR I 11 12.284 -24.361 -8.510 1.00 15.65 C ANISOU 3537 CB THR I 11 1847 1931 2168 -19 419 -263 C ATOM 3538 OG1 THR I 11 12.520 -25.796 -8.556 1.00 17.83 O ANISOU 3538 OG1 THR I 11 2113 2236 2426 -22 397 -275 O ATOM 3539 CG2 THR I 11 11.024 -24.090 -7.758 1.00 17.79 C ANISOU 3539 CG2 THR I 11 2113 2183 2464 -9 431 -271 C ATOM 3540 N GLY I 12 12.669 -21.475 -9.736 1.00 16.12 N ANISOU 3540 N GLY I 12 1934 1947 2242 -9 438 -217 N ATOM 3541 CA GLY I 12 12.313 -20.071 -9.662 1.00 16.18 C ANISOU 3541 CA GLY I 12 1959 1920 2270 -4 448 -206 C ATOM 3542 C GLY I 12 11.722 -19.667 -8.325 1.00 15.85 C ANISOU 3542 C GLY I 12 1929 1845 2246 -4 467 -228 C ATOM 3543 O GLY I 12 11.479 -20.485 -7.423 1.00 16.47 O ANISOU 3543 O GLY I 12 2002 1932 2323 -10 473 -250 O ATOM 3544 N PRO I 13 11.423 -18.358 -8.217 1.00 16.51 N ANISOU 3544 N PRO I 13 2034 1892 2347 4 475 -220 N ATOM 3545 CA PRO I 13 10.983 -17.777 -6.945 1.00 15.88 C ANISOU 3545 CA PRO I 13 1978 1776 2279 8 495 -242 C ATOM 3546 C PRO I 13 9.512 -17.864 -6.634 1.00 15.60 C ANISOU 3546 C PRO I 13 1926 1735 2266 42 512 -252 C ATOM 3547 O PRO I 13 9.128 -17.675 -5.468 1.00 15.14 O ANISOU 3547 O PRO I 13 1885 1657 2212 48 536 -273 O ATOM 3548 CB PRO I 13 11.375 -16.318 -7.110 1.00 17.20 C ANISOU 3548 CB PRO I 13 2179 1903 2452 4 491 -226 C ATOM 3549 CG PRO I 13 11.223 -16.021 -8.562 1.00 17.53 C ANISOU 3549 CG PRO I 13 2204 1958 2500 16 473 -197 C ATOM 3550 CD PRO I 13 11.647 -17.324 -9.234 1.00 16.88 C ANISOU 3550 CD PRO I 13 2090 1925 2397 8 463 -192 C ATOM 3551 N CYS I 14 8.668 -18.176 -7.611 1.00 15.19 N ANISOU 3551 N CYS I 14 1842 1702 2229 65 500 -235 N ATOM 3552 CA CYS I 14 7.256 -18.276 -7.333 1.00 16.19 C ANISOU 3552 CA CYS I 14 1943 1824 2383 97 515 -238 C ATOM 3553 C CYS I 14 6.907 -19.565 -6.626 1.00 14.06 C ANISOU 3553 C CYS I 14 1650 1583 2108 90 521 -252 C ATOM 3554 O CYS I 14 7.708 -20.504 -6.667 1.00 14.50 O ANISOU 3554 O CYS I 14 1704 1665 2139 64 506 -258 O ATOM 3555 CB CYS I 14 6.397 -18.050 -8.571 1.00 16.38 C ANISOU 3555 CB CYS I 14 1942 1849 2431 123 494 -211 C ATOM 3556 SG CYS I 14 6.467 -16.343 -9.208 1.00 17.69 S ANISOU 3556 SG CYS I 14 2137 1972 2612 137 489 -193 S ATOM 3557 N LYS I 15 5.760 -19.596 -5.963 1.00 15.78 N ANISOU 3557 N LYS I 15 1848 1797 2349 114 545 -256 N ATOM 3558 CA LYS I 15 5.450 -20.678 -5.035 1.00 14.15 C ANISOU 3558 CA LYS I 15 1625 1615 2138 104 557 -270 C ATOM 3559 C LYS I 15 4.368 -21.635 -5.456 1.00 14.17 C ANISOU 3559 C LYS I 15 1576 1645 2162 115 541 -250 C ATOM 3560 O LYS I 15 3.696 -22.274 -4.631 1.00 14.55 O ANISOU 3560 O LYS I 15 1602 1708 2217 116 558 -254 O ATOM 3561 CB LYS I 15 5.224 -20.058 -3.674 1.00 15.58 C ANISOU 3561 CB LYS I 15 1832 1770 2317 114 601 -291 C ATOM 3562 CG LYS I 15 6.505 -19.541 -3.043 1.00 16.27 C ANISOU 3562 CG LYS I 15 1975 1833 2374 87 605 -312 C ATOM 3563 CD LYS I 15 6.259 -18.929 -1.733 1.00 16.64 C ANISOU 3563 CD LYS I 15 2058 1850 2415 98 644 -334 C ATOM 3564 CE LYS I 15 7.553 -18.464 -1.164 1.00 17.01 C ANISOU 3564 CE LYS I 15 2162 1869 2432 66 636 -351 C ATOM 3565 NZ LYS I 15 7.402 -17.781 0.157 1.00 16.42 N ANISOU 3565 NZ LYS I 15 2140 1757 2344 77 670 -375 N ATOM 3566 N ALA I 16 4.190 -21.801 -6.779 1.00 14.32 N ANISOU 3566 N ALA I 16 1578 1673 2191 121 504 -227 N ATOM 3567 CA ALA I 16 3.316 -22.924 -7.202 1.00 14.65 C ANISOU 3567 CA ALA I 16 1577 1742 2248 123 475 -207 C ATOM 3568 C ALA I 16 4.113 -24.210 -7.109 1.00 13.91 C ANISOU 3568 C ALA I 16 1490 1675 2121 92 450 -220 C ATOM 3569 O ALA I 16 5.314 -24.233 -6.862 1.00 14.78 O ANISOU 3569 O ALA I 16 1631 1785 2199 70 453 -241 O ATOM 3570 CB ALA I 16 2.852 -22.697 -8.644 1.00 15.99 C ANISOU 3570 CB ALA I 16 1734 1906 2436 140 438 -178 C ATOM 3571 N ARG I 17 3.396 -25.336 -7.257 1.00 13.71 N ANISOU 3571 N ARG I 17 1432 1671 2105 87 420 -206 N ATOM 3572 CA ARG I 17 4.033 -26.640 -7.418 1.00 13.67 C ANISOU 3572 CA ARG I 17 1435 1690 2071 62 383 -215 C ATOM 3573 C ARG I 17 3.511 -27.254 -8.723 1.00 14.54 C ANISOU 3573 C ARG I 17 1531 1806 2187 71 328 -188 C ATOM 3574 O ARG I 17 2.563 -28.011 -8.739 1.00 15.12 O ANISOU 3574 O ARG I 17 1574 1889 2282 70 301 -168 O ATOM 3575 CB ARG I 17 3.783 -27.547 -6.240 1.00 14.47 C ANISOU 3575 CB ARG I 17 1521 1807 2172 42 391 -225 C ATOM 3576 CG ARG I 17 4.666 -28.859 -6.176 1.00 18.42 C ANISOU 3576 CG ARG I 17 2036 2327 2637 13 355 -241 C ATOM 3577 CD ARG I 17 4.216 -30.035 -7.055 1.00 22.64 C ANISOU 3577 CD ARG I 17 2555 2875 3171 11 293 -222 C ATOM 3578 NE ARG I 17 2.877 -30.487 -6.740 1.00 20.28 N ANISOU 3578 NE ARG I 17 2216 2584 2907 11 282 -195 N ATOM 3579 CZ ARG I 17 2.561 -31.476 -5.884 1.00 22.48 C ANISOU 3579 CZ ARG I 17 2476 2879 3186 -12 271 -195 C ATOM 3580 NH1 ARG I 17 3.504 -32.181 -5.275 1.00 27.87 N ANISOU 3580 NH1 ARG I 17 3183 3570 3836 -38 265 -222 N ATOM 3581 NH2 ARG I 17 1.302 -31.775 -5.683 1.00 21.43 N ANISOU 3581 NH2 ARG I 17 2300 2754 3090 -11 263 -162 N ATOM 3582 N ILE I 18 4.115 -26.818 -9.795 1.00 15.15 N ANISOU 3582 N ILE I 18 1633 1876 2247 79 314 -186 N ATOM 3583 CA ILE I 18 3.715 -27.243 -11.145 1.00 15.36 C ANISOU 3583 CA ILE I 18 1661 1903 2272 90 262 -162 C ATOM 3584 C ILE I 18 4.746 -28.269 -11.591 1.00 15.78 C ANISOU 3584 C ILE I 18 1743 1974 2278 78 231 -178 C ATOM 3585 O ILE I 18 5.938 -28.040 -11.551 1.00 16.41 O ANISOU 3585 O ILE I 18 1848 2058 2327 72 252 -198 O ATOM 3586 CB ILE I 18 3.665 -26.051 -12.121 1.00 16.04 C ANISOU 3586 CB ILE I 18 1759 1968 2366 110 265 -145 C ATOM 3587 CG1 ILE I 18 2.660 -25.002 -11.671 1.00 17.40 C ANISOU 3587 CG1 ILE I 18 1904 2121 2586 127 296 -131 C ATOM 3588 CG2 ILE I 18 3.347 -26.504 -13.557 1.00 16.54 C ANISOU 3588 CG2 ILE I 18 1835 2030 2420 119 209 -122 C ATOM 3589 CD1 ILE I 18 2.934 -23.595 -12.257 1.00 21.05 C ANISOU 3589 CD1 ILE I 18 2387 2558 3052 142 313 -125 C ATOM 3590 N ILE I 19 4.250 -29.414 -12.025 1.00 14.90 N ANISOU 3590 N ILE I 19 1628 1870 2163 75 179 -167 N ATOM 3591 CA ILE I 19 5.153 -30.490 -12.429 1.00 14.50 C ANISOU 3591 CA ILE I 19 1607 1834 2067 69 146 -185 C ATOM 3592 C ILE I 19 5.513 -30.330 -13.911 1.00 17.17 C ANISOU 3592 C ILE I 19 1980 2167 2376 90 121 -175 C ATOM 3593 O ILE I 19 4.646 -30.339 -14.793 1.00 21.26 O ANISOU 3593 O ILE I 19 2500 2672 2906 102 82 -149 O ATOM 3594 CB ILE I 19 4.533 -31.883 -12.148 1.00 15.38 C ANISOU 3594 CB ILE I 19 1708 1954 2184 56 96 -180 C ATOM 3595 CG1 ILE I 19 4.244 -32.055 -10.641 1.00 16.13 C ANISOU 3595 CG1 ILE I 19 1770 2056 2301 33 126 -189 C ATOM 3596 CG2 ILE I 19 5.500 -32.969 -12.654 1.00 17.16 C ANISOU 3596 CG2 ILE I 19 1972 2189 2359 56 59 -201 C ATOM 3597 CD1 ILE I 19 3.318 -33.212 -10.264 1.00 21.01 C ANISOU 3597 CD1 ILE I 19 2363 2680 2938 17 80 -171 C ATOM 3598 N ARG I 20 6.790 -30.072 -14.138 1.00 15.17 N ANISOU 3598 N ARG I 20 1753 1924 2086 93 146 -193 N ATOM 3599 CA ARG I 20 7.303 -29.850 -15.477 1.00 16.03 C ANISOU 3599 CA ARG I 20 1896 2033 2160 113 134 -184 C ATOM 3600 C ARG I 20 8.381 -30.891 -15.718 1.00 15.65 C ANISOU 3600 C ARG I 20 1877 2006 2064 117 121 -206 C ATOM 3601 O ARG I 20 8.802 -31.629 -14.808 1.00 14.77 O ANISOU 3601 O ARG I 20 1757 1906 1950 103 124 -228 O ATOM 3602 CB ARG I 20 7.890 -28.442 -15.647 1.00 14.93 C ANISOU 3602 CB ARG I 20 1760 1890 2023 115 182 -178 C ATOM 3603 CG ARG I 20 6.848 -27.319 -15.570 1.00 13.57 C ANISOU 3603 CG ARG I 20 1566 1694 1897 118 193 -157 C ATOM 3604 CD ARG I 20 5.992 -27.284 -16.837 1.00 16.90 C ANISOU 3604 CD ARG I 20 2000 2100 2321 135 148 -129 C ATOM 3605 NE ARG I 20 4.937 -26.260 -16.751 1.00 17.23 N ANISOU 3605 NE ARG I 20 2017 2117 2413 139 155 -106 N ATOM 3606 CZ ARG I 20 5.114 -24.980 -17.004 1.00 16.82 C ANISOU 3606 CZ ARG I 20 1970 2051 2371 144 182 -97 C ATOM 3607 NH1 ARG I 20 6.302 -24.525 -17.336 1.00 18.03 N ANISOU 3607 NH1 ARG I 20 2149 2214 2488 141 206 -104 N ATOM 3608 NH2 ARG I 20 4.100 -24.114 -16.859 1.00 19.61 N ANISOU 3608 NH2 ARG I 20 2298 2380 2772 152 186 -78 N ATOM 3609 N TYR I 21 8.824 -30.983 -16.962 1.00 15.15 N ANISOU 3609 N TYR I 21 1850 1947 1960 140 106 -200 N ATOM 3610 CA TYR I 21 9.850 -31.926 -17.345 1.00 13.19 C ANISOU 3610 CA TYR I 21 1633 1718 1662 154 97 -220 C ATOM 3611 C TYR I 21 11.125 -31.171 -17.748 1.00 15.98 C ANISOU 3611 C TYR I 21 1994 2089 1987 163 147 -219 C ATOM 3612 O TYR I 21 11.053 -30.078 -18.315 1.00 15.49 O ANISOU 3612 O TYR I 21 1935 2022 1930 167 168 -198 O ATOM 3613 CB TYR I 21 9.385 -32.760 -18.534 1.00 15.32 C ANISOU 3613 CB TYR I 21 1945 1979 1898 179 37 -212 C ATOM 3614 CG TYR I 21 8.323 -33.795 -18.184 1.00 16.83 C ANISOU 3614 CG TYR I 21 2132 2154 2109 168 -24 -211 C ATOM 3615 CD1 TYR I 21 7.003 -33.418 -18.036 1.00 20.03 C ANISOU 3615 CD1 TYR I 21 2510 2538 2562 154 -46 -186 C ATOM 3616 CD2 TYR I 21 8.677 -35.098 -17.979 1.00 18.04 C ANISOU 3616 CD2 TYR I 21 2304 2313 2236 171 -58 -233 C ATOM 3617 CE1 TYR I 21 6.041 -34.371 -17.694 1.00 19.93 C ANISOU 3617 CE1 TYR I 21 2487 2514 2571 141 -103 -178 C ATOM 3618 CE2 TYR I 21 7.740 -36.036 -17.643 1.00 20.48 C ANISOU 3618 CE2 TYR I 21 2609 2609 2565 157 -118 -228 C ATOM 3619 CZ TYR I 21 6.437 -35.655 -17.503 1.00 22.39 C ANISOU 3619 CZ TYR I 21 2820 2831 2854 140 -139 -199 C ATOM 3620 OH TYR I 21 5.523 -36.645 -17.194 1.00 26.17 O ANISOU 3620 OH TYR I 21 3292 3298 3353 124 -202 -187 O ATOM 3621 N PHE I 22 12.268 -31.754 -17.438 1.00 14.83 N ANISOU 3621 N PHE I 22 1852 1966 1817 166 164 -239 N ATOM 3622 CA PHE I 22 13.530 -31.278 -17.912 1.00 14.28 C ANISOU 3622 CA PHE I 22 1789 1919 1718 178 206 -234 C ATOM 3623 C PHE I 22 14.342 -32.399 -18.471 1.00 15.42 C ANISOU 3623 C PHE I 22 1962 2085 1813 207 194 -250 C ATOM 3624 O PHE I 22 14.172 -33.539 -18.062 1.00 14.64 O ANISOU 3624 O PHE I 22 1869 1983 1710 209 159 -272 O ATOM 3625 CB PHE I 22 14.310 -30.595 -16.798 1.00 14.05 C ANISOU 3625 CB PHE I 22 1725 1897 1718 149 252 -237 C ATOM 3626 CG PHE I 22 14.959 -31.521 -15.794 1.00 14.92 C ANISOU 3626 CG PHE I 22 1822 2018 1830 136 250 -264 C ATOM 3627 CD1 PHE I 22 16.327 -31.850 -15.875 1.00 15.73 C ANISOU 3627 CD1 PHE I 22 1923 2145 1907 146 273 -269 C ATOM 3628 CD2 PHE I 22 14.214 -32.108 -14.762 1.00 14.34 C ANISOU 3628 CD2 PHE I 22 1736 1929 1784 115 225 -281 C ATOM 3629 CE1 PHE I 22 16.924 -32.743 -14.974 1.00 17.74 C ANISOU 3629 CE1 PHE I 22 2166 2407 2166 135 266 -293 C ATOM 3630 CE2 PHE I 22 14.850 -32.989 -13.811 1.00 15.92 C ANISOU 3630 CE2 PHE I 22 1927 2138 1986 101 220 -305 C ATOM 3631 CZ PHE I 22 16.189 -33.315 -13.971 1.00 17.99 C ANISOU 3631 CZ PHE I 22 2191 2422 2223 112 237 -311 C ATOM 3632 N TYR I 23 15.234 -32.083 -19.397 1.00 13.63 N ANISOU 3632 N TYR I 23 1751 1879 1547 232 224 -238 N ATOM 3633 CA TYR I 23 16.092 -33.124 -19.953 1.00 13.81 C ANISOU 3633 CA TYR I 23 1803 1925 1520 268 221 -254 C ATOM 3634 C TYR I 23 17.276 -33.284 -19.050 1.00 16.25 C ANISOU 3634 C TYR I 23 2077 2256 1842 256 256 -265 C ATOM 3635 O TYR I 23 17.981 -32.326 -18.743 1.00 17.43 O ANISOU 3635 O TYR I 23 2195 2418 2009 237 302 -247 O ATOM 3636 CB TYR I 23 16.561 -32.739 -21.388 1.00 15.59 C ANISOU 3636 CB TYR I 23 2062 2168 1694 305 243 -233 C ATOM 3637 CG TYR I 23 17.269 -33.859 -22.114 1.00 17.24 C ANISOU 3637 CG TYR I 23 2310 2396 1842 353 237 -250 C ATOM 3638 CD1 TYR I 23 18.609 -33.741 -22.395 1.00 16.89 C ANISOU 3638 CD1 TYR I 23 2255 2390 1771 375 292 -242 C ATOM 3639 CD2 TYR I 23 16.566 -34.965 -22.556 1.00 18.54 C ANISOU 3639 CD2 TYR I 23 2525 2540 1978 378 177 -270 C ATOM 3640 CE1 TYR I 23 19.255 -34.712 -23.103 1.00 19.21 C ANISOU 3640 CE1 TYR I 23 2587 2703 2009 427 293 -257 C ATOM 3641 CE2 TYR I 23 17.222 -35.994 -23.246 1.00 18.99 C ANISOU 3641 CE2 TYR I 23 2628 2612 1975 428 170 -288 C ATOM 3642 CZ TYR I 23 18.544 -35.819 -23.480 1.00 19.27 C ANISOU 3642 CZ TYR I 23 2650 2688 1986 453 232 -283 C ATOM 3643 OH TYR I 23 19.167 -36.827 -24.197 1.00 26.34 O ANISOU 3643 OH TYR I 23 3592 3597 2820 510 229 -302 O ATOM 3644 N ASN I 24 17.519 -34.544 -18.656 1.00 17.55 N ANISOU 3644 N ASN I 24 2251 2424 1995 268 229 -294 N ATOM 3645 CA ASN I 24 18.716 -34.953 -17.937 1.00 20.58 C ANISOU 3645 CA ASN I 24 2608 2829 2384 264 254 -306 C ATOM 3646 C ASN I 24 19.657 -35.627 -18.920 1.00 19.71 C ANISOU 3646 C ASN I 24 2524 2746 2219 318 267 -310 C ATOM 3647 O ASN I 24 19.457 -36.744 -19.320 1.00 23.53 O ANISOU 3647 O ASN I 24 3046 3224 2669 350 228 -333 O ATOM 3648 CB ASN I 24 18.301 -35.921 -16.839 1.00 19.97 C ANISOU 3648 CB ASN I 24 2524 2733 2331 242 211 -335 C ATOM 3649 CG ASN I 24 19.468 -36.371 -16.022 1.00 27.89 C ANISOU 3649 CG ASN I 24 3501 3753 3345 234 228 -348 C ATOM 3650 OD1 ASN I 24 20.592 -36.419 -16.533 1.00 29.11 O ANISOU 3650 OD1 ASN I 24 3651 3934 3474 263 261 -342 O ATOM 3651 ND2 ASN I 24 19.218 -36.751 -14.763 1.00 28.32 N ANISOU 3651 ND2 ASN I 24 3536 3790 3433 196 206 -365 N ATOM 3652 N ALA I 25 20.636 -34.882 -19.383 1.00 21.82 N ANISOU 3652 N ALA I 25 2774 3042 2476 328 323 -285 N ATOM 3653 CA ALA I 25 21.421 -35.290 -20.537 1.00 26.95 C ANISOU 3653 CA ALA I 25 3451 3722 3067 385 346 -281 C ATOM 3654 C ALA I 25 22.169 -36.639 -20.332 1.00 31.85 C ANISOU 3654 C ALA I 25 4079 4355 3666 420 335 -311 C ATOM 3655 O ALA I 25 22.130 -37.529 -21.196 1.00 33.41 O ANISOU 3655 O ALA I 25 4329 4555 3811 473 315 -329 O ATOM 3656 CB ALA I 25 22.380 -34.168 -20.918 1.00 31.85 C ANISOU 3656 CB ALA I 25 4038 4374 3688 382 412 -240 C ATOM 3657 N LYS I 26 22.780 -36.835 -19.174 1.00 28.87 N ANISOU 3657 N LYS I 26 3657 3981 3331 391 340 -319 N ATOM 3658 CA LYS I 26 23.509 -38.105 -18.902 1.00 28.09 C ANISOU 3658 CA LYS I 26 3563 3891 3219 422 325 -348 C ATOM 3659 C LYS I 26 22.572 -39.308 -18.844 1.00 26.23 C ANISOU 3659 C LYS I 26 3377 3624 2967 434 253 -386 C ATOM 3660 O LYS I 26 22.907 -40.457 -19.241 1.00 27.05 O ANISOU 3660 O LYS I 26 3516 3730 3031 483 230 -411 O ATOM 3661 CB LYS I 26 24.248 -37.997 -17.573 1.00 35.36 C ANISOU 3661 CB LYS I 26 4425 4814 4195 378 337 -347 C ATOM 3662 CG LYS I 26 25.566 -37.235 -17.670 1.00 47.99 C ANISOU 3662 CG LYS I 26 5976 6450 5807 379 403 -311 C ATOM 3663 CD LYS I 26 26.641 -38.077 -18.357 1.00 56.80 C ANISOU 3663 CD LYS I 26 7096 7601 6884 445 427 -315 C ATOM 3664 CE LYS I 26 27.586 -37.222 -19.212 1.00 64.09 C ANISOU 3664 CE LYS I 26 7991 8567 7791 468 498 -269 C ATOM 3665 NZ LYS I 26 28.514 -38.058 -20.052 1.00 67.41 N ANISOU 3665 NZ LYS I 26 8424 9026 8165 544 529 -273 N ATOM 3666 N ALA I 27 21.409 -39.075 -18.281 1.00 23.35 N ANISOU 3666 N ALA I 27 3012 3227 2632 389 214 -388 N ATOM 3667 CA ALA I 27 20.410 -40.123 -18.159 1.00 24.81 C ANISOU 3667 CA ALA I 27 3237 3380 2809 390 141 -415 C ATOM 3668 C ALA I 27 19.686 -40.413 -19.470 1.00 29.78 C ANISOU 3668 C ALA I 27 3932 3998 3386 432 109 -415 C ATOM 3669 O ALA I 27 19.019 -41.459 -19.562 1.00 36.96 O ANISOU 3669 O ALA I 27 4885 4881 4278 443 41 -437 O ATOM 3670 CB ALA I 27 19.444 -39.767 -17.053 1.00 31.73 C ANISOU 3670 CB ALA I 27 4085 4231 3739 327 116 -413 C ATOM 3671 N GLY I 28 19.807 -39.504 -20.444 1.00 25.95 N ANISOU 3671 N GLY I 28 3455 3528 2876 451 151 -389 N ATOM 3672 CA GLY I 28 19.168 -39.592 -21.748 1.00 26.71 C ANISOU 3672 CA GLY I 28 3616 3612 2921 488 126 -384 C ATOM 3673 C GLY I 28 17.683 -39.666 -21.641 1.00 29.04 C ANISOU 3673 C GLY I 28 3931 3867 3237 457 60 -382 C ATOM 3674 O GLY I 28 16.984 -40.323 -22.453 1.00 30.67 O ANISOU 3674 O GLY I 28 4201 4048 3404 484 3 -389 O ATOM 3675 N LEU I 29 17.163 -38.969 -20.632 1.00 25.75 N ANISOU 3675 N LEU I 29 3460 3442 2883 400 66 -370 N ATOM 3676 CA LEU I 29 15.757 -38.931 -20.523 1.00 25.53 C ANISOU 3676 CA LEU I 29 3440 3381 2881 372 12 -362 C ATOM 3677 C LEU I 29 15.269 -37.636 -19.886 1.00 15.69 C ANISOU 3677 C LEU I 29 2139 2131 1690 324 46 -337 C ATOM 3678 O LEU I 29 16.011 -36.925 -19.219 1.00 19.09 O ANISOU 3678 O LEU I 29 2524 2581 2147 304 101 -333 O ATOM 3679 CB LEU I 29 15.243 -40.175 -19.805 1.00 31.16 C ANISOU 3679 CB LEU I 29 4162 4071 3606 358 -55 -385 C ATOM 3680 CG LEU I 29 14.998 -40.297 -18.304 1.00 34.24 C ANISOU 3680 CG LEU I 29 4499 4457 4054 306 -62 -392 C ATOM 3681 CD1 LEU I 29 14.961 -41.795 -17.969 1.00 35.22 C ANISOU 3681 CD1 LEU I 29 4651 4567 4165 313 -127 -419 C ATOM 3682 CD2 LEU I 29 15.963 -39.612 -17.415 1.00 32.34 C ANISOU 3682 CD2 LEU I 29 4205 4241 3843 284 5 -393 C ATOM 3683 N CYS I 30 13.974 -37.488 -20.075 1.00 18.37 N ANISOU 3683 N CYS I 30 2488 2443 2049 308 3 -323 N ATOM 3684 CA CYS I 30 13.223 -36.403 -19.476 1.00 16.78 C ANISOU 3684 CA CYS I 30 2242 2231 1903 268 21 -301 C ATOM 3685 C CYS I 30 12.725 -36.847 -18.126 1.00 17.62 C ANISOU 3685 C CYS I 30 2312 2328 2056 230 1 -312 C ATOM 3686 O CYS I 30 12.163 -37.962 -17.961 1.00 22.01 O ANISOU 3686 O CYS I 30 2885 2869 2609 228 -60 -323 O ATOM 3687 CB CYS I 30 12.102 -35.935 -20.370 1.00 19.13 C ANISOU 3687 CB CYS I 30 2563 2505 2202 272 -11 -275 C ATOM 3688 SG CYS I 30 12.869 -35.210 -21.918 1.00 26.16 S ANISOU 3688 SG CYS I 30 3496 3412 3033 313 28 -259 S ATOM 3689 N GLN I 31 12.925 -35.975 -17.164 1.00 13.65 N ANISOU 3689 N GLN I 31 1761 1832 1593 199 49 -308 N ATOM 3690 CA GLN I 31 12.602 -36.167 -15.766 1.00 14.63 C ANISOU 3690 CA GLN I 31 1848 1951 1760 161 47 -318 C ATOM 3691 C GLN I 31 11.687 -35.079 -15.257 1.00 15.24 C ANISOU 3691 C GLN I 31 1892 2015 1885 134 68 -297 C ATOM 3692 O GLN I 31 11.698 -33.933 -15.806 1.00 16.38 O ANISOU 3692 O GLN I 31 2033 2157 2032 141 101 -279 O ATOM 3693 CB GLN I 31 13.891 -36.174 -14.971 1.00 13.69 C ANISOU 3693 CB GLN I 31 1711 1851 1641 150 88 -336 C ATOM 3694 CG GLN I 31 13.772 -36.535 -13.458 1.00 19.97 C ANISOU 3694 CG GLN I 31 2476 2641 2471 110 84 -351 C ATOM 3695 CD GLN I 31 13.055 -37.854 -13.241 1.00 18.42 C ANISOU 3695 CD GLN I 31 2293 2433 2272 106 19 -362 C ATOM 3696 OE1 GLN I 31 11.797 -37.885 -13.184 1.00 15.98 O ANISOU 3696 OE1 GLN I 31 1977 2109 1985 93 -12 -346 O ATOM 3697 NE2 GLN I 31 13.843 -38.944 -13.198 1.00 21.12 N ANISOU 3697 NE2 GLN I 31 2654 2783 2588 118 -6 -385 N ATOM 3698 N THR I 32 10.916 -35.376 -14.214 1.00 13.39 N ANISOU 3698 N THR I 32 1631 1770 1686 105 52 -300 N ATOM 3699 CA THR I 32 10.016 -34.368 -13.654 1.00 14.34 C ANISOU 3699 CA THR I 32 1718 1878 1851 85 77 -281 C ATOM 3700 C THR I 32 10.749 -33.523 -12.614 1.00 16.23 C ANISOU 3700 C THR I 32 1935 2123 2108 64 136 -291 C ATOM 3701 O THR I 32 11.720 -33.952 -11.972 1.00 15.22 O ANISOU 3701 O THR I 32 1807 2006 1969 53 147 -312 O ATOM 3702 CB THR I 32 8.791 -34.993 -12.998 1.00 16.23 C ANISOU 3702 CB THR I 32 1937 2107 2123 66 39 -273 C ATOM 3703 OG1 THR I 32 9.239 -35.965 -12.054 1.00 16.22 O ANISOU 3703 OG1 THR I 32 1932 2114 2116 46 27 -296 O ATOM 3704 CG2 THR I 32 7.910 -35.671 -14.055 1.00 17.64 C ANISOU 3704 CG2 THR I 32 2137 2273 2293 82 -27 -255 C ATOM 3705 N PHE I 33 10.266 -32.292 -12.444 1.00 14.84 N ANISOU 3705 N PHE I 33 1742 1936 1962 59 170 -276 N ATOM 3706 CA PHE I 33 10.758 -31.405 -11.385 1.00 14.50 C ANISOU 3706 CA PHE I 33 1682 1889 1937 38 220 -283 C ATOM 3707 C PHE I 33 9.644 -30.436 -11.056 1.00 14.63 C ANISOU 3707 C PHE I 33 1680 1887 1991 36 238 -267 C ATOM 3708 O PHE I 33 8.677 -30.274 -11.790 1.00 14.14 O ANISOU 3708 O PHE I 33 1614 1817 1943 52 217 -247 O ATOM 3709 CB PHE I 33 12.040 -30.614 -11.796 1.00 14.88 C ANISOU 3709 CB PHE I 33 1743 1945 1966 43 254 -282 C ATOM 3710 CG PHE I 33 11.818 -29.460 -12.749 1.00 15.55 C ANISOU 3710 CG PHE I 33 1834 2021 2054 59 269 -257 C ATOM 3711 CD1 PHE I 33 11.859 -28.148 -12.263 1.00 16.25 C ANISOU 3711 CD1 PHE I 33 1914 2093 2166 47 306 -249 C ATOM 3712 CD2 PHE I 33 11.599 -29.643 -14.105 1.00 14.96 C ANISOU 3712 CD2 PHE I 33 1777 1951 1955 86 245 -243 C ATOM 3713 CE1 PHE I 33 11.722 -27.087 -13.135 1.00 15.33 C ANISOU 3713 CE1 PHE I 33 1806 1968 2052 60 316 -226 C ATOM 3714 CE2 PHE I 33 11.439 -28.580 -14.950 1.00 15.63 C ANISOU 3714 CE2 PHE I 33 1870 2028 2042 97 257 -220 C ATOM 3715 CZ PHE I 33 11.522 -27.311 -14.455 1.00 15.43 C ANISOU 3715 CZ PHE I 33 1832 1987 2042 83 292 -211 C ATOM 3716 N VAL I 34 9.805 -29.766 -9.924 1.00 15.40 N ANISOU 3716 N VAL I 34 1768 1976 2108 17 276 -276 N ATOM 3717 CA VAL I 34 8.866 -28.740 -9.458 1.00 15.18 C ANISOU 3717 CA VAL I 34 1725 1929 2115 20 303 -265 C ATOM 3718 C VAL I 34 9.228 -27.347 -9.989 1.00 14.95 C ANISOU 3718 C VAL I 34 1708 1884 2088 31 331 -253 C ATOM 3719 O VAL I 34 10.319 -26.813 -9.728 1.00 15.90 O ANISOU 3719 O VAL I 34 1843 2003 2196 18 354 -261 O ATOM 3720 CB VAL I 34 8.859 -28.695 -7.923 1.00 15.20 C ANISOU 3720 CB VAL I 34 1721 1925 2129 -3 332 -283 C ATOM 3721 CG1 VAL I 34 7.991 -27.549 -7.447 1.00 16.67 C ANISOU 3721 CG1 VAL I 34 1898 2089 2346 7 366 -274 C ATOM 3722 CG2 VAL I 34 8.280 -29.981 -7.368 1.00 16.87 C ANISOU 3722 CG2 VAL I 34 1917 2150 2343 -15 304 -288 C ATOM 3723 N TYR I 35 8.321 -26.771 -10.767 1.00 14.85 N ANISOU 3723 N TYR I 35 1688 1860 2094 51 323 -231 N ATOM 3724 CA TYR I 35 8.436 -25.419 -11.272 1.00 15.79 C ANISOU 3724 CA TYR I 35 1817 1961 2221 61 343 -217 C ATOM 3725 C TYR I 35 7.496 -24.525 -10.463 1.00 13.91 C ANISOU 3725 C TYR I 35 1565 1698 2021 67 370 -215 C ATOM 3726 O TYR I 35 6.320 -24.851 -10.206 1.00 15.35 O ANISOU 3726 O TYR I 35 1722 1880 2231 77 362 -207 O ATOM 3727 CB TYR I 35 8.027 -25.366 -12.743 1.00 16.09 C ANISOU 3727 CB TYR I 35 1860 1999 2253 82 312 -192 C ATOM 3728 CG TYR I 35 7.971 -23.968 -13.346 1.00 13.91 C ANISOU 3728 CG TYR I 35 1594 1702 1989 92 326 -173 C ATOM 3729 CD1 TYR I 35 9.055 -23.081 -13.237 1.00 14.99 C ANISOU 3729 CD1 TYR I 35 1748 1834 2112 81 353 -174 C ATOM 3730 CD2 TYR I 35 6.836 -23.542 -13.997 1.00 16.00 C ANISOU 3730 CD2 TYR I 35 1849 1949 2281 111 307 -151 C ATOM 3731 CE1 TYR I 35 8.973 -21.811 -13.780 1.00 14.44 C ANISOU 3731 CE1 TYR I 35 1688 1743 2054 87 360 -155 C ATOM 3732 CE2 TYR I 35 6.774 -22.300 -14.570 1.00 15.25 C ANISOU 3732 CE2 TYR I 35 1764 1833 2196 119 314 -133 C ATOM 3733 CZ TYR I 35 7.847 -21.441 -14.468 1.00 15.86 C ANISOU 3733 CZ TYR I 35 1862 1906 2258 107 340 -135 C ATOM 3734 OH TYR I 35 7.760 -20.191 -15.037 1.00 17.31 O ANISOU 3734 OH TYR I 35 2057 2066 2453 113 342 -115 O ATOM 3735 N GLY I 36 8.019 -23.385 -10.013 1.00 13.82 N ANISOU 3735 N GLY I 36 1570 1667 2013 62 401 -219 N ATOM 3736 CA GLY I 36 7.292 -22.470 -9.131 1.00 14.07 C ANISOU 3736 CA GLY I 36 1598 1671 2074 72 431 -223 C ATOM 3737 C GLY I 36 6.250 -21.589 -9.826 1.00 13.78 C ANISOU 3737 C GLY I 36 1551 1615 2070 101 428 -200 C ATOM 3738 O GLY I 36 5.466 -20.888 -9.159 1.00 14.45 O ANISOU 3738 O GLY I 36 1629 1678 2184 117 453 -202 O ATOM 3739 N GLY I 37 6.266 -21.541 -11.178 1.00 14.69 N ANISOU 3739 N GLY I 37 1668 1733 2179 108 398 -178 N ATOM 3740 CA GLY I 37 5.252 -20.750 -11.881 1.00 15.81 C ANISOU 3740 CA GLY I 37 1800 1854 2354 133 387 -154 C ATOM 3741 C GLY I 37 5.704 -19.478 -12.571 1.00 17.18 C ANISOU 3741 C GLY I 37 1998 2004 2525 136 388 -140 C ATOM 3742 O GLY I 37 4.942 -18.865 -13.324 1.00 17.31 O ANISOU 3742 O GLY I 37 2009 2003 2566 155 372 -118 O ATOM 3743 N CYS I 38 6.903 -19.009 -12.278 1.00 15.10 N ANISOU 3743 N CYS I 38 1762 1738 2236 117 405 -151 N ATOM 3744 CA CYS I 38 7.447 -17.856 -12.997 1.00 17.11 C ANISOU 3744 CA CYS I 38 2042 1974 2487 114 400 -132 C ATOM 3745 C CYS I 38 8.931 -17.966 -13.260 1.00 16.41 C ANISOU 3745 C CYS I 38 1972 1904 2359 87 401 -130 C ATOM 3746 O CYS I 38 9.672 -18.678 -12.594 1.00 16.73 O ANISOU 3746 O CYS I 38 2013 1965 2381 69 412 -148 O ATOM 3747 CB CYS I 38 7.145 -16.557 -12.227 1.00 18.18 C ANISOU 3747 CB CYS I 38 2191 2068 2650 123 421 -138 C ATOM 3748 SG CYS I 38 8.014 -16.407 -10.622 1.00 18.49 S ANISOU 3748 SG CYS I 38 2254 2095 2675 101 454 -169 S ATOM 3749 N ARG I 39 9.363 -17.202 -14.248 1.00 16.66 N ANISOU 3749 N ARG I 39 2019 1930 2381 83 389 -105 N ATOM 3750 CA ARG I 39 10.753 -17.072 -14.608 1.00 16.67 C ANISOU 3750 CA ARG I 39 2035 1949 2349 59 393 -92 C ATOM 3751 C ARG I 39 11.406 -18.353 -15.133 1.00 17.88 C ANISOU 3751 C ARG I 39 2180 2148 2467 56 388 -94 C ATOM 3752 O ARG I 39 12.569 -18.590 -14.915 1.00 19.15 O ANISOU 3752 O ARG I 39 2343 2328 2606 36 400 -95 O ATOM 3753 CB ARG I 39 11.584 -16.453 -13.482 1.00 20.54 C ANISOU 3753 CB ARG I 39 2539 2420 2843 34 412 -103 C ATOM 3754 CG ARG I 39 10.969 -15.245 -12.774 1.00 23.78 C ANISOU 3754 CG ARG I 39 2967 2782 3286 42 417 -108 C ATOM 3755 CD ARG I 39 10.737 -14.063 -13.659 1.00 25.47 C ANISOU 3755 CD ARG I 39 3196 2970 3512 48 401 -79 C ATOM 3756 NE ARG I 39 11.959 -13.693 -14.393 1.00 31.48 N ANISOU 3756 NE ARG I 39 3967 3745 4247 20 392 -49 N ATOM 3757 CZ ARG I 39 12.983 -13.000 -13.879 1.00 45.37 C ANISOU 3757 CZ ARG I 39 5746 5490 6003 -10 394 -40 C ATOM 3758 NH1 ARG I 39 12.948 -12.562 -12.626 1.00 49.68 N ANISOU 3758 NH1 ARG I 39 6311 6000 6565 -15 402 -62 N ATOM 3759 NH2 ARG I 39 14.054 -12.744 -14.626 1.00 50.11 N ANISOU 3759 NH2 ARG I 39 6348 6110 6583 -35 388 -5 N ATOM 3760 N ALA I 40 10.607 -19.147 -15.837 1.00 17.52 N ANISOU 3760 N ALA I 40 2127 2114 2416 77 368 -94 N ATOM 3761 CA ALA I 40 11.085 -20.412 -16.431 1.00 17.43 C ANISOU 3761 CA ALA I 40 2115 2141 2367 81 357 -98 C ATOM 3762 C ALA I 40 12.310 -20.172 -17.296 1.00 18.34 C ANISOU 3762 C ALA I 40 2245 2279 2445 73 366 -76 C ATOM 3763 O ALA I 40 12.363 -19.197 -18.085 1.00 18.96 O ANISOU 3763 O ALA I 40 2336 2347 2522 72 363 -48 O ATOM 3764 CB ALA I 40 10.006 -21.025 -17.285 1.00 19.32 C ANISOU 3764 CB ALA I 40 2356 2380 2606 104 324 -92 C ATOM 3765 N LYS I 41 13.275 -21.101 -17.205 1.00 17.85 N ANISOU 3765 N LYS I 41 2179 2250 2352 69 376 -87 N ATOM 3766 CA LYS I 41 14.338 -21.244 -18.204 1.00 17.20 C ANISOU 3766 CA LYS I 41 2107 2201 2229 73 385 -66 C ATOM 3767 C LYS I 41 13.860 -22.218 -19.272 1.00 16.36 C ANISOU 3767 C LYS I 41 2017 2110 2088 103 361 -68 C ATOM 3768 O LYS I 41 12.723 -22.716 -19.211 1.00 17.54 O ANISOU 3768 O LYS I 41 2168 2244 2253 115 333 -82 O ATOM 3769 CB LYS I 41 15.641 -21.663 -17.532 1.00 19.18 C ANISOU 3769 CB LYS I 41 2342 2476 2468 56 409 -73 C ATOM 3770 CG LYS I 41 16.113 -20.605 -16.483 1.00 22.95 C ANISOU 3770 CG LYS I 41 2811 2929 2978 23 424 -67 C ATOM 3771 CD LYS I 41 17.429 -20.920 -15.887 1.00 28.39 C ANISOU 3771 CD LYS I 41 3486 3640 3661 2 442 -66 C ATOM 3772 CE LYS I 41 17.846 -19.864 -14.853 1.00 32.13 C ANISOU 3772 CE LYS I 41 3960 4083 4167 -33 448 -59 C ATOM 3773 NZ LYS I 41 17.575 -18.469 -15.274 1.00 34.01 N ANISOU 3773 NZ LYS I 41 4212 4292 4418 -41 443 -30 N ATOM 3774 N ARG I 42 14.679 -22.449 -20.298 1.00 16.06 N ANISOU 3774 N ARG I 42 1994 2102 2005 115 370 -51 N ATOM 3775 CA ARG I 42 14.190 -23.170 -21.463 1.00 17.14 C ANISOU 3775 CA ARG I 42 2160 2247 2104 145 344 -49 C ATOM 3776 C ARG I 42 14.108 -24.691 -21.318 1.00 16.56 C ANISOU 3776 C ARG I 42 2094 2189 2010 165 325 -80 C ATOM 3777 O ARG I 42 13.264 -25.325 -22.006 1.00 17.15 O ANISOU 3777 O ARG I 42 2195 2253 2068 186 287 -84 O ATOM 3778 CB ARG I 42 14.966 -22.787 -22.724 1.00 16.33 C ANISOU 3778 CB ARG I 42 2080 2169 1955 156 361 -17 C ATOM 3779 CG ARG I 42 14.712 -21.335 -23.174 1.00 18.41 C ANISOU 3779 CG ARG I 42 2348 2411 2236 139 362 17 C ATOM 3780 CD ARG I 42 15.627 -20.949 -24.307 1.00 18.80 C ANISOU 3780 CD ARG I 42 2415 2490 2239 145 385 52 C ATOM 3781 NE ARG I 42 16.999 -20.815 -23.838 1.00 17.30 N ANISOU 3781 NE ARG I 42 2198 2332 2044 129 426 63 N ATOM 3782 CZ ARG I 42 18.012 -20.443 -24.611 1.00 20.64 C ANISOU 3782 CZ ARG I 42 2622 2788 2432 129 457 99 C ATOM 3783 NH1 ARG I 42 17.822 -20.257 -25.923 1.00 21.03 N ANISOU 3783 NH1 ARG I 42 2706 2845 2439 146 452 124 N ATOM 3784 NH2 ARG I 42 19.232 -20.308 -24.085 1.00 21.16 N ANISOU 3784 NH2 ARG I 42 2654 2881 2503 111 492 114 N ATOM 3785 N ASN I 43 14.912 -25.242 -20.428 1.00 16.23 N ANISOU 3785 N ASN I 43 2031 2165 1970 156 345 -99 N ATOM 3786 CA ASN I 43 14.844 -26.714 -20.118 1.00 15.03 C ANISOU 3786 CA ASN I 43 1885 2024 1803 172 324 -131 C ATOM 3787 C ASN I 43 13.704 -26.933 -19.108 1.00 13.75 C ANISOU 3787 C ASN I 43 1706 1833 1687 156 297 -150 C ATOM 3788 O ASN I 43 13.901 -27.259 -17.915 1.00 14.92 O ANISOU 3788 O ASN I 43 1830 1980 1858 137 305 -171 O ATOM 3789 CB ASN I 43 16.154 -27.207 -19.561 1.00 14.47 C ANISOU 3789 CB ASN I 43 1796 1982 1720 168 353 -142 C ATOM 3790 CG ASN I 43 16.267 -28.718 -19.544 1.00 13.83 C ANISOU 3790 CG ASN I 43 1729 1915 1612 191 330 -172 C ATOM 3791 OD1 ASN I 43 15.426 -29.403 -20.132 1.00 15.76 O ANISOU 3791 OD1 ASN I 43 2002 2147 1838 212 290 -180 O ATOM 3792 ND2 ASN I 43 17.327 -29.241 -18.947 1.00 16.68 N ANISOU 3792 ND2 ASN I 43 2072 2298 1969 188 350 -184 N ATOM 3793 N ASN I 44 12.500 -26.737 -19.606 1.00 15.98 N ANISOU 3793 N ASN I 44 2000 2091 1982 163 265 -140 N ATOM 3794 CA ASN I 44 11.279 -26.732 -18.822 1.00 14.77 C ANISOU 3794 CA ASN I 44 1825 1911 1876 151 244 -146 C ATOM 3795 C ASN I 44 10.147 -26.965 -19.776 1.00 18.89 C ANISOU 3795 C ASN I 44 2368 2414 2396 168 197 -132 C ATOM 3796 O ASN I 44 9.849 -26.072 -20.604 1.00 18.54 O ANISOU 3796 O ASN I 44 2336 2356 2352 173 194 -107 O ATOM 3797 CB ASN I 44 11.151 -25.395 -18.075 1.00 15.48 C ANISOU 3797 CB ASN I 44 1892 1982 2009 130 275 -138 C ATOM 3798 CG ASN I 44 9.870 -25.250 -17.284 1.00 15.62 C ANISOU 3798 CG ASN I 44 1885 1973 2076 124 263 -141 C ATOM 3799 OD1 ASN I 44 8.848 -25.815 -17.640 1.00 16.53 O ANISOU 3799 OD1 ASN I 44 2001 2079 2200 135 225 -136 O ATOM 3800 ND2 ASN I 44 9.908 -24.440 -16.247 1.00 17.17 N ANISOU 3800 ND2 ASN I 44 2063 2156 2304 108 294 -147 N ATOM 3801 N PHE I 45 9.537 -28.167 -19.708 1.00 15.33 N ANISOU 3801 N PHE I 45 1923 1961 1942 174 154 -144 N ATOM 3802 CA PHE I 45 8.552 -28.619 -20.681 1.00 14.84 C ANISOU 3802 CA PHE I 45 1888 1880 1872 189 98 -128 C ATOM 3803 C PHE I 45 7.264 -29.038 -20.015 1.00 16.84 C ANISOU 3803 C PHE I 45 2111 2113 2173 177 62 -125 C ATOM 3804 O PHE I 45 7.277 -29.560 -18.903 1.00 16.73 O ANISOU 3804 O PHE I 45 2071 2108 2179 163 70 -143 O ATOM 3805 CB PHE I 45 9.110 -29.802 -21.460 1.00 15.66 C ANISOU 3805 CB PHE I 45 2037 1998 1915 212 69 -141 C ATOM 3806 CG PHE I 45 10.381 -29.468 -22.230 1.00 15.41 C ANISOU 3806 CG PHE I 45 2034 1992 1831 230 108 -140 C ATOM 3807 CD1 PHE I 45 11.629 -29.641 -21.649 1.00 18.03 C ANISOU 3807 CD1 PHE I 45 2350 2353 2146 228 153 -158 C ATOM 3808 CD2 PHE I 45 10.331 -28.942 -23.502 1.00 15.94 C ANISOU 3808 CD2 PHE I 45 2138 2053 1866 246 101 -117 C ATOM 3809 CE1 PHE I 45 12.791 -29.321 -22.332 1.00 17.66 C ANISOU 3809 CE1 PHE I 45 2320 2333 2056 244 192 -151 C ATOM 3810 CE2 PHE I 45 11.505 -28.670 -24.195 1.00 18.30 C ANISOU 3810 CE2 PHE I 45 2459 2379 2115 263 141 -112 C ATOM 3811 CZ PHE I 45 12.727 -28.830 -23.603 1.00 17.59 C ANISOU 3811 CZ PHE I 45 2348 2322 2014 262 189 -127 C ATOM 3812 N LYS I 46 6.131 -28.803 -20.694 1.00 20.15 N ANISOU 3812 N LYS I 46 2535 2506 2614 182 20 -98 N ATOM 3813 CA LYS I 46 4.834 -29.133 -20.113 1.00 20.89 C ANISOU 3813 CA LYS I 46 2594 2582 2761 171 -14 -85 C ATOM 3814 C LYS I 46 4.516 -30.588 -20.269 1.00 23.73 C ANISOU 3814 C LYS I 46 2973 2941 3102 171 -75 -90 C ATOM 3815 O LYS I 46 3.608 -31.075 -19.589 1.00 25.15 O ANISOU 3815 O LYS I 46 3118 3114 3323 157 -101 -81 O ATOM 3816 CB LYS I 46 3.733 -28.262 -20.712 1.00 22.52 C ANISOU 3816 CB LYS I 46 2790 2759 3007 174 -36 -50 C ATOM 3817 CG LYS I 46 3.878 -26.804 -20.346 1.00 25.16 C ANISOU 3817 CG LYS I 46 3100 3089 3371 172 19 -45 C ATOM 3818 CD LYS I 46 2.823 -25.946 -21.010 1.00 29.38 C ANISOU 3818 CD LYS I 46 3627 3592 3945 178 -6 -10 C ATOM 3819 CE LYS I 46 2.999 -24.518 -20.633 1.00 34.11 C ANISOU 3819 CE LYS I 46 4207 4183 4571 178 45 -9 C ATOM 3820 NZ LYS I 46 1.925 -23.659 -21.228 1.00 34.88 N ANISOU 3820 NZ LYS I 46 4294 4247 4713 186 19 25 N ATOM 3821 N SER I 47 5.269 -31.317 -21.105 1.00 21.27 N ANISOU 3821 N SER I 47 2716 2638 2728 188 -97 -103 N ATOM 3822 CA SER I 47 5.055 -32.739 -21.270 1.00 21.68 C ANISOU 3822 CA SER I 47 2796 2685 2756 191 -160 -111 C ATOM 3823 C SER I 47 6.380 -33.454 -21.595 1.00 23.16 C ANISOU 3823 C SER I 47 3030 2895 2876 212 -147 -143 C ATOM 3824 O SER I 47 7.317 -32.830 -22.103 1.00 20.53 O ANISOU 3824 O SER I 47 2716 2577 2507 228 -101 -148 O ATOM 3825 CB SER I 47 4.078 -33.001 -22.423 1.00 22.53 C ANISOU 3825 CB SER I 47 2942 2760 2860 200 -236 -80 C ATOM 3826 OG SER I 47 4.667 -32.736 -23.699 1.00 25.64 O ANISOU 3826 OG SER I 47 3397 3151 3195 225 -237 -80 O ATOM 3827 N ALA I 48 6.424 -34.752 -21.349 1.00 19.59 N ANISOU 3827 N ALA I 48 2596 2443 2405 213 -190 -160 N ATOM 3828 CA ALA I 48 7.559 -35.587 -21.698 1.00 18.23 C ANISOU 3828 CA ALA I 48 2471 2288 2169 239 -188 -190 C ATOM 3829 C ALA I 48 7.793 -35.553 -23.199 1.00 18.00 C ANISOU 3829 C ALA I 48 2510 2250 2081 274 -208 -183 C ATOM 3830 O ALA I 48 8.943 -35.517 -23.660 1.00 19.07 O ANISOU 3830 O ALA I 48 2674 2408 2164 301 -167 -200 O ATOM 3831 CB ALA I 48 7.318 -37.014 -21.221 1.00 22.25 C ANISOU 3831 CB ALA I 48 2991 2790 2675 232 -248 -206 C ATOM 3832 N GLU I 49 6.713 -35.624 -23.990 1.00 21.24 N ANISOU 3832 N GLU I 49 2949 2625 2495 273 -274 -156 N ATOM 3833 CA GLU I 49 6.823 -35.558 -25.443 1.00 24.62 C ANISOU 3833 CA GLU I 49 3451 3040 2865 304 -298 -147 C ATOM 3834 C GLU I 49 7.487 -34.276 -25.952 1.00 20.57 C ANISOU 3834 C GLU I 49 2934 2545 2336 314 -227 -137 C ATOM 3835 O GLU I 49 8.364 -34.342 -26.807 1.00 19.52 O ANISOU 3835 O GLU I 49 2852 2427 2137 347 -206 -147 O ATOM 3836 CB GLU I 49 5.443 -35.721 -26.082 1.00 28.93 C ANISOU 3836 CB GLU I 49 4021 3540 3431 293 -384 -113 C ATOM 3837 CG GLU I 49 4.855 -37.110 -25.882 1.00 35.39 C ANISOU 3837 CG GLU I 49 4862 4335 4249 287 -470 -117 C ATOM 3838 CD GLU I 49 4.406 -37.401 -24.445 1.00 41.20 C ANISOU 3838 CD GLU I 49 5521 5081 5052 251 -467 -118 C ATOM 3839 OE1 GLU I 49 4.039 -36.465 -23.677 1.00 36.15 O ANISOU 3839 OE1 GLU I 49 4809 4452 4475 227 -418 -103 O ATOM 3840 OE2 GLU I 49 4.431 -38.601 -24.081 1.00 46.89 O ANISOU 3840 OE2 GLU I 49 6259 5797 5761 249 -514 -133 O ATOM 3841 N ASP I 50 7.090 -33.112 -25.418 1.00 20.74 N ANISOU 3841 N ASP I 50 2896 2568 2418 288 -190 -118 N ATOM 3842 CA ASP I 50 7.721 -31.840 -25.799 1.00 22.21 C ANISOU 3842 CA ASP I 50 3074 2769 2595 291 -127 -106 C ATOM 3843 C ASP I 50 9.214 -31.904 -25.452 1.00 19.12 C ANISOU 3843 C ASP I 50 2676 2421 2168 304 -58 -132 C ATOM 3844 O ASP I 50 10.070 -31.459 -26.209 1.00 18.06 O ANISOU 3844 O ASP I 50 2568 2305 1987 324 -20 -127 O ATOM 3845 CB ASP I 50 7.084 -30.664 -25.084 1.00 22.46 C ANISOU 3845 CB ASP I 50 3042 2792 2700 262 -101 -87 C ATOM 3846 CG ASP I 50 5.711 -30.263 -25.619 1.00 33.67 C ANISOU 3846 CG ASP I 50 4463 4172 4157 252 -156 -52 C ATOM 3847 OD1 ASP I 50 5.239 -30.803 -26.635 1.00 34.76 O ANISOU 3847 OD1 ASP I 50 4658 4287 4264 265 -219 -40 O ATOM 3848 OD2 ASP I 50 5.107 -29.365 -24.979 1.00 36.82 O ANISOU 3848 OD2 ASP I 50 4809 4562 4620 233 -137 -37 O ATOM 3849 N CYS I 51 9.527 -32.419 -24.275 1.00 17.40 N ANISOU 3849 N CYS I 51 2418 2217 1975 291 -42 -156 N ATOM 3850 CA CYS I 51 10.900 -32.498 -23.834 1.00 15.66 C ANISOU 3850 CA CYS I 51 2184 2034 1732 299 18 -177 C ATOM 3851 C CYS I 51 11.734 -33.407 -24.743 1.00 17.39 C ANISOU 3851 C CYS I 51 2464 2269 1875 342 11 -193 C ATOM 3852 O CYS I 51 12.840 -33.068 -25.170 1.00 16.52 O ANISOU 3852 O CYS I 51 2360 2188 1726 362 65 -192 O ATOM 3853 CB CYS I 51 10.910 -32.976 -22.383 1.00 16.74 C ANISOU 3853 CB CYS I 51 2272 2176 1913 274 23 -198 C ATOM 3854 SG CYS I 51 12.552 -33.146 -21.665 1.00 18.76 S ANISOU 3854 SG CYS I 51 2505 2472 2152 277 86 -223 S ATOM 3855 N MET I 52 11.211 -34.588 -25.066 1.00 17.54 N ANISOU 3855 N MET I 52 2528 2268 1870 358 -55 -206 N ATOM 3856 CA MET I 52 11.955 -35.530 -25.898 1.00 18.01 C ANISOU 3856 CA MET I 52 2653 2338 1853 405 -65 -225 C ATOM 3857 C MET I 52 12.101 -35.045 -27.317 1.00 17.69 C ANISOU 3857 C MET I 52 2670 2296 1755 435 -57 -206 C ATOM 3858 O MET I 52 13.108 -35.309 -27.954 1.00 21.57 O ANISOU 3858 O MET I 52 3198 2814 2184 475 -23 -217 O ATOM 3859 CB MET I 52 11.313 -36.935 -25.843 1.00 21.07 C ANISOU 3859 CB MET I 52 3081 2696 2229 413 -149 -244 C ATOM 3860 CG MET I 52 11.442 -37.500 -24.427 1.00 24.89 C ANISOU 3860 CG MET I 52 3509 3189 2759 386 -147 -266 C ATOM 3861 SD MET I 52 13.175 -37.914 -23.970 1.00 32.54 S ANISOU 3861 SD MET I 52 4465 4203 3696 413 -80 -298 S ATOM 3862 CE MET I 52 13.445 -39.324 -25.040 1.00 34.87 C ANISOU 3862 CE MET I 52 4857 4486 3908 473 -135 -323 C ATOM 3863 N ARG I 53 11.084 -34.376 -27.832 1.00 18.89 N ANISOU 3863 N ARG I 53 2833 2418 1927 418 -91 -178 N ATOM 3864 CA ARG I 53 11.194 -33.820 -29.207 1.00 21.55 C ANISOU 3864 CA ARG I 53 3227 2753 2209 442 -84 -156 C ATOM 3865 C ARG I 53 12.290 -32.750 -29.272 1.00 19.58 C ANISOU 3865 C ARG I 53 2944 2545 1951 443 6 -143 C ATOM 3866 O ARG I 53 13.013 -32.607 -30.283 1.00 23.06 O ANISOU 3866 O ARG I 53 3430 3005 2324 476 38 -136 O ATOM 3867 CB ARG I 53 9.885 -33.178 -29.595 1.00 23.19 C ANISOU 3867 CB ARG I 53 3439 2918 2453 415 -136 -124 C ATOM 3868 CG ARG I 53 9.883 -32.653 -31.039 1.00 34.27 C ANISOU 3868 CG ARG I 53 4910 4311 3799 436 -142 -101 C ATOM 3869 CD ARG I 53 8.473 -32.204 -31.465 1.00 41.11 C ANISOU 3869 CD ARG I 53 5787 5128 4703 411 -212 -69 C ATOM 3870 NE ARG I 53 7.435 -33.066 -30.883 1.00 43.40 N ANISOU 3870 NE ARG I 53 6067 5385 5039 393 -287 -74 N ATOM 3871 CZ ARG I 53 6.607 -32.683 -29.912 1.00 39.80 C ANISOU 3871 CZ ARG I 53 5536 4917 4669 355 -297 -61 C ATOM 3872 NH1 ARG I 53 6.661 -31.441 -29.441 1.00 39.91 N ANISOU 3872 NH1 ARG I 53 5488 4945 4732 334 -240 -46 N ATOM 3873 NH2 ARG I 53 5.699 -33.532 -29.452 1.00 40.65 N ANISOU 3873 NH2 ARG I 53 5635 4998 4813 341 -365 -61 N ATOM 3874 N THR I 54 12.368 -31.950 -28.233 1.00 18.00 N ANISOU 3874 N THR I 54 2667 2355 1816 406 45 -137 N ATOM 3875 CA THR I 54 13.287 -30.805 -28.238 1.00 17.84 C ANISOU 3875 CA THR I 54 2612 2368 1798 397 120 -117 C ATOM 3876 C THR I 54 14.718 -31.209 -27.891 1.00 20.16 C ANISOU 3876 C THR I 54 2887 2708 2065 417 180 -134 C ATOM 3877 O THR I 54 15.699 -30.805 -28.546 1.00 20.50 O ANISOU 3877 O THR I 54 2938 2784 2065 437 233 -118 O ATOM 3878 CB THR I 54 12.818 -29.768 -27.250 1.00 17.75 C ANISOU 3878 CB THR I 54 2533 2345 1867 351 134 -104 C ATOM 3879 OG1 THR I 54 11.527 -29.313 -27.614 1.00 19.56 O ANISOU 3879 OG1 THR I 54 2774 2533 2125 336 84 -84 O ATOM 3880 CG2 THR I 54 13.780 -28.555 -27.183 1.00 18.66 C ANISOU 3880 CG2 THR I 54 2613 2489 1988 336 204 -81 C ATOM 3881 N CYS I 55 14.863 -32.070 -26.874 1.00 18.87 N ANISOU 3881 N CYS I 55 2697 2548 1926 413 170 -164 N ATOM 3882 CA CYS I 55 16.186 -32.420 -26.369 1.00 18.92 C ANISOU 3882 CA CYS I 55 2673 2594 1920 426 223 -178 C ATOM 3883 C CYS I 55 16.595 -33.861 -26.558 1.00 20.63 C ANISOU 3883 C CYS I 55 2931 2818 2089 469 202 -211 C ATOM 3884 O CYS I 55 17.769 -34.163 -26.422 1.00 22.14 O ANISOU 3884 O CYS I 55 3107 3045 2260 492 248 -219 O ATOM 3885 CB CYS I 55 16.207 -32.149 -24.867 1.00 18.93 C ANISOU 3885 CB CYS I 55 2604 2593 1994 381 236 -187 C ATOM 3886 SG CYS I 55 15.993 -30.438 -24.418 1.00 20.23 S ANISOU 3886 SG CYS I 55 2718 2752 2218 333 270 -153 S ATOM 3887 N GLY I 56 15.665 -34.726 -26.939 1.00 22.31 N ANISOU 3887 N GLY I 56 3198 2996 2282 484 130 -227 N ATOM 3888 CA GLY I 56 15.942 -36.175 -26.999 1.00 25.33 C ANISOU 3888 CA GLY I 56 3624 3377 2623 522 97 -262 C ATOM 3889 C GLY I 56 15.929 -36.779 -28.363 1.00 30.24 C ANISOU 3889 C GLY I 56 4337 3990 3162 577 70 -266 C ATOM 3890 O GLY I 56 16.095 -38.022 -28.553 1.00 34.25 O ANISOU 3890 O GLY I 56 4898 4490 3627 616 33 -297 O ATOM 3891 N GLY I 57 15.725 -35.938 -29.360 1.00 23.78 N ANISOU 3891 N GLY I 57 3548 3170 2316 582 84 -238 N ATOM 3892 CA GLY I 57 15.908 -36.376 -30.736 1.00 29.98 C ANISOU 3892 CA GLY I 57 4426 3953 3012 638 74 -240 C ATOM 3893 C GLY I 57 14.680 -37.075 -31.285 1.00 37.10 C ANISOU 3893 C GLY I 57 5404 4799 3894 642 -25 -246 C ATOM 3894 O GLY I 57 14.760 -37.807 -32.294 1.00 39.32 O ANISOU 3894 O GLY I 57 5777 5066 4095 693 -54 -259 O ATOM 3895 N ALA I 58 13.551 -36.873 -30.609 1.00 31.86 N ANISOU 3895 N ALA I 58 4703 4101 3302 590 -79 -237 N ATOM 3896 CA ALA I 58 12.251 -37.347 -31.074 1.00 42.10 C ANISOU 3896 CA ALA I 58 6057 5341 4597 581 -178 -230 C ATOM 3897 C ALA I 58 11.656 -36.367 -32.099 1.00 48.73 C ANISOU 3897 C ALA I 58 6930 6162 5424 573 -187 -194 C ATOM 3898 O ALA I 58 12.129 -35.223 -32.306 1.00 52.53 O ANISOU 3898 O ALA I 58 7379 6672 5909 565 -119 -171 O ATOM 3899 CB ALA I 58 11.275 -37.555 -29.869 1.00 32.03 C ANISOU 3899 CB ALA I 58 4719 4041 3409 528 -228 -230 C ATOM 3900 OXT ALA I 58 10.666 -36.716 -32.749 1.00 53.30 O ANISOU 3900 OXT ALA I 58 7571 6693 5989 571 -270 -184 O TER 3901 ALA I 58 ATOM 3902 N ARG C 1 48.521 -48.870 44.881 1.00 65.72 N ANISOU 3902 N ARG C 1 11434 5640 7897 -3327 -6052 2517 N ATOM 3903 CA ARG C 1 47.658 -48.350 43.783 1.00 61.67 C ANISOU 3903 CA ARG C 1 10741 5324 7368 -3076 -5599 2305 C ATOM 3904 C ARG C 1 47.030 -47.008 44.207 1.00 62.63 C ANISOU 3904 C ARG C 1 11356 5306 7136 -3113 -5605 2115 C ATOM 3905 O ARG C 1 46.724 -46.801 45.376 1.00 61.24 O ANISOU 3905 O ARG C 1 11727 4946 6595 -3243 -5760 2029 O ATOM 3906 CB ARG C 1 46.572 -49.366 43.404 1.00 55.84 C ANISOU 3906 CB ARG C 1 9879 4813 6524 -2845 -5128 2102 C ATOM 3907 CG ARG C 1 45.376 -49.374 44.330 1.00 53.29 C ANISOU 3907 CG ARG C 1 10076 4452 5721 -2830 -4955 1850 C ATOM 3908 CD ARG C 1 44.275 -50.398 43.955 1.00 46.45 C ANISOU 3908 CD ARG C 1 9065 3811 4771 -2617 -4505 1677 C ATOM 3909 NE ARG C 1 44.650 -51.792 43.607 1.00 44.64 N ANISOU 3909 NE ARG C 1 8456 3704 4801 -2572 -4476 1803 N ATOM 3910 CZ ARG C 1 44.981 -52.758 44.470 1.00 47.35 C ANISOU 3910 CZ ARG C 1 8914 3972 5106 -2700 -4677 1905 C ATOM 3911 NH1 ARG C 1 45.046 -52.549 45.774 1.00 54.00 N ANISOU 3911 NH1 ARG C 1 10244 4614 5660 -2900 -4945 1913 N ATOM 3912 NH2 ARG C 1 45.244 -53.965 44.017 1.00 50.03 N ANISOU 3912 NH2 ARG C 1 8893 4427 5689 -2625 -4609 2001 N ATOM 3913 N PRO C 2 46.876 -46.084 43.257 1.00 62.87 N ANISOU 3913 N PRO C 2 11207 5409 7272 -2997 -5444 2058 N ATOM 3914 CA PRO C 2 46.229 -44.786 43.523 1.00 60.73 C ANISOU 3914 CA PRO C 2 11371 5014 6688 -2995 -5408 1867 C ATOM 3915 C PRO C 2 44.779 -44.883 44.038 1.00 56.53 C ANISOU 3915 C PRO C 2 11237 4525 5719 -2849 -5039 1557 C ATOM 3916 O PRO C 2 44.051 -45.796 43.672 1.00 58.94 O ANISOU 3916 O PRO C 2 11331 5039 6024 -2674 -4679 1452 O ATOM 3917 CB PRO C 2 46.267 -44.107 42.151 1.00 61.40 C ANISOU 3917 CB PRO C 2 11042 5245 7043 -2847 -5216 1873 C ATOM 3918 CG PRO C 2 47.462 -44.801 41.414 1.00 50.00 C ANISOU 3918 CG PRO C 2 9008 3899 6091 -2881 -5358 2173 C ATOM 3919 CD PRO C 2 47.828 -46.011 42.128 1.00 59.91 C ANISOU 3919 CD PRO C 2 10261 5132 7371 -2969 -5501 2284 C ATOM 3920 N ASP C 3 44.350 -43.877 44.796 1.00 55.11 N ANISOU 3920 N ASP C 3 11612 4144 5181 -2906 -5113 1417 N ATOM 3921 CA AASP C 3 43.020 -43.868 45.399 0.50 56.73 C ANISOU 3921 CA AASP C 3 12236 4359 4960 -2769 -4770 1146 C ATOM 3922 CA BASP C 3 43.007 -43.831 45.383 0.50 56.89 C ANISOU 3922 CA BASP C 3 12258 4378 4979 -2766 -4766 1142 C ATOM 3923 C ASP C 3 41.819 -43.792 44.422 1.00 54.58 C ANISOU 3923 C ASP C 3 11709 4332 4696 -2473 -4228 940 C ATOM 3924 O ASP C 3 40.883 -44.508 44.612 1.00 55.66 O ANISOU 3924 O ASP C 3 11881 4596 4672 -2344 -3904 810 O ATOM 3925 CB AASP C 3 42.921 -42.718 46.411 0.50 63.34 C ANISOU 3925 CB AASP C 3 13754 4895 5416 -2888 -4981 1054 C ATOM 3926 CB BASP C 3 42.874 -42.625 46.313 0.50 62.08 C ANISOU 3926 CB BASP C 3 13577 4744 5265 -2870 -4956 1043 C ATOM 3927 CG AASP C 3 44.019 -42.765 47.480 0.50 71.32 C ANISOU 3927 CG AASP C 3 15101 5630 6367 -3202 -5545 1251 C ATOM 3928 CG BASP C 3 41.419 -42.238 46.561 0.50 62.30 C ANISOU 3928 CG BASP C 3 13952 4805 4916 -2653 -4505 752 C ATOM 3929 OD1AASP C 3 44.134 -43.783 48.188 0.50 72.40 O ANISOU 3929 OD1AASP C 3 15322 5761 6426 -3290 -5626 1312 O ATOM 3930 OD1BASP C 3 40.544 -43.098 46.386 0.50 56.83 O ANISOU 3930 OD1BASP C 3 13081 4324 4186 -2482 -4114 650 O ATOM 3931 OD2AASP C 3 44.759 -41.772 47.615 0.50 73.80 O ANISOU 3931 OD2AASP C 3 15603 5723 6712 -3370 -5925 1355 O ATOM 3932 OD2BASP C 3 41.151 -41.075 46.939 0.50 68.13 O ANISOU 3932 OD2BASP C 3 15141 5345 5399 -2651 -4544 635 O ATOM 3933 N PHE C 4 41.834 -42.893 43.422 1.00 53.58 N ANISOU 3933 N PHE C 4 11352 4257 4749 -2381 -4150 922 N ATOM 3934 CA PHE C 4 40.656 -42.636 42.493 1.00 44.78 C ANISOU 3934 CA PHE C 4 10040 3344 3629 -2110 -3665 727 C ATOM 3935 C PHE C 4 39.972 -43.910 41.922 1.00 46.25 C ANISOU 3935 C PHE C 4 9844 3805 3925 -1944 -3302 684 C ATOM 3936 O PHE C 4 38.960 -43.876 41.188 1.00 44.30 O ANISOU 3936 O PHE C 4 9420 3729 3682 -1735 -2915 544 O ATOM 3937 CB PHE C 4 41.071 -41.676 41.384 1.00 44.02 C ANISOU 3937 CB PHE C 4 9655 3275 3798 -2075 -3711 781 C ATOM 3938 CG PHE C 4 42.264 -42.127 40.594 1.00 44.35 C ANISOU 3938 CG PHE C 4 9190 3399 4261 -2161 -3922 1027 C ATOM 3939 CD1 PHE C 4 43.495 -41.567 40.790 1.00 47.49 C ANISOU 3939 CD1 PHE C 4 9612 3620 4813 -2375 -4365 1236 C ATOM 3940 CD2 PHE C 4 42.127 -43.096 39.616 1.00 42.49 C ANISOU 3940 CD2 PHE C 4 8454 3416 4273 -2018 -3663 1057 C ATOM 3941 CE1 PHE C 4 44.577 -41.961 40.034 1.00 48.42 C ANISOU 3941 CE1 PHE C 4 9235 3823 5341 -2433 -4522 1483 C ATOM 3942 CE2 PHE C 4 43.227 -43.504 38.877 1.00 42.43 C ANISOU 3942 CE2 PHE C 4 7994 3480 4649 -2070 -3820 1286 C ATOM 3943 CZ PHE C 4 44.432 -42.941 39.089 1.00 44.06 C ANISOU 3943 CZ PHE C 4 8201 3522 5019 -2268 -4230 1501 C ATOM 3944 N ACYS C 5 40.678 -44.995 42.221 0.50 49.15 N ANISOU 3944 N ACYS C 5 10069 4190 4417 -2061 -3488 839 N ATOM 3945 N BCYS C 5 40.428 -45.043 42.388 0.50 49.34 N ANISOU 3945 N BCYS C 5 10170 4214 4363 -2043 -3433 798 N ATOM 3946 CA ACYS C 5 40.542 -46.323 41.658 0.50 46.64 C ANISOU 3946 CA ACYS C 5 9342 4088 4291 -1969 -3299 882 C ATOM 3947 CA BCYS C 5 39.873 -46.313 41.978 0.50 46.54 C ANISOU 3947 CA BCYS C 5 9507 4081 4095 -1918 -3150 774 C ATOM 3948 C ACYS C 5 39.434 -47.065 42.321 0.50 44.97 C ANISOU 3948 C ACYS C 5 9346 3940 3800 -1893 -3031 739 C ATOM 3949 C BCYS C 5 38.418 -46.594 42.395 0.50 42.15 C ANISOU 3949 C BCYS C 5 9172 3607 3237 -1772 -2765 574 C ATOM 3950 O ACYS C 5 39.047 -48.127 41.850 0.50 37.16 O ANISOU 3950 O ACYS C 5 8062 3134 2923 -1794 -2822 738 O ATOM 3951 O BCYS C 5 37.718 -47.355 41.725 0.50 35.72 O ANISOU 3951 O BCYS C 5 8052 2999 2519 -1624 -2465 527 O ATOM 3952 CB ACYS C 5 41.838 -47.107 41.891 0.50 44.68 C ANISOU 3952 CB ACYS C 5 8918 3783 4275 -2145 -3658 1123 C ATOM 3953 CB BCYS C 5 40.759 -47.393 42.557 0.50 48.16 C ANISOU 3953 CB BCYS C 5 9662 4242 4396 -2081 -3429 951 C ATOM 3954 SG ACYS C 5 43.041 -46.992 40.538 0.50 49.26 S ANISOU 3954 SG ACYS C 5 8910 4448 5360 -2135 -3789 1343 S ATOM 3955 SG BCYS C 5 41.154 -48.684 41.377 0.50101.49 S ANISOU 3955 SG BCYS C 5 15773 11229 11558 -1981 -3314 1079 S ATOM 3956 N ALEU C 6 38.966 -46.533 43.446 0.50 42.87 N ANISOU 3956 N ALEU C 6 9613 3510 3166 -1945 -3051 633 N ATOM 3957 N BLEU C 6 37.980 -46.013 43.508 0.50 40.85 N ANISOU 3957 N BLEU C 6 9541 3272 2709 -1816 -2779 470 N ATOM 3958 CA ALEU C 6 37.762 -47.038 44.065 0.50 42.35 C ANISOU 3958 CA ALEU C 6 9778 3507 2808 -1846 -2733 488 C ATOM 3959 CA BLEU C 6 36.742 -46.421 44.166 0.50 41.95 C ANISOU 3959 CA BLEU C 6 9931 3463 2546 -1709 -2449 327 C ATOM 3960 C ALEU C 6 36.558 -46.277 43.585 0.50 42.31 C ANISOU 3960 C ALEU C 6 9793 3585 2697 -1631 -2343 306 C ATOM 3961 C BLEU C 6 35.465 -45.701 43.695 0.50 44.58 C ANISOU 3961 C BLEU C 6 10272 3886 2781 -1480 -2034 149 C ATOM 3962 O ALEU C 6 35.426 -46.711 43.826 0.50 43.97 O ANISOU 3962 O ALEU C 6 10071 3898 2738 -1506 -2006 200 O ATOM 3963 O BLEU C 6 34.382 -45.960 44.218 0.50 47.86 O ANISOU 3963 O BLEU C 6 10875 4347 2961 -1375 -1728 45 O ATOM 3964 CB ALEU C 6 37.849 -46.953 45.589 0.50 45.97 C ANISOU 3964 CB ALEU C 6 10830 3741 2898 -2002 -2924 475 C ATOM 3965 CB BLEU C 6 36.901 -46.280 45.687 0.50 46.62 C ANISOU 3965 CB BLEU C 6 11128 3817 2766 -1865 -2647 315 C ATOM 3966 CG ALEU C 6 38.384 -48.229 46.212 0.50 46.98 C ANISOU 3966 CG ALEU C 6 10937 3865 3049 -2151 -3122 610 C ATOM 3967 CG BLEU C 6 38.101 -47.026 46.287 0.50 46.84 C ANISOU 3967 CG BLEU C 6 11187 3738 2873 -2107 -3078 503 C ATOM 3968 CD1ALEU C 6 38.298 -48.137 47.735 0.50 52.40 C ANISOU 3968 CD1ALEU C 6 12259 4332 3319 -2294 -3266 578 C ATOM 3969 CD1BLEU C 6 39.398 -46.681 45.545 0.50 44.34 C ANISOU 3969 CD1BLEU C 6 10545 3382 2923 -2218 -3430 675 C ATOM 3970 CD2ALEU C 6 37.592 -49.396 45.672 0.50 44.80 C ANISOU 3970 CD2ALEU C 6 10301 3841 2878 -2003 -2780 579 C ATOM 3971 CD2BLEU C 6 38.234 -46.738 47.782 0.50 51.07 C ANISOU 3971 CD2BLEU C 6 12386 4010 3009 -2271 -3296 484 C ATOM 3972 N AGLU C 7 36.803 -45.157 42.891 0.50 41.62 N ANISOU 3972 N AGLU C 7 9628 3455 2729 -1592 -2392 286 N ATOM 3973 N BGLU C 7 35.577 -44.808 42.721 0.50 40.27 N ANISOU 3973 N BGLU C 7 9515 3364 2421 -1403 -2017 129 N ATOM 3974 CA AGLU C 7 35.737 -44.307 42.384 0.50 40.17 C ANISOU 3974 CA AGLU C 7 9459 3331 2475 -1391 -2055 126 C ATOM 3975 CA BGLU C 7 34.386 -44.093 42.269 0.50 38.82 C ANISOU 3975 CA BGLU C 7 9332 3252 2164 -1189 -1644 -26 C ATOM 3976 C AGLU C 7 35.036 -45.058 41.263 0.50 35.68 C ANISOU 3976 C AGLU C 7 8391 3032 2132 -1224 -1736 112 C ATOM 3977 C BGLU C 7 33.646 -44.809 41.147 0.50 37.06 C ANISOU 3977 C BGLU C 7 8609 3297 2174 -1029 -1335 -33 C ATOM 3978 O AGLU C 7 35.693 -45.744 40.484 0.50 36.22 O ANISOU 3978 O AGLU C 7 8059 3214 2491 -1259 -1839 230 O ATOM 3979 O BGLU C 7 34.252 -45.510 40.326 0.50 32.52 O ANISOU 3979 O BGLU C 7 7629 2843 1884 -1066 -1437 75 O ATOM 3980 CB AGLU C 7 36.302 -42.986 41.836 0.50 43.98 C ANISOU 3980 CB AGLU C 7 9944 3699 3067 -1412 -2232 135 C ATOM 3981 CB BGLU C 7 34.720 -42.656 41.868 0.50 37.46 C ANISOU 3981 CB BGLU C 7 9255 2948 2029 -1179 -1766 -62 C ATOM 3982 CG AGLU C 7 36.984 -42.105 42.884 0.50 47.04 C ANISOU 3982 CG AGLU C 7 10856 3788 3228 -1586 -2581 150 C ATOM 3983 CG BGLU C 7 35.246 -41.831 43.040 0.50 46.78 C ANISOU 3983 CG BGLU C 7 11018 3833 2923 -1323 -2050 -79 C ATOM 3984 CD AGLU C 7 35.999 -41.494 43.864 0.50 51.76 C ANISOU 3984 CD AGLU C 7 12014 4246 3409 -1497 -2377 -31 C ATOM 3985 CD BGLU C 7 34.348 -41.920 44.271 0.50 51.04 C ANISOU 3985 CD BGLU C 7 12060 4279 3053 -1266 -1838 -203 C ATOM 3986 OE1AGLU C 7 34.932 -41.003 43.433 0.50 51.29 O ANISOU 3986 OE1AGLU C 7 11919 4269 3299 -1283 -2012 -171 O ATOM 3987 OE1BGLU C 7 33.167 -41.529 44.163 0.50 51.60 O ANISOU 3987 OE1BGLU C 7 12189 4410 3006 -1054 -1450 -340 O ATOM 3988 OE2AGLU C 7 36.299 -41.492 45.073 0.50 59.37 O ANISOU 3988 OE2AGLU C 7 13464 5004 4090 -1638 -2581 -26 O ATOM 3989 OE2BGLU C 7 34.815 -42.365 45.352 0.50 55.19 O ANISOU 3989 OE2BGLU C 7 12928 4667 3375 -1429 -2055 -153 O ATOM 3990 N APRO C 8 33.697 -44.968 41.199 0.50 36.93 N ANISOU 3990 N APRO C 8 8584 3287 2161 -1043 -1350 -21 N ATOM 3991 N BPRO C 8 32.313 -44.648 41.110 0.50 37.73 N ANISOU 3991 N BPRO C 8 8731 3467 2139 -847 -954 -152 N ATOM 3992 CA APRO C 8 32.925 -45.608 40.124 0.50 34.20 C ANISOU 3992 CA APRO C 8 7794 3182 2021 -892 -1060 -32 C ATOM 3993 CA BPRO C 8 31.630 -45.252 39.968 0.50 34.46 C ANISOU 3993 CA BPRO C 8 7843 3288 1962 -714 -705 -144 C ATOM 3994 C APRO C 8 33.180 -44.977 38.768 0.50 32.06 C ANISOU 3994 C APRO C 8 7174 2981 2025 -823 -1066 -18 C ATOM 3995 C BPRO C 8 32.261 -44.667 38.723 0.50 29.95 C ANISOU 3995 C BPRO C 8 6954 2751 1675 -703 -830 -105 C ATOM 3996 O APRO C 8 33.947 -43.991 38.710 0.50 35.60 O ANISOU 3996 O APRO C 8 7731 3293 2505 -892 -1290 2 O ATOM 3997 O BPRO C 8 32.550 -43.450 38.733 0.50 28.78 O ANISOU 3997 O BPRO C 8 6987 2465 1483 -707 -933 -146 O ATOM 3998 CB APRO C 8 31.467 -45.375 40.546 0.50 36.46 C ANISOU 3998 CB APRO C 8 8268 3502 2082 -730 -681 -159 C ATOM 3999 CB BPRO C 8 30.184 -44.766 40.128 0.50 37.89 C ANISOU 3999 CB BPRO C 8 8399 3759 2238 -524 -318 -262 C ATOM 4000 CG APRO C 8 31.523 -45.051 42.014 0.50 39.39 C ANISOU 4000 CG APRO C 8 9194 3673 2100 -807 -756 -204 C ATOM 4001 CG BPRO C 8 30.021 -44.515 41.590 0.50 40.59 C ANISOU 4001 CG BPRO C 8 9275 3929 2218 -561 -306 -318 C ATOM 4002 CD APRO C 8 32.815 -44.318 42.182 0.50 40.18 C ANISOU 4002 CD APRO C 8 9469 3579 2220 -969 -1160 -154 C ATOM 4003 CD BPRO C 8 31.376 -44.032 42.069 0.50 39.75 C ANISOU 4003 CD BPRO C 8 9431 3614 2057 -752 -727 -277 C ATOM 4004 N PRO C 9 32.540 -45.507 37.703 1.00 30.21 N ANISOU 4004 N PRO C 9 6554 2946 1980 -698 -838 -22 N ATOM 4005 CA APRO C 9 32.900 -44.979 36.382 0.50 28.67 C ANISOU 4005 CA APRO C 9 6037 2813 2044 -649 -868 7 C ATOM 4006 CA BPRO C 9 33.008 -44.893 36.464 0.50 28.60 C ANISOU 4006 CA BPRO C 9 6060 2782 2025 -664 -900 10 C ATOM 4007 C PRO C 9 32.022 -43.830 35.993 1.00 30.11 C ANISOU 4007 C PRO C 9 6273 2985 2181 -509 -666 -105 C ATOM 4008 O PRO C 9 30.815 -43.866 36.261 1.00 32.32 O ANISOU 4008 O PRO C 9 6634 3315 2332 -389 -387 -189 O ATOM 4009 CB APRO C 9 32.629 -46.169 35.450 0.50 27.35 C ANISOU 4009 CB APRO C 9 5475 2842 2075 -590 -736 56 C ATOM 4010 CB BPRO C 9 33.101 -46.093 35.508 0.50 27.03 C ANISOU 4010 CB BPRO C 9 5447 2762 2059 -637 -845 88 C ATOM 4011 CG APRO C 9 31.487 -46.918 36.104 0.50 27.20 C ANISOU 4011 CG APRO C 9 5559 2889 1885 -535 -504 3 C ATOM 4012 CG BPRO C 9 32.346 -47.248 36.237 0.50 28.69 C ANISOU 4012 CG BPRO C 9 5734 3039 2127 -631 -699 72 C ATOM 4013 CD APRO C 9 31.670 -46.706 37.595 0.50 27.91 C ANISOU 4013 CD APRO C 9 6086 2820 1700 -630 -607 -20 C ATOM 4014 CD BPRO C 9 32.633 -46.981 37.662 0.50 28.57 C ANISOU 4014 CD BPRO C 9 6141 2857 1858 -740 -838 58 C ATOM 4015 N TYR C 10 32.571 -42.845 35.284 1.00 26.55 N ANISOU 4015 N TYR C 10 5741 2483 1862 -513 -789 -91 N ATOM 4016 CA TYR C 10 31.861 -41.630 34.931 1.00 27.12 C ANISOU 4016 CA TYR C 10 5888 2518 1900 -391 -641 -190 C ATOM 4017 C TYR C 10 31.751 -41.503 33.398 1.00 24.99 C ANISOU 4017 C TYR C 10 5209 2388 1896 -309 -559 -161 C ATOM 4018 O TYR C 10 32.732 -41.262 32.693 1.00 24.79 O ANISOU 4018 O TYR C 10 5008 2358 2052 -380 -751 -74 O ATOM 4019 CB TYR C 10 32.582 -40.424 35.559 1.00 29.52 C ANISOU 4019 CB TYR C 10 6539 2595 2083 -482 -885 -204 C ATOM 4020 CG TYR C 10 31.905 -39.105 35.325 1.00 29.24 C ANISOU 4020 CG TYR C 10 6641 2482 1988 -358 -755 -311 C ATOM 4021 CD1 TYR C 10 32.465 -38.167 34.477 1.00 30.93 C ANISOU 4021 CD1 TYR C 10 6729 2654 2368 -379 -902 -277 C ATOM 4022 CD2 TYR C 10 30.712 -38.782 35.969 1.00 32.64 C ANISOU 4022 CD2 TYR C 10 7329 2872 2199 -213 -479 -437 C ATOM 4023 CE1 TYR C 10 31.876 -36.951 34.269 1.00 30.32 C ANISOU 4023 CE1 TYR C 10 6787 2493 2242 -268 -802 -371 C ATOM 4024 CE2 TYR C 10 30.098 -37.557 35.772 1.00 33.44 C ANISOU 4024 CE2 TYR C 10 7564 2888 2256 -83 -355 -532 C ATOM 4025 CZ TYR C 10 30.683 -36.647 34.905 1.00 34.60 C ANISOU 4025 CZ TYR C 10 7584 2989 2573 -114 -527 -502 C ATOM 4026 OH TYR C 10 30.082 -35.445 34.666 1.00 38.71 O ANISOU 4026 OH TYR C 10 8225 3419 3062 15 -416 -591 O ATOM 4027 N THR C 11 30.533 -41.654 32.888 1.00 24.92 N ANISOU 4027 N THR C 11 5055 2502 1912 -161 -271 -221 N ATOM 4028 CA THR C 11 30.266 -41.503 31.468 1.00 20.54 C ANISOU 4028 CA THR C 11 4162 2067 1577 -81 -184 -202 C ATOM 4029 C THR C 11 30.446 -40.017 31.041 1.00 21.40 C ANISOU 4029 C THR C 11 4338 2071 1721 -53 -252 -237 C ATOM 4030 O THR C 11 31.005 -39.760 29.979 1.00 20.70 O ANISOU 4030 O THR C 11 4020 2025 1822 -73 -343 -176 O ATOM 4031 CB THR C 11 28.873 -42.000 31.172 1.00 21.89 C ANISOU 4031 CB THR C 11 4197 2367 1754 50 108 -242 C ATOM 4032 OG1 THR C 11 28.835 -43.434 31.404 1.00 24.61 O ANISOU 4032 OG1 THR C 11 4443 2810 2097 3 130 -189 O ATOM 4033 CG2 THR C 11 28.471 -41.717 29.713 1.00 23.02 C ANISOU 4033 CG2 THR C 11 4034 2610 2103 131 189 -227 C ATOM 4034 N GLY C 12 29.962 -39.056 31.828 1.00 22.70 N ANISOU 4034 N GLY C 12 4823 2097 1704 0 -196 -330 N ATOM 4035 CA GLY C 12 30.022 -37.658 31.455 1.00 22.84 C ANISOU 4035 CA GLY C 12 4927 2004 1747 38 -251 -370 C ATOM 4036 C GLY C 12 28.902 -37.260 30.549 1.00 21.69 C ANISOU 4036 C GLY C 12 4585 1949 1707 200 -10 -415 C ATOM 4037 O GLY C 12 28.097 -38.095 30.149 1.00 22.52 O ANISOU 4037 O GLY C 12 4468 2207 1881 273 186 -402 O ATOM 4038 N PRO C 13 28.866 -35.963 30.211 1.00 22.99 N ANISOU 4038 N PRO C 13 4833 2006 1894 247 -47 -455 N ATOM 4039 CA PRO C 13 27.740 -35.386 29.473 1.00 24.07 C ANISOU 4039 CA PRO C 13 4834 2192 2120 409 173 -501 C ATOM 4040 C PRO C 13 27.811 -35.540 27.983 1.00 22.72 C ANISOU 4040 C PRO C 13 4278 2161 2194 405 155 -427 C ATOM 4041 O PRO C 13 26.803 -35.414 27.311 1.00 22.04 O ANISOU 4041 O PRO C 13 4022 2149 2202 523 337 -439 O ATOM 4042 CB PRO C 13 27.826 -33.903 29.813 1.00 25.19 C ANISOU 4042 CB PRO C 13 5274 2130 2168 446 98 -573 C ATOM 4043 CG PRO C 13 29.266 -33.653 30.089 1.00 26.25 C ANISOU 4043 CG PRO C 13 5547 2149 2277 260 -238 -518 C ATOM 4044 CD PRO C 13 29.790 -34.922 30.714 1.00 23.92 C ANISOU 4044 CD PRO C 13 5244 1921 1924 149 -303 -464 C ATOM 4045 N CYS C 14 28.975 -35.848 27.434 1.00 20.35 N ANISOU 4045 N CYS C 14 3833 1897 2004 272 -57 -338 N ATOM 4046 CA CYS C 14 29.041 -35.983 25.981 1.00 19.97 C ANISOU 4046 CA CYS C 14 3452 1972 2165 278 -53 -270 C ATOM 4047 C CYS C 14 28.449 -37.289 25.532 1.00 18.84 C ANISOU 4047 C CYS C 14 3078 1997 2083 313 98 -241 C ATOM 4048 O CYS C 14 28.312 -38.246 26.313 1.00 17.86 O ANISOU 4048 O CYS C 14 3013 1907 1865 295 149 -246 O ATOM 4049 CB CYS C 14 30.458 -35.776 25.469 1.00 17.75 C ANISOU 4049 CB CYS C 14 3085 1667 1990 146 -296 -170 C ATOM 4050 SG CYS C 14 31.076 -34.107 25.603 1.00 21.60 S ANISOU 4050 SG CYS C 14 3779 1963 2465 94 -498 -174 S ATOM 4051 N LYS C 15 28.131 -37.367 24.242 1.00 16.92 N ANISOU 4051 N LYS C 15 2584 1852 1993 350 149 -201 N ATOM 4052 CA LYS C 15 27.292 -38.436 23.712 1.00 16.23 C ANISOU 4052 CA LYS C 15 2303 1901 1963 396 296 -180 C ATOM 4053 C LYS C 15 27.946 -39.398 22.798 1.00 16.82 C ANISOU 4053 C LYS C 15 2181 2074 2137 335 229 -101 C ATOM 4054 O LYS C 15 27.275 -40.064 21.995 1.00 16.42 O ANISOU 4054 O LYS C 15 1968 2116 2155 370 317 -76 O ATOM 4055 CB LYS C 15 25.966 -37.874 23.211 1.00 15.98 C ANISOU 4055 CB LYS C 15 2195 1884 1991 513 453 -207 C ATOM 4056 CG LYS C 15 25.050 -37.397 24.291 1.00 18.87 C ANISOU 4056 CG LYS C 15 2741 2181 2248 610 605 -276 C ATOM 4057 CD LYS C 15 23.715 -36.826 23.871 1.00 19.57 C ANISOU 4057 CD LYS C 15 2734 2278 2423 741 775 -281 C ATOM 4058 CE LYS C 15 22.914 -36.353 24.991 1.00 20.80 C ANISOU 4058 CE LYS C 15 3081 2356 2467 857 951 -340 C ATOM 4059 NZ LYS C 15 21.690 -35.697 24.620 1.00 22.82 N ANISOU 4059 NZ LYS C 15 3236 2605 2831 998 1118 -330 N ATOM 4060 N ALA C 16 29.247 -39.567 22.813 1.00 14.47 N ANISOU 4060 N ALA C 16 1883 1756 1858 246 76 -46 N ATOM 4061 CA ALA C 16 29.950 -40.642 22.135 1.00 14.10 C ANISOU 4061 CA ALA C 16 1676 1793 1890 206 39 33 C ATOM 4062 C ALA C 16 29.658 -41.944 22.908 1.00 16.25 C ANISOU 4062 C ALA C 16 1981 2110 2082 194 91 23 C ATOM 4063 O ALA C 16 29.153 -41.950 24.035 1.00 16.88 O ANISOU 4063 O ALA C 16 2217 2153 2044 198 134 -30 O ATOM 4064 CB ALA C 16 31.396 -40.337 22.003 1.00 16.82 C ANISOU 4064 CB ALA C 16 1996 2094 2300 127 -125 116 C ATOM 4065 N ARG C 17 30.006 -43.052 22.237 1.00 15.64 N ANISOU 4065 N ARG C 17 1767 2109 2069 184 92 81 N ATOM 4066 CA ARG C 17 30.056 -44.378 22.893 1.00 16.23 C ANISOU 4066 CA ARG C 17 1862 2216 2088 155 98 95 C ATOM 4067 C ARG C 17 31.456 -44.873 22.734 1.00 16.95 C ANISOU 4067 C ARG C 17 1892 2298 2249 104 -22 180 C ATOM 4068 O ARG C 17 31.785 -45.599 21.775 1.00 16.75 O ANISOU 4068 O ARG C 17 1738 2324 2303 131 3 231 O ATOM 4069 CB ARG C 17 28.994 -45.323 22.321 1.00 16.92 C ANISOU 4069 CB ARG C 17 1861 2385 2184 199 215 87 C ATOM 4070 CG ARG C 17 28.788 -46.636 23.114 1.00 20.20 C ANISOU 4070 CG ARG C 17 2318 2828 2529 167 229 96 C ATOM 4071 CD ARG C 17 29.770 -47.750 22.848 1.00 22.97 C ANISOU 4071 CD ARG C 17 2616 3192 2922 137 152 157 C ATOM 4072 NE ARG C 17 29.729 -48.214 21.475 1.00 20.61 N ANISOU 4072 NE ARG C 17 2200 2931 2702 180 183 185 N ATOM 4073 CZ ARG C 17 28.975 -49.227 20.994 1.00 20.84 C ANISOU 4073 CZ ARG C 17 2199 2998 2722 194 231 189 C ATOM 4074 NH1 ARG C 17 28.159 -49.875 21.758 1.00 23.76 N ANISOU 4074 NH1 ARG C 17 2612 3387 3028 167 261 179 N ATOM 4075 NH2 ARG C 17 29.049 -49.531 19.712 1.00 24.36 N ANISOU 4075 NH2 ARG C 17 2585 3453 3218 232 242 212 N ATOM 4076 N ILE C 18 32.328 -44.451 23.655 1.00 14.49 N ANISOU 4076 N ILE C 18 1683 1909 1913 32 -156 208 N ATOM 4077 CA ILE C 18 33.712 -44.799 23.602 1.00 13.70 C ANISOU 4077 CA ILE C 18 1505 1788 1910 -23 -286 319 C ATOM 4078 C ILE C 18 33.939 -45.844 24.695 1.00 16.59 C ANISOU 4078 C ILE C 18 1957 2138 2208 -79 -346 335 C ATOM 4079 O ILE C 18 33.643 -45.599 25.856 1.00 18.09 O ANISOU 4079 O ILE C 18 2336 2268 2269 -129 -391 285 O ATOM 4080 CB ILE C 18 34.601 -43.618 23.807 1.00 17.40 C ANISOU 4080 CB ILE C 18 2011 2171 2430 -89 -438 374 C ATOM 4081 CG1 ILE C 18 34.399 -42.627 22.637 1.00 18.09 C ANISOU 4081 CG1 ILE C 18 2002 2278 2593 -36 -379 369 C ATOM 4082 CG2 ILE C 18 36.039 -44.057 23.834 1.00 20.22 C ANISOU 4082 CG2 ILE C 18 2257 2508 2917 -151 -578 523 C ATOM 4083 CD1 ILE C 18 34.903 -41.272 22.932 1.00 22.48 C ANISOU 4083 CD1 ILE C 18 2642 2735 3165 -100 -520 394 C ATOM 4084 N ILE C 19 34.443 -47.022 24.347 1.00 15.28 N ANISOU 4084 N ILE C 19 1674 2016 2117 -65 -343 402 N ATOM 4085 CA ILE C 19 34.644 -48.088 25.324 1.00 15.41 C ANISOU 4085 CA ILE C 19 1762 2015 2078 -117 -405 424 C ATOM 4086 C ILE C 19 35.964 -47.839 26.059 1.00 17.97 C ANISOU 4086 C ILE C 19 2111 2252 2465 -216 -613 534 C ATOM 4087 O ILE C 19 37.056 -47.789 25.469 1.00 19.83 O ANISOU 4087 O ILE C 19 2186 2481 2868 -215 -681 655 O ATOM 4088 CB ILE C 19 34.644 -49.428 24.654 1.00 15.57 C ANISOU 4088 CB ILE C 19 1662 2097 2155 -58 -329 454 C ATOM 4089 CG1 ILE C 19 33.287 -49.653 23.996 1.00 18.52 C ANISOU 4089 CG1 ILE C 19 2034 2540 2465 12 -166 362 C ATOM 4090 CG2 ILE C 19 34.973 -50.522 25.703 1.00 18.84 C ANISOU 4090 CG2 ILE C 19 2148 2482 2527 -121 -419 492 C ATOM 4091 CD1 ILE C 19 33.157 -50.869 23.079 1.00 22.34 C ANISOU 4091 CD1 ILE C 19 2429 3068 2991 76 -92 381 C ATOM 4092 N ARG C 20 35.875 -47.627 27.365 1.00 16.32 N ANISOU 4092 N ARG C 20 2112 1966 2124 -307 -721 505 N ATOM 4093 CA ARG C 20 37.033 -47.424 28.190 1.00 17.86 C ANISOU 4093 CA ARG C 20 2369 2057 2360 -426 -956 614 C ATOM 4094 C ARG C 20 37.044 -48.480 29.324 1.00 17.30 C ANISOU 4094 C ARG C 20 2431 1955 2189 -496 -1032 624 C ATOM 4095 O ARG C 20 36.048 -49.198 29.527 1.00 17.41 O ANISOU 4095 O ARG C 20 2507 2027 2081 -452 -888 534 O ATOM 4096 CB ARG C 20 37.029 -46.009 28.806 1.00 17.59 C ANISOU 4096 CB ARG C 20 2539 1913 2230 -498 -1071 577 C ATOM 4097 CG ARG C 20 37.222 -44.887 27.747 1.00 16.91 C ANISOU 4097 CG ARG C 20 2324 1838 2264 -455 -1047 595 C ATOM 4098 CD ARG C 20 38.666 -44.798 27.353 1.00 19.14 C ANISOU 4098 CD ARG C 20 2414 2091 2765 -517 -1218 784 C ATOM 4099 NE ARG C 20 38.872 -43.786 26.310 1.00 21.23 N ANISOU 4099 NE ARG C 20 2545 2374 3146 -481 -1187 818 N ATOM 4100 CZ ARG C 20 39.018 -42.486 26.511 1.00 22.53 C ANISOU 4100 CZ ARG C 20 2827 2444 3290 -548 -1314 819 C ATOM 4101 NH1 ARG C 20 39.008 -41.989 27.726 1.00 22.75 N ANISOU 4101 NH1 ARG C 20 3132 2338 3173 -654 -1486 783 N ATOM 4102 NH2 ARG C 20 39.192 -41.676 25.467 1.00 23.25 N ANISOU 4102 NH2 ARG C 20 2773 2565 3498 -511 -1273 859 N ATOM 4103 N TYR C 21 38.137 -48.518 30.086 1.00 19.49 N ANISOU 4103 N TYR C 21 2754 2132 2517 -616 -1271 746 N ATOM 4104 CA TYR C 21 38.256 -49.423 31.208 1.00 19.95 C ANISOU 4104 CA TYR C 21 2957 2142 2483 -702 -1381 771 C ATOM 4105 C TYR C 21 38.237 -48.640 32.512 1.00 22.43 C ANISOU 4105 C TYR C 21 3602 2318 2603 -831 -1549 738 C ATOM 4106 O TYR C 21 38.736 -47.528 32.581 1.00 23.37 O ANISOU 4106 O TYR C 21 3789 2347 2745 -892 -1691 773 O ATOM 4107 CB TYR C 21 39.550 -50.235 31.139 1.00 21.71 C ANISOU 4107 CB TYR C 21 2990 2341 2920 -746 -1546 956 C ATOM 4108 CG TYR C 21 39.548 -51.281 30.067 1.00 21.86 C ANISOU 4108 CG TYR C 21 2753 2470 3083 -612 -1375 981 C ATOM 4109 CD1 TYR C 21 39.796 -50.940 28.760 1.00 22.03 C ANISOU 4109 CD1 TYR C 21 2551 2556 3264 -505 -1254 1012 C ATOM 4110 CD2 TYR C 21 39.285 -52.617 30.375 1.00 22.94 C ANISOU 4110 CD2 TYR C 21 2902 2633 3181 -596 -1337 972 C ATOM 4111 CE1 TYR C 21 39.747 -51.893 27.740 1.00 25.74 C ANISOU 4111 CE1 TYR C 21 2839 3109 3832 -371 -1084 1021 C ATOM 4112 CE2 TYR C 21 39.220 -53.592 29.374 1.00 23.63 C ANISOU 4112 CE2 TYR C 21 2801 2801 3376 -467 -1181 981 C ATOM 4113 CZ TYR C 21 39.483 -53.232 28.082 1.00 25.75 C ANISOU 4113 CZ TYR C 21 2873 3122 3787 -355 -1059 1005 C ATOM 4114 OH TYR C 21 39.454 -54.162 27.081 1.00 29.63 O ANISOU 4114 OH TYR C 21 3226 3672 4362 -223 -907 1011 O ATOM 4115 N PHE C 22 37.676 -49.245 33.548 1.00 21.06 N ANISOU 4115 N PHE C 22 3652 2119 2231 -875 -1539 679 N ATOM 4116 CA PHE C 22 37.756 -48.751 34.927 1.00 22.25 C ANISOU 4116 CA PHE C 22 4168 2119 2167 -1008 -1715 661 C ATOM 4117 C PHE C 22 38.090 -49.876 35.863 1.00 25.39 C ANISOU 4117 C PHE C 22 4661 2475 2508 -1109 -1849 732 C ATOM 4118 O PHE C 22 37.748 -51.027 35.577 1.00 23.93 O ANISOU 4118 O PHE C 22 4324 2397 2370 -1046 -1720 732 O ATOM 4119 CB PHE C 22 36.445 -48.094 35.374 1.00 26.55 C ANISOU 4119 CB PHE C 22 4983 2658 2446 -943 -1509 483 C ATOM 4120 CG PHE C 22 35.293 -49.057 35.674 1.00 23.45 C ANISOU 4120 CG PHE C 22 4631 2366 1911 -873 -1273 399 C ATOM 4121 CD1 PHE C 22 34.901 -49.286 37.002 1.00 29.34 C ANISOU 4121 CD1 PHE C 22 5715 3035 2399 -945 -1288 359 C ATOM 4122 CD2 PHE C 22 34.572 -49.656 34.657 1.00 21.88 C ANISOU 4122 CD2 PHE C 22 4162 2327 1822 -745 -1042 366 C ATOM 4123 CE1 PHE C 22 33.832 -50.144 37.305 1.00 33.04 C ANISOU 4123 CE1 PHE C 22 6212 3598 2743 -888 -1066 304 C ATOM 4124 CE2 PHE C 22 33.485 -50.491 34.950 1.00 21.92 C ANISOU 4124 CE2 PHE C 22 4202 2417 1709 -697 -844 310 C ATOM 4125 CZ PHE C 22 33.123 -50.751 36.250 1.00 26.70 C ANISOU 4125 CZ PHE C 22 5103 2960 2083 -766 -849 286 C ATOM 4126 N ATYR C 23 38.980 -49.630 36.848 0.50 26.33 N ANISOU 4126 N ATYR C 23 4987 2433 2585 -1278 -2158 830 N ATOM 4127 N BTYR C 23 38.457 -49.456 37.075 0.50 27.44 N ANISOU 4127 N BTYR C 23 5252 2574 2602 -1257 -2075 755 N ATOM 4128 CA ATYR C 23 39.491 -50.717 37.736 0.50 23.49 C ANISOU 4128 CA ATYR C 23 4703 2016 2205 -1396 -2342 933 C ATOM 4129 CA BTYR C 23 38.438 -50.330 38.235 0.50 26.51 C ANISOU 4129 CA BTYR C 23 5356 2395 2321 -1361 -2176 778 C ATOM 4130 C ATYR C 23 38.409 -50.999 38.761 0.50 25.01 C ANISOU 4130 C ATYR C 23 5240 2195 2067 -1407 -2212 798 C ATOM 4131 C BTYR C 23 37.060 -50.466 38.896 0.50 25.66 C ANISOU 4131 C BTYR C 23 5518 2323 1908 -1302 -1924 616 C ATOM 4132 O ATYR C 23 37.931 -50.075 39.386 0.50 27.23 O ANISOU 4132 O ATYR C 23 5845 2386 2114 -1429 -2191 698 O ATOM 4133 O BTYR C 23 36.516 -49.484 39.428 0.50 27.15 O ANISOU 4133 O BTYR C 23 6013 2429 1872 -1295 -1865 509 O ATOM 4134 CB ATYR C 23 40.793 -50.307 38.457 0.50 25.68 C ANISOU 4134 CB ATYR C 23 5099 2109 2550 -1591 -2746 1102 C ATOM 4135 CB BTYR C 23 39.413 -49.837 39.277 0.50 29.50 C ANISOU 4135 CB BTYR C 23 6009 2566 2631 -1560 -2544 881 C ATOM 4136 CG ATYR C 23 41.424 -51.385 39.359 0.50 29.14 C ANISOU 4136 CG ATYR C 23 5603 2471 2997 -1728 -2978 1233 C ATOM 4137 CG BTYR C 23 39.666 -50.916 40.305 0.50 35.07 C ANISOU 4137 CG BTYR C 23 6867 3213 3243 -1682 -2699 955 C ATOM 4138 CD1ATYR C 23 42.028 -52.503 38.811 0.50 27.37 C ANISOU 4138 CD1ATYR C 23 5032 2326 3042 -1687 -2992 1366 C ATOM 4139 CD1BTYR C 23 40.945 -51.391 40.543 0.50 35.64 C ANISOU 4139 CD1BTYR C 23 6828 3197 3515 -1822 -3031 1158 C ATOM 4140 CD2ATYR C 23 41.442 -51.263 40.766 0.50 32.71 C ANISOU 4140 CD2ATYR C 23 6489 2757 3183 -1897 -3192 1229 C ATOM 4141 CD2BTYR C 23 38.605 -51.502 40.993 0.50 41.07 C ANISOU 4141 CD2BTYR C 23 7853 4014 3738 -1651 -2503 837 C ATOM 4142 CE1ATYR C 23 42.609 -53.479 39.612 0.50 27.98 C ANISOU 4142 CE1ATYR C 23 5158 2327 3145 -1807 -3212 1495 C ATOM 4143 CE1BTYR C 23 41.161 -52.368 41.459 0.50 36.74 C ANISOU 4143 CE1BTYR C 23 7104 3278 3576 -1935 -3182 1229 C ATOM 4144 CE2ATYR C 23 42.028 -52.233 41.573 0.50 32.32 C ANISOU 4144 CE2ATYR C 23 6502 2632 3147 -2032 -3423 1359 C ATOM 4145 CE2BTYR C 23 38.808 -52.486 41.912 0.50 35.79 C ANISOU 4145 CE2BTYR C 23 7328 3294 2977 -1765 -2641 906 C ATOM 4146 CZ ATYR C 23 42.604 -53.353 40.990 0.50 32.87 C ANISOU 4146 CZ ATYR C 23 6191 2790 3508 -1986 -3434 1494 C ATOM 4147 CZ BTYR C 23 40.089 -52.911 42.122 0.50 34.87 C ANISOU 4147 CZ BTYR C 23 7112 3082 3055 -1907 -2986 1097 C ATOM 4148 OH ATYR C 23 43.192 -54.337 41.768 0.50 35.23 O ANISOU 4148 OH ATYR C 23 6536 3010 3841 -2114 -3669 1632 O ATOM 4149 OH BTYR C 23 40.334 -53.891 42.993 0.50 40.68 O ANISOU 4149 OH BTYR C 23 7976 3760 3721 -2024 -3143 1177 O ATOM 4150 N AASN C 24 38.075 -52.273 38.960 0.50 23.99 N ANISOU 4150 N AASN C 24 5053 2142 1920 -1393 -2131 809 N ATOM 4151 N BASN C 24 36.537 -51.688 38.880 0.50 22.87 N ANISOU 4151 N BASN C 24 5056 2081 1552 -1259 -1782 612 N ATOM 4152 CA AASN C 24 36.868 -52.746 39.712 0.50 27.27 C ANISOU 4152 CA AASN C 24 5709 2597 2056 -1370 -1926 693 C ATOM 4153 CA BASN C 24 35.324 -52.047 39.641 0.50 25.39 C ANISOU 4153 CA BASN C 24 5611 2435 1601 -1228 -1565 508 C ATOM 4154 C AASN C 24 36.409 -53.087 41.161 0.50 36.98 C ANISOU 4154 C AASN C 24 7342 3740 2968 -1473 -1953 661 C ATOM 4155 C BASN C 24 35.503 -52.964 40.842 0.50 33.29 C ANISOU 4155 C BASN C 24 6842 3364 2442 -1363 -1705 567 C ATOM 4156 O AASN C 24 35.976 -54.243 41.377 0.50 28.79 O ANISOU 4156 O AASN C 24 6259 2780 1900 -1470 -1866 676 O ATOM 4157 O BASN C 24 35.569 -54.186 40.675 0.50 28.30 O ANISOU 4157 O BASN C 24 6024 2809 1919 -1370 -1708 634 O ATOM 4158 CB AASN C 24 36.132 -53.782 38.878 0.50 28.87 C ANISOU 4158 CB AASN C 24 5623 2978 2366 -1239 -1677 665 C ATOM 4159 CB BASN C 24 34.299 -52.730 38.729 0.50 29.53 C ANISOU 4159 CB BASN C 24 5857 3149 2214 -1078 -1262 455 C ATOM 4160 CG AASN C 24 34.668 -53.857 39.242 0.50 33.33 C ANISOU 4160 CG AASN C 24 6347 3619 2699 -1167 -1386 539 C ATOM 4161 CG BASN C 24 33.032 -53.132 39.494 0.50 28.47 C ANISOU 4161 CG BASN C 24 5923 3061 1834 -1049 -1030 382 C ATOM 4162 OD1AASN C 24 34.163 -54.884 39.649 0.50 33.93 O ANISOU 4162 OD1AASN C 24 6448 3746 2698 -1183 -1314 551 O ATOM 4163 OD1BASN C 24 32.881 -52.799 40.681 0.50 30.25 O ANISOU 4163 OD1BASN C 24 6515 3178 1799 -1120 -1059 351 O ATOM 4164 ND2AASN C 24 33.980 -52.744 39.080 0.50 33.30 N ANISOU 4164 ND2AASN C 24 6437 3619 2595 -1082 -1215 430 N ATOM 4165 ND2BASN C 24 32.098 -53.764 38.798 0.50 25.69 N ANISOU 4165 ND2BASN C 24 5342 2861 1557 -943 -795 359 N ATOM 4166 N AALA C 25 36.364 -52.141 42.099 0.50 44.67 N ANISOU 4166 N AALA C 25 8718 4564 3691 -1549 -2035 607 N ATOM 4167 N BALA C 25 35.557 -52.358 42.033 0.50 43.67 N ANISOU 4167 N BALA C 25 8583 4521 3489 -1468 -1819 539 N ATOM 4168 CA AALA C 25 35.958 -52.488 43.472 0.50 50.49 C ANISOU 4168 CA AALA C 25 9869 5211 4105 -1643 -2049 582 C ATOM 4169 CA BALA C 25 35.271 -53.034 43.315 0.50 50.17 C ANISOU 4169 CA BALA C 25 9734 5280 4048 -1570 -1849 547 C ATOM 4170 C AALA C 25 36.803 -53.667 43.902 0.50 55.38 C ANISOU 4170 C AALA C 25 10426 5794 4822 -1788 -2314 733 C ATOM 4171 C BALA C 25 36.250 -54.064 43.832 0.50 51.92 C ANISOU 4171 C BALA C 25 9943 5434 4351 -1733 -2158 698 C ATOM 4172 O AALA C 25 38.012 -53.649 43.720 0.50 60.63 O ANISOU 4172 O AALA C 25 10957 6378 5700 -1887 -2622 867 O ATOM 4173 O BALA C 25 37.459 -53.856 43.888 0.50 57.62 O ANISOU 4173 O BALA C 25 10640 6037 5215 -1853 -2489 815 O ATOM 4174 CB AALA C 25 34.468 -52.859 43.550 0.50 51.78 C ANISOU 4174 CB AALA C 25 10067 5513 4095 -1507 -1650 467 C ATOM 4175 CB BALA C 25 33.879 -53.646 43.301 0.50 48.17 C ANISOU 4175 CB BALA C 25 9445 5181 3678 -1448 -1482 467 C ATOM 4176 N ALYS C 26 36.179 -54.706 44.449 0.50 49.22 N ANISOU 4176 N ALYS C 26 9720 5073 3908 -1799 -2197 729 N ATOM 4177 N BLYS C 26 35.697 -55.184 44.264 0.50 44.91 N ANISOU 4177 N BLYS C 26 9077 4615 3371 -1744 -2054 710 N ATOM 4178 CA ALYS C 26 36.942 -55.837 44.904 0.50 46.33 C ANISOU 4178 CA ALYS C 26 9315 4661 3626 -1936 -2452 872 C ATOM 4179 CA BLYS C 26 36.472 -56.060 45.093 0.50 46.54 C ANISOU 4179 CA BLYS C 26 9401 4722 3561 -1917 -2345 839 C ATOM 4180 C ALYS C 26 37.003 -56.942 43.852 0.50 43.04 C ANISOU 4180 C ALYS C 26 8434 4404 3515 -1841 -2369 932 C ATOM 4181 C BLYS C 26 37.265 -56.985 44.188 0.50 42.63 C ANISOU 4181 C BLYS C 26 8464 4299 3435 -1900 -2471 964 C ATOM 4182 O ALYS C 26 37.025 -58.121 44.215 0.50 40.54 O ANISOU 4182 O ALYS C 26 8094 4104 3205 -1897 -2424 1002 O ATOM 4183 O BLYS C 26 38.098 -57.811 44.694 0.50 31.92 O ANISOU 4183 O BLYS C 26 7113 2861 2155 -2033 -2746 1103 O ATOM 4184 CB ALYS C 26 36.360 -56.408 46.211 0.50 44.26 C ANISOU 4184 CB ALYS C 26 9440 4344 3031 -2032 -2423 856 C ATOM 4185 CB BLYS C 26 35.541 -56.851 46.006 0.50 42.14 C ANISOU 4185 CB BLYS C 26 9084 4196 2731 -1943 -2182 806 C ATOM 4186 CG ALYS C 26 35.958 -55.371 47.255 0.50 44.14 C ANISOU 4186 CG ALYS C 26 9947 4185 2638 -2079 -2393 759 C ATOM 4187 CG BLYS C 26 34.356 -56.080 46.593 0.50 41.18 C ANISOU 4187 CG BLYS C 26 9300 4074 2270 -1868 -1881 663 C ATOM 4188 CD ALYS C 26 35.482 -56.049 48.538 0.50 46.24 C ANISOU 4188 CD ALYS C 26 10594 4396 2579 -2180 -2369 766 C ATOM 4189 CD BLYS C 26 34.782 -55.077 47.656 0.50 45.58 C ANISOU 4189 CD BLYS C 26 10360 4411 2548 -1985 -2070 636 C ATOM 4190 CE ALYS C 26 35.064 -55.037 49.616 0.50 50.35 C ANISOU 4190 CE ALYS C 26 11691 4754 2684 -2211 -2311 664 C ATOM 4191 CE BLYS C 26 33.871 -55.132 48.897 0.50 48.35 C ANISOU 4191 CE BLYS C 26 11181 4710 2481 -2003 -1878 571 C ATOM 4192 NZ ALYS C 26 34.752 -55.668 50.933 0.50 53.49 N ANISOU 4192 NZ ALYS C 26 12509 5071 2745 -2330 -2322 689 N ATOM 4193 NZ BLYS C 26 34.336 -56.112 49.933 0.50 50.14 N ANISOU 4193 NZ BLYS C 26 11634 4844 2575 -2195 -2119 682 N ATOM 4194 N AALA C 27 37.027 -56.624 42.556 0.50 39.79 N ANISOU 4194 N AALA C 27 7674 4099 3347 -1699 -2241 906 N ATOM 4195 N BALA C 27 37.014 -56.764 42.879 0.50 42.47 N ANISOU 4195 N BALA C 27 8093 4415 3629 -1734 -2272 915 N ATOM 4196 CA AALA C 27 37.248 -57.726 41.642 0.50 36.79 C ANISOU 4196 CA AALA C 27 6915 3828 3236 -1623 -2207 975 C ATOM 4197 CA BALA C 27 37.303 -57.679 41.763 0.50 38.10 C ANISOU 4197 CA BALA C 27 7114 3977 3385 -1640 -2232 980 C ATOM 4198 C AALA C 27 38.741 -57.895 41.362 0.50 39.33 C ANISOU 4198 C AALA C 27 7035 4064 3843 -1687 -2512 1142 C ATOM 4199 C BALA C 27 38.452 -57.181 40.913 0.50 38.04 C ANISOU 4199 C BALA C 27 6841 3937 3674 -1618 -2394 1072 C ATOM 4200 O AALA C 27 39.201 -58.981 41.023 0.50 34.63 O ANISOU 4200 O AALA C 27 6218 3496 3443 -1669 -2574 1240 O ATOM 4201 O BALA C 27 38.301 -56.948 39.720 0.50 43.70 O ANISOU 4201 O BALA C 27 7283 4759 4562 -1474 -2223 1033 O ATOM 4202 CB AALA C 27 36.422 -57.616 40.411 0.50 36.41 C ANISOU 4202 CB AALA C 27 6606 3941 3288 -1439 -1901 878 C ATOM 4203 CB BALA C 27 36.021 -57.979 40.900 0.50 30.78 C ANISOU 4203 CB BALA C 27 6009 3231 2456 -1469 -1866 864 C ATOM 4204 N GLY C 28 39.522 -56.855 41.641 1.00 42.21 N ANISOU 4204 N GLY C 28 7509 4305 4224 -1776 -2726 1193 N ATOM 4205 CA GLY C 28 40.938 -56.866 41.280 1.00 43.82 C ANISOU 4205 CA GLY C 28 7475 4436 4740 -1829 -3001 1379 C ATOM 4206 C GLY C 28 41.181 -56.992 39.802 1.00 43.86 C ANISOU 4206 C GLY C 28 7049 4565 5050 -1655 -2839 1402 C ATOM 4207 O GLY C 28 42.198 -57.553 39.338 1.00 42.96 O ANISOU 4207 O GLY C 28 6654 4437 5231 -1640 -2971 1566 O ATOM 4208 N LEU C 29 40.239 -56.403 39.076 1.00 35.05 N ANISOU 4208 N LEU C 29 5898 3563 3856 -1519 -2549 1244 N ATOM 4209 CA LEU C 29 40.205 -56.471 37.662 1.00 34.08 C ANISOU 4209 CA LEU C 29 5433 3564 3952 -1347 -2351 1229 C ATOM 4210 C LEU C 29 39.505 -55.233 37.005 1.00 33.78 C ANISOU 4210 C LEU C 29 5405 3588 3841 -1254 -2148 1091 C ATOM 4211 O LEU C 29 38.498 -54.639 37.452 1.00 32.09 O ANISOU 4211 O LEU C 29 5434 3383 3377 -1252 -2015 949 O ATOM 4212 CB LEU C 29 39.669 -57.833 37.153 1.00 36.15 C ANISOU 4212 CB LEU C 29 5541 3934 4261 -1239 -2172 1201 C ATOM 4213 CG LEU C 29 38.217 -58.355 37.282 1.00 35.88 C ANISOU 4213 CG LEU C 29 5632 3997 4005 -1189 -1929 1054 C ATOM 4214 CD1 LEU C 29 37.352 -57.250 36.850 1.00 28.66 C ANISOU 4214 CD1 LEU C 29 4761 3146 2982 -1113 -1723 917 C ATOM 4215 CD2 LEU C 29 38.008 -59.554 36.445 1.00 38.51 C ANISOU 4215 CD2 LEU C 29 5747 4414 4471 -1078 -1807 1064 C ATOM 4216 N CYS C 30 40.006 -54.954 35.846 1.00 32.77 N ANISOU 4216 N CYS C 30 4989 3513 3950 -1154 -2095 1140 N ATOM 4217 CA CYS C 30 39.525 -53.853 35.100 1.00 24.34 C ANISOU 4217 CA CYS C 30 3885 2499 2865 -1068 -1935 1041 C ATOM 4218 C CYS C 30 38.321 -54.351 34.248 1.00 20.83 C ANISOU 4218 C CYS C 30 3339 2203 2373 -912 -1618 906 C ATOM 4219 O CYS C 30 38.298 -55.493 33.780 1.00 25.39 O ANISOU 4219 O CYS C 30 3761 2841 3046 -847 -1548 935 O ATOM 4220 CB CYS C 30 40.675 -53.388 34.285 1.00 30.21 C ANISOU 4220 CB CYS C 30 4368 3225 3886 -1049 -2039 1181 C ATOM 4221 SG CYS C 30 41.891 -52.634 35.441 1.00 38.15 S ANISOU 4221 SG CYS C 30 5545 4034 4914 -1271 -2449 1344 S ATOM 4222 N GLN C 31 37.307 -53.493 34.130 1.00 20.95 N ANISOU 4222 N GLN C 31 3467 2259 2236 -862 -1446 767 N ATOM 4223 CA GLN C 31 36.081 -53.764 33.429 1.00 18.39 C ANISOU 4223 CA GLN C 31 3070 2057 1859 -739 -1174 652 C ATOM 4224 C GLN C 31 35.832 -52.629 32.424 1.00 19.17 C ANISOU 4224 C GLN C 31 3062 2198 2022 -646 -1053 593 C ATOM 4225 O GLN C 31 36.382 -51.532 32.564 1.00 20.00 O ANISOU 4225 O GLN C 31 3228 2229 2143 -691 -1166 612 O ATOM 4226 CB GLN C 31 34.886 -53.901 34.390 1.00 20.61 C ANISOU 4226 CB GLN C 31 3599 2350 1883 -766 -1058 554 C ATOM 4227 CG GLN C 31 34.912 -55.089 35.327 1.00 24.51 C ANISOU 4227 CG GLN C 31 4204 2818 2290 -854 -1141 604 C ATOM 4228 CD GLN C 31 33.524 -55.640 35.553 1.00 35.83 C ANISOU 4228 CD GLN C 31 5705 4339 3570 -815 -924 528 C ATOM 4229 OE1 GLN C 31 32.738 -55.104 36.346 1.00 39.31 O ANISOU 4229 OE1 GLN C 31 6370 4765 3801 -830 -821 459 O ATOM 4230 NE2 GLN C 31 33.195 -56.707 34.804 1.00 35.33 N ANISOU 4230 NE2 GLN C 31 5446 4361 3615 -756 -843 549 N ATOM 4231 N THR C 32 35.059 -52.887 31.382 1.00 16.08 N ANISOU 4231 N THR C 32 2515 1914 1679 -527 -850 535 N ATOM 4232 CA THR C 32 34.712 -51.866 30.404 1.00 15.01 C ANISOU 4232 CA THR C 32 2285 1821 1597 -441 -731 478 C ATOM 4233 C THR C 32 33.469 -51.068 30.826 1.00 16.28 C ANISOU 4233 C THR C 32 2616 1993 1578 -417 -587 358 C ATOM 4234 O THR C 32 32.593 -51.564 31.577 1.00 17.63 O ANISOU 4234 O THR C 32 2919 2183 1598 -431 -499 313 O ATOM 4235 CB THR C 32 34.459 -52.518 29.028 1.00 17.11 C ANISOU 4235 CB THR C 32 2325 2182 1994 -328 -594 480 C ATOM 4236 OG1 THR C 32 33.413 -53.494 29.169 1.00 15.36 O ANISOU 4236 OG1 THR C 32 2137 2018 1681 -310 -481 433 O ATOM 4237 CG2 THR C 32 35.735 -53.155 28.474 1.00 21.56 C ANISOU 4237 CG2 THR C 32 2718 2728 2748 -313 -694 602 C ATOM 4238 N PHE C 33 33.386 -49.857 30.297 1.00 16.06 N ANISOU 4238 N PHE C 33 2569 1954 1580 -373 -549 317 N ATOM 4239 CA PHE C 33 32.217 -49.007 30.483 1.00 15.99 C ANISOU 4239 CA PHE C 33 2682 1954 1441 -317 -389 210 C ATOM 4240 C PHE C 33 32.142 -48.055 29.321 1.00 16.33 C ANISOU 4240 C PHE C 33 2581 2023 1601 -240 -330 188 C ATOM 4241 O PHE C 33 33.101 -47.906 28.566 1.00 16.19 O ANISOU 4241 O PHE C 33 2415 2000 1736 -247 -430 258 O ATOM 4242 CB PHE C 33 32.226 -48.256 31.817 1.00 17.61 C ANISOU 4242 CB PHE C 33 3198 2041 1453 -384 -457 168 C ATOM 4243 CG PHE C 33 33.114 -47.062 31.852 1.00 19.99 C ANISOU 4243 CG PHE C 33 3582 2231 1785 -433 -628 186 C ATOM 4244 CD1 PHE C 33 32.566 -45.768 31.796 1.00 19.66 C ANISOU 4244 CD1 PHE C 33 3658 2140 1672 -375 -549 101 C ATOM 4245 CD2 PHE C 33 34.480 -47.197 31.988 1.00 19.71 C ANISOU 4245 CD2 PHE C 33 3510 2125 1852 -541 -877 301 C ATOM 4246 CE1 PHE C 33 33.398 -44.631 31.856 1.00 21.20 C ANISOU 4246 CE1 PHE C 33 3951 2214 1890 -436 -734 124 C ATOM 4247 CE2 PHE C 33 35.311 -46.087 32.064 1.00 23.25 C ANISOU 4247 CE2 PHE C 33 4034 2460 2339 -608 -1064 342 C ATOM 4248 CZ PHE C 33 34.749 -44.792 31.989 1.00 21.77 C ANISOU 4248 CZ PHE C 33 3984 2221 2067 -559 -995 247 C ATOM 4249 N VAL C 34 31.007 -47.360 29.187 1.00 16.55 N ANISOU 4249 N VAL C 34 2651 2075 1564 -162 -163 103 N ATOM 4250 CA VAL C 34 30.798 -46.372 28.126 1.00 16.36 C ANISOU 4250 CA VAL C 34 2511 2068 1639 -89 -105 78 C ATOM 4251 C VAL C 34 31.173 -44.962 28.617 1.00 16.57 C ANISOU 4251 C VAL C 34 2717 1976 1604 -114 -195 44 C ATOM 4252 O VAL C 34 30.599 -44.417 29.587 1.00 19.36 O ANISOU 4252 O VAL C 34 3306 2258 1792 -104 -141 -27 O ATOM 4253 CB VAL C 34 29.361 -46.373 27.654 1.00 18.82 C ANISOU 4253 CB VAL C 34 2750 2458 1943 8 106 24 C ATOM 4254 CG1 VAL C 34 29.118 -45.193 26.700 1.00 19.04 C ANISOU 4254 CG1 VAL C 34 2697 2481 2057 76 148 -4 C ATOM 4255 CG2 VAL C 34 29.010 -47.702 26.949 1.00 19.61 C ANISOU 4255 CG2 VAL C 34 2670 2659 2120 22 160 68 C ATOM 4256 N TYR C 35 32.192 -44.405 27.987 1.00 17.80 N ANISOU 4256 N TYR C 35 2779 2098 1888 -149 -337 105 N ATOM 4257 CA TYR C 35 32.618 -43.044 28.194 1.00 17.21 C ANISOU 4257 CA TYR C 35 2838 1908 1793 -181 -450 93 C ATOM 4258 C TYR C 35 32.030 -42.170 27.079 1.00 16.81 C ANISOU 4258 C TYR C 35 2663 1896 1827 -86 -336 54 C ATOM 4259 O TYR C 35 32.085 -42.544 25.906 1.00 16.08 O ANISOU 4259 O TYR C 35 2334 1900 1876 -46 -282 98 O ATOM 4260 CB TYR C 35 34.126 -42.950 28.158 1.00 18.49 C ANISOU 4260 CB TYR C 35 2945 2009 2071 -292 -692 218 C ATOM 4261 CG TYR C 35 34.685 -41.537 28.241 1.00 17.62 C ANISOU 4261 CG TYR C 35 2949 1773 1971 -347 -851 235 C ATOM 4262 CD1 TYR C 35 34.315 -40.632 29.252 1.00 19.92 C ANISOU 4262 CD1 TYR C 35 3567 1926 2076 -371 -898 147 C ATOM 4263 CD2 TYR C 35 35.668 -41.131 27.355 1.00 19.50 C ANISOU 4263 CD2 TYR C 35 2989 2018 2404 -384 -967 353 C ATOM 4264 CE1 TYR C 35 34.871 -39.388 29.333 1.00 21.05 C ANISOU 4264 CE1 TYR C 35 3838 1935 2226 -433 -1073 169 C ATOM 4265 CE2 TYR C 35 36.191 -39.872 27.406 1.00 19.62 C ANISOU 4265 CE2 TYR C 35 3098 1916 2442 -449 -1131 387 C ATOM 4266 CZ TYR C 35 35.807 -38.994 28.409 1.00 20.74 C ANISOU 4266 CZ TYR C 35 3575 1910 2396 -481 -1202 293 C ATOM 4267 OH TYR C 35 36.344 -37.744 28.487 1.00 22.08 O ANISOU 4267 OH TYR C 35 3869 1941 2579 -556 -1393 328 O ATOM 4268 N GLY C 36 31.482 -41.020 27.437 1.00 16.79 N ANISOU 4268 N GLY C 36 2839 1808 1733 -48 -302 -26 N ATOM 4269 CA GLY C 36 30.813 -40.169 26.459 1.00 16.71 C ANISOU 4269 CA GLY C 36 2724 1825 1801 45 -193 -64 C ATOM 4270 C GLY C 36 31.715 -39.281 25.637 1.00 17.96 C ANISOU 4270 C GLY C 36 2790 1943 2091 2 -339 0 C ATOM 4271 O GLY C 36 31.223 -38.618 24.691 1.00 17.67 O ANISOU 4271 O GLY C 36 2648 1935 2133 71 -262 -18 O ATOM 4272 N GLY C 37 32.994 -39.174 26.000 1.00 17.65 N ANISOU 4272 N GLY C 37 2793 1830 2083 -116 -557 88 N ATOM 4273 CA GLY C 37 33.978 -38.403 25.232 1.00 18.55 C ANISOU 4273 CA GLY C 37 2788 1911 2347 -173 -708 188 C ATOM 4274 C GLY C 37 34.510 -37.110 25.790 1.00 21.27 C ANISOU 4274 C GLY C 37 3342 2089 2651 -255 -907 198 C ATOM 4275 O GLY C 37 35.430 -36.525 25.258 1.00 22.76 O ANISOU 4275 O GLY C 37 3428 2245 2973 -327 -1061 310 O ATOM 4276 N CYS C 38 33.940 -36.643 26.894 1.00 20.24 N ANISOU 4276 N CYS C 38 3525 1839 2327 -246 -908 89 N ATOM 4277 CA CYS C 38 34.463 -35.481 27.561 1.00 21.42 C ANISOU 4277 CA CYS C 38 3941 1795 2402 -335 -1125 91 C ATOM 4278 C CYS C 38 34.328 -35.524 29.091 1.00 22.46 C ANISOU 4278 C CYS C 38 4454 1783 2294 -379 -1192 17 C ATOM 4279 O CYS C 38 33.511 -36.267 29.636 1.00 23.51 O ANISOU 4279 O CYS C 38 4664 1972 2298 -302 -1005 -69 O ATOM 4280 CB CYS C 38 33.790 -34.175 27.043 1.00 23.57 C ANISOU 4280 CB CYS C 38 4280 2006 2670 -246 -1058 11 C ATOM 4281 SG CYS C 38 32.004 -34.023 27.435 1.00 25.08 S ANISOU 4281 SG CYS C 38 4641 2201 2687 -47 -738 -182 S ATOM 4282 N ARG C 39 35.155 -34.735 29.766 1.00 24.63 N ANISOU 4282 N ARG C 39 4978 1868 2511 -512 -1471 62 N ATOM 4283 CA ARG C 39 35.069 -34.531 31.225 1.00 26.41 C ANISOU 4283 CA ARG C 39 5652 1908 2474 -564 -1570 -14 C ATOM 4284 C ARG C 39 35.378 -35.792 32.016 1.00 27.99 C ANISOU 4284 C ARG C 39 5878 2149 2608 -639 -1607 29 C ATOM 4285 O ARG C 39 34.820 -36.041 33.098 1.00 31.06 O ANISOU 4285 O ARG C 39 6581 2466 2755 -615 -1532 -70 O ATOM 4286 CB ARG C 39 33.691 -34.013 31.642 1.00 29.65 C ANISOU 4286 CB ARG C 39 6324 2268 2675 -390 -1306 -204 C ATOM 4287 CG ARG C 39 33.162 -32.790 30.921 1.00 34.04 C ANISOU 4287 CG ARG C 39 6873 2778 3281 -284 -1228 -268 C ATOM 4288 CD ARG C 39 34.087 -31.642 30.974 1.00 36.26 C ANISOU 4288 CD ARG C 39 7329 2867 3583 -416 -1546 -206 C ATOM 4289 NE ARG C 39 34.311 -31.154 32.340 1.00 44.36 N ANISOU 4289 NE ARG C 39 8867 3643 4346 -495 -1725 -263 N ATOM 4290 CZ ARG C 39 33.595 -30.214 32.957 1.00 51.77 C ANISOU 4290 CZ ARG C 39 10209 4398 5063 -392 -1646 -411 C ATOM 4291 NH1 ARG C 39 32.582 -29.615 32.349 1.00 56.36 N ANISOU 4291 NH1 ARG C 39 10720 5019 5675 -200 -1390 -511 N ATOM 4292 NH2 ARG C 39 33.908 -29.864 34.195 1.00 53.23 N ANISOU 4292 NH2 ARG C 39 10888 4344 4993 -479 -1832 -453 N ATOM 4293 N ALA C 40 36.273 -36.604 31.479 1.00 26.21 N ANISOU 4293 N ALA C 40 5327 2035 2596 -722 -1713 185 N ATOM 4294 CA ALA C 40 36.696 -37.819 32.149 1.00 29.31 C ANISOU 4294 CA ALA C 40 5711 2462 2964 -802 -1780 250 C ATOM 4295 C ALA C 40 37.133 -37.571 33.592 1.00 28.31 C ANISOU 4295 C ALA C 40 6017 2118 2622 -947 -2032 252 C ATOM 4296 O ALA C 40 37.817 -36.599 33.890 1.00 30.67 O ANISOU 4296 O ALA C 40 6511 2235 2907 -1068 -2306 307 O ATOM 4297 CB ALA C 40 37.807 -38.456 31.394 1.00 25.59 C ANISOU 4297 CB ALA C 40 4861 2089 2772 -879 -1909 442 C ATOM 4298 N LYS C 41 36.726 -38.502 34.467 1.00 29.26 N ANISOU 4298 N LYS C 41 6290 2255 2571 -942 -1947 199 N ATOM 4299 CA LYS C 41 37.300 -38.618 35.809 1.00 30.17 C ANISOU 4299 CA LYS C 41 6776 2185 2501 -1106 -2210 237 C ATOM 4300 C LYS C 41 38.499 -39.596 35.725 1.00 28.82 C ANISOU 4300 C LYS C 41 6334 2064 2551 -1252 -2444 442 C ATOM 4301 O LYS C 41 38.791 -40.136 34.636 1.00 31.81 O ANISOU 4301 O LYS C 41 6268 2618 3200 -1199 -2358 533 O ATOM 4302 CB LYS C 41 36.223 -39.077 36.812 1.00 35.11 C ANISOU 4302 CB LYS C 41 7725 2798 2819 -1021 -1983 82 C ATOM 4303 CG LYS C 41 35.247 -37.947 37.164 1.00 38.83 C ANISOU 4303 CG LYS C 41 8555 3149 3050 -897 -1811 -95 C ATOM 4304 CD LYS C 41 34.231 -38.319 38.238 1.00 43.93 C ANISOU 4304 CD LYS C 41 9550 3762 3379 -809 -1574 -228 C ATOM 4305 CE LYS C 41 33.131 -37.268 38.313 1.00 47.44 C ANISOU 4305 CE LYS C 41 10241 4134 3650 -623 -1311 -394 C ATOM 4306 NZ LYS C 41 33.614 -35.867 38.121 1.00 54.47 N ANISOU 4306 NZ LYS C 41 11314 4834 4547 -664 -1524 -406 N ATOM 4307 N ARG C 42 39.205 -39.813 36.816 1.00 32.95 N ANISOU 4307 N ARG C 42 7120 2429 2970 -1429 -2736 525 N ATOM 4308 CA ARG C 42 40.497 -40.486 36.712 1.00 34.13 C ANISOU 4308 CA ARG C 42 7006 2588 3374 -1581 -3014 756 C ATOM 4309 C ARG C 42 40.401 -42.036 36.577 1.00 35.58 C ANISOU 4309 C ARG C 42 6919 2952 3650 -1525 -2857 792 C ATOM 4310 O ARG C 42 41.309 -42.654 36.076 1.00 30.94 O ANISOU 4310 O ARG C 42 5988 2432 3335 -1572 -2971 972 O ATOM 4311 CB ARG C 42 41.401 -40.125 37.897 1.00 35.99 C ANISOU 4311 CB ARG C 42 7607 2567 3501 -1819 -3447 868 C ATOM 4312 CG ARG C 42 41.985 -38.750 37.747 1.00 37.57 C ANISOU 4312 CG ARG C 42 7925 2596 3752 -1923 -3709 934 C ATOM 4313 CD ARG C 42 42.842 -38.380 38.933 1.00 41.72 C ANISOU 4313 CD ARG C 42 8850 2845 4157 -2176 -4169 1051 C ATOM 4314 NE ARG C 42 41.993 -38.169 40.093 1.00 47.31 N ANISOU 4314 NE ARG C 42 10140 3400 4436 -2159 -4105 847 N ATOM 4315 CZ ARG C 42 42.467 -37.908 41.300 1.00 55.34 C ANISOU 4315 CZ ARG C 42 11636 4155 5236 -2359 -4457 890 C ATOM 4316 NH1 ARG C 42 43.765 -37.819 41.452 1.00 55.65 N ANISOU 4316 NH1 ARG C 42 11599 4066 5481 -2597 -4912 1142 N ATOM 4317 NH2 ARG C 42 41.650 -37.740 42.330 1.00 58.44 N ANISOU 4317 NH2 ARG C 42 12580 4411 5215 -2321 -4354 697 N ATOM 4318 N ASN C 43 39.305 -42.657 36.998 1.00 33.35 N ANISOU 4318 N ASN C 43 6781 2742 3150 -1417 -2589 633 N ATOM 4319 CA ASN C 43 39.153 -44.106 36.858 1.00 30.35 C ANISOU 4319 CA ASN C 43 6162 2521 2847 -1367 -2448 663 C ATOM 4320 C ASN C 43 38.583 -44.384 35.455 1.00 27.41 C ANISOU 4320 C ASN C 43 5390 2366 2660 -1180 -2137 618 C ATOM 4321 O ASN C 43 37.409 -44.741 35.279 1.00 25.90 O ANISOU 4321 O ASN C 43 5195 2289 2357 -1041 -1833 479 O ATOM 4322 CB ASN C 43 38.235 -44.652 37.916 1.00 31.80 C ANISOU 4322 CB ASN C 43 6671 2685 2725 -1349 -2310 535 C ATOM 4323 CG ASN C 43 38.335 -46.171 38.027 1.00 32.84 C ANISOU 4323 CG ASN C 43 6620 2928 2931 -1360 -2277 606 C ATOM 4324 OD1 ASN C 43 39.215 -46.805 37.419 1.00 30.47 O ANISOU 4324 OD1 ASN C 43 5981 2689 2905 -1390 -2392 758 O ATOM 4325 ND2 ASN C 43 37.473 -46.740 38.838 1.00 32.97 N ANISOU 4325 ND2 ASN C 43 6871 2956 2701 -1336 -2124 506 N ATOM 4326 N ASN C 44 39.430 -44.219 34.452 1.00 27.02 N ANISOU 4326 N ASN C 44 5006 2365 2896 -1183 -2219 752 N ATOM 4327 CA ASN C 44 39.017 -44.173 33.049 1.00 24.96 C ANISOU 4327 CA ASN C 44 4416 2269 2797 -1023 -1968 717 C ATOM 4328 C ASN C 44 40.281 -44.374 32.236 1.00 24.13 C ANISOU 4328 C ASN C 44 3961 2198 3008 -1062 -2109 923 C ATOM 4329 O ASN C 44 41.144 -43.476 32.190 1.00 29.17 O ANISOU 4329 O ASN C 44 4591 2735 3758 -1163 -2333 1042 O ATOM 4330 CB ASN C 44 38.363 -42.823 32.716 1.00 23.37 C ANISOU 4330 CB ASN C 44 4341 2030 2507 -958 -1874 596 C ATOM 4331 CG ASN C 44 38.002 -42.667 31.220 1.00 23.91 C ANISOU 4331 CG ASN C 44 4082 2253 2750 -812 -1650 577 C ATOM 4332 OD1 ASN C 44 38.648 -43.225 30.350 1.00 23.00 O ANISOU 4332 OD1 ASN C 44 3648 2232 2857 -792 -1644 696 O ATOM 4333 ND2 ASN C 44 36.970 -41.905 30.943 1.00 23.11 N ANISOU 4333 ND2 ASN C 44 4076 2166 2539 -709 -1467 431 N ATOM 4334 N PHE C 45 40.370 -45.523 31.578 1.00 25.38 N ANISOU 4334 N PHE C 45 3838 2494 3312 -975 -1969 972 N ATOM 4335 CA PHE C 45 41.625 -46.003 30.981 1.00 24.64 C ANISOU 4335 CA PHE C 45 3422 2427 3514 -997 -2080 1187 C ATOM 4336 C PHE C 45 41.394 -46.446 29.552 1.00 27.55 C ANISOU 4336 C PHE C 45 3482 2958 4029 -823 -1809 1175 C ATOM 4337 O PHE C 45 40.356 -46.977 29.207 1.00 23.73 O ANISOU 4337 O PHE C 45 3012 2571 3432 -707 -1571 1027 O ATOM 4338 CB PHE C 45 42.247 -47.153 31.766 1.00 28.16 C ANISOU 4338 CB PHE C 45 3863 2833 4003 -1077 -2233 1300 C ATOM 4339 CG PHE C 45 42.587 -46.814 33.166 1.00 29.32 C ANISOU 4339 CG PHE C 45 4326 2806 4010 -1266 -2532 1337 C ATOM 4340 CD1 PHE C 45 41.678 -47.021 34.179 1.00 29.54 C ANISOU 4340 CD1 PHE C 45 4697 2789 3736 -1291 -2492 1177 C ATOM 4341 CD2 PHE C 45 43.823 -46.266 33.483 1.00 32.71 C ANISOU 4341 CD2 PHE C 45 4721 3102 4603 -1425 -2863 1546 C ATOM 4342 CE1 PHE C 45 41.996 -46.712 35.494 1.00 33.75 C ANISOU 4342 CE1 PHE C 45 5574 3144 4107 -1468 -2772 1208 C ATOM 4343 CE2 PHE C 45 44.144 -45.974 34.781 1.00 34.86 C ANISOU 4343 CE2 PHE C 45 5321 3192 4731 -1615 -3172 1585 C ATOM 4344 CZ PHE C 45 43.228 -46.163 35.790 1.00 34.98 C ANISOU 4344 CZ PHE C 45 5720 3155 4414 -1636 -3126 1406 C ATOM 4345 N LYS C 46 42.391 -46.238 28.715 1.00 27.69 N ANISOU 4345 N LYS C 46 3223 2995 4301 -811 -1851 1347 N ATOM 4346 CA LYS C 46 42.259 -46.557 27.311 1.00 26.09 C ANISOU 4346 CA LYS C 46 2762 2928 4222 -647 -1597 1345 C ATOM 4347 C LYS C 46 42.602 -48.023 27.058 1.00 28.77 C ANISOU 4347 C LYS C 46 2931 3330 4669 -564 -1506 1414 C ATOM 4348 O LYS C 46 42.320 -48.542 25.990 1.00 31.13 O ANISOU 4348 O LYS C 46 3085 3730 5014 -416 -1276 1379 O ATOM 4349 CB LYS C 46 43.143 -45.627 26.473 1.00 31.17 C ANISOU 4349 CB LYS C 46 3196 3567 5078 -656 -1648 1503 C ATOM 4350 CG LYS C 46 42.618 -44.201 26.476 1.00 31.23 C ANISOU 4350 CG LYS C 46 3371 3525 4971 -704 -1689 1404 C ATOM 4351 CD LYS C 46 43.626 -43.219 25.903 1.00 35.60 C ANISOU 4351 CD LYS C 46 3746 4044 5737 -763 -1816 1594 C ATOM 4352 CE LYS C 46 43.014 -41.869 25.868 1.00 36.94 C ANISOU 4352 CE LYS C 46 4097 4158 5778 -797 -1846 1478 C ATOM 4353 NZ LYS C 46 43.889 -40.877 25.149 1.00 40.17 N ANISOU 4353 NZ LYS C 46 4322 4547 6394 -848 -1946 1659 N ATOM 4354 N SER C 47 43.146 -48.712 28.050 1.00 30.14 N ANISOU 4354 N SER C 47 3155 3432 4865 -658 -1688 1504 N ATOM 4355 CA SER C 47 43.423 -50.132 27.880 1.00 34.13 C ANISOU 4355 CA SER C 47 3522 3981 5464 -575 -1609 1562 C ATOM 4356 C SER C 47 43.337 -50.831 29.212 1.00 29.02 C ANISOU 4356 C SER C 47 3071 3258 4698 -688 -1778 1549 C ATOM 4357 O SER C 47 43.491 -50.218 30.265 1.00 30.30 O ANISOU 4357 O SER C 47 3431 3313 4770 -847 -2009 1567 O ATOM 4358 CB SER C 47 44.821 -50.340 27.306 1.00 35.59 C ANISOU 4358 CB SER C 47 3396 4160 5969 -542 -1659 1815 C ATOM 4359 OG SER C 47 45.776 -50.005 28.278 1.00 38.00 O ANISOU 4359 OG SER C 47 3710 4345 6384 -716 -1976 1995 O ATOM 4360 N ALA C 48 43.087 -52.143 29.181 1.00 30.65 N ANISOU 4360 N ALA C 48 3247 3508 4890 -610 -1673 1520 N ATOM 4361 CA ALA C 48 43.131 -52.950 30.404 1.00 31.52 C ANISOU 4361 CA ALA C 48 3515 3547 4915 -717 -1841 1538 C ATOM 4362 C ALA C 48 44.500 -52.904 31.097 1.00 31.93 C ANISOU 4362 C ALA C 48 3487 3481 5163 -853 -2148 1776 C ATOM 4363 O ALA C 48 44.584 -52.864 32.308 1.00 34.58 O ANISOU 4363 O ALA C 48 4038 3713 5386 -1014 -2379 1795 O ATOM 4364 CB ALA C 48 42.757 -54.376 30.114 1.00 32.86 C ANISOU 4364 CB ALA C 48 3632 3777 5078 -605 -1687 1494 C ATOM 4365 N GLU C 49 45.553 -52.861 30.296 1.00 35.47 N ANISOU 4365 N GLU C 49 3628 3941 5906 -789 -2146 1967 N ATOM 4366 CA GLU C 49 46.927 -52.827 30.827 1.00 41.25 C ANISOU 4366 CA GLU C 49 4218 4566 6891 -910 -2438 2240 C ATOM 4367 C GLU C 49 47.204 -51.548 31.608 1.00 42.23 C ANISOU 4367 C GLU C 49 4512 4575 6959 -1116 -2725 2292 C ATOM 4368 O GLU C 49 47.734 -51.625 32.695 1.00 41.32 O ANISOU 4368 O GLU C 49 4517 4333 6850 -1290 -3030 2407 O ATOM 4369 CB GLU C 49 47.953 -52.988 29.707 1.00 45.69 C ANISOU 4369 CB GLU C 49 4387 5177 7796 -774 -2327 2450 C ATOM 4370 CG GLU C 49 47.987 -54.363 29.051 1.00 48.63 C ANISOU 4370 CG GLU C 49 4600 5615 8263 -576 -2097 2454 C ATOM 4371 CD GLU C 49 46.851 -54.627 28.078 1.00 50.32 C ANISOU 4371 CD GLU C 49 4886 5946 8288 -400 -1757 2212 C ATOM 4372 OE1 GLU C 49 46.068 -53.702 27.748 1.00 47.33 O ANISOU 4372 OE1 GLU C 49 4625 5616 7742 -408 -1667 2057 O ATOM 4373 OE2 GLU C 49 46.733 -55.790 27.634 1.00 54.56 O ANISOU 4373 OE2 GLU C 49 5369 6515 8848 -253 -1590 2184 O ATOM 4374 N ASP C 50 46.835 -50.355 31.129 1.00 37.26 N ANISOU 4374 N ASP C 50 3931 3969 6257 -1111 -2657 2206 N ATOM 4375 CA ASP C 50 47.225 -49.262 32.018 1.00 43.08 C ANISOU 4375 CA ASP C 50 4865 4559 6946 -1325 -2985 2279 C ATOM 4376 C ASP C 50 46.206 -49.127 33.149 1.00 37.58 C ANISOU 4376 C ASP C 50 4612 3791 5875 -1418 -3044 2059 C ATOM 4377 O ASP C 50 46.534 -48.648 34.221 1.00 40.52 O ANISOU 4377 O ASP C 50 5232 4007 6157 -1610 -3352 2116 O ATOM 4378 CB ASP C 50 47.693 -47.967 31.308 1.00 64.58 C ANISOU 4378 CB ASP C 50 7449 7274 9813 -1346 -3025 2376 C ATOM 4379 CG ASP C 50 46.671 -47.387 30.465 1.00 65.19 C ANISOU 4379 CG ASP C 50 7577 7457 9735 -1210 -2735 2156 C ATOM 4380 OD1 ASP C 50 45.515 -47.735 30.735 1.00 66.45 O ANISOU 4380 OD1 ASP C 50 7963 7658 9626 -1149 -2571 1919 O ATOM 4381 OD2 ASP C 50 47.006 -46.574 29.567 1.00 64.02 O ANISOU 4381 OD2 ASP C 50 7246 7346 9735 -1173 -2679 2233 O ATOM 4382 N CYS C 51 45.013 -49.714 32.992 1.00 34.47 N ANISOU 4382 N CYS C 51 4327 3503 5269 -1287 -2760 1830 N ATOM 4383 CA CYS C 51 44.163 -49.840 34.150 1.00 30.12 C ANISOU 4383 CA CYS C 51 4162 2888 4395 -1369 -2803 1669 C ATOM 4384 C CYS C 51 44.856 -50.738 35.199 1.00 35.90 C ANISOU 4384 C CYS C 51 4963 3517 5162 -1507 -3067 1812 C ATOM 4385 O CYS C 51 44.902 -50.395 36.384 1.00 37.10 O ANISOU 4385 O CYS C 51 5443 3523 5132 -1680 -3312 1812 O ATOM 4386 CB CYS C 51 42.793 -50.439 33.744 1.00 28.99 C ANISOU 4386 CB CYS C 51 4062 2886 4065 -1204 -2450 1441 C ATOM 4387 SG CYS C 51 41.684 -50.584 35.074 1.00 32.85 S ANISOU 4387 SG CYS C 51 4989 3319 4173 -1278 -2439 1259 S ATOM 4388 N AMET C 52 45.295 -51.938 34.843 0.50 35.84 N ANISOU 4388 N AMET C 52 4697 3572 5349 -1431 -3014 1918 N ATOM 4389 N BMET C 52 45.425 -51.841 34.684 0.50 36.23 N ANISOU 4389 N BMET C 52 4697 3626 5443 -1423 -3013 1941 N ATOM 4390 CA AMET C 52 45.847 -52.834 35.881 0.50 37.68 C ANISOU 4390 CA AMET C 52 5014 3704 5601 -1561 -3262 2045 C ATOM 4391 CA BMET C 52 46.172 -52.874 35.442 0.50 37.38 C ANISOU 4391 CA BMET C 52 4814 3692 5697 -1517 -3236 2108 C ATOM 4392 C AMET C 52 46.987 -52.162 36.678 0.50 38.35 C ANISOU 4392 C AMET C 52 5165 3605 5799 -1784 -3685 2266 C ATOM 4393 C BMET C 52 47.672 -52.628 35.707 0.50 38.66 C ANISOU 4393 C BMET C 52 4799 3728 6163 -1660 -3587 2415 C ATOM 4394 O AMET C 52 47.106 -52.329 37.891 0.50 40.47 O ANISOU 4394 O AMET C 52 5719 3739 5921 -1960 -3948 2298 O ATOM 4395 O BMET C 52 48.227 -53.116 36.711 0.50 41.53 O ANISOU 4395 O BMET C 52 5267 3968 6546 -1816 -3878 2548 O ATOM 4396 CB AMET C 52 46.330 -54.128 35.237 0.50 35.37 C ANISOU 4396 CB AMET C 52 4388 3490 5561 -1429 -3153 2160 C ATOM 4397 CB BMET C 52 46.113 -54.188 34.688 0.50 33.18 C ANISOU 4397 CB BMET C 52 4022 3279 5307 -1337 -3004 2114 C ATOM 4398 CG AMET C 52 45.205 -54.982 34.716 0.50 35.19 C ANISOU 4398 CG AMET C 52 4376 3603 5390 -1257 -2816 1955 C ATOM 4399 CG BMET C 52 44.765 -54.808 34.493 0.50 32.34 C ANISOU 4399 CG BMET C 52 4048 3283 4956 -1215 -2709 1870 C ATOM 4400 SD AMET C 52 44.107 -55.362 36.067 0.50 38.30 S ANISOU 4400 SD AMET C 52 5205 3954 5394 -1373 -2854 1778 S ATOM 4401 SD BMET C 52 45.283 -56.493 34.272 0.50 44.04 S ANISOU 4401 SD BMET C 52 5305 4786 6640 -1121 -2680 1991 S ATOM 4402 CE AMET C 52 45.075 -56.600 36.930 0.50 83.39 C ANISOU 4402 CE AMET C 52 10879 9557 11250 -1487 -3139 1987 C ATOM 4403 CE BMET C 52 45.654 -56.912 35.974 0.50 83.21 C ANISOU 4403 CE BMET C 52 10532 9590 11496 -1359 -3048 2088 C ATOM 4404 N AARG C 53 47.810 -51.415 35.963 0.50 40.13 N ANISOU 4404 N AARG C 53 5133 3827 6289 -1781 -3753 2427 N ATOM 4405 N BARG C 53 48.355 -51.950 34.786 0.50 41.26 N ANISOU 4405 N BARG C 53 4837 4090 6751 -1609 -3564 2552 N ATOM 4406 CA AARG C 53 49.034 -50.817 36.483 0.50 41.19 C ANISOU 4406 CA AARG C 53 5230 3798 6622 -1986 -4161 2695 C ATOM 4407 CA BARG C 53 49.744 -51.583 35.057 0.50 44.53 C ANISOU 4407 CA BARG C 53 5075 4380 7466 -1763 -3913 2868 C ATOM 4408 C AARG C 53 48.694 -49.664 37.412 0.50 42.68 C ANISOU 4408 C AARG C 53 5865 3832 6520 -2173 -4390 2598 C ATOM 4409 C BARG C 53 49.695 -50.517 36.116 0.50 41.51 C ANISOU 4409 C BARG C 53 5071 3828 6871 -2000 -4238 2847 C ATOM 4410 O AARG C 53 49.163 -49.605 38.566 0.50 47.23 O ANISOU 4410 O AARG C 53 6698 4225 7023 -2392 -4760 2705 O ATOM 4411 O BARG C 53 50.584 -50.416 36.961 0.50 49.64 O ANISOU 4411 O BARG C 53 6159 4694 8009 -2209 -4634 3064 O ATOM 4412 CB AARG C 53 49.858 -50.362 35.281 0.50 44.50 C ANISOU 4412 CB AARG C 53 5215 4289 7404 -1895 -4090 2884 C ATOM 4413 CB BARG C 53 50.449 -51.012 33.835 0.50 51.55 C ANISOU 4413 CB BARG C 53 5572 5343 8671 -1660 -3801 3031 C ATOM 4414 CG AARG C 53 51.322 -50.004 35.512 0.50 59.06 C ANISOU 4414 CG AARG C 53 6844 6004 9594 -2066 -4470 3246 C ATOM 4415 CG BARG C 53 51.704 -50.262 34.243 0.50 62.89 C ANISOU 4415 CG BARG C 53 6895 6633 10366 -1867 -4201 3345 C ATOM 4416 CD AARG C 53 51.985 -49.802 34.158 0.50 67.70 C ANISOU 4416 CD AARG C 53 7463 7217 11045 -1912 -4277 3417 C ATOM 4417 CD BARG C 53 52.463 -49.719 33.068 0.50 71.11 C ANISOU 4417 CD BARG C 53 7526 7749 11742 -1773 -4092 3544 C ATOM 4418 NE AARG C 53 53.383 -49.407 34.245 0.50 77.28 N ANISOU 4418 NE AARG C 53 8404 8324 12634 -2060 -4607 3795 N ATOM 4419 NE BARG C 53 53.817 -49.375 33.466 0.50 80.08 N ANISOU 4419 NE BARG C 53 8462 8752 13214 -1962 -4479 3917 N ATOM 4420 CZ AARG C 53 54.409 -50.236 34.100 0.00 84.07 C ANISOU 4420 CZ AARG C 53 8896 9184 13862 -2026 -4668 4085 C ATOM 4421 CZ BARG C 53 54.694 -50.258 33.926 0.00 85.49 C ANISOU 4421 CZ BARG C 53 8959 9372 14153 -2012 -4669 4167 C ATOM 4422 NH1AARG C 53 55.639 -49.763 34.190 0.00 88.63 N ANISOU 4422 NH1AARG C 53 9219 9663 14794 -2174 -4979 4449 N ATOM 4423 NH1BARG C 53 55.910 -49.862 34.260 0.00 89.69 N ANISOU 4423 NH1BARG C 53 9289 9778 15012 -2195 -5038 4530 N ATOM 4424 NH2AARG C 53 54.214 -51.528 33.866 0.00 84.42 N ANISOU 4424 NH2AARG C 53 8823 9319 13935 -1843 -4427 4027 N ATOM 4425 NH2BARG C 53 54.357 -51.535 34.046 0.00 84.88 N ANISOU 4425 NH2BARG C 53 8887 9348 14016 -1883 -4502 4068 N ATOM 4426 N ATHR C 54 47.866 -48.743 36.918 0.50 40.88 N ANISOU 4426 N ATHR C 54 5755 3662 6116 -2085 -4175 2394 N ATOM 4427 N BTHR C 54 48.632 -49.731 36.055 0.50 41.76 N ANISOU 4427 N BTHR C 54 5376 3890 6600 -1963 -4071 2587 N ATOM 4428 CA ATHR C 54 47.494 -47.602 37.720 0.50 41.64 C ANISOU 4428 CA ATHR C 54 6292 3603 5926 -2229 -4353 2285 C ATOM 4429 CA BTHR C 54 48.451 -48.566 36.913 0.50 43.00 C ANISOU 4429 CA BTHR C 54 5935 3884 6519 -2147 -4319 2525 C ATOM 4430 C ATHR C 54 46.708 -48.059 38.912 0.50 46.44 C ANISOU 4430 C ATHR C 54 7341 4137 6165 -2290 -4368 2115 C ATOM 4431 C BTHR C 54 47.848 -48.932 38.264 0.50 44.02 C ANISOU 4431 C BTHR C 54 6528 3901 6297 -2265 -4440 2388 C ATOM 4432 O ATHR C 54 46.656 -47.353 39.915 0.50 51.33 O ANISOU 4432 O ATHR C 54 8389 4570 6542 -2455 -4610 2079 O ATOM 4433 O BTHR C 54 48.550 -48.898 39.286 0.50 45.49 O ANISOU 4433 O BTHR C 54 6905 3903 6477 -2484 -4833 2545 O ATOM 4434 CB ATHR C 54 46.633 -46.598 36.955 0.50 35.94 C ANISOU 4434 CB ATHR C 54 5615 2962 5077 -2094 -4081 2082 C ATOM 4435 CB BTHR C 54 47.580 -47.506 36.216 0.50 38.74 C ANISOU 4435 CB BTHR C 54 5480 3417 5822 -2035 -4068 2313 C ATOM 4436 OG1ATHR C 54 47.290 -46.232 35.744 0.50 37.23 O ANISOU 4436 OG1ATHR C 54 5358 3215 5573 -2019 -4019 2232 O ATOM 4437 OG1BTHR C 54 48.247 -47.050 35.038 0.50 37.68 O ANISOU 4437 OG1BTHR C 54 4948 3362 6008 -1960 -4004 2467 O ATOM 4438 CG2ATHR C 54 46.387 -45.361 37.806 0.50 36.78 C ANISOU 4438 CG2ATHR C 54 6190 2874 4910 -2243 -4295 1993 C ATOM 4439 CG2BTHR C 54 47.297 -46.360 37.145 0.50 35.63 C ANISOU 4439 CG2BTHR C 54 5550 2839 5147 -2200 -4296 2222 C ATOM 4440 N ACYS C 55 46.091 -49.241 38.825 0.50 45.50 N ANISOU 4440 N ACYS C 55 7144 4154 5991 -2160 -4112 2014 N ATOM 4441 N BCYS C 55 46.560 -49.291 38.284 0.50 45.07 N ANISOU 4441 N BCYS C 55 6844 4139 6141 -2128 -4114 2115 N ATOM 4442 CA ACYS C 55 45.159 -49.621 39.869 0.50 44.32 C ANISOU 4442 CA ACYS C 55 7411 3961 5467 -2193 -4056 1832 C ATOM 4443 CA BCYS C 55 45.915 -49.654 39.559 0.50 44.82 C ANISOU 4443 CA BCYS C 55 7258 4013 5757 -2224 -4182 1986 C ATOM 4444 C ACYS C 55 45.170 -51.018 40.396 0.50 45.70 C ANISOU 4444 C ACYS C 55 7570 4161 5634 -2210 -4070 1875 C ATOM 4445 C BCYS C 55 45.969 -51.187 39.889 0.50 47.27 C ANISOU 4445 C BCYS C 55 7470 4377 6115 -2207 -4159 2039 C ATOM 4446 O ACYS C 55 44.331 -51.294 41.225 0.50 42.49 O ANISOU 4446 O ACYS C 55 7509 3730 4906 -2232 -3993 1724 O ATOM 4447 O BCYS C 55 45.714 -51.597 41.030 0.50 47.23 O ANISOU 4447 O BCYS C 55 7806 4272 5867 -2327 -4291 2000 O ATOM 4448 CB ACYS C 55 43.761 -49.412 39.377 0.50 42.29 C ANISOU 4448 CB ACYS C 55 7227 3848 4994 -1999 -3636 1563 C ATOM 4449 CB BCYS C 55 44.516 -48.972 39.743 0.50 42.17 C ANISOU 4449 CB BCYS C 55 7278 3704 5041 -2136 -3914 1689 C ATOM 4450 SG ACYS C 55 43.654 -47.847 38.797 0.50 35.85 S ANISOU 4450 SG ACYS C 55 6451 3000 4172 -1969 -3608 1499 S ATOM 4451 SG BCYS C 55 44.421 -47.218 40.566 0.50 41.41 S ANISOU 4451 SG BCYS C 55 7709 3370 4654 -2292 -4150 1609 S ATOM 4452 N AGLY C 56 46.126 -51.839 39.954 0.50 47.59 N ANISOU 4452 N AGLY C 56 7426 4436 6218 -2202 -4170 2089 N ATOM 4453 N BGLY C 56 46.340 -52.008 38.895 0.50 42.57 N ANISOU 4453 N BGLY C 56 6427 3922 5825 -2061 -4002 2134 N ATOM 4454 CA AGLY C 56 46.065 -53.298 40.009 0.50 50.69 C ANISOU 4454 CA AGLY C 56 7679 4905 6676 -2140 -4083 2117 C ATOM 4455 CA BGLY C 56 46.731 -53.398 39.095 0.50 49.31 C ANISOU 4455 CA BGLY C 56 7124 4795 6817 -2053 -4046 2249 C ATOM 4456 C AGLY C 56 45.676 -53.937 41.314 0.50 54.62 C ANISOU 4456 C AGLY C 56 8552 5309 6892 -2271 -4210 2067 C ATOM 4457 C BGLY C 56 45.688 -54.408 39.523 0.50 50.49 C ANISOU 4457 C BGLY C 56 7458 5014 6713 -1993 -3847 2071 C ATOM 4458 O AGLY C 56 45.612 -55.176 41.414 0.50 55.46 O ANISOU 4458 O AGLY C 56 8559 5469 7045 -2232 -4156 2094 O ATOM 4459 O BGLY C 56 45.882 -55.626 39.371 0.50 56.24 O ANISOU 4459 O BGLY C 56 7997 5794 7580 -1931 -3803 2140 O TER 4460 GLY C 56 HETATM 4461 CA CA A 1 25.214 -53.228 8.043 1.00 22.20 CA HETATM 4462 S SO4 A 6 43.534 -41.158 19.013 1.00 55.67 S HETATM 4463 O1 SO4 A 6 44.725 -41.466 18.234 1.00 58.42 O HETATM 4464 O2 SO4 A 6 42.506 -42.154 18.739 1.00 62.17 O HETATM 4465 O3 SO4 A 6 43.849 -41.221 20.432 1.00 57.40 O HETATM 4466 O4 SO4 A 6 43.064 -39.831 18.634 1.00 56.82 O HETATM 4467 S SO4 A 10 13.542 -17.896 20.790 1.00 54.26 S HETATM 4468 O1 SO4 A 10 13.938 -17.266 19.521 1.00 56.84 O HETATM 4469 O2 SO4 A 10 12.215 -18.547 20.565 1.00 43.97 O HETATM 4470 O3 SO4 A 10 14.681 -18.681 21.253 1.00 46.23 O HETATM 4471 O4 SO4 A 10 13.392 -16.941 21.909 1.00 54.75 O HETATM 4472 S SO4 A 12 28.233 -16.992 23.921 1.00 74.03 S HETATM 4473 O1 SO4 A 12 28.739 -17.432 22.626 1.00 70.64 O HETATM 4474 O2 SO4 A 12 26.799 -17.255 24.065 1.00 71.38 O HETATM 4475 O3 SO4 A 12 28.973 -17.677 24.991 1.00 76.30 O HETATM 4476 O4 SO4 A 12 28.445 -15.541 24.014 1.00 76.59 O HETATM 4477 S SO4 A 14 40.985 -33.952 23.152 1.00 82.71 S HETATM 4478 O1 SO4 A 14 41.939 -32.913 23.550 1.00 82.82 O HETATM 4479 O2 SO4 A 14 41.292 -34.413 21.800 1.00 82.21 O HETATM 4480 O3 SO4 A 14 41.037 -35.100 24.061 1.00 82.12 O HETATM 4481 O4 SO4 A 14 39.652 -33.364 23.192 1.00 82.23 O HETATM 4482 S SO4 A 247 31.549 -17.763 20.984 1.00 94.89 S HETATM 4483 O1 SO4 A 247 32.447 -18.518 20.112 1.00 93.19 O HETATM 4484 O2 SO4 A 247 30.176 -17.882 20.503 1.00 96.04 O HETATM 4485 O3 SO4 A 247 31.608 -18.250 22.366 1.00 93.65 O HETATM 4486 O4 SO4 A 247 31.927 -16.350 20.927 1.00 96.14 O HETATM 4487 S SO4 A 248 37.613 -41.528 -6.089 1.00 88.96 S HETATM 4488 O1 SO4 A 248 37.697 -41.039 -7.464 1.00 91.21 O HETATM 4489 O2 SO4 A 248 36.596 -42.576 -5.999 1.00 87.99 O HETATM 4490 O3 SO4 A 248 38.901 -42.089 -5.673 1.00 87.43 O HETATM 4491 O4 SO4 A 248 37.265 -40.379 -5.253 1.00 88.37 O HETATM 4492 S SO4 A 249 29.300 -29.254 30.582 1.00 98.36 S HETATM 4493 O1 SO4 A 249 30.569 -29.669 29.986 1.00 97.50 O HETATM 4494 O2 SO4 A 249 28.190 -29.701 29.748 1.00 98.34 O HETATM 4495 O3 SO4 A 249 29.136 -29.879 31.893 1.00 97.39 O HETATM 4496 O4 SO4 A 249 29.298 -27.790 30.688 1.00 97.28 O HETATM 4497 CA CA B 1 -9.730 -35.324 0.711 1.00 20.16 CA HETATM 4498 S SO4 B 4 12.293 -11.930 13.322 1.00 29.80 S HETATM 4499 O1 SO4 B 4 13.552 -11.195 13.530 1.00 33.21 O HETATM 4500 O2 SO4 B 4 11.557 -11.110 12.237 1.00 20.73 O HETATM 4501 O3 SO4 B 4 12.682 -13.299 12.891 1.00 24.70 O HETATM 4502 O4 SO4 B 4 11.507 -11.982 14.556 1.00 33.24 O HETATM 4503 S SO4 B 5 -23.051 -27.620 8.729 1.00 27.49 S HETATM 4504 O1 SO4 B 5 -21.748 -28.259 8.485 1.00 23.81 O HETATM 4505 O2 SO4 B 5 -24.084 -28.470 8.107 1.00 29.03 O HETATM 4506 O3 SO4 B 5 -23.340 -27.408 10.212 1.00 26.90 O HETATM 4507 O4 SO4 B 5 -23.156 -26.279 8.067 1.00 28.96 O HETATM 4508 S SO4 B 7 -2.143 -24.247 -19.875 1.00 52.05 S HETATM 4509 O1 SO4 B 7 -0.855 -24.668 -20.438 1.00 52.28 O HETATM 4510 O2 SO4 B 7 -3.133 -24.016 -20.921 1.00 53.47 O HETATM 4511 O3 SO4 B 7 -2.565 -25.331 -18.992 1.00 57.41 O HETATM 4512 O4 SO4 B 7 -2.039 -22.979 -19.167 1.00 55.68 O HETATM 4513 S SO4 B 8 -21.408 -18.461 -18.576 1.00 47.53 S HETATM 4514 O1 SO4 B 8 -21.046 -17.098 -18.986 1.00 50.28 O HETATM 4515 O2 SO4 B 8 -21.798 -19.266 -19.754 1.00 45.83 O HETATM 4516 O3 SO4 B 8 -20.295 -19.077 -17.792 1.00 37.47 O HETATM 4517 O4 SO4 B 8 -22.598 -18.437 -17.710 1.00 51.38 O HETATM 4518 S SO4 B 11 0.827 -0.154 -9.908 1.00 48.89 S HETATM 4519 O1 SO4 B 11 2.006 -0.962 -9.518 1.00 46.17 O HETATM 4520 O2 SO4 B 11 0.792 0.120 -11.361 1.00 44.90 O HETATM 4521 O3 SO4 B 11 -0.390 -0.904 -9.479 1.00 43.62 O HETATM 4522 O4 SO4 B 11 0.932 1.127 -9.188 1.00 46.79 O HETATM 4523 S SO4 B 15 -25.470 -23.653 -9.175 1.00 80.30 S HETATM 4524 O1 SO4 B 15 -25.150 -22.286 -9.605 1.00 81.04 O HETATM 4525 O2 SO4 B 15 -25.980 -22.588 -8.312 1.00 83.18 O HETATM 4526 O3 SO4 B 15 -25.657 -24.734 -10.152 1.00 79.05 O HETATM 4527 O4 SO4 B 15 -26.031 -24.819 -8.496 1.00 79.28 O HETATM 4528 S SO4 B 247 1.672 -33.816 10.353 1.00 88.89 S HETATM 4529 O1 SO4 B 247 1.561 -33.764 8.893 1.00 86.60 O HETATM 4530 O2 SO4 B 247 1.243 -32.434 10.174 1.00 88.66 O HETATM 4531 O3 SO4 B 247 1.285 -35.192 10.670 1.00 90.01 O HETATM 4532 O4 SO4 B 247 2.030 -33.104 11.583 1.00 88.50 O HETATM 4533 S SO4 B 248 5.098 -0.170 -8.400 1.00 36.52 S HETATM 4534 O1 SO4 B 248 5.009 0.717 -9.567 1.00 40.77 O HETATM 4535 O2 SO4 B 248 5.470 0.339 -7.106 1.00 24.40 O HETATM 4536 O3 SO4 B 248 3.783 -0.859 -8.229 1.00 38.65 O HETATM 4537 O4 SO4 B 248 6.267 -1.042 -8.664 1.00 37.34 O HETATM 4538 S SO4 B 249 11.808 -11.404 -8.951 1.00 96.27 S HETATM 4539 O1 SO4 B 249 12.865 -10.989 -9.868 1.00 96.45 O HETATM 4540 O2 SO4 B 249 10.826 -12.212 -9.677 1.00 94.97 O HETATM 4541 O3 SO4 B 249 12.401 -12.197 -7.866 1.00 94.30 O HETATM 4542 O4 SO4 B 249 11.169 -10.189 -8.445 1.00 95.03 O HETATM 4543 S SO4 B 250 -17.711 -10.589 -2.410 1.00101.03 S HETATM 4544 O1 SO4 B 250 -16.791 -11.531 -3.040 1.00102.53 O HETATM 4545 O2 SO4 B 250 -17.676 -9.322 -3.143 1.00 99.66 O HETATM 4546 O3 SO4 B 250 -19.058 -11.164 -2.422 1.00 99.21 O HETATM 4547 O4 SO4 B 250 -17.294 -10.344 -1.029 1.00100.77 O HETATM 4548 S SO4 I 59 18.502 -20.883 -20.265 1.00 21.94 S HETATM 4549 O1 SO4 I 59 19.525 -20.774 -21.318 1.00 31.65 O HETATM 4550 O2 SO4 I 59 17.191 -21.093 -20.898 1.00 22.59 O HETATM 4551 O3 SO4 I 59 18.867 -21.906 -19.334 1.00 20.38 O HETATM 4552 O4 SO4 I 59 18.421 -19.623 -19.522 1.00 29.16 O HETATM 4553 S SO4 I 60 5.524 -20.653 -17.805 1.00 24.20 S HETATM 4554 O1 SO4 I 60 6.549 -21.753 -18.004 1.00 22.66 O HETATM 4555 O2 SO4 I 60 5.356 -19.936 -19.080 1.00 28.01 O HETATM 4556 O3 SO4 I 60 4.273 -21.303 -17.382 1.00 26.36 O HETATM 4557 O4 SO4 I 60 5.913 -19.650 -16.759 1.00 23.34 O HETATM 4558 S SO4 I 61 18.960 -28.704 -32.593 1.00 60.99 S HETATM 4559 O1 SO4 I 61 19.956 -28.133 -31.679 1.00 64.05 O HETATM 4560 O2 SO4 I 61 19.489 -28.391 -33.932 1.00 64.39 O HETATM 4561 O3 SO4 I 61 18.773 -30.122 -32.372 1.00 54.62 O HETATM 4562 O4 SO4 I 61 17.649 -28.100 -32.388 1.00 56.60 O HETATM 4563 S SO4 I 62 16.010 -23.077 -8.030 1.00 38.01 S HETATM 4564 O1 SO4 I 62 17.413 -22.600 -8.165 1.00 44.16 O HETATM 4565 O2 SO4 I 62 15.868 -24.299 -8.947 1.00 27.84 O HETATM 4566 O3 SO4 I 62 15.738 -23.582 -6.666 1.00 41.68 O HETATM 4567 O4 SO4 I 62 15.117 -21.903 -8.253 1.00 25.63 O HETATM 4568 S SO4 I 63 18.999 -40.942 -25.804 1.00 60.46 S HETATM 4569 O1 SO4 I 63 19.987 -40.585 -26.826 1.00 64.26 O HETATM 4570 O2 SO4 I 63 17.707 -41.146 -26.521 1.00 53.33 O HETATM 4571 O3 SO4 I 63 19.391 -42.103 -24.949 1.00 33.03 O HETATM 4572 O4 SO4 I 63 18.891 -39.808 -24.872 1.00 64.32 O HETATM 4573 S SO4 C 59 39.539 -38.121 27.095 1.00 27.91 S HETATM 4574 O1 SO4 C 59 39.701 -38.774 25.807 1.00 25.27 O HETATM 4575 O2 SO4 C 59 38.383 -37.217 27.140 1.00 25.89 O HETATM 4576 O3 SO4 C 59 39.413 -39.141 28.187 1.00 26.51 O HETATM 4577 O4 SO4 C 59 40.800 -37.395 27.404 1.00 33.25 O HETATM 4578 S ASO4 C 60 37.602 -37.854 40.399 0.50 28.18 S HETATM 4579 S BSO4 C 60 39.084 -38.794 39.980 0.50 30.55 S HETATM 4580 O1 ASO4 C 60 38.709 -38.012 39.445 0.50 30.43 O HETATM 4581 O1 BSO4 C 60 39.666 -38.214 38.819 0.50 34.63 O HETATM 4582 O2 ASO4 C 60 36.872 -36.652 39.975 0.50 28.51 O HETATM 4583 O2 BSO4 C 60 37.921 -38.036 40.463 0.50 30.60 O HETATM 4584 O3 ASO4 C 60 36.782 -39.065 40.640 0.50 27.64 O HETATM 4585 O3 BSO4 C 60 38.457 -40.093 39.831 0.50 32.17 O HETATM 4586 O4 ASO4 C 60 38.217 -37.566 41.704 0.50 30.35 O HETATM 4587 O4 BSO4 C 60 40.140 -38.899 40.975 0.50 35.20 O HETATM 4588 O HOH A 250 23.933 -40.261 15.412 1.00 15.93 O HETATM 4589 O HOH A 251 24.422 -49.602 19.102 1.00 20.95 O HETATM 4590 O HOH A 252 21.896 -24.499 12.935 1.00 18.52 O HETATM 4591 O HOH A 253 18.241 -37.295 10.996 1.00 17.40 O HETATM 4592 O HOH A 254 24.887 -42.881 15.947 1.00 16.67 O HETATM 4593 O HOH A 255 26.107 -34.326 12.006 1.00 19.44 O HETATM 4594 O HOH A 256 17.013 -34.341 22.219 1.00 20.44 O HETATM 4595 O HOH A 257 19.609 -45.303 19.049 1.00 18.72 O HETATM 4596 O HOH A 258 20.487 -35.059 27.114 1.00 22.24 O HETATM 4597 O HOH A 259 24.516 -37.249 28.221 1.00 23.77 O HETATM 4598 O HOH A 260 28.952 -51.076 11.096 1.00 20.13 O HETATM 4599 O HOH A 261 9.327 -39.722 17.643 1.00 25.49 O HETATM 4600 O HOH A 262 30.063 -49.086 12.824 1.00 19.82 O HETATM 4601 O HOH A 263 15.343 -36.431 6.986 1.00 25.44 O HETATM 4602 O HOH A 264 29.071 -25.824 20.120 1.00 24.35 O HETATM 4603 O HOH A 265 13.587 -46.109 24.355 1.00 25.54 O HETATM 4604 O HOH A 266 9.480 -25.485 21.233 1.00 24.61 O HETATM 4605 O HOH A 267 18.755 -35.765 29.975 1.00 21.88 O HETATM 4606 O HOH A 268 24.257 -44.051 28.465 1.00 26.56 O HETATM 4607 O HOH A 269 25.442 -45.358 7.500 1.00 20.81 O HETATM 4608 O HOH A 270 14.918 -25.066 12.822 1.00 22.72 O HETATM 4609 O HOH A 271 15.197 -23.000 10.868 1.00 25.06 O HETATM 4610 O HOH A 272 10.139 -23.738 23.344 1.00 26.74 O HETATM 4611 O HOH A 273 17.857 -52.978 16.912 1.00 27.55 O HETATM 4612 O HOH A 274 23.050 -52.589 7.109 1.00 25.16 O HETATM 4613 O HOH A 275 20.675 -18.505 16.479 1.00 26.75 O HETATM 4614 O HOH A 276 15.254 -19.384 12.255 1.00 22.28 O HETATM 4615 O HOH A 277 8.269 -37.523 19.232 1.00 29.61 O HETATM 4616 O HOH A 278 19.636 -37.169 1.453 1.00 28.89 O HETATM 4617 O HOH A 279 28.061 -41.063 -7.052 1.00 34.74 O HETATM 4618 O HOH A 280 14.464 -18.272 14.680 1.00 26.42 O HETATM 4619 O HOH A 281 31.470 -20.105 10.241 1.00 26.74 O HETATM 4620 O HOH A 282 25.872 -18.815 8.549 1.00 28.06 O HETATM 4621 O HOH A 283 24.746 -43.257 4.689 1.00 24.85 O HETATM 4622 O HOH A 284 14.684 -45.550 20.339 1.00 25.57 O HETATM 4623 O HOH A 285 24.403 -27.641 1.325 1.00 30.40 O HETATM 4624 O HOH A 286 14.557 -34.203 25.502 1.00 23.50 O HETATM 4625 O HOH A 287 34.323 -44.643 -2.881 1.00 33.84 O HETATM 4626 O HOH A 288 8.922 -29.540 26.284 1.00 33.67 O HETATM 4627 O HOH A 289 22.628 -54.545 19.942 1.00 26.57 O HETATM 4628 O HOH A 290 25.253 -30.317 1.894 1.00 27.36 O HETATM 4629 O HOH A 291 29.823 -51.422 16.615 1.00 25.96 O HETATM 4630 O HOH A 292 28.672 -19.017 8.910 1.00 29.17 O HETATM 4631 O HOH A 293 17.386 -37.616 2.779 1.00 31.98 O HETATM 4632 O HOH A 294 16.490 -25.913 8.293 1.00 25.68 O HETATM 4633 O HOH A 295 25.868 -48.071 -1.235 1.00 27.35 O HETATM 4634 O HOH A 296 8.119 -27.599 22.401 1.00 29.76 O HETATM 4635 O HOH A 297 21.927 -57.992 14.408 1.00 29.73 O HETATM 4636 O HOH A 298 15.182 -23.760 8.302 1.00 29.65 O HETATM 4637 O HOH A 299 8.244 -27.858 11.458 1.00 29.98 O HETATM 4638 O HOH A 300 15.964 -18.733 30.707 1.00 26.88 O HETATM 4639 O HOH A 301 32.450 -46.268 -2.033 1.00 30.88 O HETATM 4640 O HOH A 302 20.900 -45.897 4.204 1.00 29.94 O HETATM 4641 O HOH A 303 13.254 -19.159 16.866 1.00 29.84 O HETATM 4642 O HOH A 304 41.466 -42.425 8.931 1.00 27.16 O HETATM 4643 O HOH A 305 40.435 -28.433 17.864 1.00 29.06 O HETATM 4644 O HOH A 306 39.965 -27.930 24.176 1.00 34.08 O HETATM 4645 O HOH A 307 17.526 -23.858 22.154 1.00 24.54 O HETATM 4646 O HOH A 308 30.319 -21.999 28.318 1.00 33.56 O HETATM 4647 O HOH A 309 20.382 -54.379 23.276 1.00 30.56 O HETATM 4648 O HOH A 310 25.438 -55.581 -2.660 1.00 35.37 O HETATM 4649 O HOH A 311 27.612 -53.391 8.621 1.00 25.68 O HETATM 4650 O HOH A 312 9.026 -29.870 23.681 1.00 27.67 O HETATM 4651 O HOH A 313 28.131 -28.047 22.007 1.00 24.22 O HETATM 4652 O HOH A 314 29.415 -24.682 28.264 1.00 28.72 O HETATM 4653 O HOH A 315 36.986 -33.053 28.191 1.00 25.32 O HETATM 4654 O HOH A 316 15.445 -34.949 28.108 1.00 26.40 O HETATM 4655 O HOH A 317 20.175 -40.568 31.950 1.00 28.63 O HETATM 4656 O HOH A 318 18.791 -44.808 6.233 1.00 31.13 O HETATM 4657 O HOH A 319 21.686 -25.340 1.768 1.00 26.02 O HETATM 4658 O HOH A 320 25.804 -46.551 28.421 1.00 37.95 O HETATM 4659 O HOH A 321 22.734 -17.950 14.668 1.00 30.62 O HETATM 4660 O HOH A 322 16.644 -22.989 35.721 1.00 29.48 O HETATM 4661 O HOH A 323 23.075 -36.425 -2.619 1.00 27.97 O HETATM 4662 O HOH A 324 29.073 -55.079 10.326 1.00 34.77 O HETATM 4663 O HOH A 325 10.215 -19.798 25.888 1.00 38.36 O HETATM 4664 O HOH A 326 41.788 -31.181 13.863 1.00 38.57 O HETATM 4665 O HOH A 327 11.556 -43.651 9.446 1.00 39.13 O HETATM 4666 O HOH A 328 15.866 -35.658 4.375 1.00 37.70 O HETATM 4667 O HOH A 329 36.510 -39.266 20.408 1.00 29.40 O HETATM 4668 O HOH A 330 22.184 -19.121 31.240 1.00 34.52 O HETATM 4669 O HOH A 331 41.736 -27.653 13.307 1.00 37.34 O HETATM 4670 O HOH A 332 9.085 -41.967 19.261 1.00 30.78 O HETATM 4671 O HOH A 333 21.941 -45.045 6.572 1.00 31.68 O HETATM 4672 O HOH A 334 24.015 -17.458 17.205 1.00 31.46 O HETATM 4673 O HOH A 335 33.581 -20.703 12.907 1.00 32.31 O HETATM 4674 O HOH A 336 23.084 -21.229 29.717 1.00 32.43 O HETATM 4675 O HOH A 337 26.416 -30.086 32.508 1.00 30.98 O HETATM 4676 O HOH A 338 34.778 -19.434 19.804 1.00 32.26 O HETATM 4677 O HOH A 339 24.033 -40.727 30.264 1.00 33.11 O HETATM 4678 O HOH A 340 20.092 -48.368 3.945 1.00 38.54 O HETATM 4679 O HOH A 341 40.378 -45.824 9.568 1.00 41.54 O HETATM 4680 O HOH A 342 19.317 -41.438 -1.165 1.00 33.64 O HETATM 4681 O HOH A 343 20.959 -17.970 4.462 1.00 34.34 O HETATM 4682 O HOH A 344 23.520 -21.032 4.738 1.00 32.43 O HETATM 4683 O HOH A 345 18.033 -19.303 16.269 1.00 30.96 O HETATM 4684 O HOH A 346 37.591 -33.891 23.706 1.00 30.09 O HETATM 4685 O HOH A 347 43.783 -34.671 9.242 1.00 41.19 O HETATM 4686 O HOH A 348 14.438 -46.153 29.115 1.00 39.97 O HETATM 4687 O HOH A 349 8.511 -42.817 23.226 1.00 40.69 O HETATM 4688 O HOH A 350 28.207 -33.745 -3.285 1.00 39.24 O HETATM 4689 O HOH A 351 14.047 -17.569 24.087 1.00 34.58 O HETATM 4690 O HOH A 352 39.863 -24.660 7.950 1.00 42.32 O HETATM 4691 O HOH A 353 21.145 -44.281 30.026 1.00 39.45 O HETATM 4692 O HOH A 354 14.157 -38.878 6.597 1.00 38.09 O HETATM 4693 O HOH A 355 15.714 -21.520 19.371 1.00 49.21 O HETATM 4694 O HOH A 356 28.386 -20.199 28.520 1.00 41.74 O HETATM 4695 O HOH A 357 23.663 -14.803 9.165 1.00 43.12 O HETATM 4696 O HOH A 358 37.972 -40.948 21.945 1.00 39.62 O HETATM 4697 O HOH A 359 11.606 -41.217 9.828 1.00 50.97 O HETATM 4698 O HOH A 360 30.289 -40.075 -6.230 1.00 40.44 O HETATM 4699 O HOH A 361 28.004 -59.640 8.615 1.00 37.65 O HETATM 4700 O HOH A 362 10.956 -30.189 9.764 1.00 36.28 O HETATM 4701 O HOH A 363 23.304 -51.829 4.416 1.00 32.99 O HETATM 4702 O HOH A 364 40.032 -24.147 10.509 1.00 37.37 O HETATM 4703 O HOH A 365 8.125 -27.048 26.807 1.00 36.00 O HETATM 4704 O HOH A 366 33.432 -24.746 -0.408 1.00 35.98 O HETATM 4705 O HOH A 367 24.932 -30.652 35.691 1.00 33.13 O HETATM 4706 O HOH A 368 36.935 -31.275 -1.411 1.00 38.36 O HETATM 4707 O AHOH A 369 21.315 -20.785 22.617 0.50 24.39 O HETATM 4708 O BHOH A 369 19.641 -21.592 22.356 0.50 26.94 O HETATM 4709 O HOH A 370 35.005 -20.943 23.497 1.00 38.48 O HETATM 4710 O HOH A 371 41.889 -26.385 7.012 1.00 49.47 O HETATM 4711 O HOH A 372 18.933 -47.141 7.532 1.00 40.84 O HETATM 4712 O HOH A 373 10.070 -49.125 16.256 1.00 39.29 O HETATM 4713 O HOH A 374 44.149 -41.875 8.030 1.00 42.47 O HETATM 4714 O HOH A 375 7.174 -39.993 15.859 1.00 42.29 O HETATM 4715 O HOH A 376 13.282 -47.389 21.945 1.00 35.24 O HETATM 4716 O HOH A 377 15.380 -39.259 2.574 1.00 46.56 O HETATM 4717 O HOH A 378 27.612 -28.369 36.649 1.00 38.94 O HETATM 4718 O HOH A 379 13.371 -29.952 37.676 1.00 45.87 O HETATM 4719 O HOH A 380 39.101 -21.259 1.948 1.00 39.14 O HETATM 4720 O HOH A 381 33.736 -42.973 -6.019 1.00 46.08 O HETATM 4721 O HOH A 382 31.967 -54.844 10.753 1.00 35.87 O HETATM 4722 O HOH A 383 41.020 -30.046 22.831 1.00 44.37 O HETATM 4723 O HOH A 384 32.753 -52.786 13.985 1.00 36.04 O HETATM 4724 O HOH A 385 32.395 -35.276 -5.781 1.00 46.91 O HETATM 4725 O HOH A 386 37.801 -38.044 -1.699 1.00 40.20 O HETATM 4726 O HOH A 387 16.687 -33.591 3.090 1.00 35.27 O HETATM 4727 O HOH A 388 24.999 -18.799 5.910 1.00 34.26 O HETATM 4728 O HOH A 389 34.277 -47.758 -0.815 1.00 38.69 O HETATM 4729 O HOH A 390 19.474 -20.129 33.639 1.00 36.18 O HETATM 4730 O HOH A 391 22.242 -42.247 31.426 1.00 39.26 O HETATM 4731 O HOH A 392 20.627 -35.341 -1.343 1.00 40.69 O HETATM 4732 O HOH A 393 12.945 -48.962 18.737 1.00 37.15 O HETATM 4733 O HOH A 394 24.742 -24.425 36.105 1.00 39.60 O HETATM 4734 O HOH A 395 37.064 -54.248 17.535 1.00 38.52 O HETATM 4735 O HOH A 396 37.500 -21.785 22.489 1.00 37.62 O HETATM 4736 O HOH A 397 20.585 -51.135 3.730 1.00 44.30 O HETATM 4737 O HOH A 398 42.408 -43.670 16.083 1.00 40.56 O HETATM 4738 O HOH A 399 22.817 -18.926 24.880 1.00 41.81 O HETATM 4739 O HOH A 400 39.339 -26.010 28.233 1.00 54.42 O HETATM 4740 O HOH A 401 22.413 -44.989 34.087 1.00 53.07 O HETATM 4741 O HOH A 402 10.671 -46.026 22.127 1.00 40.79 O HETATM 4742 O HOH A 403 40.905 -26.867 20.169 1.00 47.29 O HETATM 4743 O HOH A 404 15.399 -42.365 33.636 1.00 41.91 O HETATM 4744 O HOH A 405 36.291 -19.597 8.594 1.00 44.76 O HETATM 4745 O HOH A 406 20.019 -35.308 34.476 1.00 40.03 O HETATM 4746 O HOH A 407 27.986 -54.402 1.600 1.00 45.26 O HETATM 4747 O HOH A 408 17.985 -36.665 -1.520 1.00 42.93 O HETATM 4748 O AHOH A 409 38.319 -47.703 22.746 0.50 34.77 O HETATM 4749 O BHOH A 409 38.226 -46.231 21.529 0.50 33.29 O HETATM 4750 O HOH A 410 36.570 -47.414 0.336 1.00 37.12 O HETATM 4751 O HOH A 411 34.485 -21.856 25.743 1.00 36.63 O HETATM 4752 O HOH A 412 17.909 -54.786 9.598 1.00 49.70 O HETATM 4753 O HOH A 413 39.022 -47.428 19.437 1.00 49.81 O HETATM 4754 O HOH A 414 31.997 -20.920 26.564 1.00 49.31 O HETATM 4755 O HOH A 415 21.559 -51.747 32.191 1.00 36.75 O HETATM 4756 O HOH A 416 43.867 -35.356 12.515 1.00 45.26 O HETATM 4757 O HOH A 417 15.055 -49.503 25.890 1.00 48.13 O HETATM 4758 O HOH A 418 22.076 -17.397 19.764 1.00 50.65 O HETATM 4759 O HOH A 419 12.957 -50.459 9.676 1.00 47.16 O HETATM 4760 O HOH A 420 19.057 -57.151 16.351 1.00 48.42 O HETATM 4761 O HOH A 421 33.273 -32.919 -3.549 1.00 50.00 O HETATM 4762 O HOH A 422 26.935 -38.577 -7.812 1.00 49.94 O HETATM 4763 O HOH A 423 26.567 -34.323 33.125 1.00 51.31 O HETATM 4764 O HOH A 424 39.511 -46.551 12.218 1.00 45.92 O HETATM 4765 O HOH A 425 22.345 -32.112 -0.291 1.00 39.97 O HETATM 4766 O HOH A 426 27.552 -22.679 34.639 1.00 48.37 O HETATM 4767 O HOH A 427 14.041 -37.329 35.059 1.00 42.87 O HETATM 4768 O HOH A 428 30.691 -33.172 -4.522 1.00 56.79 O HETATM 4769 O HOH A 429 11.740 -33.181 9.874 1.00 50.39 O HETATM 4770 O HOH A 430 12.984 -32.125 8.185 1.00 26.49 O HETATM 4771 O HOH A 431 13.151 -34.850 8.036 1.00 44.38 O HETATM 4772 O AHOH A 432 18.687 -31.761 2.347 0.50 12.38 O HETATM 4773 O BHOH A 432 18.036 -32.644 1.329 0.50 21.23 O HETATM 4774 O HOH A 433 19.269 -31.886 -0.329 1.00 31.61 O HETATM 4775 O HOH A 434 19.848 -33.151 36.419 1.00 39.86 O HETATM 4776 O HOH A 435 25.091 -35.387 -4.181 1.00 41.75 O HETATM 4777 O HOH A 436 22.282 -27.602 -0.702 1.00 50.49 O HETATM 4778 O HOH A 437 7.235 -23.957 20.445 1.00 37.42 O HETATM 4779 O HOH A 438 11.297 -43.255 27.344 1.00 38.95 O HETATM 4780 O HOH A 439 11.914 -45.529 26.614 1.00 44.57 O HETATM 4781 O HOH A 440 25.639 -36.802 32.265 1.00 46.85 O HETATM 4782 O HOH A 441 19.003 -54.555 18.602 1.00 41.26 O HETATM 4783 O HOH A 442 8.351 -37.270 26.263 1.00 50.71 O HETATM 4784 O HOH A 443 25.291 -47.482 -6.558 1.00 44.57 O HETATM 4785 O HOH A 444 17.386 -16.124 27.110 1.00 48.78 O HETATM 4786 O HOH A 445 45.714 -36.461 16.645 1.00 45.69 O HETATM 4787 O HOH A 446 13.543 -15.211 17.087 1.00 49.01 O HETATM 4788 O HOH A 447 8.597 -21.354 23.503 1.00 42.30 O HETATM 4789 O HOH A 448 22.859 -16.956 5.763 1.00 47.30 O HETATM 4790 O HOH A 449 39.133 -46.146 2.195 1.00 35.18 O HETATM 4791 O HOH A 450 25.766 -16.315 9.757 1.00 36.52 O HETATM 4792 O HOH A 451 41.906 -25.638 11.414 1.00 44.39 O HETATM 4793 O HOH A 452 31.768 -48.553 -3.314 1.00 44.03 O HETATM 4794 O HOH A 453 11.360 -17.422 25.095 1.00 42.28 O HETATM 4795 O HOH A 454 7.936 -19.496 18.733 1.00 42.36 O HETATM 4796 O HOH A 455 6.469 -21.995 18.408 1.00 51.68 O HETATM 4797 O HOH A 456 5.425 -25.523 19.550 1.00 48.31 O HETATM 4798 O HOH A 457 6.355 -28.168 20.515 1.00 51.07 O HETATM 4799 O HOH A 458 6.500 -30.761 22.891 1.00 41.35 O HETATM 4800 O HOH A 459 5.981 -31.389 20.329 1.00 49.34 O HETATM 4801 O HOH A 460 5.691 -36.081 23.244 1.00 49.62 O HETATM 4802 O HOH A 461 33.008 -17.809 10.415 1.00 47.32 O HETATM 4803 O HOH A 462 41.049 -44.148 19.634 1.00 47.39 O HETATM 4804 O HOH A 463 25.142 -44.601 -8.223 1.00 51.19 O HETATM 4805 O HOH A 464 28.804 -17.555 17.400 1.00 44.11 O HETATM 4806 O HOH A 465 31.548 -18.617 25.097 1.00 49.83 O HETATM 4807 O HOH A 466 15.440 -46.985 31.470 1.00 60.64 O HETATM 4808 O HOH A 467 42.570 -39.373 -1.089 1.00 54.20 O HETATM 4809 O HOH A 468 42.060 -41.660 22.483 1.00 57.17 O HETATM 4810 O HOH A 469 18.996 -17.872 19.864 1.00 48.42 O HETATM 4811 O HOH A 470 20.028 -16.083 17.604 1.00 49.69 O HETATM 4812 O HOH A 471 40.365 -49.397 13.706 1.00 49.76 O HETATM 4813 O HOH A 472 41.061 -45.992 1.126 1.00 58.06 O HETATM 4814 O HOH A 473 38.979 -50.726 19.269 1.00 54.59 O HETATM 4815 O HOH A 474 15.316 -52.052 17.482 1.00 47.02 O HETATM 4816 O HOH A 475 24.806 -19.414 28.792 1.00 47.34 O HETATM 4817 O HOH A 476 38.658 -45.282 -0.233 1.00 54.60 O HETATM 4818 O HOH A 477 12.672 -52.116 11.386 1.00 49.43 O HETATM 4819 O HOH A 478 29.794 -52.753 14.225 1.00 52.47 O HETATM 4820 O HOH A 479 20.510 -40.306 -4.432 1.00 52.40 O HETATM 4821 O HOH A 480 20.882 -37.672 -4.103 1.00 46.47 O HETATM 4822 O HOH A 481 42.961 -31.999 15.961 1.00 55.79 O HETATM 4823 O HOH A 482 31.139 -26.222 -0.239 1.00 49.05 O HETATM 4824 O HOH A 483 32.470 -19.672 17.142 1.00 35.45 O HETATM 4825 O HOH A 484 36.090 -45.127 20.256 1.00 49.63 O HETATM 4826 O HOH B 251 -5.334 -19.249 6.215 1.00 17.64 O HETATM 4827 O HOH B 252 2.277 -27.273 3.576 1.00 17.10 O HETATM 4828 O HOH B 253 -1.786 -24.923 -1.112 1.00 14.52 O HETATM 4829 O HOH B 254 -4.355 -6.617 1.907 1.00 13.59 O HETATM 4830 O HOH B 255 -2.097 -22.351 -0.074 1.00 13.67 O HETATM 4831 O HOH B 256 -5.856 -16.433 -1.623 1.00 18.22 O HETATM 4832 O HOH B 257 10.035 -17.046 0.845 1.00 17.11 O HETATM 4833 O HOH B 258 5.918 -16.278 5.185 1.00 17.19 O HETATM 4834 O HOH B 259 -9.528 -1.272 -4.663 1.00 17.80 O HETATM 4835 O HOH B 260 9.567 -16.019 6.997 1.00 17.55 O HETATM 4836 O HOH B 261 -8.857 -2.449 -7.216 1.00 17.64 O HETATM 4837 O HOH B 262 10.423 -19.378 -3.448 1.00 18.62 O HETATM 4838 O HOH B 263 5.199 -15.919 -0.202 1.00 15.63 O HETATM 4839 O HOH B 264 6.275 -7.109 12.480 1.00 18.80 O HETATM 4840 O HOH B 265 -12.815 -25.309 1.236 1.00 20.77 O HETATM 4841 O HOH B 266 12.003 -16.810 5.559 1.00 17.69 O HETATM 4842 O HOH B 267 13.210 -17.751 1.940 1.00 17.74 O HETATM 4843 O HOH B 268 8.729 -11.518 12.584 1.00 18.90 O HETATM 4844 O HOH B 269 -18.942 -30.051 1.605 1.00 22.14 O HETATM 4845 O HOH B 270 -0.473 -0.565 1.842 1.00 19.17 O HETATM 4846 O HOH B 271 -11.899 -25.332 -15.742 1.00 21.60 O HETATM 4847 O HOH B 272 -5.878 -31.500 -5.130 1.00 18.53 O HETATM 4848 O HOH B 273 5.779 -5.710 4.257 1.00 21.53 O HETATM 4849 O HOH B 274 -10.167 -27.475 0.078 1.00 20.46 O HETATM 4850 O HOH B 275 1.958 -8.582 -6.959 1.00 20.11 O HETATM 4851 O HOH B 276 11.150 -2.044 -4.161 1.00 20.58 O HETATM 4852 O HOH B 277 8.161 -5.346 11.372 1.00 20.87 O HETATM 4853 O HOH B 278 14.633 -0.606 4.137 1.00 21.77 O HETATM 4854 O HOH B 279 -7.452 -33.439 -3.735 1.00 18.37 O HETATM 4855 O HOH B 280 2.849 -21.278 13.676 1.00 21.46 O HETATM 4856 O HOH B 281 -2.911 -11.130 -17.375 1.00 24.35 O HETATM 4857 O HOH B 282 -15.776 -12.497 0.828 1.00 23.92 O HETATM 4858 O HOH B 283 -12.534 -27.620 5.487 1.00 27.16 O HETATM 4859 O HOH B 284 -25.085 -23.082 0.345 1.00 28.89 O HETATM 4860 O HOH B 285 -7.363 -7.771 8.810 1.00 23.38 O HETATM 4861 O AHOH B 286 2.726 -10.510 -5.055 0.50 13.03 O HETATM 4862 O BHOH B 286 3.868 -10.406 -6.116 0.50 25.96 O HETATM 4863 O HOH B 287 4.647 -27.277 8.121 1.00 22.19 O HETATM 4864 O HOH B 288 8.600 0.733 7.314 1.00 22.37 O HETATM 4865 O HOH B 289 15.606 -22.622 6.066 1.00 28.90 O HETATM 4866 O HOH B 290 7.483 -15.561 -15.685 1.00 25.01 O HETATM 4867 O HOH B 291 -9.607 -35.662 -1.665 1.00 23.27 O HETATM 4868 O HOH B 292 -9.936 -42.090 -0.851 1.00 30.75 O HETATM 4869 O HOH B 293 -12.325 -43.485 -0.605 1.00 24.13 O HETATM 4870 O HOH B 294 -0.241 -1.658 4.268 1.00 30.21 O HETATM 4871 O HOH B 295 11.099 -1.647 10.659 1.00 28.22 O HETATM 4872 O HOH B 296 9.488 -7.207 -8.534 1.00 22.41 O HETATM 4873 O HOH B 297 -6.391 -3.303 -10.323 1.00 25.59 O HETATM 4874 O HOH B 298 -18.387 -32.183 -5.990 1.00 23.16 O HETATM 4875 O HOH B 299 9.610 -4.496 -9.614 1.00 27.60 O HETATM 4876 O HOH B 300 12.438 -22.869 -3.261 1.00 29.31 O HETATM 4877 O HOH B 301 -13.173 -33.687 3.063 1.00 27.85 O HETATM 4878 O HOH B 302 11.976 -17.652 13.202 1.00 26.78 O HETATM 4879 O HOH B 303 -11.561 -1.049 -0.826 1.00 26.80 O HETATM 4880 O HOH B 304 -23.714 -29.297 3.236 1.00 31.16 O HETATM 4881 O HOH B 305 -6.937 -14.133 -17.848 1.00 30.29 O HETATM 4882 O HOH B 306 -8.381 -29.078 -14.990 1.00 37.25 O HETATM 4883 O HOH B 307 4.824 -23.344 13.626 1.00 31.74 O HETATM 4884 O HOH B 308 -12.886 0.010 -3.099 1.00 30.21 O HETATM 4885 O HOH B 309 -9.512 -8.754 -17.629 1.00 31.67 O HETATM 4886 O HOH B 310 -14.686 -14.079 7.143 1.00 32.68 O HETATM 4887 O HOH B 311 -8.718 -18.107 9.737 1.00 26.90 O HETATM 4888 O HOH B 312 17.559 -6.996 -5.074 1.00 29.46 O HETATM 4889 O HOH B 313 5.985 -5.483 14.723 1.00 29.35 O HETATM 4890 O HOH B 314 -8.048 -25.236 -22.093 1.00 32.54 O HETATM 4891 O HOH B 315 10.442 -26.187 -2.788 1.00 26.35 O HETATM 4892 O HOH B 316 1.279 -23.962 -15.618 1.00 33.28 O HETATM 4893 O HOH B 317 -22.041 -26.973 -6.602 1.00 32.87 O HETATM 4894 O HOH B 318 8.730 -27.933 8.122 1.00 27.11 O HETATM 4895 O HOH B 319 -14.524 -42.459 0.945 1.00 34.40 O HETATM 4896 O HOH B 320 8.300 -12.493 15.268 1.00 27.99 O HETATM 4897 O HOH B 321 0.642 -29.269 -15.110 1.00 29.41 O HETATM 4898 O HOH B 322 7.599 -9.193 13.597 1.00 21.14 O HETATM 4899 O HOH B 323 -11.415 -28.098 -15.103 1.00 23.24 O HETATM 4900 O HOH B 324 -10.135 -7.168 -15.570 1.00 25.53 O HETATM 4901 O HOH B 325 -19.588 -7.411 -7.232 1.00 27.63 O HETATM 4902 O HOH B 326 -20.751 -28.707 -4.767 0.50 28.73 O HETATM 4903 O HOH B 327 12.081 -25.706 -0.457 1.00 30.14 O HETATM 4904 O HOH B 328 -15.351 -7.503 4.393 1.00 28.78 O HETATM 4905 O HOH B 329 12.073 -8.466 12.387 1.00 29.03 O HETATM 4906 O HOH B 330 -16.284 -9.822 1.699 1.00 28.47 O HETATM 4907 O HOH B 331 -8.208 -14.478 11.876 1.00 29.71 O HETATM 4908 O HOH B 332 1.475 -30.597 13.608 1.00 32.05 O HETATM 4909 O HOH B 333 4.663 -19.142 14.441 1.00 30.86 O HETATM 4910 O HOH B 334 12.083 -15.280 14.601 1.00 29.12 O HETATM 4911 O HOH B 335 12.586 -33.269 4.573 1.00 36.13 O HETATM 4912 O HOH B 336 1.974 -4.371 -15.471 1.00 33.95 O HETATM 4913 O AHOH B 337 10.454 -29.823 -4.206 0.50 20.57 O HETATM 4914 O BHOH B 337 10.126 -28.451 -4.651 0.50 24.94 O HETATM 4915 O AHOH B 338 -14.275 -26.401 12.987 0.50 22.21 O HETATM 4916 O BHOH B 338 -13.937 -25.344 14.252 0.50 31.87 O HETATM 4917 O HOH B 339 14.053 -32.662 2.453 1.00 29.39 O HETATM 4918 O HOH B 340 3.414 0.000 0.000 0.50 32.52 O HETATM 4919 O HOH B 341 -13.920 -9.198 -16.561 1.00 36.44 O HETATM 4920 O HOH B 342 -8.195 -28.361 7.295 1.00 34.54 O HETATM 4921 O HOH B 343 -1.540 -30.537 -15.817 1.00 34.73 O HETATM 4922 O HOH B 344 6.576 -29.040 9.386 1.00 37.68 O HETATM 4923 O HOH B 345 -3.113 -1.876 -7.336 1.00 35.10 O HETATM 4924 O HOH B 346 -7.410 -10.661 -17.731 1.00 28.49 O HETATM 4925 O HOH B 347 -13.284 -19.049 8.445 1.00 31.45 O HETATM 4926 O HOH B 348 8.313 -2.858 12.741 1.00 29.91 O HETATM 4927 O HOH B 349 -5.989 -2.053 -8.096 1.00 27.48 O HETATM 4928 O HOH B 350 9.827 -14.596 16.277 1.00 38.53 O HETATM 4929 O HOH B 351 19.058 -8.109 1.091 1.00 34.82 O HETATM 4930 O HOH B 352 0.559 -21.722 -13.818 1.00 35.33 O HETATM 4931 O HOH B 353 -9.534 -1.096 -9.622 1.00 35.73 O HETATM 4932 O HOH B 354 -12.708 -7.456 -14.774 1.00 33.23 O HETATM 4933 O HOH B 355 -16.513 -37.096 -0.505 1.00 34.71 O HETATM 4934 O HOH B 356 -0.387 -9.929 -18.248 1.00 39.93 O HETATM 4935 O HOH B 357 9.571 -7.635 14.600 1.00 35.79 O HETATM 4936 O HOH B 358 -8.590 -4.885 8.110 1.00 35.92 O HETATM 4937 O HOH B 359 0.620 -34.723 5.814 1.00 33.59 O HETATM 4938 O HOH B 360 13.972 -19.088 -5.337 1.00 35.58 O HETATM 4939 O HOH B 361 -6.123 -4.256 8.684 1.00 33.88 O HETATM 4940 O HOH B 362 3.589 -3.254 6.531 1.00 33.36 O HETATM 4941 O HOH B 363 5.977 -4.049 -12.758 1.00 33.40 O HETATM 4942 O HOH B 364 19.424 -4.560 2.168 1.00 33.71 O HETATM 4943 O HOH B 365 -16.361 -34.268 9.121 1.00 31.97 O HETATM 4944 O HOH B 366 3.362 -10.412 -18.195 1.00 33.38 O HETATM 4945 O HOH B 367 13.890 -34.731 0.292 1.00 32.56 O HETATM 4946 O HOH B 368 -22.370 -21.792 -20.384 1.00 33.71 O HETATM 4947 O HOH B 369 -18.260 -4.350 -13.277 1.00 30.87 O HETATM 4948 O HOH B 370 9.793 -2.902 -7.277 1.00 31.28 O HETATM 4949 O HOH B 371 -5.261 -13.239 12.664 1.00 34.11 O HETATM 4950 O HOH B 372 -19.546 -33.045 -3.323 1.00 32.75 O HETATM 4951 O HOH B 373 -12.558 -19.928 -19.224 1.00 42.58 O HETATM 4952 O HOH B 374 -11.856 -26.616 8.568 1.00 35.89 O HETATM 4953 O HOH B 375 -19.887 -18.233 3.405 1.00 33.56 O HETATM 4954 O HOH B 376 -1.838 -29.549 14.791 1.00 38.96 O HETATM 4955 O HOH B 377 -14.196 -20.819 10.351 1.00 33.85 O HETATM 4956 O HOH B 378 -21.097 -14.137 -10.168 1.00 41.83 O HETATM 4957 O AHOH B 379 -10.812 -2.234 -11.545 0.50 25.22 O HETATM 4958 O BHOH B 379 -12.052 -2.754 -12.288 0.50 30.56 O HETATM 4959 O HOH B 380 4.595 -2.467 -0.699 1.00 30.92 O HETATM 4960 O HOH B 381 0.638 -19.317 -15.843 1.00 35.89 O HETATM 4961 O HOH B 382 -18.367 -35.007 -0.777 1.00 36.04 O HETATM 4962 O HOH B 383 -2.738 -2.460 -9.999 1.00 32.65 O HETATM 4963 O HOH B 384 -21.557 -30.856 6.995 1.00 42.50 O HETATM 4964 O HOH B 385 -24.484 -22.269 -2.238 1.00 34.49 O HETATM 4965 O HOH B 386 -5.072 -35.224 -7.625 1.00 32.50 O HETATM 4966 O HOH B 387 -0.310 -2.042 -12.505 1.00 29.53 O HETATM 4967 O HOH B 388 3.494 -3.207 -13.247 1.00 33.61 O HETATM 4968 O HOH B 389 -2.182 0.647 -8.199 1.00 37.13 O HETATM 4969 O HOH B 390 -9.425 -20.036 11.059 1.00 49.29 O HETATM 4970 O HOH B 391 -12.309 -16.942 -18.485 1.00 42.80 O HETATM 4971 O HOH B 392 11.819 -4.569 14.774 1.00 47.17 O HETATM 4972 O HOH B 393 3.521 -0.495 -12.707 1.00 42.45 O HETATM 4973 O HOH B 394 17.659 -9.648 10.350 1.00 48.06 O HETATM 4974 O HOH B 395 1.263 -21.197 16.021 1.00 36.86 O HETATM 4975 O HOH B 396 -10.308 -3.707 8.926 1.00 39.43 O HETATM 4976 O HOH B 397 -14.999 -18.902 6.578 1.00 31.69 O HETATM 4977 O AHOH B 398 -10.560 -23.995 -22.388 0.50 24.20 O HETATM 4978 O HOH B 399 -1.719 -27.079 -17.592 1.00 38.82 O HETATM 4979 O HOH B 400 11.416 -9.159 15.797 1.00 43.19 O HETATM 4980 O HOH B 401 19.219 -9.165 -1.553 1.00 46.99 O HETATM 4981 O HOH B 402 19.602 -15.880 3.122 1.00 37.56 O HETATM 4982 O HOH B 403 -14.904 -4.097 8.652 1.00 45.26 O HETATM 4983 O HOH B 404 21.889 -15.941 12.974 1.00 43.99 O HETATM 4984 O HOH B 405 6.907 -0.365 11.878 1.00 44.29 O HETATM 4985 O HOH B 406 -2.733 -39.745 3.418 1.00 38.71 O HETATM 4986 O HOH B 407 0.805 -24.039 17.215 1.00 45.05 O HETATM 4987 O HOH B 408 -5.190 0.399 -8.996 1.00 34.50 O HETATM 4988 O HOH B 409 -6.286 2.242 -10.128 1.00 39.72 O HETATM 4989 O HOH B 410 16.668 -9.260 -3.819 1.00 36.40 O HETATM 4990 O HOH B 411 -8.698 1.241 -10.586 1.00 42.62 O HETATM 4991 O HOH B 412 -5.321 -6.684 10.006 1.00 40.25 O HETATM 4992 O HOH B 413 -21.772 -24.308 -16.258 1.00 32.27 O HETATM 4993 O HOH B 414 15.267 -22.186 -0.026 1.00 33.78 O HETATM 4994 O HOH B 415 3.577 -30.393 10.462 1.00 37.98 O HETATM 4995 O HOH B 416 -14.498 -8.893 8.799 1.00 50.45 O HETATM 4996 O HOH B 417 16.915 -21.528 -2.391 1.00 40.73 O HETATM 4997 O HOH B 418 -20.405 -18.891 -15.381 1.00 35.28 O HETATM 4998 O HOH B 419 -20.302 -33.169 4.063 1.00 45.45 O HETATM 4999 O HOH B 420 -4.339 -19.510 14.205 1.00 42.96 O HETATM 5000 O HOH B 421 -20.661 -31.914 1.189 1.00 46.36 O HETATM 5001 O HOH B 422 6.019 -9.777 15.817 1.00 37.82 O HETATM 5002 O HOH B 423 13.815 -23.687 -1.182 1.00 42.12 O HETATM 5003 O HOH B 424 16.670 -16.909 15.630 1.00 37.22 O HETATM 5004 O HOH B 425 21.539 -12.609 5.697 1.00 50.72 O HETATM 5005 O HOH B 426 -21.430 -15.626 -1.737 1.00 41.51 O HETATM 5006 O HOH B 427 16.320 -10.954 12.596 1.00 38.16 O HETATM 5007 O HOH B 428 -20.094 -14.110 0.654 1.00 49.19 O HETATM 5008 O HOH B 429 -13.948 -4.710 1.196 1.00 39.55 O HETATM 5009 O HOH B 430 -9.721 -27.220 5.375 1.00 39.47 O HETATM 5010 O HOH B 431 20.844 -11.044 2.942 1.00 52.20 O HETATM 5011 O HOH B 432 -12.439 -2.883 1.109 1.00 37.55 O HETATM 5012 O HOH B 433 -17.129 -40.271 0.325 1.00 37.43 O HETATM 5013 O HOH B 434 -12.842 -33.576 5.976 1.00 40.96 O HETATM 5014 O AHOH B 435 -2.925 -0.657 0.684 0.50 17.40 O HETATM 5015 O BHOH B 435 -2.879 -2.041 1.120 0.50 18.59 O HETATM 5016 O HOH B 436 2.392 -36.202 -0.235 1.00 34.36 O HETATM 5017 O HOH B 437 -16.022 -5.685 1.883 1.00 45.81 O HETATM 5018 O HOH B 438 -6.947 -2.705 -14.278 1.00 51.11 O HETATM 5019 O AHOH B 439 -2.873 -7.180 8.901 0.50 18.28 O HETATM 5020 O HOH B 440 -9.603 -22.274 14.305 1.00 38.25 O HETATM 5021 O HOH B 441 -14.453 -25.530 10.172 1.00 42.14 O HETATM 5022 O HOH B 442 16.320 -1.694 -0.255 1.00 40.62 O HETATM 5023 O HOH B 443 -2.768 -36.610 -8.216 1.00 36.08 O HETATM 5024 O HOH B 444 -9.085 -17.666 -19.115 1.00 37.27 O HETATM 5025 O HOH B 445 -17.347 -13.781 3.531 1.00 40.33 O HETATM 5026 O HOH B 446 6.453 -27.099 13.309 1.00 42.84 O HETATM 5027 O HOH B 447 1.936 -36.530 4.434 1.00 38.00 O HETATM 5028 O HOH B 448 16.769 -28.016 -2.648 1.00 50.73 O HETATM 5029 O HOH B 449 17.157 -23.338 1.250 1.00 37.71 O HETATM 5030 O HOH B 450 -4.025 -7.807 -20.305 1.00 42.31 O HETATM 5031 O AHOH B 451 1.974 -16.439 -18.900 0.50 44.50 O HETATM 5032 O BHOH B 451 2.994 -15.632 -18.705 0.50 45.77 O HETATM 5033 O HOH B 452 5.903 -3.868 1.537 1.00 43.55 O HETATM 5034 O HOH B 453 -5.038 -10.838 -19.544 1.00 52.23 O HETATM 5035 O HOH B 454 19.600 -24.289 0.142 1.00 39.57 O HETATM 5036 O BHOH B 455 -2.510 -4.540 2.331 0.50 16.87 O HETATM 5037 O BHOH B 456 -0.459 -5.219 3.626 0.50 22.99 O HETATM 5038 O HOH B 457 14.065 -13.717 -5.359 1.00 43.36 O HETATM 5039 O HOH B 458 -20.084 -30.629 -6.742 1.00 42.39 O HETATM 5040 O HOH B 459 11.045 -31.236 6.285 1.00 41.97 O HETATM 5041 O HOH B 460 -17.890 -22.381 7.503 1.00 40.16 O HETATM 5042 O HOH B 461 -5.225 -27.795 -16.159 1.00 38.79 O HETATM 5043 O HOH B 462 13.600 -27.367 -1.530 1.00 41.85 O HETATM 5044 O HOH B 463 -9.913 -20.170 -19.569 1.00 44.98 O HETATM 5045 O HOH B 464 16.273 -11.380 -10.494 1.00 58.03 O HETATM 5046 O HOH B 465 -18.151 -17.042 6.045 1.00 42.74 O HETATM 5047 O HOH B 466 3.846 -2.118 2.043 1.00 44.56 O HETATM 5048 O HOH B 467 18.901 -26.343 -0.901 1.00 48.12 O HETATM 5049 O HOH B 468 -11.625 -41.987 3.995 1.00 49.68 O HETATM 5050 O HOH B 469 -23.562 -16.424 -12.362 1.00 49.65 O HETATM 5051 O HOH B 470 2.142 -3.611 4.135 1.00 34.09 O HETATM 5052 O HOH B 471 -17.570 -18.217 8.315 1.00 40.51 O HETATM 5053 O HOH B 472 -18.781 -20.605 8.761 1.00 39.06 O HETATM 5054 O HOH B 473 -3.903 -42.423 -4.231 1.00 49.10 O HETATM 5055 O HOH B 474 -20.593 -34.354 0.384 1.00 46.93 O HETATM 5056 O HOH B 475 -25.232 -27.058 3.553 1.00 51.34 O HETATM 5057 O AHOH B 476 -9.206 -28.375 9.698 0.50 34.18 O HETATM 5058 O BHOH B 476 -10.607 -29.839 9.943 0.50 29.47 O HETATM 5059 O HOH B 477 -3.210 -1.811 -13.205 1.00 51.11 O HETATM 5060 O HOH B 478 -4.342 -8.065 16.124 1.00 52.74 O HETATM 5061 O HOH B 479 -8.636 -36.479 6.979 1.00 51.77 O HETATM 5062 O HOH B 480 10.561 -2.501 13.487 1.00 43.63 O HETATM 5063 O HOH B 481 -7.798 -2.228 -12.056 1.00 52.03 O HETATM 5064 O HOH B 482 -11.231 -16.824 9.825 1.00 40.98 O HETATM 5065 O HOH B 483 -13.751 -17.800 -20.368 1.00 35.07 O HETATM 5066 O HOH B 484 -9.695 -4.332 -16.004 1.00 36.25 O HETATM 5067 O HOH B 485 0.937 -1.715 13.344 1.00 41.18 O HETATM 5068 O HOH B 486 8.122 -5.121 -16.511 1.00 44.07 O HETATM 5069 O HOH B 487 -22.852 -26.614 -14.343 1.00 52.57 O HETATM 5070 O HOH B 488 19.675 -21.383 -0.941 1.00 47.83 O HETATM 5071 O HOH B 489 -0.623 -27.629 -21.232 1.00 44.78 O HETATM 5072 O HOH B 490 -19.552 -30.015 -9.063 1.00 39.97 O HETATM 5073 O HOH B 491 -24.939 -25.347 -5.525 1.00 44.60 O HETATM 5074 O HOH B 492 -0.110 -4.948 15.417 1.00 46.79 O HETATM 5075 O HOH B 493 -8.044 -37.127 -8.828 1.00 45.77 O HETATM 5076 O HOH B 494 -8.424 -37.448 -3.566 1.00 35.33 O HETATM 5077 O HOH B 495 -10.020 -38.152 -5.847 1.00 51.74 O HETATM 5078 O HOH B 496 15.859 -5.372 8.022 1.00 41.98 O HETATM 5079 O HOH B 497 14.823 -2.726 7.937 1.00 41.80 O HETATM 5080 O HOH B 498 15.883 -0.427 6.567 1.00 44.21 O HETATM 5081 O HOH B 499 13.804 -1.907 10.185 1.00 43.89 O HETATM 5082 O HOH B 500 -17.915 -9.811 3.825 1.00 53.85 O HETATM 5083 O HOH B 501 -25.944 -19.605 -10.113 1.00 52.89 O HETATM 5084 O HOH B 502 -16.634 0.235 -8.165 1.00 51.32 O HETATM 5085 O HOH B 503 -8.952 -12.605 -18.922 1.00 45.23 O HETATM 5086 O HOH B 504 7.431 -3.130 -10.971 1.00 41.81 O HETATM 5087 O HOH B 505 -11.892 -10.112 -18.341 1.00 42.75 O HETATM 5088 O HOH B 506 -21.911 -17.445 1.747 1.00 44.58 O HETATM 5089 O HOH B 507 9.903 0.632 10.195 1.00 37.98 O HETATM 5090 O HOH B 508 11.150 -32.251 -5.445 1.00 34.52 O HETATM 5091 O HOH B 509 -3.151 -37.162 -12.602 1.00 36.90 O HETATM 5092 O HOH B 510 -0.531 -36.148 -14.077 1.00 54.34 O HETATM 5093 O HOH B 511 -19.097 -8.357 -4.990 1.00 44.38 O HETATM 5094 O HOH B 512 -5.332 3.034 -12.888 1.00 48.52 O HETATM 5095 O HOH B 513 -0.085 -22.354 -17.413 1.00 44.73 O HETATM 5096 O HOH B 514 -25.452 -20.524 1.301 1.00 51.41 O HETATM 5097 O HOH B 515 17.171 -12.392 -2.886 1.00 48.28 O HETATM 5098 O HOH B 516 -7.459 -3.343 -17.940 1.00 49.88 O HETATM 5099 O HOH B 517 -5.116 -26.213 -18.606 1.00 45.33 O HETATM 5100 O HOH B 518 -17.277 -36.532 6.584 1.00 58.78 O HETATM 5101 O HOH B 519 3.700 -5.154 -17.317 1.00 48.52 O HETATM 5102 O HOH B 520 2.714 -7.060 -18.599 1.00 51.14 O HETATM 5103 O HOH B 521 -10.712 -14.881 -19.097 1.00 45.00 O HETATM 5104 O HOH B 522 3.571 -9.070 16.321 1.00 46.85 O HETATM 5105 O HOH B 523 -10.949 -20.800 -22.336 1.00 53.92 O HETATM 5106 O HOH B 524 15.838 -22.080 2.474 1.00 50.43 O HETATM 5107 O HOH B 525 14.539 -13.952 -9.329 1.00 43.25 O HETATM 5108 O HOH B 526 15.372 -15.425 -6.599 1.00 57.92 O HETATM 5109 O HOH B 527 16.413 -19.433 -4.111 1.00 52.41 O HETATM 5110 O AHOH B 528 15.312 -7.068 6.073 0.50 24.96 O HETATM 5111 O BHOH B 528 16.337 -8.373 5.728 0.50 22.75 O HETATM 5112 O HOH B 529 0.292 -16.536 -15.408 1.00 32.33 O HETATM 5113 O AHOH B 530 -22.614 -16.004 -5.595 0.50 41.63 O HETATM 5114 O BHOH B 530 -21.325 -14.589 -7.360 0.50 42.96 O HETATM 5115 O AHOH B 531 4.270 -16.372 -14.599 0.50 17.63 O HETATM 5116 O BHOH B 531 3.143 -16.328 -15.849 0.50 34.84 O HETATM 5117 O HOH I 64 12.549 -23.389 -15.413 1.00 17.73 O HETATM 5118 O HOH I 65 14.432 -25.300 -16.068 1.00 18.16 O HETATM 5119 O HOH I 66 17.623 -24.293 -19.590 1.00 19.70 O HETATM 5120 O HOH I 67 9.021 -19.772 -10.114 1.00 16.74 O HETATM 5121 O HOH I 68 16.954 -24.765 -16.913 1.00 20.26 O HETATM 5122 O HOH I 69 6.357 -32.205 -5.473 1.00 25.01 O HETATM 5123 O HOH I 70 6.633 -27.762 -23.277 1.00 25.19 O HETATM 5124 O HOH I 71 20.619 -23.288 -26.279 1.00 25.28 O HETATM 5125 O HOH I 72 2.998 -20.213 -14.859 1.00 36.12 O HETATM 5126 O HOH I 73 4.012 -36.050 -20.311 1.00 33.46 O HETATM 5127 O HOH I 74 12.069 -30.579 -8.201 1.00 26.68 O HETATM 5128 O HOH I 75 11.037 -39.241 -20.447 1.00 35.33 O HETATM 5129 O HOH I 76 14.930 -17.206 -15.420 1.00 30.09 O HETATM 5130 O HOH I 77 24.334 -32.485 -26.484 1.00 30.52 O HETATM 5131 O HOH I 78 2.380 -27.233 -16.768 1.00 30.89 O HETATM 5132 O HOH I 79 7.726 -22.159 -20.299 1.00 37.85 O HETATM 5133 O HOH I 80 21.750 -22.456 -22.088 1.00 32.92 O HETATM 5134 O HOH I 81 14.642 -29.582 -8.991 1.00 36.01 O HETATM 5135 O AHOH I 82 16.916 -38.417 -13.540 0.50 23.27 O HETATM 5136 O BHOH I 82 16.283 -37.267 -13.985 0.50 25.42 O HETATM 5137 O HOH I 83 15.345 -41.991 -12.093 1.00 33.24 O HETATM 5138 O HOH I 84 19.468 -23.615 -14.460 1.00 38.59 O HETATM 5139 O HOH I 85 18.651 -27.667 -10.285 1.00 31.90 O HETATM 5140 O HOH I 86 24.309 -25.455 -21.686 1.00 37.78 O HETATM 5141 O HOH I 87 23.745 -29.599 -26.890 1.00 36.76 O HETATM 5142 O HOH I 88 20.472 -21.890 -17.075 1.00 34.55 O HETATM 5143 O HOH I 89 7.456 -24.750 -20.838 1.00 42.73 O HETATM 5144 O HOH I 90 10.445 -22.051 -20.858 1.00 38.03 O HETATM 5145 O HOH I 91 15.853 -18.398 -20.473 1.00 34.23 O HETATM 5146 O HOH I 92 14.949 -18.565 -7.489 1.00 48.66 O HETATM 5147 O HOH I 93 14.783 -27.204 -9.822 1.00 34.22 O HETATM 5148 O HOH I 94 16.663 -33.181 -29.870 1.00 29.92 O HETATM 5149 O HOH I 95 21.950 -36.828 -23.741 1.00 35.09 O HETATM 5150 O HOH I 96 18.615 -24.291 -10.736 1.00 42.56 O HETATM 5151 O HOH I 97 14.383 -15.509 -11.425 1.00 38.67 O HETATM 5152 O HOH I 98 2.117 -31.346 -15.536 1.00 45.48 O HETATM 5153 O HOH I 99 4.133 -35.828 -14.495 1.00 37.70 O HETATM 5154 O HOH I 100 16.343 -39.408 -24.870 1.00 45.35 O HETATM 5155 O HOH I 101 3.125 -29.627 -16.722 1.00 41.05 O HETATM 5156 O HOH I 102 13.165 -21.825 -5.779 1.00 33.08 O HETATM 5157 O HOH I 103 18.920 -17.402 -12.413 1.00 51.73 O HETATM 5158 O HOH I 104 8.018 -17.887 -17.440 1.00 39.93 O HETATM 5159 O HOH I 105 22.960 -34.691 -17.206 1.00 43.19 O HETATM 5160 O HOH I 106 13.164 -18.996 -20.615 1.00 46.04 O HETATM 5161 O HOH I 107 19.092 -17.999 -17.679 1.00 42.18 O HETATM 5162 O HOH I 108 8.440 -36.710 -28.622 1.00 40.59 O HETATM 5163 O HOH I 109 17.173 -36.471 -11.560 1.00 55.39 O HETATM 5164 O HOH I 110 23.639 -31.347 -30.215 1.00 52.45 O HETATM 5165 O HOH I 111 15.187 -35.322 -10.329 1.00 44.64 O HETATM 5166 O HOH I 112 15.774 -31.710 -10.074 1.00 45.29 O HETATM 5167 O HOH I 113 4.558 -36.218 -29.819 1.00 49.94 O HETATM 5168 O HOH I 114 1.910 -35.232 -24.801 1.00 52.29 O HETATM 5169 O HOH I 115 7.540 -34.749 -33.816 1.00 43.14 O HETATM 5170 O HOH I 116 2.539 -32.911 -25.645 1.00 47.61 O HETATM 5171 O HOH I 117 18.916 -43.217 -16.735 1.00 38.20 O HETATM 5172 O HOH I 118 11.210 -16.872 -18.176 1.00 40.13 O HETATM 5173 O HOH I 119 25.423 -21.959 -25.335 1.00 46.72 O HETATM 5174 O HOH I 120 2.198 -21.675 -19.093 1.00 46.69 O HETATM 5175 O HOH I 121 18.625 -38.626 -27.265 1.00 36.93 O HETATM 5176 O AHOH I 122 20.303 -31.223 -17.017 0.50 25.82 O HETATM 5177 O BHOH I 122 20.837 -32.014 -18.744 0.50 18.15 O HETATM 5178 O HOH I 123 17.890 -40.710 -13.164 1.00 53.91 O HETATM 5179 O HOH I 124 16.058 -43.937 -10.146 1.00 47.12 O HETATM 5180 O AHOH I 125 16.747 -46.181 -11.565 0.50 34.42 O HETATM 5181 O BHOH I 125 16.240 -48.345 -11.245 0.50 26.21 O HETATM 5182 O HOH I 126 13.486 -33.255 -9.774 1.00 33.84 O HETATM 5183 O HOH I 127 11.347 -25.185 -23.597 0.50 44.76 O HETATM 5184 O HOH I 128 5.496 -17.061 -16.835 1.00 41.27 O HETATM 5185 O HOH C 61 22.408 -33.883 22.600 1.00 19.09 O HETATM 5186 O HOH C 62 31.310 -37.431 28.461 1.00 19.22 O HETATM 5187 O HOH C 63 44.309 -61.609 44.086 1.00 19.20 O HETATM 5188 O HOH C 64 47.135 -59.589 39.478 1.00 23.15 O HETATM 5189 O HOH C 65 28.817 -48.125 30.960 1.00 32.14 O HETATM 5190 O HOH C 66 36.810 -36.815 23.080 1.00 38.42 O HETATM 5191 O HOH C 67 44.693 -45.214 30.020 1.00 30.27 O HETATM 5192 O HOH C 68 27.672 -49.717 24.690 1.00 27.84 O HETATM 5193 O HOH C 69 44.277 -42.547 30.693 1.00 26.93 O HETATM 5194 O HOH C 70 40.919 -56.589 33.302 1.00 30.49 O HETATM 5195 O HOH C 71 39.725 -45.068 23.553 1.00 44.17 O HETATM 5196 O HOH C 72 42.867 -53.580 26.475 1.00 38.97 O HETATM 5197 O HOH C 73 37.916 -34.611 26.290 1.00 32.36 O HETATM 5198 O HOH C 74 44.304 -59.875 42.035 1.00 33.61 O HETATM 5199 O HOH C 75 49.563 -58.572 39.951 1.00 45.51 O HETATM 5200 O HOH C 76 38.033 -53.107 24.929 1.00 43.00 O HETATM 5201 O HOH C 77 40.952 -39.695 30.271 1.00 41.63 O HETATM 5202 O HOH C 78 36.245 -53.248 22.965 1.00 45.41 O HETATM 5203 O AHOH C 79 33.710 -56.174 41.765 0.50 26.40 O HETATM 5204 O BHOH C 79 32.987 -57.346 43.386 0.50 25.12 O HETATM 5205 O HOH C 80 30.417 -53.645 35.182 1.00 44.57 O HETATM 5206 O HOH C 81 35.273 -40.896 33.276 1.00 23.00 O HETATM 5207 O AHOH C 82 35.145 -42.627 35.431 0.50 16.26 O HETATM 5208 O BHOH C 82 36.326 -42.977 35.037 0.50 22.66 O HETATM 5209 O HOH C 83 44.602 -47.174 46.477 1.00 51.49 O HETATM 5210 O AHOH C 84 37.297 -41.502 39.441 0.50 16.81 O HETATM 5211 O BHOH C 84 39.114 -41.960 38.982 0.50 25.07 O HETATM 5212 O HOH C 85 38.643 -54.302 40.793 1.00 30.32 O HETATM 5213 O AHOH C 86 34.941 -42.059 38.045 0.50 20.99 O HETATM 5214 O BHOH C 86 36.523 -42.417 37.671 0.50 20.46 O HETATM 5215 O AHOH C 87 35.547 -49.367 42.267 0.50 20.87 O HETATM 5216 O BHOH C 87 37.262 -49.650 42.028 0.50 22.84 O HETATM 5217 O HOH C 88 40.837 -39.655 33.234 1.00 46.46 O HETATM 5218 O HOH C 89 42.145 -40.107 44.616 1.00 39.87 O HETATM 5219 O HOH C 90 30.839 -41.289 38.853 1.00 40.82 O HETATM 5220 O HOH C 91 34.437 -34.532 35.440 1.00 39.40 O HETATM 5221 O HOH C 92 46.124 -57.307 42.311 1.00 55.79 O HETATM 5222 O HOH C 93 46.392 -36.533 43.273 1.00 51.47 O HETATM 5223 O HOH C 94 29.780 -54.955 39.876 1.00 50.33 O HETATM 5224 O HOH C 95 44.254 -36.503 44.420 1.00 53.50 O HETATM 5225 O HOH C 96 44.959 -57.938 40.126 1.00 48.86 O HETATM 5226 O HOH C 97 42.299 -54.537 44.183 1.00 36.76 O HETATM 5227 O HOH C 98 38.558 -34.375 32.465 1.00 40.04 O HETATM 5228 O HOH C 99 28.954 -45.376 37.580 1.00 46.65 O HETATM 5229 O HOH C 100 26.166 -39.445 31.473 1.00 44.21 O HETATM 5230 O HOH C 101 41.955 -42.234 29.782 1.00 48.19 O HETATM 5231 O HOH C 102 33.799 -48.529 40.597 1.00 41.00 O HETATM 5232 O HOH C 103 27.701 -39.612 33.892 1.00 34.58 O HETATM 5233 O HOH C 104 28.198 -41.872 34.813 1.00 38.99 O HETATM 5234 O HOH C 105 39.498 -54.738 44.520 1.00 31.72 O HETATM 5235 O BHOH C 106 42.289 -47.015 39.641 0.50 13.82 O HETATM 5236 O HOH C 107 38.839 -43.320 44.978 1.00 36.84 O HETATM 5237 O HOH C 108 44.952 -40.841 43.467 1.00 41.63 O HETATM 5238 O HOH C 109 38.800 -35.673 37.949 1.00 50.67 O HETATM 5239 O HOH C 110 41.457 -34.649 38.749 1.00 51.02 O HETATM 5240 O HOH C 111 48.951 -53.899 39.614 1.00 37.38 O HETATM 5241 O HOH C 112 53.354 -52.752 37.111 1.00 49.85 O HETATM 5242 O HOH C 113 31.691 -54.552 43.598 1.00 49.75 O HETATM 5243 O HOH C 114 45.840 -38.630 40.557 1.00 45.13 O HETATM 5244 O HOH C 115 47.228 -41.387 44.735 1.00 46.52 O HETATM 5245 O HOH C 116 41.886 -56.678 35.783 1.00 49.06 O HETATM 5246 O HOH C 117 42.500 -51.186 24.477 1.00 52.27 O HETATM 5247 O HOH C 118 50.375 -54.707 37.322 1.00 64.56 O HETATM 5248 O HOH C 119 31.799 -46.882 44.646 1.00 54.48 O HETATM 5249 O BHOH C 120 46.491 -47.431 40.736 0.50 24.08 O HETATM 5250 O AHOH C 121 42.662 -44.999 41.347 0.50 28.52 O HETATM 5251 O BHOH C 121 42.387 -46.282 41.692 0.50 15.55 O HETATM 5252 O HOH C 122 40.272 -43.283 22.901 1.00 50.77 O CONECT 49 1061 CONECT 194 309 CONECT 309 194 CONECT 403 4461 CONECT 417 4461 CONECT 442 4461 CONECT 488 4461 CONECT 909 1382 CONECT 1061 49 CONECT 1139 1245 CONECT 1245 1139 CONECT 1321 1480 CONECT 1382 909 CONECT 1480 1321 CONECT 1758 2800 CONECT 1906 2031 CONECT 2031 1906 CONECT 2125 4497 CONECT 2139 4497 CONECT 2164 4497 CONECT 2184 4497 CONECT 2205 4497 CONECT 2648 3127 CONECT 2800 1758 CONECT 2878 2990 CONECT 2990 2878 CONECT 3066 3225 CONECT 3127 2648 CONECT 3225 3066 CONECT 3489 3886 CONECT 3556 3748 CONECT 3688 3854 CONECT 3748 3556 CONECT 3854 3688 CONECT 3886 3489 CONECT 3954 4450 CONECT 4050 4281 CONECT 4221 4387 CONECT 4281 4050 CONECT 4387 4221 CONECT 4450 3954 CONECT 4461 403 417 442 488 CONECT 4461 4612 4649 CONECT 4462 4463 4464 4465 4466 CONECT 4463 4462 CONECT 4464 4462 CONECT 4465 4462 CONECT 4466 4462 CONECT 4467 4468 4469 4470 4471 CONECT 4468 4467 CONECT 4469 4467 CONECT 4470 4467 CONECT 4471 4467 CONECT 4472 4473 4474 4475 4476 CONECT 4473 4472 CONECT 4474 4472 CONECT 4475 4472 CONECT 4476 4472 CONECT 4477 4478 4479 4480 4481 CONECT 4478 4477 CONECT 4479 4477 CONECT 4480 4477 CONECT 4481 4477 CONECT 4482 4483 4484 4485 4486 CONECT 4483 4482 CONECT 4484 4482 CONECT 4485 4482 CONECT 4486 4482 CONECT 4487 4488 4489 4490 4491 CONECT 4488 4487 CONECT 4489 4487 CONECT 4490 4487 CONECT 4491 4487 CONECT 4492 4493 4494 4495 4496 CONECT 4493 4492 CONECT 4494 4492 CONECT 4495 4492 CONECT 4496 4492 CONECT 4497 2125 2139 2164 2184 CONECT 4497 2205 4867 CONECT 4498 4499 4500 4501 4502 CONECT 4499 4498 CONECT 4500 4498 CONECT 4501 4498 CONECT 4502 4498 CONECT 4503 4504 4505 4506 4507 CONECT 4504 4503 CONECT 4505 4503 CONECT 4506 4503 CONECT 4507 4503 CONECT 4508 4509 4510 4511 4512 CONECT 4509 4508 CONECT 4510 4508 CONECT 4511 4508 CONECT 4512 4508 CONECT 4513 4514 4515 4516 4517 CONECT 4514 4513 CONECT 4515 4513 CONECT 4516 4513 CONECT 4517 4513 CONECT 4518 4519 4520 4521 4522 CONECT 4519 4518 CONECT 4520 4518 CONECT 4521 4518 CONECT 4522 4518 CONECT 4523 4524 4525 4526 4527 CONECT 4524 4523 CONECT 4525 4523 CONECT 4526 4523 CONECT 4527 4523 CONECT 4528 4529 4530 4531 4532 CONECT 4529 4528 CONECT 4530 4528 CONECT 4531 4528 CONECT 4532 4528 CONECT 4533 4534 4535 4536 4537 CONECT 4534 4533 CONECT 4535 4533 CONECT 4536 4533 CONECT 4537 4533 CONECT 4538 4539 4540 4541 4542 CONECT 4539 4538 CONECT 4540 4538 CONECT 4541 4538 CONECT 4542 4538 CONECT 4543 4544 4545 4546 4547 CONECT 4544 4543 CONECT 4545 4543 CONECT 4546 4543 CONECT 4547 4543 CONECT 4548 4549 4550 4551 4552 CONECT 4549 4548 CONECT 4550 4548 CONECT 4551 4548 CONECT 4552 4548 CONECT 4553 4554 4555 4556 4557 CONECT 4554 4553 CONECT 4555 4553 CONECT 4556 4553 CONECT 4557 4553 CONECT 4558 4559 4560 4561 4562 CONECT 4559 4558 CONECT 4560 4558 CONECT 4561 4558 CONECT 4562 4558 CONECT 4563 4564 4565 4566 4567 CONECT 4564 4563 CONECT 4565 4563 CONECT 4566 4563 CONECT 4567 4563 CONECT 4568 4569 4570 4571 4572 CONECT 4569 4568 CONECT 4570 4568 CONECT 4571 4568 CONECT 4572 4568 CONECT 4573 4574 4575 4576 4577 CONECT 4574 4573 CONECT 4575 4573 CONECT 4576 4573 CONECT 4577 4573 CONECT 4578 4580 4582 4584 4586 CONECT 4579 4581 4583 4585 4587 CONECT 4580 4578 CONECT 4581 4579 CONECT 4582 4578 CONECT 4583 4579 CONECT 4584 4578 CONECT 4585 4579 CONECT 4586 4578 CONECT 4587 4579 CONECT 4612 4461 CONECT 4649 4461 CONECT 4867 4497 MASTER 475 0 26 12 32 0 47 6 5248 4 173 46 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
2r9p
RCSB PDB
PDBbind
bovine pancreatic trypsin inhibitor(BPTI)
Entry Information
PDB ID
2ra3
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Human cationic trypsin
Ligand Name
bovine pancreatic trypsin inhibitor(BPTI)
EC.Number
E.C.3.4.21.4
Resolution
1.46(Å)
Affinity (Kd/Ki/IC50)
Kd=20pM
Release Year
2007
Protein/NA Sequence
Check fasta file
Primary Reference
(2008) J.Biol.Chem. Vol. 283: pp. 4115-4123
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P07477
P00974
Entrez Gene ID
NCBI Entrez Gene ID:
5644
ASD
Information of known allosteric effects of PDB entries
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