Browse entries in the PDBbind-CN Database
HEADER HYDROLASE/HYDROLASE INHIBITOR 15-OCT-10 3P95 TITLE HUMAN MESOTRYPSIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR TITLE 2 VARIANT (BPTI-K15R/R17D) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRSS3 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 EC: 3.4.21.4; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: PANCREATIC TRYPSIN INHIBITOR; COMPND 9 CHAIN: E; COMPND 10 FRAGMENT: UNP RESIDUES 36-93; COMPND 11 SYNONYM: APROTININ, BASIC PROTEASE INHIBITOR, BPI, BPTI; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: PRSS3; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 11 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW; SOURCE 12 ORGANISM_TAXID: 9913; SOURCE 13 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 4922 KEYWDS HUMAN MESOTRYPSIN-CANONICAL INHIBITOR COMPLEX, MESOTRYPSIN, TRYPSIN KEYWDS 2 IV, BOVINE PANCREATIC TRYPSIN INHIBITOR, CANONICAL INHIBITOR, BPTI- KEYWDS 3 K15R/R17D, HYDROLASE-HYDROLASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.A.SALAMEH,A.S.SOARES,E.S.RADISKY REVDAT 2 09-NOV-11 3P95 1 JRNL REVDAT 1 31-AUG-11 3P95 0 JRNL AUTH M.A.SALAMEH,A.S.SOARES,A.HOCKLA,D.C.RADISKY,E.S.RADISKY JRNL TITL THE P2' RESIDUE IS A KEY DETERMINANT OF MESOTRYPSIN JRNL TITL 2 SPECIFICITY: ENGINEERING A HIGH-AFFINITY INHIBITOR WITH JRNL TITL 3 ANTICANCER ACTIVITY. JRNL REF BIOCHEM.J. V. 440 95 2011 JRNL REFN ISSN 0264-6021 JRNL PMID 21806544 JRNL DOI 10.1042/BJ20110788 REMARK 2 REMARK 2 RESOLUTION. 1.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) 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 : MLHL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.82 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3 REMARK 3 NUMBER OF REFLECTIONS : 52821 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.111 REMARK 3 R VALUE (WORKING SET) : 0.111 REMARK 3 FREE R VALUE : 0.132 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.790 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 33.8282 - 3.1302 0.93 3756 148 0.1535 0.1449 REMARK 3 2 3.1302 - 2.4848 1.00 3929 154 0.1174 0.1403 REMARK 3 3 2.4848 - 2.1707 1.00 3894 153 0.0991 0.1272 REMARK 3 4 2.1707 - 1.9723 1.00 3891 153 0.0872 0.1131 REMARK 3 5 1.9723 - 1.8309 1.00 3863 153 0.0892 0.1180 REMARK 3 6 1.8309 - 1.7230 0.99 3882 152 0.0851 0.1167 REMARK 3 7 1.7230 - 1.6367 0.99 3811 151 0.0782 0.1007 REMARK 3 8 1.6367 - 1.5655 0.99 3835 150 0.0771 0.1131 REMARK 3 9 1.5655 - 1.5052 0.98 3788 149 0.0775 0.1257 REMARK 3 10 1.5052 - 1.4533 0.97 3769 149 0.0819 0.1188 REMARK 3 11 1.4533 - 1.4078 0.96 3706 146 0.0821 0.1190 REMARK 3 12 1.4078 - 1.3676 0.89 3452 136 0.0896 0.1199 REMARK 3 13 1.3676 - 1.3316 0.74 2842 111 0.0970 0.1485 REMARK 3 14 1.3316 - 1.2991 0.62 2403 95 0.1060 0.1605 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.48 REMARK 3 B_SOL : 62.55 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.070 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 10.340 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.23 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.10260 REMARK 3 B22 (A**2) : 0.91990 REMARK 3 B33 (A**2) : -3.61180 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.46920 REMARK 3 B23 (A**2) : -0.00000 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 : 0.016 4349 REMARK 3 ANGLE : 1.335 7818 REMARK 3 CHIRALITY : 0.130 334 REMARK 3 PLANARITY : 0.009 699 REMARK 3 DIHEDRAL : 16.634 1087 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 3P95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-10. REMARK 100 THE RCSB ID CODE IS RCSB062112. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : 8 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) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53441 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.299 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : 0.06800 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 65.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.80 REMARK 200 R MERGE FOR SHELL (I) : 0.22700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2R9P REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 34.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG4000, 0.2M NA ACETATE AND 100MM REMARK 280 TRIS PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 19.54750 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 12090 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E 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 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 ARG A 62 CD NE CZ NH1 NH2 REMARK 480 ARG A 96 CZ NH1 NH2 REMARK 480 ARG A 117 CZ NH1 NH2 REMARK 480 LYS A 222 CE NZ REMARK 480 SER A 246 OXT REMARK 480 LYS E 26 CG CD CE NZ REMARK 480 ARG E 42 NE 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 OG SER A 246 O HOH A 297 2.11 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 O HOH A 320 O HOH A 348 2546 1.86 REMARK 500 OE2 GLU E 49 O HOH A 403 1565 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 GLU A 77 CD GLU A 77 OE1 0.085 REMARK 500 GLU A 186 CG GLU A 186 CD 0.107 REMARK 500 LYS A 188A CE LYS A 188A NZ 0.154 REMARK 500 ASP E 3 CB ASP E 3 CG 0.129 REMARK 500 GLU E 7 CG GLU E 7 CD 0.100 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 A 96 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES REMARK 500 ASP A 97 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES REMARK 500 ASP E 3 CB - CG - OD1 ANGL. DEV. = 7.0 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 LEU A 27 74.40 -118.60 REMARK 500 HIS A 71 -64.52 -124.64 REMARK 500 ARG A 193 -6.53 85.47 REMARK 500 SER A 214 -73.61 -124.62 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 ASN A 72 O REMARK 620 2 GLU A 70 OE1 88.1 REMARK 620 3 VAL A 75 O 85.2 164.7 REMARK 620 4 GLU A 80 OE2 168.4 98.5 90.5 REMARK 620 5 GLU A 77 OE1 86.0 89.0 104.2 84.6 REMARK 620 6 HOH A 308 O 100.6 80.2 87.5 89.9 167.1 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 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2R9P RELATED DB: PDB REMARK 900 HUMAN MESOTRYPSIN COMPLEXED WITH BPTI-K15R/R17D DBREF 3P95 A 16 246 UNP Q8N2U3 Q8N2U3_HUMAN 28 251 DBREF 3P95 E 1 58 UNP P00974 BPT1_BOVIN 36 93 SEQADV 3P95 ALA A 195 UNP Q8N2U3 SER 204 ENGINEERED MUTATION SEQADV 3P95 ARG E 15 UNP P00974 LYS 50 ENGINEERED MUTATION SEQADV 3P95 ASP E 17 UNP P00974 ARG 52 ENGINEERED MUTATION SEQRES 1 A 224 ILE VAL GLY GLY TYR THR CYS GLU GLU ASN SER LEU PRO SEQRES 2 A 224 TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY SEQRES 3 A 224 GLY SER LEU ILE SER GLU GLN TRP VAL VAL SER ALA ALA SEQRES 4 A 224 HIS CYS TYR LYS THR ARG ILE GLN VAL ARG LEU GLY GLU SEQRES 5 A 224 HIS ASN ILE LYS VAL LEU GLU GLY ASN GLU GLN PHE ILE SEQRES 6 A 224 ASN ALA ALA LYS ILE ILE ARG HIS PRO LYS TYR ASN ARG SEQRES 7 A 224 ASP THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER SEQRES 8 A 224 SER PRO ALA VAL ILE ASN ALA ARG VAL SER THR ILE SER SEQRES 9 A 224 LEU PRO THR ALA PRO PRO ALA ALA GLY THR GLU CYS LEU SEQRES 10 A 224 ILE SER GLY TRP GLY ASN THR LEU SER PHE GLY ALA ASP SEQRES 11 A 224 TYR PRO ASP GLU LEU LYS CYS LEU ASP ALA PRO VAL LEU SEQRES 12 A 224 THR GLN ALA GLU CYS LYS ALA SER TYR PRO GLY LYS ILE SEQRES 13 A 224 THR ASN SER MET PHE CYS VAL GLY PHE LEU GLU GLY GLY SEQRES 14 A 224 LYS ASP SER CYS GLN ARG ASP ALA GLY GLY PRO VAL VAL SEQRES 15 A 224 CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY HIS SEQRES 16 A 224 GLY CYS ALA TRP LYS ASN ARG PRO GLY VAL TYR THR LYS SEQRES 17 A 224 VAL TYR ASN TYR VAL ASP TRP ILE LYS ASP THR ILE ALA SEQRES 18 A 224 ALA ASN SER SEQRES 1 E 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO SEQRES 2 E 58 CYS ARG ALA ASP ILE ILE ARG TYR PHE TYR ASN ALA LYS SEQRES 3 E 58 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG SEQRES 4 E 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET SEQRES 5 E 58 ARG THR CYS GLY GLY ALA HET CA A 1 1 HETNAM CA CALCIUM ION FORMUL 3 CA CA 2+ FORMUL 4 HOH *280(H2 O) HELIX 1 1 ALA A 55 TYR A 59 5 5 HELIX 2 2 THR A 164 TYR A 172 1 9 HELIX 3 3 TYR A 234 ASN A 245 1 12 HELIX 4 4 PRO E 2 GLU E 7 5 6 HELIX 5 5 SER E 47 GLY E 56 1 10 SHEET 1 A 7 TYR A 20 THR A 21 0 SHEET 2 A 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20 SHEET 3 A 7 GLU 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 210 N VAL A 199 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 SER 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 MET A 104 N SER A 54 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 2 ILE E 18 ASN E 24 0 SHEET 2 C 2 LEU E 29 TYR E 35 -1 O TYR E 35 N ILE E 18 SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.02 SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.04 SSBOND 3 CYS A 136 CYS A 201 1555 1555 2.04 SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.07 SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.08 SSBOND 6 CYS E 5 CYS E 55 1555 1555 2.02 SSBOND 7 CYS E 14 CYS E 38 1555 1555 2.05 SSBOND 8 CYS E 30 CYS E 51 1555 1555 2.09 LINK O ASN A 72 CA CA A 1 1555 1555 2.27 LINK OE1 GLU A 70 CA CA A 1 1555 1555 2.29 LINK O VAL A 75 CA CA A 1 1555 1555 2.29 LINK OE2 GLU A 80 CA CA A 1 1555 1555 2.31 LINK OE1 GLU A 77 CA CA A 1 1555 1555 2.39 LINK CA CA A 1 O HOH A 308 1555 1555 2.36 CISPEP 1 GLY E 56 GLY E 57 0 1.36 SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 77 SITE 2 AC1 6 GLU A 80 HOH A 308 CRYST1 43.915 39.095 68.460 90.00 100.13 90.00 P 1 21 1 2 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 0.022771 0.000000 0.004070 0.00000 SCALE2 0.000000 0.025579 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014839 0.00000 ATOM 1 N ILE A 16 9.998 -12.581 12.157 1.00 10.51 N ANISOU 1 N ILE A 16 1381 1229 1382 138 50 29 N ATOM 2 CA ILE A 16 10.328 -13.760 12.979 1.00 9.49 C ANISOU 2 CA ILE A 16 1176 1131 1298 127 56 47 C ATOM 3 C ILE A 16 11.554 -14.438 12.343 1.00 9.56 C ANISOU 3 C ILE A 16 1278 1125 1228 164 94 -140 C ATOM 4 O ILE A 16 11.541 -14.804 11.162 1.00 10.23 O ANISOU 4 O ILE A 16 1412 1161 1314 108 101 -188 O ATOM 5 CB ILE A 16 9.170 -14.794 12.966 1.00 9.56 C ANISOU 5 CB ILE A 16 1259 1086 1288 12 59 -23 C ATOM 6 CG1 ILE A 16 7.834 -14.184 13.454 1.00 10.36 C ANISOU 6 CG1 ILE A 16 1359 1185 1394 -49 132 -131 C ATOM 7 CG2 ILE A 16 9.542 -16.052 13.718 1.00 11.42 C ANISOU 7 CG2 ILE A 16 1472 1384 1484 -80 76 111 C ATOM 8 CD1 ILE A 16 7.802 -13.880 14.972 1.00 11.61 C ANISOU 8 CD1 ILE A 16 1480 1409 1523 119 44 -189 C ATOM 9 HA ILE A 16 10.532 -13.499 13.901 1.00 11.40 H ATOM 10 HB ILE A 16 9.037 -15.051 12.041 1.00 11.49 H ATOM 11 HG12 ILE A 16 7.680 -13.351 12.981 1.00 12.45 H ATOM 12 HG13 ILE A 16 7.118 -14.808 13.262 1.00 12.45 H ATOM 13 HG21 ILE A 16 8.803 -16.664 13.688 1.00 13.72 H ATOM 14 HG22 ILE A 16 10.313 -16.447 13.304 1.00 13.72 H ATOM 15 HG23 ILE A 16 9.741 -15.824 14.629 1.00 13.72 H ATOM 16 HD11 ILE A 16 6.947 -13.506 15.197 1.00 13.95 H ATOM 17 HD12 ILE A 16 7.941 -14.697 15.457 1.00 13.95 H ATOM 18 HD13 ILE A 16 8.499 -13.253 15.179 1.00 13.95 H ATOM 19 N VAL A 17 12.619 -14.567 13.130 1.00 9.83 N ANISOU 19 N VAL A 17 1272 1144 1318 225 14 -195 N ATOM 20 CA VAL A 17 13.859 -15.198 12.756 1.00 10.61 C ANISOU 20 CA VAL A 17 1316 1277 1436 262 -10 -213 C ATOM 21 C VAL A 17 13.886 -16.612 13.343 1.00 11.04 C ANISOU 21 C VAL A 17 1304 1321 1568 246 94 -238 C ATOM 22 O VAL A 17 13.568 -16.805 14.515 1.00 10.98 O ANISOU 22 O VAL A 17 1358 1234 1578 146 -8 -171 O ATOM 23 CB VAL A 17 15.066 -14.414 13.323 1.00 11.09 C ANISOU 23 CB VAL A 17 1339 1272 1604 88 21 -221 C ATOM 24 CG1 VAL A 17 16.398 -15.088 12.910 1.00 11.87 C ANISOU 24 CG1 VAL A 17 1424 1498 1587 -47 71 -315 C ATOM 25 CG2 VAL A 17 15.063 -12.964 12.821 1.00 13.36 C ANISOU 25 CG2 VAL A 17 1672 1548 1855 107 32 -208 C ATOM 26 H VAL A 17 12.635 -14.272 13.938 1.00 11.81 H ATOM 27 HA VAL A 17 13.934 -15.250 11.781 1.00 12.74 H ATOM 28 HB VAL A 17 15.017 -14.402 14.301 1.00 13.33 H ATOM 29 HG11 VAL A 17 17.129 -14.583 13.273 1.00 14.26 H ATOM 30 HG12 VAL A 17 16.414 -15.983 13.255 1.00 14.26 H ATOM 31 HG13 VAL A 17 16.455 -15.105 11.952 1.00 14.26 H ATOM 32 HG21 VAL A 17 15.821 -12.504 13.188 1.00 16.04 H ATOM 33 HG22 VAL A 17 15.113 -12.965 11.862 1.00 16.04 H ATOM 34 HG23 VAL A 17 14.251 -12.537 13.106 1.00 16.04 H ATOM 35 N GLY A 18 14.218 -17.610 12.524 1.00 11.34 N ANISOU 35 N GLY A 18 1428 1314 1567 174 91 -294 N ATOM 36 CA GLY A 18 14.334 -18.975 13.024 1.00 11.50 C ANISOU 36 CA GLY A 18 1486 1261 1624 142 84 -265 C ATOM 37 C GLY A 18 13.031 -19.720 13.268 1.00 11.37 C ANISOU 37 C GLY A 18 1482 1150 1689 193 41 -183 C ATOM 38 O GLY A 18 13.049 -20.723 13.972 1.00 13.12 O ANISOU 38 O GLY A 18 1743 1316 1926 124 10 -133 O ATOM 39 H GLY A 18 14.379 -17.523 11.684 1.00 13.62 H ATOM 40 HA2 GLY A 18 14.853 -19.493 12.389 1.00 13.82 H ATOM 41 HA3 GLY A 18 14.823 -18.957 13.861 1.00 13.82 H ATOM 42 N GLY A 19 11.963 -19.188 12.707 1.00 11.43 N ANISOU 42 N GLY A 19 1387 1344 1613 66 31 -322 N ATOM 43 CA GLY A 19 10.680 -19.823 12.799 1.00 11.42 C ANISOU 43 CA GLY A 19 1443 1321 1575 10 57 -195 C ATOM 44 C GLY A 19 10.290 -20.608 11.585 1.00 11.24 C ANISOU 44 C GLY A 19 1436 1195 1640 48 189 -243 C ATOM 45 O GLY A 19 11.131 -21.166 10.887 1.00 12.64 O ANISOU 45 O GLY A 19 1343 1569 1893 -69 200 -430 O ATOM 46 H GLY A 19 11.961 -18.451 12.263 1.00 13.73 H ATOM 47 HA2 GLY A 19 10.680 -20.426 13.560 1.00 13.72 H ATOM 48 HA3 GLY A 19 10.002 -19.147 12.951 1.00 13.72 H ATOM 49 N TYR A 20 9.009 -20.676 11.335 1.00 10.92 N ANISOU 49 N TYR A 20 1375 1276 1499 124 79 -182 N ATOM 50 CA TYR A 20 8.445 -21.467 10.254 1.00 11.31 C ANISOU 50 CA TYR A 20 1469 1230 1600 148 6 -174 C ATOM 51 C TYR A 20 7.180 -20.791 9.771 1.00 10.94 C ANISOU 51 C TYR A 20 1526 1033 1597 213 -7 -317 C ATOM 52 O TYR A 20 6.589 -19.979 10.449 1.00 11.87 O ANISOU 52 O TYR A 20 1627 1247 1635 414 -106 -393 O ATOM 53 CB TYR A 20 8.165 -22.922 10.705 1.00 11.84 C ANISOU 53 CB TYR A 20 1579 1300 1620 160 -41 -235 C ATOM 54 CG TYR A 20 7.231 -23.063 11.924 1.00 11.74 C ANISOU 54 CG TYR A 20 1570 1177 1712 -105 21 -117 C ATOM 55 CD1 TYR A 20 7.723 -22.907 13.205 1.00 11.83 C ANISOU 55 CD1 TYR A 20 1553 1241 1701 -8 -8 29 C ATOM 56 CD2 TYR A 20 5.865 -23.241 11.765 1.00 11.89 C ANISOU 56 CD2 TYR A 20 1589 1226 1703 -15 0 -100 C ATOM 57 CE1 TYR A 20 6.870 -23.014 14.322 1.00 12.59 C ANISOU 57 CE1 TYR A 20 1713 1341 1729 -16 -24 36 C ATOM 58 CE2 TYR A 20 5.024 -23.339 12.863 1.00 12.62 C ANISOU 58 CE2 TYR A 20 1663 1367 1765 -81 22 -123 C ATOM 59 CZ TYR A 20 5.550 -23.209 14.140 1.00 12.86 C ANISOU 59 CZ TYR A 20 1729 1352 1803 52 166 -181 C ATOM 60 OH TYR A 20 4.673 -23.254 15.214 1.00 14.51 O ANISOU 60 OH TYR A 20 1882 1778 1852 -138 245 -235 O ATOM 61 H TYR A 20 8.414 -20.256 11.793 1.00 13.12 H ATOM 62 HA TYR A 20 9.082 -21.495 9.509 1.00 13.59 H ATOM 63 HB2 TYR A 20 7.755 -23.400 9.966 1.00 14.22 H ATOM 64 HB3 TYR A 20 9.009 -23.342 10.934 1.00 14.22 H ATOM 65 HD1 TYR A 20 8.634 -22.776 13.335 1.00 14.21 H ATOM 66 HD2 TYR A 20 5.511 -23.330 10.909 1.00 14.29 H ATOM 67 HE1 TYR A 20 7.212 -22.913 15.181 1.00 15.12 H ATOM 68 HE2 TYR A 20 4.111 -23.464 12.743 1.00 15.16 H ATOM 69 HH TYR A 20 4.293 -23.980 15.236 1.00 17.42 H ATOM 70 N THR A 21 6.744 -21.163 8.573 1.00 12.33 N ANISOU 70 N THR A 21 1642 1421 1622 202 -72 -452 N ATOM 71 CA THR A 21 5.538 -20.558 8.079 1.00 12.55 C ANISOU 71 CA THR A 21 1680 1471 1619 231 -50 -420 C ATOM 72 C THR A 21 4.343 -21.182 8.786 1.00 12.76 C ANISOU 72 C THR A 21 1668 1476 1704 57 47 -169 C ATOM 73 O THR A 21 4.194 -22.409 8.902 1.00 13.31 O ANISOU 73 O THR A 21 1705 1403 1949 104 -56 -166 O ATOM 74 CB THR A 21 5.356 -20.813 6.531 1.00 13.49 C ANISOU 74 CB THR A 21 1746 1669 1711 230 -50 -364 C ATOM 75 OG1 THR A 21 6.511 -20.266 5.887 1.00 15.82 O ANISOU 75 OG1 THR A 21 1954 2183 1875 118 141 -198 O ATOM 76 CG2 THR A 21 4.108 -20.189 5.995 1.00 14.88 C ANISOU 76 CG2 THR A 21 1952 1832 1871 259 -259 -239 C ATOM 77 H THR A 21 7.115 -21.738 8.053 1.00 14.81 H ATOM 78 HA THR A 21 5.547 -19.593 8.249 1.00 15.08 H ATOM 79 HB THR A 21 5.317 -21.768 6.364 1.00 16.20 H ATOM 80 HG1 THR A 21 7.188 -20.637 6.164 1.00 19.00 H ATOM 81 HG21 THR A 21 4.031 -20.365 5.055 1.00 17.87 H ATOM 82 HG22 THR A 21 3.341 -20.553 6.444 1.00 17.87 H ATOM 83 HG23 THR A 21 4.130 -19.240 6.135 1.00 17.87 H ATOM 84 N CYS A 22 3.493 -20.339 9.342 1.00 11.86 N ANISOU 84 N CYS A 22 1631 1344 1531 179 89 -125 N ATOM 85 CA CYS A 22 2.306 -20.803 10.049 1.00 12.03 C ANISOU 85 CA CYS A 22 1557 1320 1694 37 44 -154 C ATOM 86 C CYS A 22 1.400 -21.527 9.069 1.00 13.45 C ANISOU 86 C CYS A 22 1724 1485 1903 37 173 -30 C ATOM 87 O CYS A 22 1.352 -21.154 7.884 1.00 13.71 O ANISOU 87 O CYS A 22 1750 1599 1859 4 -15 -83 O ATOM 88 CB CYS A 22 1.542 -19.605 10.660 1.00 12.54 C ANISOU 88 CB CYS A 22 1600 1423 1743 5 18 -287 C ATOM 89 SG CYS A 22 2.432 -18.463 11.701 1.00 12.48 S ANISOU 89 SG CYS A 22 1627 1362 1752 37 2 -63 S ATOM 90 H CYS A 22 3.579 -19.483 9.325 1.00 14.24 H ATOM 91 HA CYS A 22 2.561 -21.420 10.766 1.00 14.45 H ATOM 92 HB2 CYS A 22 1.173 -19.086 9.928 1.00 15.07 H ATOM 93 HB3 CYS A 22 0.814 -19.960 11.193 1.00 15.07 H ATOM 94 N GLU A 23 0.629 -22.467 9.579 1.00 14.67 N ANISOU 94 N GLU A 23 1871 1544 2159 18 82 -129 N ATOM 95 CA GLU A 23 -0.453 -23.036 8.710 1.00 17.97 C ANISOU 95 CA GLU A 23 2293 2019 2517 -242 -37 -367 C ATOM 96 C GLU A 23 -1.430 -21.926 8.364 1.00 16.35 C ANISOU 96 C GLU A 23 2027 1819 2366 -407 -319 -532 C ATOM 97 O GLU A 23 -1.711 -21.056 9.170 1.00 16.10 O ANISOU 97 O GLU A 23 2023 1747 2348 -47 -193 -454 O ATOM 98 CB GLU A 23 -1.132 -24.154 9.498 1.00 25.06 C ANISOU 98 CB GLU A 23 3171 2990 3361 -235 12 -246 C ATOM 99 CG GLU A 23 -0.150 -25.307 9.617 1.00 32.35 C ANISOU 99 CG GLU A 23 4100 3982 4209 -301 180 18 C ATOM 100 CD GLU A 23 -0.548 -26.423 10.569 1.00 33.98 C ANISOU 100 CD GLU A 23 4335 4202 4375 -261 322 291 C ATOM 101 OE1 GLU A 23 -1.754 -26.459 10.927 1.00 34.27 O ANISOU 101 OE1 GLU A 23 4350 4250 4420 -432 502 431 O ATOM 102 OE2 GLU A 23 0.406 -27.209 10.956 1.00 35.19 O ANISOU 102 OE2 GLU A 23 4517 4336 4518 -161 301 342 O ATOM 103 H GLU A 23 0.685 -22.794 10.372 1.00 17.62 H ATOM 104 HA GLU A 23 -0.072 -23.404 7.886 1.00 21.58 H ATOM 105 HB2 GLU A 23 -1.360 -23.841 10.388 1.00 30.09 H ATOM 106 HB3 GLU A 23 -1.922 -24.460 9.025 1.00 30.09 H ATOM 107 HG2 GLU A 23 -0.037 -25.703 8.738 1.00 38.83 H ATOM 108 HG3 GLU A 23 0.700 -24.953 9.923 1.00 38.83 H ATOM 109 N GLU A 24 -1.910 -21.919 7.142 1.00 18.54 N ANISOU 109 N GLU A 24 2269 2284 2491 -440 -408 -575 N ATOM 110 CA GLU A 24 -2.708 -20.786 6.667 1.00 20.25 C ANISOU 110 CA GLU A 24 2524 2527 2642 -370 -536 -461 C ATOM 111 C GLU A 24 -3.972 -20.556 7.472 1.00 18.22 C ANISOU 111 C GLU A 24 2196 2283 2444 -557 -434 -338 C ATOM 112 O GLU A 24 -4.757 -21.488 7.728 1.00 19.13 O ANISOU 112 O GLU A 24 2397 2320 2553 -703 -290 -423 O ATOM 113 CB GLU A 24 -3.090 -21.017 5.163 1.00 26.20 C ANISOU 113 CB GLU A 24 3322 3267 3367 -130 -477 -489 C ATOM 114 CG GLU A 24 -4.031 -19.985 4.557 1.00 31.85 C ANISOU 114 CG GLU A 24 4059 4037 4004 134 -284 -523 C ATOM 115 CD GLU A 24 -4.056 -20.002 2.994 1.00 34.22 C ANISOU 115 CD GLU A 24 4499 4495 4006 398 -146 -388 C ATOM 116 OE1 GLU A 24 -3.370 -20.953 2.463 1.00 35.49 O ANISOU 116 OE1 GLU A 24 4751 4732 4001 546 -13 -447 O ATOM 117 OE2 GLU A 24 -4.720 -19.061 2.367 1.00 35.06 O ANISOU 117 OE2 GLU A 24 4568 4693 4059 421 -174 -253 O ATOM 118 H GLU A 24 -1.797 -22.545 6.563 1.00 22.26 H ATOM 119 HA GLU A 24 -2.165 -19.971 6.719 1.00 24.31 H ATOM 120 HB2 GLU A 24 -2.276 -21.013 4.636 1.00 31.46 H ATOM 121 HB3 GLU A 24 -3.521 -21.882 5.086 1.00 31.46 H ATOM 122 HG2 GLU A 24 -4.932 -20.160 4.870 1.00 38.23 H ATOM 123 HG3 GLU A 24 -3.750 -19.101 4.840 1.00 38.23 H ATOM 124 N ASN A 25 -4.115 -19.330 7.957 1.00 16.93 N ANISOU 124 N ASN A 25 2013 2140 2279 -329 -237 -91 N ATOM 125 CA ASN A 25 -5.282 -18.898 8.753 1.00 18.03 C ANISOU 125 CA ASN A 25 2100 2358 2391 -214 -395 -120 C ATOM 126 C ASN A 25 -5.459 -19.701 10.042 1.00 16.29 C ANISOU 126 C ASN A 25 1886 2002 2301 -329 -277 -136 C ATOM 127 O ASN A 25 -6.538 -19.715 10.625 1.00 17.78 O ANISOU 127 O ASN A 25 1920 2299 2537 -340 -186 52 O ATOM 128 CB ASN A 25 -6.606 -18.844 7.920 1.00 20.46 C ANISOU 128 CB ASN A 25 2474 2613 2688 -130 -521 29 C ATOM 129 CG ASN A 25 -6.492 -17.934 6.718 1.00 23.15 C ANISOU 129 CG ASN A 25 2807 2969 3020 -130 -543 102 C ATOM 130 OD1 ASN A 25 -6.179 -16.722 6.794 1.00 23.80 O ANISOU 130 OD1 ASN A 25 2817 3131 3096 25 -447 376 O ATOM 131 ND2 ASN A 25 -6.632 -18.538 5.627 1.00 26.80 N ANISOU 131 ND2 ASN A 25 3379 3387 3415 -364 -567 10 N ATOM 132 H ASN A 25 -3.537 -18.705 7.839 1.00 20.33 H ATOM 133 HA ASN A 25 -5.106 -17.976 9.035 1.00 21.65 H ATOM 134 HB2 ASN A 25 -6.818 -19.736 7.603 1.00 24.57 H ATOM 135 HB3 ASN A 25 -7.322 -18.511 8.483 1.00 24.57 H ATOM 136 HD21 ASN A 25 -6.576 -18.043 4.783 1.00 32.17 H ATOM 137 HD22 ASN A 25 -6.797 -19.504 5.619 1.00 32.17 H ATOM 138 N SER A 26 -4.400 -20.329 10.539 1.00 14.89 N ANISOU 138 N SER A 26 1766 1833 2060 -180 -341 -362 N ATOM 139 CA SER A 26 -4.461 -21.048 11.816 1.00 14.30 C ANISOU 139 CA SER A 26 1744 1618 2069 -263 -261 -288 C ATOM 140 C SER A 26 -4.300 -20.154 13.049 1.00 13.39 C ANISOU 140 C SER A 26 1615 1445 2026 -149 -237 -155 C ATOM 141 O SER A 26 -4.468 -20.635 14.164 1.00 14.75 O ANISOU 141 O SER A 26 1889 1518 2198 -75 -25 98 O ATOM 142 CB SER A 26 -3.396 -22.112 11.894 1.00 16.26 C ANISOU 142 CB SER A 26 2004 1898 2275 -35 -243 -389 C ATOM 143 OG SER A 26 -2.085 -21.580 11.777 1.00 16.83 O ANISOU 143 OG SER A 26 2074 1901 2420 184 -359 -518 O ATOM 144 H SER A 26 -3.630 -20.357 10.158 1.00 17.89 H ATOM 145 HA SER A 26 -5.332 -21.493 11.883 1.00 17.17 H ATOM 146 HB2 SER A 26 -3.472 -22.565 12.748 1.00 19.52 H ATOM 147 HB3 SER A 26 -3.538 -22.747 11.174 1.00 19.52 H ATOM 148 HG SER A 26 -1.532 -22.183 11.823 1.00 20.21 H ATOM 149 N LEU A 27 -3.951 -18.910 12.825 1.00 12.19 N ANISOU 149 N LEU A 27 1480 1303 1850 -118 -142 -163 N ATOM 150 CA ALEU A 27 -3.878 -17.883 13.873 0.24 11.78 C ANISOU 150 CA ALEU A 27 1463 1340 1674 -149 -111 -102 C ATOM 151 CA BLEU A 27 -3.863 -17.871 13.886 0.76 11.41 C ANISOU 151 CA BLEU A 27 1341 1176 1816 -124 -213 -193 C ATOM 152 C LEU A 27 -4.887 -16.783 13.505 1.00 10.96 C ANISOU 152 C LEU A 27 1385 1052 1727 -224 -106 -146 C ATOM 153 O LEU A 27 -4.551 -15.690 13.074 1.00 11.27 O ANISOU 153 O LEU A 27 1466 1011 1804 -97 72 -124 O ATOM 154 CB ALEU A 27 -2.461 -17.310 14.007 0.24 12.60 C ANISOU 154 CB ALEU A 27 1570 1553 1664 -105 -41 83 C ATOM 155 CB BLEU A 27 -2.448 -17.263 13.995 0.76 12.28 C ANISOU 155 CB BLEU A 27 1369 1325 1973 9 -116 -34 C ATOM 156 CG ALEU A 27 -1.303 -18.309 14.155 0.24 12.91 C ANISOU 156 CG ALEU A 27 1652 1590 1664 -135 15 202 C ATOM 157 CG BLEU A 27 -1.399 -18.153 14.614 0.76 13.04 C ANISOU 157 CG BLEU A 27 1557 1368 2031 -154 29 -41 C ATOM 158 CD1ALEU A 27 -1.669 -19.409 15.176 0.24 13.99 C ANISOU 158 CD1ALEU A 27 1757 1747 1811 -159 -22 187 C ATOM 159 CD1BLEU A 27 -1.075 -19.397 13.825 0.76 14.34 C ANISOU 159 CD1BLEU A 27 1887 1657 1903 -187 78 -109 C ATOM 160 CD2ALEU A 27 -0.810 -18.919 12.834 0.24 12.96 C ANISOU 160 CD2ALEU A 27 1652 1582 1690 -186 102 280 C ATOM 161 CD2BLEU A 27 -0.164 -17.307 14.768 0.76 12.49 C ANISOU 161 CD2BLEU A 27 1292 1328 2126 -514 -168 -31 C ATOM 162 H ALEU A 27 -3.740 -18.612 12.046 1.00 14.64 H ATOM 163 HA ALEU A 27 -4.140 -18.272 14.733 0.24 14.15 H ATOM 164 HB2ALEU A 27 -2.277 -16.778 13.218 0.24 15.14 H ATOM 165 HB3ALEU A 27 -2.442 -16.736 14.789 0.24 15.14 H ATOM 166 HG ALEU A 27 -0.550 -17.826 14.531 0.24 15.51 H ATOM 167 HD11ALEU A 27 -0.933 -20.021 15.253 0.24 16.80 H ATOM 168 HD12ALEU A 27 -1.845 -19.000 16.026 0.24 16.80 H ATOM 169 HD13ALEU A 27 -2.450 -19.873 14.868 0.24 16.80 H ATOM 170 HD21ALEU A 27 -0.091 -19.527 13.020 0.24 15.57 H ATOM 171 HD22ALEU A 27 -1.536 -19.388 12.417 0.24 15.57 H ATOM 172 HD23ALEU A 27 -0.503 -18.214 12.260 0.24 15.57 H ATOM 173 N PRO A 28 -6.189 -17.073 13.696 1.00 10.85 N ANISOU 173 N PRO A 28 1330 1088 1706 -246 -60 -33 N ATOM 174 CA PRO A 28 -7.207 -16.169 13.123 1.00 10.53 C ANISOU 174 CA PRO A 28 1293 1133 1576 -367 -147 -101 C ATOM 175 C PRO A 28 -7.281 -14.829 13.844 1.00 9.32 C ANISOU 175 C PRO A 28 1171 997 1375 -167 -117 -56 C ATOM 176 O PRO A 28 -7.968 -13.918 13.367 1.00 9.90 O ANISOU 176 O PRO A 28 1232 1109 1420 -91 -142 9 O ATOM 177 CB PRO A 28 -8.521 -17.011 13.301 1.00 12.67 C ANISOU 177 CB PRO A 28 1455 1565 1793 -272 -136 -129 C ATOM 178 CG PRO A 28 -8.222 -17.942 14.401 1.00 13.70 C ANISOU 178 CG PRO A 28 1516 1743 1946 -334 -51 -3 C ATOM 179 CD PRO A 28 -6.765 -18.309 14.229 1.00 12.66 C ANISOU 179 CD PRO A 28 1493 1461 1856 -261 122 -50 C ATOM 180 HA PRO A 28 -7.039 -16.020 12.169 1.00 12.65 H ATOM 181 HB2 PRO A 28 -9.257 -16.425 13.537 1.00 15.21 H ATOM 182 HB3 PRO A 28 -8.714 -17.495 12.483 1.00 15.21 H ATOM 183 HG2 PRO A 28 -8.365 -17.499 15.252 1.00 16.45 H ATOM 184 HG3 PRO A 28 -8.784 -18.729 14.325 1.00 16.45 H ATOM 185 HD2 PRO A 28 -6.366 -18.530 15.085 1.00 15.20 H ATOM 186 HD3 PRO A 28 -6.669 -19.033 13.591 1.00 15.20 H ATOM 187 N TYR A 29 -6.631 -14.727 14.992 1.00 8.80 N ANISOU 187 N TYR A 29 1100 1003 1240 -84 -157 -39 N ATOM 188 CA TYR A 29 -6.507 -13.503 15.766 1.00 9.06 C ANISOU 188 CA TYR A 29 1093 1077 1272 -151 -43 -131 C ATOM 189 C TYR A 29 -5.402 -12.593 15.302 1.00 8.78 C ANISOU 189 C TYR A 29 1037 1013 1286 -92 -42 -152 C ATOM 190 O TYR A 29 -5.307 -11.444 15.739 1.00 8.93 O ANISOU 190 O TYR A 29 1088 915 1391 -63 -17 -171 O ATOM 191 CB TYR A 29 -6.297 -13.826 17.261 1.00 9.49 C ANISOU 191 CB TYR A 29 1090 1189 1327 -200 -35 76 C ATOM 192 CG TYR A 29 -5.156 -14.769 17.492 1.00 9.20 C ANISOU 192 CG TYR A 29 1016 1070 1408 -56 -97 54 C ATOM 193 CD1 TYR A 29 -3.845 -14.263 17.605 1.00 9.24 C ANISOU 193 CD1 TYR A 29 1088 1040 1382 -129 -191 -4 C ATOM 194 CD2 TYR A 29 -5.329 -16.138 17.529 1.00 10.03 C ANISOU 194 CD2 TYR A 29 1180 1212 1418 -50 -87 -20 C ATOM 195 CE1 TYR A 29 -2.766 -15.101 17.792 1.00 9.96 C ANISOU 195 CE1 TYR A 29 1163 1176 1445 -123 -151 -26 C ATOM 196 CE2 TYR A 29 -4.229 -17.006 17.688 1.00 9.51 C ANISOU 196 CE2 TYR A 29 1200 950 1465 -221 -78 58 C ATOM 197 CZ TYR A 29 -2.966 -16.467 17.815 1.00 9.71 C ANISOU 197 CZ TYR A 29 1112 1088 1489 -49 -131 21 C ATOM 198 OH TYR A 29 -1.897 -17.311 18.001 1.00 10.62 O ANISOU 198 OH TYR A 29 1247 1217 1572 12 -197 46 O ATOM 199 H TYR A 29 -6.231 -15.393 15.361 1.00 10.57 H ATOM 200 HA TYR A 29 -7.347 -13.005 15.690 1.00 10.89 H ATOM 201 HB2 TYR A 29 -6.109 -13.004 17.739 1.00 11.40 H ATOM 202 HB3 TYR A 29 -7.102 -14.238 17.612 1.00 11.40 H ATOM 203 HD1 TYR A 29 -3.708 -13.343 17.579 1.00 11.10 H ATOM 204 HD2 TYR A 29 -6.182 -16.495 17.428 1.00 12.05 H ATOM 205 HE1 TYR A 29 -1.908 -14.751 17.873 1.00 11.96 H ATOM 206 HE2 TYR A 29 -4.356 -17.926 17.726 1.00 11.43 H ATOM 207 HH TYR A 29 -1.538 -17.154 18.721 1.00 12.76 H ATOM 208 N GLN A 30 -4.478 -13.070 14.469 1.00 8.82 N ANISOU 208 N GLN A 30 1050 950 1352 -113 -38 -119 N ATOM 209 CA GLN A 30 -3.355 -12.250 14.018 1.00 8.42 C ANISOU 209 CA GLN A 30 982 1047 1171 27 -71 10 C ATOM 210 C GLN A 30 -3.807 -11.209 13.012 1.00 8.90 C ANISOU 210 C GLN A 30 1107 1025 1249 -119 -124 -57 C ATOM 211 O GLN A 30 -4.426 -11.571 12.005 1.00 10.47 O ANISOU 211 O GLN A 30 1358 1326 1293 -267 -253 -5 O ATOM 212 CB GLN A 30 -2.286 -13.148 13.401 1.00 9.60 C ANISOU 212 CB GLN A 30 1148 1164 1334 127 52 -58 C ATOM 213 CG GLN A 30 -1.159 -12.376 12.694 1.00 10.24 C ANISOU 213 CG GLN A 30 1277 1175 1440 -59 110 -55 C ATOM 214 CD GLN A 30 -0.072 -11.836 13.599 1.00 9.48 C ANISOU 214 CD GLN A 30 1240 1016 1345 74 35 -95 C ATOM 215 OE1 GLN A 30 0.249 -10.603 13.604 1.00 12.07 O ANISOU 215 OE1 GLN A 30 1692 1231 1662 -106 200 -119 O ATOM 216 NE2 GLN A 30 0.519 -12.680 14.311 1.00 8.99 N ANISOU 216 NE2 GLN A 30 1170 957 1287 211 -238 -102 N ATOM 217 H GLN A 30 -4.479 -13.868 14.149 1.00 10.60 H ATOM 218 HA GLN A 30 -2.962 -11.786 14.787 1.00 10.12 H ATOM 219 HB2 GLN A 30 -1.883 -13.683 14.103 1.00 11.53 H ATOM 220 HB3 GLN A 30 -2.705 -13.728 12.746 1.00 11.53 H ATOM 221 HG2 GLN A 30 -0.737 -12.969 12.053 1.00 12.30 H ATOM 222 HG3 GLN A 30 -1.551 -11.621 12.228 1.00 12.30 H ATOM 223 HE21 GLN A 30 1.146 -12.430 14.844 1.00 10.80 H ATOM 224 HE22 GLN A 30 0.298 -13.510 14.267 1.00 10.80 H ATOM 225 N VAL A 31 -3.456 -9.969 13.242 1.00 8.52 N ANISOU 225 N VAL A 31 1078 928 1230 -49 -94 -13 N ATOM 226 CA VAL A 31 -3.751 -8.923 12.235 1.00 9.56 C ANISOU 226 CA VAL A 31 1275 951 1405 116 79 18 C ATOM 227 C VAL A 31 -2.447 -8.243 11.780 1.00 9.02 C ANISOU 227 C VAL A 31 1211 1005 1213 83 -46 62 C ATOM 228 O VAL A 31 -1.408 -8.310 12.458 1.00 8.99 O ANISOU 228 O VAL A 31 1328 932 1156 184 -36 -12 O ATOM 229 CB VAL A 31 -4.790 -7.899 12.682 1.00 12.17 C ANISOU 229 CB VAL A 31 1479 1528 1617 -23 219 -40 C ATOM 230 CG1 VAL A 31 -6.056 -8.577 13.144 1.00 13.30 C ANISOU 230 CG1 VAL A 31 1617 1657 1779 269 92 18 C ATOM 231 CG2 VAL A 31 -4.230 -6.950 13.686 1.00 13.34 C ANISOU 231 CG2 VAL A 31 1537 1787 1744 -82 -17 -234 C ATOM 232 H VAL A 31 -3.054 -9.689 13.949 1.00 10.24 H ATOM 233 HA VAL A 31 -4.123 -9.371 11.447 1.00 11.48 H ATOM 234 HB VAL A 31 -5.032 -7.363 11.898 1.00 14.62 H ATOM 235 HG11 VAL A 31 -6.687 -7.906 13.417 1.00 15.97 H ATOM 236 HG12 VAL A 31 -6.418 -9.091 12.419 1.00 15.97 H ATOM 237 HG13 VAL A 31 -5.849 -9.153 13.884 1.00 15.97 H ATOM 238 HG21 VAL A 31 -4.913 -6.324 13.939 1.00 16.02 H ATOM 239 HG22 VAL A 31 -3.937 -7.445 14.454 1.00 16.02 H ATOM 240 HG23 VAL A 31 -3.487 -6.484 13.294 1.00 16.02 H ATOM 241 N SER A 32 -2.555 -7.624 10.616 1.00 9.99 N ANISOU 241 N SER A 32 1283 1159 1354 42 -135 265 N ATOM 242 CA SER A 32 -1.498 -6.781 10.099 1.00 10.02 C ANISOU 242 CA SER A 32 1268 1148 1391 25 -144 233 C ATOM 243 C SER A 32 -1.961 -5.349 10.151 1.00 9.81 C ANISOU 243 C SER A 32 1125 1110 1493 32 -143 355 C ATOM 244 O SER A 32 -3.107 -5.058 9.781 1.00 12.32 O ANISOU 244 O SER A 32 1527 1300 1855 -22 -280 364 O ATOM 245 CB SER A 32 -1.235 -7.182 8.604 1.00 12.33 C ANISOU 245 CB SER A 32 1655 1499 1529 -16 98 204 C ATOM 246 OG SER A 32 -0.503 -6.248 7.875 1.00 13.93 O ANISOU 246 OG SER A 32 2162 1571 1557 -68 112 104 O ATOM 247 H SER A 32 -3.241 -7.679 10.101 1.00 12.00 H ATOM 248 HA SER A 32 -0.677 -6.886 10.623 1.00 12.04 H ATOM 249 HB2 SER A 32 -0.749 -8.022 8.597 1.00 14.81 H ATOM 250 HB3 SER A 32 -2.093 -7.304 8.168 1.00 14.81 H ATOM 251 HG SER A 32 -0.312 -5.607 8.350 1.00 16.72 H ATOM 252 N LEU A 33 -1.107 -4.447 10.647 1.00 9.73 N ANISOU 252 N LEU A 33 1237 1095 1365 102 -93 217 N ATOM 253 CA LEU A 33 -1.365 -3.013 10.622 1.00 9.80 C ANISOU 253 CA LEU A 33 1285 1080 1357 -27 -46 196 C ATOM 254 C LEU A 33 -0.654 -2.433 9.409 1.00 10.09 C ANISOU 254 C LEU A 33 1202 1198 1432 209 -82 234 C ATOM 255 O LEU A 33 0.532 -2.657 9.221 1.00 10.66 O ANISOU 255 O LEU A 33 1279 1353 1419 103 47 182 O ATOM 256 CB LEU A 33 -0.875 -2.341 11.895 1.00 10.47 C ANISOU 256 CB LEU A 33 1355 1260 1362 -108 180 52 C ATOM 257 CG LEU A 33 -1.456 -2.934 13.160 1.00 11.21 C ANISOU 257 CG LEU A 33 1448 1338 1473 45 126 -11 C ATOM 258 CD1 LEU A 33 -1.025 -2.089 14.350 1.00 11.88 C ANISOU 258 CD1 LEU A 33 1556 1438 1519 339 -5 118 C ATOM 259 CD2 LEU A 33 -2.975 -3.113 13.147 1.00 12.97 C ANISOU 259 CD2 LEU A 33 1617 1561 1750 -86 216 -49 C ATOM 260 H LEU A 33 -0.355 -4.652 11.010 1.00 11.69 H ATOM 261 HA LEU A 33 -2.327 -2.851 10.531 1.00 11.77 H ATOM 262 HB2 LEU A 33 0.090 -2.427 11.943 1.00 12.57 H ATOM 263 HB3 LEU A 33 -1.121 -1.403 11.868 1.00 12.57 H ATOM 264 HG LEU A 33 -1.069 -3.815 13.282 1.00 13.47 H ATOM 265 HD11 LEU A 33 -1.394 -2.468 15.152 1.00 14.27 H ATOM 266 HD12 LEU A 33 -0.066 -2.087 14.401 1.00 14.27 H ATOM 267 HD13 LEU A 33 -1.349 -1.194 14.231 1.00 14.27 H ATOM 268 HD21 LEU A 33 -3.252 -3.492 13.984 1.00 15.58 H ATOM 269 HD22 LEU A 33 -3.388 -2.255 13.023 1.00 15.58 H ATOM 270 HD23 LEU A 33 -3.214 -3.699 12.426 1.00 15.58 H ATOM 271 N ASN A 34 -1.416 -1.707 8.603 1.00 11.52 N ANISOU 271 N ASN A 34 1452 1400 1526 230 98 429 N ATOM 272 CA ASN A 34 -0.966 -1.249 7.312 1.00 12.89 C ANISOU 272 CA ASN A 34 1578 1666 1654 -55 -27 443 C ATOM 273 C ASN A 34 -1.139 0.255 7.201 1.00 13.18 C ANISOU 273 C ASN A 34 1567 1788 1652 48 -89 475 C ATOM 274 O ASN A 34 -2.180 0.830 7.506 1.00 14.34 O ANISOU 274 O ASN A 34 1794 1824 1829 77 -46 534 O ATOM 275 CB ASN A 34 -1.756 -2.067 6.234 1.00 15.10 C ANISOU 275 CB ASN A 34 1929 1943 1865 93 -140 541 C ATOM 276 CG ASN A 34 -1.335 -1.772 4.821 1.00 17.33 C ANISOU 276 CG ASN A 34 2474 2159 1950 206 -78 530 C ATOM 277 OD1 ASN A 34 -1.524 -0.676 4.339 1.00 19.24 O ANISOU 277 OD1 ASN A 34 3109 2329 1873 112 -120 520 O ATOM 278 ND2 ASN A 34 -0.713 -2.721 4.200 1.00 18.36 N ANISOU 278 ND2 ASN A 34 2476 2316 2186 176 111 405 N ATOM 279 H ASN A 34 -2.219 -1.463 8.793 1.00 13.84 H ATOM 280 HA ASN A 34 -0.013 -1.454 7.212 1.00 15.48 H ATOM 281 HB2 ASN A 34 -1.614 -3.013 6.394 1.00 18.13 H ATOM 282 HB3 ASN A 34 -2.699 -1.857 6.312 1.00 18.13 H ATOM 283 HD21 ASN A 34 -0.413 -2.589 3.276 1.00 22.05 H ATOM 284 HD22 ASN A 34 -0.540 -3.573 4.653 1.00 22.05 H ATOM 285 N SER A 37 -0.076 0.913 6.738 1.00 13.90 N ANISOU 285 N SER A 37 1715 1772 1793 87 -131 599 N ATOM 286 CA SER A 37 -0.135 2.294 6.352 1.00 16.92 C ANISOU 286 CA SER A 37 2187 2081 2160 -78 33 696 C ATOM 287 C SER A 37 0.813 2.429 5.187 1.00 19.50 C ANISOU 287 C SER A 37 2533 2462 2416 163 171 747 C ATOM 288 O SER A 37 2.044 2.497 5.362 1.00 19.84 O ANISOU 288 O SER A 37 2456 2607 2476 -100 298 709 O ATOM 289 CB SER A 37 0.321 3.161 7.532 1.00 19.36 C ANISOU 289 CB SER A 37 2604 2285 2467 -115 59 687 C ATOM 290 OG SER A 37 0.398 4.527 7.092 1.00 20.57 O ANISOU 290 OG SER A 37 2945 2345 2527 -314 12 514 O ATOM 291 H SER A 37 0.702 0.561 6.642 1.00 16.69 H ATOM 292 HA SER A 37 -1.042 2.545 6.079 1.00 20.32 H ATOM 293 HB2 SER A 37 -0.324 3.091 8.253 1.00 23.25 H ATOM 294 HB3 SER A 37 1.196 2.868 7.830 1.00 23.25 H ATOM 295 HG SER A 37 0.641 5.008 7.711 1.00 24.70 H ATOM 296 N GLY A 38 0.257 2.322 3.993 1.00 21.30 N ANISOU 296 N GLY A 38 2851 2637 2606 604 251 966 N ATOM 297 CA GLY A 38 1.171 2.118 2.814 1.00 23.97 C ANISOU 297 CA GLY A 38 3177 3039 2892 775 278 948 C ATOM 298 C GLY A 38 1.525 0.663 2.695 1.00 24.76 C ANISOU 298 C GLY A 38 3483 3238 2688 950 247 759 C ATOM 299 O GLY A 38 1.259 0.008 1.688 1.00 27.80 O ANISOU 299 O GLY A 38 4118 3657 2787 1048 -41 473 O ATOM 300 H GLY A 38 -0.584 2.357 3.817 1.00 25.58 H ATOM 301 HA2 GLY A 38 0.731 2.404 1.999 1.00 28.78 H ATOM 302 HA3 GLY A 38 1.985 2.633 2.932 1.00 28.78 H ATOM 303 N SER A 39 2.293 0.151 3.653 1.00 22.36 N ANISOU 303 N SER A 39 3039 2850 2605 814 471 1088 N ATOM 304 CA SER A 39 2.760 -1.209 3.756 1.00 21.36 C ANISOU 304 CA SER A 39 2773 2791 2551 713 625 1105 C ATOM 305 C SER A 39 2.507 -1.689 5.178 1.00 16.25 C ANISOU 305 C SER A 39 2092 2193 1891 439 349 747 C ATOM 306 O SER A 39 2.129 -0.912 6.084 1.00 15.08 O ANISOU 306 O SER A 39 1890 2038 1803 205 195 499 O ATOM 307 CB SER A 39 4.307 -1.212 3.556 1.00 26.19 C ANISOU 307 CB SER A 39 3360 3349 3241 521 1028 1252 C ATOM 308 OG SER A 39 4.606 -0.939 2.193 1.00 30.17 O ANISOU 308 OG SER A 39 3925 3918 3618 331 1122 1155 O ATOM 309 H SER A 39 2.574 0.629 4.309 1.00 26.84 H ATOM 310 HA SER A 39 2.322 -1.797 3.105 1.00 25.65 H ATOM 311 HB2 SER A 39 4.703 -0.526 4.115 1.00 31.44 H ATOM 312 HB3 SER A 39 4.658 -2.084 3.794 1.00 31.44 H ATOM 313 HG SER A 39 5.418 -0.939 2.079 1.00 36.21 H ATOM 314 N HIS A 40 2.627 -2.972 5.326 1.00 15.68 N ANISOU 314 N HIS A 40 2050 2114 1793 531 298 491 N ATOM 315 CA HIS A 40 2.602 -3.589 6.646 1.00 14.12 C ANISOU 315 CA HIS A 40 1781 1884 1700 355 228 565 C ATOM 316 C HIS A 40 3.756 -2.970 7.498 1.00 12.48 C ANISOU 316 C HIS A 40 1505 1655 1580 352 313 453 C ATOM 317 O HIS A 40 4.908 -2.927 7.075 1.00 14.63 O ANISOU 317 O HIS A 40 1749 1951 1859 283 339 321 O ATOM 318 CB HIS A 40 2.847 -5.091 6.515 1.00 14.55 C ANISOU 318 CB HIS A 40 1813 1884 1829 236 210 436 C ATOM 319 CG HIS A 40 3.080 -5.791 7.836 1.00 14.65 C ANISOU 319 CG HIS A 40 1882 1838 1845 -48 137 613 C ATOM 320 ND1 HIS A 40 2.094 -6.322 8.627 1.00 13.89 N ANISOU 320 ND1 HIS A 40 1989 1447 1841 67 211 306 N ATOM 321 CD2 HIS A 40 4.223 -5.951 8.535 1.00 17.40 C ANISOU 321 CD2 HIS A 40 2162 2225 2227 170 121 801 C ATOM 322 CE1 HIS A 40 2.610 -6.790 9.740 1.00 13.17 C ANISOU 322 CE1 HIS A 40 1799 1328 1877 273 86 358 C ATOM 323 NE2 HIS A 40 3.897 -6.560 9.740 1.00 16.64 N ANISOU 323 NE2 HIS A 40 2255 1880 2186 284 178 623 N ATOM 324 H HIS A 40 2.727 -3.529 4.679 1.00 18.83 H ATOM 325 HA HIS A 40 1.742 -3.430 7.088 1.00 16.96 H ATOM 326 HB2 HIS A 40 2.072 -5.498 6.097 1.00 17.47 H ATOM 327 HB3 HIS A 40 3.631 -5.233 5.962 1.00 17.47 H ATOM 328 HD2 HIS A 40 5.069 -5.663 8.277 1.00 20.90 H ATOM 329 HE1 HIS A 40 2.137 -7.214 10.419 1.00 15.82 H ATOM 330 N PHE A 41 3.414 -2.532 8.732 1.00 12.57 N ANISOU 330 N PHE A 41 1542 1747 1487 145 165 340 N ATOM 331 CA PHE A 41 4.458 -1.968 9.589 1.00 12.27 C ANISOU 331 CA PHE A 41 1436 1752 1473 35 95 480 C ATOM 332 C PHE A 41 4.481 -2.550 11.001 1.00 10.62 C ANISOU 332 C PHE A 41 1221 1444 1367 -17 117 430 C ATOM 333 O PHE A 41 5.432 -2.335 11.714 1.00 10.96 O ANISOU 333 O PHE A 41 1154 1513 1499 -83 57 333 O ATOM 334 CB PHE A 41 4.356 -0.417 9.637 1.00 12.92 C ANISOU 334 CB PHE A 41 1611 1681 1617 -27 33 553 C ATOM 335 CG PHE A 41 3.160 0.098 10.361 1.00 12.07 C ANISOU 335 CG PHE A 41 1590 1433 1563 2 -40 556 C ATOM 336 CD1 PHE A 41 3.204 0.420 11.705 1.00 12.61 C ANISOU 336 CD1 PHE A 41 1785 1324 1683 -131 -89 418 C ATOM 337 CD2 PHE A 41 1.936 0.284 9.673 1.00 12.24 C ANISOU 337 CD2 PHE A 41 1586 1488 1576 73 -24 306 C ATOM 338 CE1 PHE A 41 2.063 0.805 12.365 1.00 13.33 C ANISOU 338 CE1 PHE A 41 2005 1338 1722 3 -21 218 C ATOM 339 CE2 PHE A 41 0.843 0.726 10.325 1.00 12.43 C ANISOU 339 CE2 PHE A 41 1686 1324 1713 -10 82 275 C ATOM 340 CZ PHE A 41 0.886 0.987 11.664 1.00 12.68 C ANISOU 340 CZ PHE A 41 1782 1282 1755 33 92 416 C ATOM 341 H PHE A 41 2.625 -2.552 9.074 1.00 15.10 H ATOM 342 HA PHE A 41 5.323 -2.182 9.182 1.00 14.73 H ATOM 343 HB2 PHE A 41 5.144 -0.067 10.083 1.00 15.52 H ATOM 344 HB3 PHE A 41 4.319 -0.079 8.728 1.00 15.52 H ATOM 345 HD1 PHE A 41 3.985 0.269 12.187 1.00 15.15 H ATOM 346 HD2 PHE A 41 1.885 0.091 8.765 1.00 14.70 H ATOM 347 HE1 PHE A 41 2.101 1.020 13.269 1.00 16.01 H ATOM 348 HE2 PHE A 41 0.044 0.834 9.861 1.00 14.93 H ATOM 349 HZ PHE A 41 0.128 1.302 12.101 1.00 15.23 H ATOM 350 N CYS A 42 3.420 -3.242 11.392 1.00 9.96 N ANISOU 350 N CYS A 42 1224 1304 1255 -38 57 352 N ATOM 351 CA CYS A 42 3.293 -3.803 12.733 1.00 8.72 C ANISOU 351 CA CYS A 42 1157 943 1213 -16 13 90 C ATOM 352 C CYS A 42 2.227 -4.875 12.698 1.00 8.55 C ANISOU 352 C CYS A 42 1084 964 1200 -21 -142 54 C ATOM 353 O CYS A 42 1.419 -4.906 11.794 1.00 9.60 O ANISOU 353 O CYS A 42 1194 1191 1261 77 -68 89 O ATOM 354 CB CYS A 42 2.920 -2.737 13.803 1.00 9.51 C ANISOU 354 CB CYS A 42 1356 970 1287 -103 -83 37 C ATOM 355 SG CYS A 42 4.269 -1.777 14.500 1.00 9.90 S ANISOU 355 SG CYS A 42 1260 1061 1442 6 3 129 S ATOM 356 H CYS A 42 2.743 -3.406 10.887 1.00 11.97 H ATOM 357 HA CYS A 42 4.142 -4.218 12.993 1.00 10.48 H ATOM 358 HB2 CYS A 42 2.300 -2.109 13.399 1.00 11.43 H ATOM 359 HB3 CYS A 42 2.481 -3.190 14.539 1.00 11.43 H ATOM 360 N GLY A 43 2.246 -5.723 13.711 1.00 8.77 N ANISOU 360 N GLY A 43 1096 1044 1191 -53 -80 102 N ATOM 361 CA GLY A 43 1.156 -6.656 13.935 1.00 8.80 C ANISOU 361 CA GLY A 43 1108 1067 1169 -22 -90 17 C ATOM 362 C GLY A 43 0.180 -6.192 15.022 1.00 8.15 C ANISOU 362 C GLY A 43 1158 764 1176 98 -28 123 C ATOM 363 O GLY A 43 0.321 -5.115 15.605 1.00 8.58 O ANISOU 363 O GLY A 43 1093 837 1331 70 41 -13 O ATOM 364 H GLY A 43 2.881 -5.779 14.287 1.00 10.53 H ATOM 365 HA2 GLY A 43 0.660 -6.774 13.110 1.00 10.57 H ATOM 366 HA3 GLY A 43 1.519 -7.516 14.199 1.00 10.57 H ATOM 367 N GLY A 44 -0.793 -7.043 15.303 1.00 8.24 N ANISOU 367 N GLY A 44 1103 849 1180 -101 95 -13 N ATOM 368 CA GLY A 44 -1.773 -6.812 16.317 1.00 8.26 C ANISOU 368 CA GLY A 44 1035 912 1192 -151 -31 48 C ATOM 369 C GLY A 44 -2.524 -8.107 16.558 1.00 7.57 C ANISOU 369 C GLY A 44 918 809 1150 -16 -107 4 C ATOM 370 O GLY A 44 -2.362 -9.074 15.817 1.00 8.69 O ANISOU 370 O GLY A 44 1132 933 1238 -20 -45 -51 O ATOM 371 H GLY A 44 -0.900 -7.792 14.894 1.00 9.91 H ATOM 372 HA2 GLY A 44 -1.344 -6.531 17.141 1.00 9.92 H ATOM 373 HA3 GLY A 44 -2.397 -6.127 16.031 1.00 9.92 H ATOM 374 N SER A 45 -3.403 -8.092 17.564 1.00 7.78 N ANISOU 374 N SER A 45 956 785 1216 -30 46 -1 N ATOM 375 CA SER A 45 -4.212 -9.212 17.928 1.00 8.21 C ANISOU 375 CA SER A 45 952 867 1300 -79 0 181 C ATOM 376 C SER A 45 -5.676 -8.814 18.104 1.00 8.28 C ANISOU 376 C SER A 45 956 848 1342 -114 -152 -70 C ATOM 377 O SER A 45 -5.956 -7.845 18.851 1.00 9.01 O ANISOU 377 O SER A 45 1039 948 1437 -35 -69 -170 O ATOM 378 CB SER A 45 -3.712 -9.784 19.288 1.00 9.21 C ANISOU 378 CB SER A 45 1036 1052 1411 -42 -18 230 C ATOM 379 OG SER A 45 -2.359 -10.177 19.186 1.00 10.24 O ANISOU 379 OG SER A 45 1159 1197 1535 248 -76 166 O ATOM 380 H SER A 45 -3.539 -7.403 18.062 1.00 9.35 H ATOM 381 HA SER A 45 -4.149 -9.911 17.243 1.00 9.86 H ATOM 382 HB2 SER A 45 -3.793 -9.098 19.969 1.00 11.07 H ATOM 383 HB3 SER A 45 -4.250 -10.555 19.526 1.00 11.07 H ATOM 384 HG SER A 45 -2.099 -10.477 19.904 1.00 12.30 H ATOM 385 N LEU A 46 -6.564 -9.559 17.485 1.00 8.51 N ANISOU 385 N LEU A 46 974 960 1300 -6 -115 -61 N ATOM 386 CA LEU A 46 -7.995 -9.260 17.586 1.00 8.11 C ANISOU 386 CA LEU A 46 854 939 1291 -28 -179 17 C ATOM 387 C LEU A 46 -8.507 -9.836 18.906 1.00 8.58 C ANISOU 387 C LEU A 46 913 906 1441 -46 -134 23 C ATOM 388 O LEU A 46 -8.429 -11.025 19.128 1.00 9.40 O ANISOU 388 O LEU A 46 1072 877 1621 27 -40 -31 O ATOM 389 CB LEU A 46 -8.743 -9.899 16.442 1.00 8.95 C ANISOU 389 CB LEU A 46 1039 1097 1263 -82 -197 4 C ATOM 390 CG LEU A 46 -10.224 -9.517 16.325 1.00 9.91 C ANISOU 390 CG LEU A 46 1113 1207 1447 -121 -228 39 C ATOM 391 CD1 LEU A 46 -10.386 -8.045 15.906 1.00 10.81 C ANISOU 391 CD1 LEU A 46 1253 1326 1529 -94 -126 82 C ATOM 392 CD2 LEU A 46 -10.932 -10.402 15.326 1.00 12.11 C ANISOU 392 CD2 LEU A 46 1450 1472 1681 -275 -290 -16 C ATOM 393 H LEU A 46 -6.377 -10.244 16.999 1.00 10.23 H ATOM 394 HA LEU A 46 -8.144 -8.292 17.573 1.00 9.75 H ATOM 395 HB2 LEU A 46 -8.311 -9.643 15.612 1.00 10.75 H ATOM 396 HB3 LEU A 46 -8.698 -10.862 16.546 1.00 10.75 H ATOM 397 HG LEU A 46 -10.651 -9.634 17.188 1.00 11.91 H ATOM 398 HD11 LEU A 46 -11.322 -7.840 15.843 1.00 12.99 H ATOM 399 HD12 LEU A 46 -9.972 -7.485 16.566 1.00 12.99 H ATOM 400 HD13 LEU A 46 -9.964 -7.915 15.053 1.00 12.99 H ATOM 401 HD21 LEU A 46 -11.855 -10.140 15.276 1.00 14.55 H ATOM 402 HD22 LEU A 46 -10.515 -10.300 14.468 1.00 14.55 H ATOM 403 HD23 LEU A 46 -10.867 -11.315 15.616 1.00 14.55 H ATOM 404 N ILE A 47 -9.021 -8.973 19.774 1.00 9.37 N ANISOU 404 N ILE A 47 1160 993 1406 149 -59 70 N ATOM 405 CA ILE A 47 -9.529 -9.382 21.072 1.00 9.70 C ANISOU 405 CA ILE A 47 1131 1153 1402 99 0 -30 C ATOM 406 C ILE A 47 -11.053 -9.275 21.214 1.00 11.55 C ANISOU 406 C ILE A 47 1203 1562 1624 147 50 316 C ATOM 407 O ILE A 47 -11.616 -9.812 22.182 1.00 12.73 O ANISOU 407 O ILE A 47 1348 1732 1759 154 235 506 O ATOM 408 CB ILE A 47 -8.793 -8.715 22.232 1.00 10.34 C ANISOU 408 CB ILE A 47 1324 1222 1383 211 46 -81 C ATOM 409 CG1 ILE A 47 -9.037 -7.222 22.155 1.00 12.16 C ANISOU 409 CG1 ILE A 47 1598 1449 1574 335 26 -71 C ATOM 410 CG2 ILE A 47 -7.350 -9.117 22.260 1.00 10.93 C ANISOU 410 CG2 ILE A 47 1415 1271 1465 192 -45 -150 C ATOM 411 CD1 ILE A 47 -8.803 -6.502 23.482 1.00 13.75 C ANISOU 411 CD1 ILE A 47 1769 1700 1754 240 96 -43 C ATOM 412 H ILE A 47 -9.086 -8.128 19.629 1.00 11.25 H ATOM 413 HA ILE A 47 -9.329 -10.338 21.154 1.00 11.65 H ATOM 414 HB ILE A 47 -9.197 -9.033 23.054 1.00 12.42 H ATOM 415 HG12 ILE A 47 -8.436 -6.838 21.497 1.00 14.61 H ATOM 416 HG13 ILE A 47 -9.958 -7.067 21.890 1.00 14.61 H ATOM 417 HG21 ILE A 47 -6.919 -8.682 22.999 1.00 13.13 H ATOM 418 HG22 ILE A 47 -7.293 -10.070 22.363 1.00 13.13 H ATOM 419 HG23 ILE A 47 -6.936 -8.851 21.436 1.00 13.13 H ATOM 420 HD11 ILE A 47 -8.974 -5.565 23.363 1.00 16.51 H ATOM 421 HD12 ILE A 47 -9.399 -6.863 24.142 1.00 16.51 H ATOM 422 HD13 ILE A 47 -7.892 -6.637 23.753 1.00 16.51 H ATOM 423 N SER A 48 -11.698 -8.553 20.321 1.00 12.36 N ANISOU 423 N SER A 48 1243 1677 1776 186 33 407 N ATOM 424 CA ASER A 48 -13.147 -8.579 20.256 0.63 12.95 C ANISOU 424 CA ASER A 48 1360 1760 1802 292 94 397 C ATOM 425 CA BSER A 48 -13.139 -8.348 20.350 0.37 12.95 C ANISOU 425 CA BSER A 48 1157 1841 1924 310 51 376 C ATOM 426 C SER A 48 -13.530 -8.216 18.879 1.00 13.41 C ANISOU 426 C SER A 48 1232 1960 1904 201 -47 417 C ATOM 427 O SER A 48 -12.642 -7.986 18.036 1.00 15.02 O ANISOU 427 O SER A 48 1305 2495 1908 315 -50 601 O ATOM 428 CB ASER A 48 -13.773 -7.602 21.246 0.63 14.12 C ANISOU 428 CB ASER A 48 1629 1827 1909 353 243 464 C ATOM 429 CB BSER A 48 -13.538 -7.114 21.264 0.37 14.15 C ANISOU 429 CB BSER A 48 1158 2070 2150 409 120 348 C ATOM 430 OG ASER A 48 -13.679 -6.343 20.646 0.63 13.92 O ANISOU 430 OG ASER A 48 1690 1559 2040 51 200 329 O ATOM 431 OG BSER A 48 -14.900 -7.265 21.710 0.37 15.04 O ANISOU 431 OG BSER A 48 1231 2170 2313 252 139 190 O ATOM 432 H ASER A 48 -11.324 -8.041 19.740 1.00 14.85 H ATOM 433 HA ASER A 48 -13.474 -9.482 20.451 0.63 15.56 H ATOM 434 HB2ASER A 48 -14.704 -7.830 21.393 0.63 16.96 H ATOM 435 HB3ASER A 48 -13.276 -7.610 22.079 0.63 16.96 H ATOM 436 HG ASER A 48 -14.003 -5.773 21.138 0.63 16.72 H ATOM 437 N GLU A 49 -14.823 -8.200 18.569 1.00 13.19 N ANISOU 437 N GLU A 49 1235 1841 1934 56 -21 292 N ATOM 438 CA GLU A 49 -15.239 -7.948 17.225 1.00 13.59 C ANISOU 438 CA GLU A 49 1343 1811 2009 -108 -171 157 C ATOM 439 C GLU A 49 -14.740 -6.605 16.707 1.00 12.66 C ANISOU 439 C GLU A 49 1236 1743 1831 -12 -260 165 C ATOM 440 O GLU A 49 -14.578 -6.404 15.498 1.00 14.63 O ANISOU 440 O GLU A 49 1930 1743 1887 -248 -131 42 O ATOM 441 CB GLU A 49 -16.820 -7.939 17.086 1.00 15.90 C ANISOU 441 CB GLU A 49 1759 2052 2231 -379 -120 182 C ATOM 442 CG GLU A 49 -17.483 -9.260 17.380 1.00 18.37 C ANISOU 442 CG GLU A 49 2019 2418 2544 -579 -90 80 C ATOM 443 CD GLU A 49 -17.619 -9.587 18.851 1.00 19.55 C ANISOU 443 CD GLU A 49 1790 2771 2866 -790 32 148 C ATOM 444 OE1 GLU A 49 -18.233 -10.661 19.127 1.00 21.44 O ANISOU 444 OE1 GLU A 49 2078 2929 3140 -542 -4 462 O ATOM 445 OE2 GLU A 49 -17.186 -8.798 19.743 1.00 20.42 O ANISOU 445 OE2 GLU A 49 1665 3111 2983 -895 334 55 O ATOM 446 H GLU A 49 -15.466 -8.334 19.125 1.00 15.84 H ATOM 447 HA GLU A 49 -14.885 -8.652 16.641 1.00 16.32 H ATOM 448 HB2 GLU A 49 -17.181 -7.285 17.705 1.00 19.09 H ATOM 449 HB3 GLU A 49 -17.050 -7.690 16.177 1.00 19.09 H ATOM 450 HG2 GLU A 49 -18.375 -9.251 16.998 1.00 22.06 H ATOM 451 HG3 GLU A 49 -16.960 -9.967 16.969 1.00 22.06 H ATOM 452 N GLN A 50 -14.550 -5.643 17.593 1.00 11.95 N ANISOU 452 N GLN A 50 1133 1599 1809 -90 -313 122 N ATOM 453 CA AGLN A 50 -14.249 -4.303 17.203 0.60 11.75 C ANISOU 453 CA AGLN A 50 1351 1414 1698 51 -252 78 C ATOM 454 CA BGLN A 50 -14.160 -4.343 17.109 0.40 12.26 C ANISOU 454 CA BGLN A 50 1272 1548 1839 50 -170 69 C ATOM 455 C GLN A 50 -12.894 -3.763 17.718 1.00 10.97 C ANISOU 455 C GLN A 50 1192 1362 1614 66 -194 60 C ATOM 456 O GLN A 50 -12.612 -2.612 17.535 1.00 11.44 O ANISOU 456 O GLN A 50 1219 1384 1743 -6 -245 153 O ATOM 457 CB AGLN A 50 -15.314 -3.289 17.654 0.60 14.31 C ANISOU 457 CB AGLN A 50 1599 1917 1919 16 -318 121 C ATOM 458 CB BGLN A 50 -15.269 -3.315 17.191 0.40 14.91 C ANISOU 458 CB BGLN A 50 1500 2028 2139 67 -55 59 C ATOM 459 CG AGLN A 50 -15.450 -2.141 16.503 0.60 16.39 C ANISOU 459 CG AGLN A 50 1912 2158 2157 9 -76 223 C ATOM 460 CG BGLN A 50 -15.911 -3.107 18.497 0.40 16.44 C ANISOU 460 CG BGLN A 50 1730 2250 2267 22 29 -2 C ATOM 461 CD AGLN A 50 -16.824 -1.537 16.253 0.60 16.75 C ANISOU 461 CD AGLN A 50 1824 2344 2196 168 -45 507 C ATOM 462 CD BGLN A 50 -17.499 -2.722 18.344 0.40 16.56 C ANISOU 462 CD BGLN A 50 1665 2265 2363 86 36 21 C ATOM 463 OE1AGLN A 50 -16.911 -0.631 15.483 0.60 17.45 O ANISOU 463 OE1AGLN A 50 1588 2468 2574 159 154 747 O ATOM 464 OE1BGLN A 50 -17.883 -1.785 17.576 0.40 17.71 O ANISOU 464 OE1BGLN A 50 1874 2513 2343 152 109 -191 O ATOM 465 NE2AGLN A 50 -17.872 -2.057 16.848 0.60 16.39 N ANISOU 465 NE2AGLN A 50 1917 2237 2071 262 -209 582 N ATOM 466 NE2BGLN A 50 -18.356 -3.348 19.215 0.40 14.82 N ANISOU 466 NE2BGLN A 50 1207 2021 2402 -31 -41 37 N ATOM 467 H AGLN A 50 -14.593 -5.756 18.444 1.00 14.35 H ATOM 468 HA AGLN A 50 -14.217 -4.274 16.224 0.61 14.11 H ATOM 469 HB2AGLN A 50 -16.170 -3.733 17.756 0.61 17.18 H ATOM 470 HB3AGLN A 50 -15.040 -2.870 18.485 0.61 17.18 H ATOM 471 HG2AGLN A 50 -14.859 -1.409 16.742 0.61 19.68 H ATOM 472 HG3AGLN A 50 -15.153 -2.525 15.663 0.61 19.68 H ATOM 473 HE21AGLN A 50 -18.653 -1.723 16.714 0.61 19.68 H ATOM 474 HE22AGLN A 50 -17.778 -2.732 17.373 0.61 19.68 H ATOM 475 N TRP A 51 -12.125 -4.599 18.408 1.00 9.85 N ANISOU 475 N TRP A 51 1142 1149 1450 54 -187 -54 N ATOM 476 CA TRP A 51 -10.910 -4.106 19.078 1.00 9.49 C ANISOU 476 CA TRP A 51 1083 1134 1388 103 -177 -120 C ATOM 477 C TRP A 51 -9.688 -5.011 18.864 1.00 8.67 C ANISOU 477 C TRP A 51 996 945 1353 58 -183 -22 C ATOM 478 O TRP A 51 -9.777 -6.225 18.955 1.00 9.73 O ANISOU 478 O TRP A 51 1013 1095 1591 54 29 -42 O ATOM 479 CB TRP A 51 -11.150 -3.959 20.585 1.00 10.13 C ANISOU 479 CB TRP A 51 1114 1310 1424 111 -119 -184 C ATOM 480 CG TRP A 51 -12.100 -2.859 20.905 1.00 9.77 C ANISOU 480 CG TRP A 51 946 1370 1398 332 5 -87 C ATOM 481 CD1 TRP A 51 -13.465 -2.926 21.013 1.00 11.57 C ANISOU 481 CD1 TRP A 51 1276 1494 1626 209 132 -81 C ATOM 482 CD2 TRP A 51 -11.740 -1.488 21.193 1.00 10.33 C ANISOU 482 CD2 TRP A 51 1029 1421 1476 230 9 -182 C ATOM 483 NE1 TRP A 51 -13.974 -1.666 21.300 1.00 11.76 N ANISOU 483 NE1 TRP A 51 1225 1603 1640 270 59 -215 N ATOM 484 CE2 TRP A 51 -12.949 -0.768 21.460 1.00 10.60 C ANISOU 484 CE2 TRP A 51 1109 1366 1554 206 10 -240 C ATOM 485 CE3 TRP A 51 -10.542 -0.805 21.260 1.00 11.33 C ANISOU 485 CE3 TRP A 51 1276 1400 1629 131 -35 -30 C ATOM 486 CZ2 TRP A 51 -12.951 0.557 21.840 1.00 11.55 C ANISOU 486 CZ2 TRP A 51 1261 1503 1623 263 46 4 C ATOM 487 CZ3 TRP A 51 -10.547 0.549 21.650 1.00 11.60 C ANISOU 487 CZ3 TRP A 51 1303 1404 1700 162 -167 36 C ATOM 488 CH2 TRP A 51 -11.759 1.203 21.918 1.00 11.24 C ANISOU 488 CH2 TRP A 51 1226 1389 1656 340 -18 -1 C ATOM 489 H TRP A 51 -12.275 -5.441 18.506 1.00 11.83 H ATOM 490 HA TRP A 51 -10.692 -3.220 18.721 1.00 11.40 H ATOM 491 HB2 TRP A 51 -11.522 -4.786 20.929 1.00 12.17 H ATOM 492 HB3 TRP A 51 -10.307 -3.765 21.023 1.00 12.17 H ATOM 493 HD1 TRP A 51 -13.978 -3.681 20.832 1.00 13.90 H ATOM 494 HE1 TRP A 51 -14.805 -1.492 21.437 1.00 14.13 H ATOM 495 HE3 TRP A 51 -9.738 -1.254 21.132 1.00 13.61 H ATOM 496 HZ2 TRP A 51 -13.747 0.997 22.036 1.00 13.87 H ATOM 497 HZ3 TRP A 51 -9.746 1.019 21.699 1.00 13.93 H ATOM 498 HH2 TRP A 51 -11.748 2.112 22.116 1.00 13.50 H ATOM 499 N VAL A 52 -8.562 -4.336 18.654 1.00 9.00 N ANISOU 499 N VAL A 52 1000 989 1430 40 -157 -149 N ATOM 500 CA VAL A 52 -7.251 -4.939 18.437 1.00 8.40 C ANISOU 500 CA VAL A 52 930 934 1327 67 -14 -104 C ATOM 501 C VAL A 52 -6.275 -4.374 19.463 1.00 7.84 C ANISOU 501 C VAL A 52 844 762 1372 70 36 9 C ATOM 502 O VAL A 52 -6.251 -3.194 19.734 1.00 9.36 O ANISOU 502 O VAL A 52 1095 965 1498 97 -140 -33 O ATOM 503 CB VAL A 52 -6.776 -4.585 16.997 1.00 8.71 C ANISOU 503 CB VAL A 52 996 1020 1293 115 2 -7 C ATOM 504 CG1 VAL A 52 -5.305 -4.835 16.782 1.00 10.06 C ANISOU 504 CG1 VAL A 52 1218 1202 1401 53 -20 114 C ATOM 505 CG2 VAL A 52 -7.657 -5.300 15.958 1.00 9.62 C ANISOU 505 CG2 VAL A 52 1217 1150 1289 -8 -153 -4 C ATOM 506 H VAL A 52 -8.533 -3.477 18.632 1.00 10.81 H ATOM 507 HA VAL A 52 -7.301 -5.913 18.535 1.00 10.09 H ATOM 508 HB VAL A 52 -6.917 -3.623 16.868 1.00 10.46 H ATOM 509 HG11 VAL A 52 -5.077 -4.599 15.881 1.00 12.08 H ATOM 510 HG12 VAL A 52 -4.804 -4.298 17.400 1.00 12.08 H ATOM 511 HG13 VAL A 52 -5.122 -5.765 16.934 1.00 12.08 H ATOM 512 HG21 VAL A 52 -7.350 -5.070 15.078 1.00 11.56 H ATOM 513 HG22 VAL A 52 -7.589 -6.248 16.091 1.00 11.56 H ATOM 514 HG23 VAL A 52 -8.567 -5.016 16.072 1.00 11.56 H ATOM 515 N VAL A 53 -5.437 -5.267 19.979 1.00 8.26 N ANISOU 515 N VAL A 53 903 870 1365 30 -83 -53 N ATOM 516 CA VAL A 53 -4.299 -4.882 20.825 1.00 8.87 C ANISOU 516 CA VAL A 53 982 1071 1318 -34 -50 -52 C ATOM 517 C VAL A 53 -3.043 -4.857 19.990 1.00 8.25 C ANISOU 517 C VAL A 53 928 871 1334 129 -23 -182 C ATOM 518 O VAL A 53 -2.780 -5.760 19.204 1.00 8.62 O ANISOU 518 O VAL A 53 890 977 1410 55 -37 -188 O ATOM 519 CB VAL A 53 -4.106 -5.960 21.968 1.00 10.44 C ANISOU 519 CB VAL A 53 1125 1513 1330 -136 -202 58 C ATOM 520 CG1 VAL A 53 -2.796 -5.740 22.708 1.00 12.56 C ANISOU 520 CG1 VAL A 53 1482 1678 1612 -284 -324 125 C ATOM 521 CG2 VAL A 53 -5.261 -5.938 22.947 1.00 11.50 C ANISOU 521 CG2 VAL A 53 1376 1451 1542 239 -39 36 C ATOM 522 H VAL A 53 -5.503 -6.116 19.856 1.00 9.92 H ATOM 523 HA VAL A 53 -4.448 -3.999 21.225 1.00 10.66 H ATOM 524 HB VAL A 53 -4.075 -6.851 21.561 1.00 12.54 H ATOM 525 HG11 VAL A 53 -2.708 -6.408 23.392 1.00 15.09 H ATOM 526 HG12 VAL A 53 -2.069 -5.813 22.084 1.00 15.09 H ATOM 527 HG13 VAL A 53 -2.803 -4.865 23.102 1.00 15.09 H ATOM 528 HG21 VAL A 53 -5.110 -6.602 23.623 1.00 13.81 H ATOM 529 HG22 VAL A 53 -5.314 -5.067 23.348 1.00 13.81 H ATOM 530 HG23 VAL A 53 -6.074 -6.130 22.474 1.00 13.81 H ATOM 531 N SER A 54 -2.221 -3.820 20.212 1.00 7.95 N ANISOU 531 N SER A 54 997 844 1180 18 34 -7 N ATOM 532 CA SER A 54 -0.933 -3.701 19.567 1.00 7.70 C ANISOU 532 CA SER A 54 993 781 1154 -192 29 -95 C ATOM 533 C SER A 54 0.047 -3.003 20.527 1.00 7.57 C ANISOU 533 C SER A 54 999 728 1149 30 67 51 C ATOM 534 O SER A 54 -0.235 -2.893 21.725 1.00 8.15 O ANISOU 534 O SER A 54 915 887 1293 16 33 -59 O ATOM 535 CB SER A 54 -1.085 -3.001 18.212 1.00 8.51 C ANISOU 535 CB SER A 54 1024 1013 1198 -112 -27 -91 C ATOM 536 OG SER A 54 0.104 -2.996 17.470 1.00 8.62 O ANISOU 536 OG SER A 54 1044 1055 1176 30 -14 162 O ATOM 537 H SER A 54 -2.403 -3.168 20.742 1.00 9.56 H ATOM 538 HA SER A 54 -0.586 -4.601 19.395 1.00 9.26 H ATOM 539 HB2 SER A 54 -1.768 -3.462 17.700 1.00 10.23 H ATOM 540 HB3 SER A 54 -1.358 -2.083 18.366 1.00 10.23 H ATOM 541 HG SER A 54 -0.014 -2.614 16.754 1.00 10.36 H ATOM 542 N ALA A 55 1.187 -2.564 20.000 1.00 8.04 N ANISOU 542 N ALA A 55 999 915 1142 -79 85 -61 N ATOM 543 CA ALA A 55 2.215 -1.862 20.794 1.00 7.87 C ANISOU 543 CA ALA A 55 905 891 1195 -30 37 -21 C ATOM 544 C ALA A 55 2.021 -0.348 20.615 1.00 7.43 C ANISOU 544 C ALA A 55 959 752 1112 139 -13 146 C ATOM 545 O ALA A 55 1.727 0.129 19.531 1.00 8.73 O ANISOU 545 O ALA A 55 1196 869 1254 19 -177 57 O ATOM 546 CB ALA A 55 3.588 -2.250 20.328 1.00 8.57 C ANISOU 546 CB ALA A 55 1014 979 1263 41 27 89 C ATOM 547 H ALA A 55 1.398 -2.659 19.172 1.00 9.67 H ATOM 548 HA ALA A 55 2.121 -2.089 21.743 1.00 9.46 H ATOM 549 HB1 ALA A 55 4.240 -1.783 20.857 1.00 10.30 H ATOM 550 HB2 ALA A 55 3.698 -3.197 20.434 1.00 10.30 H ATOM 551 HB3 ALA A 55 3.683 -2.010 19.404 1.00 10.30 H ATOM 552 N ALA A 56 2.239 0.429 21.690 1.00 8.14 N ANISOU 552 N ALA A 56 1115 782 1197 -15 47 45 N ATOM 553 CA ALA A 56 2.172 1.865 21.612 1.00 8.68 C ANISOU 553 CA ALA A 56 1136 856 1307 41 128 -60 C ATOM 554 C ALA A 56 3.193 2.448 20.632 1.00 8.74 C ANISOU 554 C ALA A 56 1083 831 1408 67 -48 -72 C ATOM 555 O ALA A 56 2.890 3.493 20.023 1.00 10.36 O ANISOU 555 O ALA A 56 1453 871 1613 209 81 97 O ATOM 556 CB ALA A 56 2.332 2.505 22.973 1.00 9.47 C ANISOU 556 CB ALA A 56 1243 999 1358 -5 85 -73 C ATOM 557 H ALA A 56 2.427 0.130 22.474 1.00 9.79 H ATOM 558 HA ALA A 56 1.283 2.110 21.281 1.00 10.43 H ATOM 559 HB1 ALA A 56 2.282 3.459 22.878 1.00 11.38 H ATOM 560 HB2 ALA A 56 1.628 2.196 23.549 1.00 11.38 H ATOM 561 HB3 ALA A 56 3.185 2.257 23.337 1.00 11.38 H ATOM 562 N HIS A 57 4.345 1.820 20.443 1.00 8.62 N ANISOU 562 N HIS A 57 1034 891 1351 -149 25 82 N ATOM 563 CA HIS A 57 5.321 2.399 19.544 1.00 9.70 C ANISOU 563 CA HIS A 57 1088 1096 1502 -129 19 211 C ATOM 564 C HIS A 57 4.897 2.188 18.079 1.00 10.24 C ANISOU 564 C HIS A 57 1197 1142 1551 -48 118 284 C ATOM 565 O HIS A 57 5.562 2.715 17.198 1.00 11.95 O ANISOU 565 O HIS A 57 1393 1537 1610 -197 96 359 O ATOM 566 CB HIS A 57 6.754 1.920 19.814 1.00 10.22 C ANISOU 566 CB HIS A 57 1281 1136 1467 -263 31 50 C ATOM 567 CG HIS A 57 7.053 0.553 19.323 1.00 9.17 C ANISOU 567 CG HIS A 57 1169 915 1399 -151 65 22 C ATOM 568 ND1 HIS A 57 7.054 -0.573 20.142 1.00 9.69 N ANISOU 568 ND1 HIS A 57 1215 1141 1327 43 142 -9 N ATOM 569 CD2 HIS A 57 7.462 0.124 18.092 1.00 10.10 C ANISOU 569 CD2 HIS A 57 1240 1185 1412 -93 128 90 C ATOM 570 CE1 HIS A 57 7.403 -1.628 19.383 1.00 9.46 C ANISOU 570 CE1 HIS A 57 1166 1082 1346 56 183 -37 C ATOM 571 NE2 HIS A 57 7.677 -1.219 18.143 1.00 10.83 N ANISOU 571 NE2 HIS A 57 1239 1349 1529 -105 124 -26 N ATOM 572 H HIS A 57 4.578 1.080 20.812 1.00 10.36 H ATOM 573 HA HIS A 57 5.321 3.368 19.696 1.00 11.66 H ATOM 574 HB2 HIS A 57 7.371 2.529 19.379 1.00 12.28 H ATOM 575 HB3 HIS A 57 6.908 1.928 20.771 1.00 12.28 H ATOM 576 HD2 HIS A 57 7.574 0.662 17.342 1.00 12.13 H ATOM 577 HE1 HIS A 57 7.468 -2.506 19.684 1.00 11.37 H ATOM 578 N CYS A 58 3.852 1.393 17.836 1.00 9.62 N ANISOU 578 N CYS A 58 1298 981 1378 58 -73 188 N ATOM 579 CA CYS A 58 3.235 1.239 16.528 1.00 10.11 C ANISOU 579 CA CYS A 58 1387 1070 1383 115 32 211 C ATOM 580 C CYS A 58 2.229 2.341 16.192 1.00 11.12 C ANISOU 580 C CYS A 58 1703 1054 1468 84 -52 161 C ATOM 581 O CYS A 58 1.580 2.286 15.159 1.00 12.43 O ANISOU 581 O CYS A 58 2011 1195 1518 263 -172 62 O ATOM 582 CB CYS A 58 2.569 -0.107 16.366 1.00 10.37 C ANISOU 582 CB CYS A 58 1388 1150 1404 114 -24 144 C ATOM 583 SG CYS A 58 3.689 -1.529 16.437 1.00 10.77 S ANISOU 583 SG CYS A 58 1447 1132 1512 126 -4 84 S ATOM 584 H CYS A 58 3.472 0.916 18.443 1.00 11.56 H ATOM 585 HA CYS A 58 3.946 1.288 15.855 1.00 12.14 H ATOM 586 HB2 CYS A 58 1.914 -0.214 17.073 1.00 12.46 H ATOM 587 HB3 CYS A 58 2.123 -0.128 15.504 1.00 12.46 H ATOM 588 N TYR A 59 2.080 3.338 17.081 1.00 10.55 N ANISOU 588 N TYR A 59 1543 975 1491 268 -68 81 N ATOM 589 CA TYR A 59 1.091 4.375 16.862 1.00 11.47 C ANISOU 589 CA TYR A 59 1613 1171 1575 146 -102 189 C ATOM 590 C TYR A 59 1.362 5.126 15.565 1.00 12.33 C ANISOU 590 C TYR A 59 1839 1174 1672 -65 -127 190 C ATOM 591 O TYR A 59 2.469 5.555 15.292 1.00 13.32 O ANISOU 591 O TYR A 59 1883 1342 1838 -91 -186 462 O ATOM 592 CB TYR A 59 1.109 5.363 18.047 1.00 12.08 C ANISOU 592 CB TYR A 59 1579 1269 1742 136 3 49 C ATOM 593 CG TYR A 59 0.118 6.454 17.895 1.00 13.00 C ANISOU 593 CG TYR A 59 1803 1189 1949 330 68 215 C ATOM 594 CD1 TYR A 59 -1.177 6.294 18.294 1.00 14.18 C ANISOU 594 CD1 TYR A 59 1906 1451 2031 400 67 52 C ATOM 595 CD2 TYR A 59 0.481 7.674 17.302 1.00 14.90 C ANISOU 595 CD2 TYR A 59 2002 1429 2230 372 189 179 C ATOM 596 CE1 TYR A 59 -2.133 7.285 18.100 1.00 15.78 C ANISOU 596 CE1 TYR A 59 2077 1679 2238 512 -7 115 C ATOM 597 CE2 TYR A 59 -0.477 8.694 17.113 1.00 16.16 C ANISOU 597 CE2 TYR A 59 2153 1589 2400 525 161 175 C ATOM 598 CZ TYR A 59 -1.785 8.482 17.504 1.00 16.22 C ANISOU 598 CZ TYR A 59 2183 1479 2501 881 69 171 C ATOM 599 OH TYR A 59 -2.727 9.456 17.276 1.00 19.75 O ANISOU 599 OH TYR A 59 2640 2010 2853 988 24 140 O ATOM 600 H TYR A 59 2.536 3.424 17.805 1.00 12.68 H ATOM 601 HA TYR A 59 0.200 3.972 16.808 1.00 13.78 H ATOM 602 HB2 TYR A 59 0.903 4.881 18.864 1.00 14.51 H ATOM 603 HB3 TYR A 59 1.990 5.764 18.111 1.00 14.51 H ATOM 604 HD1 TYR A 59 -1.436 5.484 18.670 1.00 17.03 H ATOM 605 HD2 TYR A 59 1.356 7.805 17.015 1.00 17.89 H ATOM 606 HE1 TYR A 59 -3.013 7.137 18.364 1.00 18.95 H ATOM 607 HE2 TYR A 59 -0.236 9.491 16.698 1.00 19.41 H ATOM 608 HH TYR A 59 -3.064 9.692 17.985 1.00 23.71 H ATOM 609 N LYS A 60 0.275 5.346 14.813 1.00 12.59 N ANISOU 609 N LYS A 60 1702 1255 1827 -51 -235 298 N ATOM 610 CA LYS A 60 0.144 6.314 13.739 1.00 14.24 C ANISOU 610 CA LYS A 60 1907 1521 1981 -74 -248 414 C ATOM 611 C LYS A 60 -1.227 6.883 13.817 1.00 15.05 C ANISOU 611 C LYS A 60 2005 1525 2189 8 -235 423 C ATOM 612 O LYS A 60 -2.103 6.298 14.428 1.00 15.54 O ANISOU 612 O LYS A 60 1991 1534 2379 192 6 398 O ATOM 613 CB LYS A 60 0.311 5.656 12.373 1.00 15.92 C ANISOU 613 CB LYS A 60 2054 1902 2093 -56 -150 546 C ATOM 614 CG LYS A 60 1.647 5.058 12.103 1.00 17.83 C ANISOU 614 CG LYS A 60 2336 2147 2291 88 -42 486 C ATOM 615 CD LYS A 60 1.763 4.524 10.690 1.00 19.93 C ANISOU 615 CD LYS A 60 2583 2415 2575 -109 -150 473 C ATOM 616 CE LYS A 60 3.171 3.939 10.405 1.00 22.18 C ANISOU 616 CE LYS A 60 2858 2657 2914 -53 -205 600 C ATOM 617 NZ LYS A 60 4.090 4.994 9.940 1.00 25.64 N ANISOU 617 NZ LYS A 60 3193 3194 3353 -43 -255 526 N ATOM 618 H LYS A 60 -0.453 4.901 14.927 1.00 15.12 H ATOM 619 HA LYS A 60 0.804 7.032 13.840 1.00 17.10 H ATOM 620 HB2 LYS A 60 -0.346 4.947 12.293 1.00 19.12 H ATOM 621 HB3 LYS A 60 0.149 6.325 11.689 1.00 19.12 H ATOM 622 HG2 LYS A 60 2.329 5.736 12.226 1.00 21.41 H ATOM 623 HG3 LYS A 60 1.795 4.321 12.716 1.00 21.41 H ATOM 624 HD2 LYS A 60 1.110 3.818 10.561 1.00 23.93 H ATOM 625 HD3 LYS A 60 1.602 5.246 10.062 1.00 23.93 H ATOM 626 HE2 LYS A 60 3.532 3.556 11.220 1.00 26.64 H ATOM 627 HE3 LYS A 60 3.106 3.262 9.713 1.00 26.64 H ATOM 628 HZ1 LYS A 60 4.957 4.621 9.767 1.00 30.78 H ATOM 629 HZ2 LYS A 60 3.753 5.388 9.132 1.00 30.78 H ATOM 630 HZ3 LYS A 60 4.171 5.676 10.610 1.00 30.78 H ATOM 631 N THR A 61 -1.478 8.053 13.228 1.00 15.46 N ANISOU 631 N THR A 61 2116 1507 2250 75 -442 310 N ATOM 632 CA ATHR A 61 -2.751 8.746 13.298 0.28 16.39 C ANISOU 632 CA ATHR A 61 2179 1781 2267 200 -391 388 C ATOM 633 CA BTHR A 61 -2.791 8.671 13.399 0.72 15.98 C ANISOU 633 CA BTHR A 61 2335 1270 2465 188 -469 411 C ATOM 634 C THR A 61 -3.831 8.017 12.541 1.00 16.84 C ANISOU 634 C THR A 61 2319 1644 2436 341 -382 429 C ATOM 635 O THR A 61 -5.012 8.187 12.835 1.00 18.91 O ANISOU 635 O THR A 61 2509 1967 2709 341 -238 240 O ATOM 636 CB ATHR A 61 -2.702 10.168 12.655 0.28 17.31 C ANISOU 636 CB ATHR A 61 2242 2080 2256 157 -331 402 C ATOM 637 CB BTHR A 61 -2.767 10.163 13.059 0.72 17.34 C ANISOU 637 CB BTHR A 61 2607 1309 2674 52 -499 484 C ATOM 638 OG1ATHR A 61 -1.527 10.900 13.043 0.28 17.70 O ANISOU 638 OG1ATHR A 61 2265 2185 2276 80 -273 452 O ATOM 639 OG1BTHR A 61 -2.276 10.261 11.724 0.72 18.00 O ANISOU 639 OG1BTHR A 61 2583 1457 2801 -8 -439 756 O ATOM 640 CG2ATHR A 61 -3.944 10.948 13.069 0.28 18.55 C ANISOU 640 CG2ATHR A 61 2341 2309 2397 136 -243 354 C ATOM 641 CG2BTHR A 61 -1.772 10.876 13.961 0.72 18.39 C ANISOU 641 CG2BTHR A 61 2805 1486 2697 -38 -413 156 C ATOM 642 H ATHR A 61 -0.893 8.478 12.762 1.00 18.56 H ATOM 643 HA ATHR A 61 -3.027 8.834 14.234 0.28 19.68 H ATOM 644 HB ATHR A 61 -2.713 10.078 11.689 0.28 20.79 H ATOM 645 HG1ATHR A 61 -0.854 10.496 12.808 0.28 21.26 H ATOM 646 HG21ATHR A 61 -3.926 11.825 12.680 0.28 22.27 H ATOM 647 HG22ATHR A 61 -4.733 10.490 12.770 0.28 22.27 H ATOM 648 HG23ATHR A 61 -3.975 11.032 14.025 0.28 22.27 H ATOM 649 N ARG A 62 -3.438 7.280 11.494 1.00 17.02 N ANISOU 649 N ARG A 62 2271 1807 2390 483 -509 507 N ATOM 650 CA ARG A 62 -4.334 6.527 10.648 1.00 17.47 C ANISOU 650 CA ARG A 62 2222 1954 2461 584 -488 509 C ATOM 651 C ARG A 62 -3.744 5.153 10.431 1.00 15.13 C ANISOU 651 C ARG A 62 1906 1517 2325 330 -286 422 C ATOM 652 O ARG A 62 -2.578 5.041 10.110 1.00 16.11 O ANISOU 652 O ARG A 62 1965 1595 2560 123 -146 250 O ATOM 653 CB ARG A 62 -4.563 7.223 9.344 1.00 21.79 C ANISOU 653 CB ARG A 62 2798 2595 2885 863 -538 635 C ATOM 654 CG ARG A 62 -5.241 8.614 9.525 1.00 25.38 C ANISOU 654 CG ARG A 62 3307 3047 3291 991 -572 960 C ATOM 655 CD ARG A 62 -5.599 9.264 8.202 0.00 29.65 C ANISOU 655 CD ARG A 62 3766 3689 3812 787 -573 826 C ATOM 656 NE ARG A 62 -6.160 10.597 8.407 0.00 32.49 N ANISOU 656 NE ARG A 62 4113 4089 4142 605 -552 703 N ATOM 657 CZ ARG A 62 -6.762 11.315 7.463 0.00 34.91 C ANISOU 657 CZ ARG A 62 4423 4423 4418 455 -553 597 C ATOM 658 NH1 ARG A 62 -6.892 10.832 6.235 0.00 37.00 N ANISOU 658 NH1 ARG A 62 4669 4652 4737 403 -587 560 N ATOM 659 NH2 ARG A 62 -7.239 12.518 7.752 0.00 36.97 N ANISOU 659 NH2 ARG A 62 4666 4649 4733 403 -586 560 N ATOM 660 H ARG A 62 -2.615 7.208 11.255 1.00 20.44 H ATOM 661 HA ARG A 62 -5.198 6.424 11.099 1.00 20.98 H ATOM 662 HB2 ARG A 62 -3.710 7.359 8.903 1.00 26.16 H ATOM 663 HB3 ARG A 62 -5.141 6.676 8.789 1.00 26.16 H ATOM 664 HG2 ARG A 62 -6.058 8.504 10.036 1.00 30.48 H ATOM 665 HG3 ARG A 62 -4.632 9.205 9.995 1.00 30.48 H ATOM 666 HD2 ARG A 62 -4.800 9.349 7.659 0.00 35.60 H ATOM 667 HD3 ARG A 62 -6.260 8.721 7.746 0.00 35.60 H ATOM 668 HE ARG A 62 -6.089 10.986 9.292 0.00 39.00 H ATOM 669 HH11 ARG A 62 -6.584 10.052 6.044 0.00 44.42 H ATOM 670 HH12 ARG A 62 -7.283 11.300 5.628 0.00 44.42 H ATOM 671 HH21 ARG A 62 -7.157 12.833 8.548 0.00 44.38 H ATOM 672 HH22 ARG A 62 -7.630 12.983 7.143 0.00 44.38 H ATOM 673 N ILE A 63 -4.552 4.117 10.585 1.00 13.46 N ANISOU 673 N ILE A 63 1724 1316 2073 363 -192 283 N ATOM 674 CA ILE A 63 -4.100 2.711 10.418 1.00 12.48 C ANISOU 674 CA ILE A 63 1559 1318 1865 165 -158 247 C ATOM 675 C ILE A 63 -5.189 1.972 9.743 1.00 12.15 C ANISOU 675 C ILE A 63 1412 1453 1751 140 -60 269 C ATOM 676 O ILE A 63 -6.343 2.093 10.137 1.00 13.56 O ANISOU 676 O ILE A 63 1470 1745 1935 160 -42 -12 O ATOM 677 CB ILE A 63 -3.740 2.106 11.742 1.00 12.12 C ANISOU 677 CB ILE A 63 1487 1355 1766 95 -271 172 C ATOM 678 CG1 ILE A 63 -2.576 2.817 12.449 1.00 13.66 C ANISOU 678 CG1 ILE A 63 1768 1528 1896 194 -322 118 C ATOM 679 CG2 ILE A 63 -3.442 0.621 11.610 1.00 12.33 C ANISOU 679 CG2 ILE A 63 1561 1392 1732 -91 -285 270 C ATOM 680 CD1 ILE A 63 -2.237 2.326 13.814 1.00 14.54 C ANISOU 680 CD1 ILE A 63 1861 1685 1978 162 -305 48 C ATOM 681 H ILE A 63 -5.384 4.187 10.789 1.00 16.16 H ATOM 682 HA ILE A 63 -3.308 2.690 9.842 1.00 14.99 H ATOM 683 HB ILE A 63 -4.517 2.192 12.316 1.00 14.56 H ATOM 684 HG12 ILE A 63 -1.782 2.719 11.901 1.00 16.41 H ATOM 685 HG13 ILE A 63 -2.798 3.758 12.528 1.00 16.41 H ATOM 686 HG21 ILE A 63 -3.216 0.270 12.474 1.00 14.81 H ATOM 687 HG22 ILE A 63 -4.222 0.176 11.268 1.00 14.81 H ATOM 688 HG23 ILE A 63 -2.706 0.503 11.005 1.00 14.81 H ATOM 689 HD11 ILE A 63 -1.501 2.839 14.156 1.00 17.46 H ATOM 690 HD12 ILE A 63 -3.002 2.431 14.383 1.00 17.46 H ATOM 691 HD13 ILE A 63 -1.993 1.399 13.760 1.00 17.46 H ATOM 692 N GLN A 64 -4.846 1.127 8.746 1.00 12.38 N ANISOU 692 N GLN A 64 1488 1417 1798 -15 18 316 N ATOM 693 CA GLN A 64 -5.780 0.131 8.225 1.00 12.67 C ANISOU 693 CA GLN A 64 1524 1559 1732 119 -123 278 C ATOM 694 C GLN A 64 -5.428 -1.206 8.833 1.00 11.55 C ANISOU 694 C GLN A 64 1273 1480 1635 179 -179 217 C ATOM 695 O GLN A 64 -4.297 -1.688 8.732 1.00 13.10 O ANISOU 695 O GLN A 64 1336 1653 1988 164 91 292 O ATOM 696 CB GLN A 64 -5.713 0.082 6.718 1.00 14.24 C ANISOU 696 CB GLN A 64 1843 1651 1919 60 -138 271 C ATOM 697 CG GLN A 64 -6.757 -0.878 6.153 1.00 16.51 C ANISOU 697 CG GLN A 64 2210 1948 2113 241 -261 210 C ATOM 698 CD GLN A 64 -6.752 -0.933 4.656 1.00 19.00 C ANISOU 698 CD GLN A 64 2769 2172 2279 596 -286 356 C ATOM 699 OE1 GLN A 64 -5.876 -1.519 4.078 1.00 20.56 O ANISOU 699 OE1 GLN A 64 3423 2277 2111 883 129 463 O ATOM 700 NE2 GLN A 64 -7.643 -0.196 4.052 1.00 22.52 N ANISOU 700 NE2 GLN A 64 2960 2848 2750 677 -493 535 N ATOM 701 H GLN A 64 -4.077 1.118 8.362 1.00 14.87 H ATOM 702 HA GLN A 64 -6.694 0.366 8.491 1.00 15.22 H ATOM 703 HB2 GLN A 64 -5.886 0.967 6.359 1.00 17.11 H ATOM 704 HB3 GLN A 64 -4.835 -0.226 6.445 1.00 17.11 H ATOM 705 HG2 GLN A 64 -6.577 -1.771 6.487 1.00 19.82 H ATOM 706 HG3 GLN A 64 -7.638 -0.589 6.439 1.00 19.82 H ATOM 707 HE21 GLN A 64 -7.685 -0.190 3.193 1.00 27.04 H ATOM 708 HE22 GLN A 64 -8.189 0.282 4.513 1.00 27.04 H ATOM 709 N VAL A 65 -6.402 -1.840 9.444 1.00 11.30 N ANISOU 709 N VAL A 65 1280 1414 1600 282 -126 92 N ATOM 710 CA VAL A 65 -6.212 -3.168 10.026 1.00 10.44 C ANISOU 710 CA VAL A 65 1248 1230 1489 225 -226 79 C ATOM 711 C VAL A 65 -6.609 -4.229 8.988 1.00 10.63 C ANISOU 711 C VAL A 65 1140 1378 1521 162 -335 46 C ATOM 712 O VAL A 65 -7.648 -4.148 8.364 1.00 11.98 O ANISOU 712 O VAL A 65 1357 1558 1637 151 -419 -12 O ATOM 713 CB VAL A 65 -7.067 -3.337 11.267 1.00 11.70 C ANISOU 713 CB VAL A 65 1501 1333 1610 45 -144 3 C ATOM 714 CG1 VAL A 65 -6.877 -4.718 11.823 1.00 13.67 C ANISOU 714 CG1 VAL A 65 1725 1734 1733 207 -209 144 C ATOM 715 CG2 VAL A 65 -6.714 -2.281 12.321 1.00 13.17 C ANISOU 715 CG2 VAL A 65 1671 1599 1734 12 -242 -147 C ATOM 716 H VAL A 65 -7.197 -1.527 9.542 1.00 13.58 H ATOM 717 HA VAL A 65 -5.271 -3.296 10.268 1.00 12.54 H ATOM 718 HB VAL A 65 -8.011 -3.228 11.027 1.00 14.05 H ATOM 719 HG11 VAL A 65 -7.422 -4.816 12.608 1.00 16.41 H ATOM 720 HG12 VAL A 65 -7.140 -5.360 11.160 1.00 16.41 H ATOM 721 HG13 VAL A 65 -5.952 -4.840 12.049 1.00 16.41 H ATOM 722 HG21 VAL A 65 -7.269 -2.413 13.093 1.00 15.82 H ATOM 723 HG22 VAL A 65 -5.790 -2.378 12.562 1.00 15.82 H ATOM 724 HG23 VAL A 65 -6.867 -1.408 11.952 1.00 15.82 H ATOM 725 N ARG A 66 -5.711 -5.185 8.781 1.00 10.64 N ANISOU 725 N ARG A 66 1290 1198 1554 -3 -272 -32 N ATOM 726 CA ARG A 66 -5.952 -6.244 7.808 1.00 10.36 C ANISOU 726 CA ARG A 66 1278 1223 1435 124 -285 85 C ATOM 727 C ARG A 66 -6.026 -7.549 8.520 1.00 10.74 C ANISOU 727 C ARG A 66 1338 1247 1494 156 -397 116 C ATOM 728 O ARG A 66 -5.082 -8.055 9.138 1.00 11.19 O ANISOU 728 O ARG A 66 1327 1291 1633 -7 -322 209 O ATOM 729 CB ARG A 66 -4.871 -6.215 6.741 1.00 11.36 C ANISOU 729 CB ARG A 66 1478 1338 1501 16 -322 114 C ATOM 730 CG ARG A 66 -4.895 -4.953 5.943 1.00 12.43 C ANISOU 730 CG ARG A 66 1688 1424 1611 99 -215 211 C ATOM 731 CD ARG A 66 -3.914 -4.968 4.777 1.00 13.30 C ANISOU 731 CD ARG A 66 1867 1502 1686 81 -139 149 C ATOM 732 NE ARG A 66 -4.126 -3.795 3.913 1.00 14.48 N ANISOU 732 NE ARG A 66 2060 1678 1764 305 46 353 N ATOM 733 CZ ARG A 66 -3.685 -3.658 2.689 1.00 16.26 C ANISOU 733 CZ ARG A 66 2373 1872 1931 435 236 500 C ATOM 734 NH1 ARG A 66 -2.914 -4.563 2.155 1.00 16.80 N ANISOU 734 NH1 ARG A 66 2318 2010 2055 436 194 740 N ATOM 735 NH2 ARG A 66 -4.039 -2.585 2.018 1.00 17.97 N ANISOU 735 NH2 ARG A 66 2620 2042 2166 651 380 406 N ATOM 736 H ARG A 66 -4.956 -5.244 9.190 1.00 12.78 H ATOM 737 HA ARG A 66 -6.815 -6.087 7.371 1.00 12.45 H ATOM 738 HB2 ARG A 66 -4.003 -6.285 7.168 1.00 13.65 H ATOM 739 HB3 ARG A 66 -5.005 -6.958 6.133 1.00 13.65 H ATOM 740 HG2 ARG A 66 -5.787 -4.825 5.583 1.00 14.93 H ATOM 741 HG3 ARG A 66 -4.662 -4.210 6.521 1.00 14.93 H ATOM 742 HD2 ARG A 66 -3.006 -4.940 5.118 1.00 15.98 H ATOM 743 HD3 ARG A 66 -4.053 -5.769 4.248 1.00 15.98 H ATOM 744 HE ARG A 66 -4.637 -3.059 4.284 1.00 17.39 H ATOM 745 HH11 ARG A 66 -2.711 -5.271 2.599 1.00 20.17 H ATOM 746 HH12 ARG A 66 -2.618 -4.457 1.355 1.00 20.17 H ATOM 747 HH21 ARG A 66 -4.532 -1.988 2.393 1.00 21.58 H ATOM 748 HH22 ARG A 66 -3.730 -2.451 1.227 1.00 21.58 H ATOM 749 N LEU A 67 -7.231 -8.120 8.507 1.00 10.75 N ANISOU 749 N LEU A 67 1305 1337 1443 -12 -293 -20 N ATOM 750 CA LEU A 67 -7.604 -9.369 9.186 1.00 10.81 C ANISOU 750 CA LEU A 67 1338 1326 1442 -151 -329 -67 C ATOM 751 C LEU A 67 -7.705 -10.507 8.170 1.00 10.68 C ANISOU 751 C LEU A 67 1315 1313 1429 -9 -350 60 C ATOM 752 O LEU A 67 -7.882 -10.259 6.975 1.00 12.18 O ANISOU 752 O LEU A 67 1661 1517 1452 148 -313 -7 O ATOM 753 CB LEU A 67 -8.947 -9.239 9.902 1.00 11.87 C ANISOU 753 CB LEU A 67 1477 1413 1622 -66 -271 -21 C ATOM 754 CG LEU A 67 -9.010 -8.036 10.844 1.00 12.82 C ANISOU 754 CG LEU A 67 1551 1527 1794 -61 -184 -50 C ATOM 755 CD1 LEU A 67 -9.680 -6.836 10.216 1.00 15.76 C ANISOU 755 CD1 LEU A 67 2009 1879 2101 83 -43 42 C ATOM 756 CD2 LEU A 67 -9.681 -8.390 12.172 1.00 17.18 C ANISOU 756 CD2 LEU A 67 2167 2134 2226 -149 40 -104 C ATOM 757 H LEU A 67 -7.895 -7.777 8.081 1.00 12.92 H ATOM 758 HA LEU A 67 -6.918 -9.601 9.847 1.00 12.98 H ATOM 759 HB2 LEU A 67 -9.648 -9.137 9.240 1.00 14.26 H ATOM 760 HB3 LEU A 67 -9.102 -10.039 10.429 1.00 14.26 H ATOM 761 HG LEU A 67 -8.100 -7.773 11.051 1.00 15.40 H ATOM 762 HD11 LEU A 67 -9.690 -6.116 10.852 1.00 18.93 H ATOM 763 HD12 LEU A 67 -9.187 -6.576 9.435 1.00 18.93 H ATOM 764 HD13 LEU A 67 -10.578 -7.071 9.974 1.00 18.93 H ATOM 765 HD21 LEU A 67 -9.700 -7.610 12.730 1.00 20.63 H ATOM 766 HD22 LEU A 67 -10.576 -8.691 11.998 1.00 20.63 H ATOM 767 HD23 LEU A 67 -9.178 -9.087 12.599 1.00 20.63 H ATOM 768 N GLY A 69 -7.532 -11.742 8.636 1.00 10.85 N ANISOU 768 N GLY A 69 1454 1228 1439 80 -263 5 N ATOM 769 CA GLY A 69 -7.712 -12.897 7.740 1.00 11.20 C ANISOU 769 CA GLY A 69 1439 1293 1521 0 -319 -180 C ATOM 770 C GLY A 69 -6.553 -13.068 6.763 1.00 12.06 C ANISOU 770 C GLY A 69 1528 1442 1613 -12 -323 -186 C ATOM 771 O GLY A 69 -6.737 -13.726 5.734 1.00 14.90 O ANISOU 771 O GLY A 69 1835 2010 1817 -139 -193 -608 O ATOM 772 H GLY A 69 -7.315 -11.941 9.444 1.00 13.03 H ATOM 773 HA2 GLY A 69 -7.789 -13.707 8.269 1.00 13.45 H ATOM 774 HA3 GLY A 69 -8.530 -12.785 7.230 1.00 13.45 H ATOM 775 N GLU A 70 -5.411 -12.481 7.029 1.00 11.74 N ANISOU 775 N GLU A 70 1457 1455 1548 14 -167 -201 N ATOM 776 CA GLU A 70 -4.275 -12.567 6.121 1.00 11.72 C ANISOU 776 CA GLU A 70 1449 1527 1476 88 -278 -101 C ATOM 777 C GLU A 70 -3.418 -13.776 6.350 1.00 12.07 C ANISOU 777 C GLU A 70 1571 1528 1485 143 -225 -74 C ATOM 778 O GLU A 70 -3.204 -14.225 7.492 1.00 12.90 O ANISOU 778 O GLU A 70 1618 1713 1572 167 -147 -4 O ATOM 779 CB GLU A 70 -3.356 -11.339 6.279 1.00 12.46 C ANISOU 779 CB GLU A 70 1558 1557 1621 56 -263 74 C ATOM 780 CG GLU A 70 -3.916 -10.075 5.699 1.00 13.04 C ANISOU 780 CG GLU A 70 1713 1561 1681 36 -271 119 C ATOM 781 CD GLU A 70 -3.755 -9.982 4.205 1.00 14.15 C ANISOU 781 CD GLU A 70 2069 1710 1597 -42 -329 85 C ATOM 782 OE1 GLU A 70 -3.572 -11.063 3.569 1.00 14.44 O ANISOU 782 OE1 GLU A 70 2234 1710 1543 88 -167 -60 O ATOM 783 OE2 GLU A 70 -3.861 -8.846 3.651 1.00 15.18 O ANISOU 783 OE2 GLU A 70 2180 1945 1641 -29 -205 202 O ATOM 784 H GLU A 70 -5.258 -12.018 7.737 1.00 14.10 H ATOM 785 HA GLU A 70 -4.600 -12.592 5.197 1.00 14.07 H ATOM 786 HB2 GLU A 70 -3.200 -11.186 7.224 1.00 14.97 H ATOM 787 HB3 GLU A 70 -2.514 -11.520 5.833 1.00 14.97 H ATOM 788 HG2 GLU A 70 -4.864 -10.031 5.899 1.00 15.66 H ATOM 789 HG3 GLU A 70 -3.459 -9.318 6.095 1.00 15.66 H ATOM 790 N HIS A 71 -2.837 -14.279 5.273 1.00 13.05 N ANISOU 790 N HIS A 71 1719 1617 1623 369 -305 -189 N ATOM 791 CA HIS A 71 -1.732 -15.205 5.337 1.00 13.39 C ANISOU 791 CA HIS A 71 1823 1612 1651 252 -337 -218 C ATOM 792 C HIS A 71 -0.573 -14.669 4.543 1.00 13.85 C ANISOU 792 C HIS A 71 1969 1662 1632 333 -114 -229 C ATOM 793 O HIS A 71 0.446 -14.299 5.091 1.00 14.05 O ANISOU 793 O HIS A 71 1955 1831 1554 255 -47 -234 O ATOM 794 CB HIS A 71 -2.121 -16.617 4.923 1.00 14.74 C ANISOU 794 CB HIS A 71 1971 1744 1887 179 -282 -242 C ATOM 795 CG HIS A 71 -0.996 -17.551 5.109 1.00 15.38 C ANISOU 795 CG HIS A 71 2080 1733 2032 325 -152 -377 C ATOM 796 ND1 HIS A 71 -0.268 -18.202 4.146 1.00 17.98 N ANISOU 796 ND1 HIS A 71 2478 2132 2222 489 -153 -465 N ATOM 797 CD2 HIS A 71 -0.412 -17.844 6.274 1.00 14.05 C ANISOU 797 CD2 HIS A 71 1967 1585 1787 366 -301 -323 C ATOM 798 CE1 HIS A 71 0.715 -18.875 4.758 1.00 16.65 C ANISOU 798 CE1 HIS A 71 2258 1917 2152 797 -159 -590 C ATOM 799 NE2 HIS A 71 0.602 -18.689 6.060 1.00 17.39 N ANISOU 799 NE2 HIS A 71 2411 1929 2267 446 -111 -258 N ATOM 800 H HIS A 71 -3.077 -14.089 4.469 1.00 15.67 H ATOM 801 HA HIS A 71 -1.438 -15.255 6.271 1.00 16.08 H ATOM 802 HB2 HIS A 71 -2.863 -16.920 5.470 1.00 17.71 H ATOM 803 HB3 HIS A 71 -2.369 -16.620 3.985 1.00 17.71 H ATOM 804 HD2 HIS A 71 -0.694 -17.543 7.108 1.00 16.88 H ATOM 805 HE1 HIS A 71 1.330 -19.434 4.341 1.00 20.00 H ATOM 806 N ASN A 72 -0.780 -14.550 3.226 1.00 14.55 N ANISOU 806 N ASN A 72 1924 1863 1740 198 -172 -52 N ATOM 807 CA ASN A 72 0.178 -13.903 2.374 1.00 14.70 C ANISOU 807 CA ASN A 72 1961 1873 1751 243 -93 -221 C ATOM 808 C ASN A 72 -0.252 -12.459 2.197 1.00 14.43 C ANISOU 808 C ASN A 72 1985 1884 1614 319 -223 65 C ATOM 809 O ASN A 72 -1.336 -12.179 1.617 1.00 15.30 O ANISOU 809 O ASN A 72 2245 2017 1553 334 -324 106 O ATOM 810 CB ASN A 72 0.156 -14.601 1.007 1.00 16.18 C ANISOU 810 CB ASN A 72 2163 1978 2005 365 -101 -394 C ATOM 811 CG ASN A 72 1.214 -14.059 0.081 1.00 17.76 C ANISOU 811 CG ASN A 72 2508 2166 2074 319 51 -382 C ATOM 812 OD1 ASN A 72 1.434 -12.845 0.031 1.00 17.75 O ANISOU 812 OD1 ASN A 72 2635 2149 1960 395 152 -53 O ATOM 813 ND2 ASN A 72 1.769 -14.949 -0.723 1.00 20.54 N ANISOU 813 ND2 ASN A 72 2628 2649 2528 482 165 -385 N ATOM 814 H ASN A 72 -1.476 -14.843 2.815 1.00 17.47 H ATOM 815 HA ASN A 72 1.079 -13.943 2.759 1.00 17.65 H ATOM 816 HB2 ASN A 72 0.318 -15.549 1.131 1.00 19.42 H ATOM 817 HB3 ASN A 72 -0.710 -14.461 0.593 1.00 19.42 H ATOM 818 HD21 ASN A 72 2.465 -14.672 -1.355 1.00 24.67 H ATOM 819 HD22 ASN A 72 1.484 -15.886 -0.688 1.00 24.67 H ATOM 820 N ILE A 73 0.499 -11.495 2.784 1.00 14.51 N ANISOU 820 N ILE A 73 1926 1824 1762 330 -237 86 N ATOM 821 CA ILE A 73 0.063 -10.106 2.773 1.00 15.76 C ANISOU 821 CA ILE A 73 2107 1894 1985 253 -196 141 C ATOM 822 C ILE A 73 0.225 -9.419 1.440 1.00 16.42 C ANISOU 822 C ILE A 73 2308 1991 1939 404 6 84 C ATOM 823 O ILE A 73 -0.238 -8.288 1.283 1.00 16.42 O ANISOU 823 O ILE A 73 2530 1925 1782 175 143 105 O ATOM 824 CB ILE A 73 0.772 -9.264 3.885 1.00 16.00 C ANISOU 824 CB ILE A 73 2096 1951 2034 209 -156 147 C ATOM 825 CG1 ILE A 73 2.280 -9.438 3.808 1.00 16.86 C ANISOU 825 CG1 ILE A 73 2241 2032 2132 212 -318 9 C ATOM 826 CG2 ILE A 73 0.182 -9.654 5.235 1.00 17.88 C ANISOU 826 CG2 ILE A 73 2266 2270 2258 315 -66 166 C ATOM 827 CD1 ILE A 73 3.057 -8.423 4.722 1.00 18.82 C ANISOU 827 CD1 ILE A 73 2425 2299 2429 250 -382 -33 C ATOM 828 H ILE A 73 1.248 -11.631 3.183 1.00 17.42 H ATOM 829 HA ILE A 73 -0.895 -10.095 2.980 1.00 18.92 H ATOM 830 HB ILE A 73 0.570 -8.328 3.728 1.00 19.22 H ATOM 831 HG12 ILE A 73 2.510 -10.336 4.095 1.00 20.25 H ATOM 832 HG13 ILE A 73 2.568 -9.299 2.892 1.00 20.25 H ATOM 833 HG21 ILE A 73 0.612 -9.142 5.923 1.00 21.47 H ATOM 834 HG22 ILE A 73 -0.760 -9.470 5.229 1.00 21.47 H ATOM 835 HG23 ILE A 73 0.332 -10.591 5.382 1.00 21.47 H ATOM 836 HD11 ILE A 73 4.000 -8.580 4.632 1.00 22.60 H ATOM 837 HD12 ILE A 73 2.846 -7.529 4.444 1.00 22.60 H ATOM 838 HD13 ILE A 73 2.788 -8.555 5.634 1.00 22.60 H ATOM 839 N LYS A 74 0.846 -10.089 0.465 1.00 17.49 N ANISOU 839 N LYS A 74 2467 2077 2100 403 84 282 N ATOM 840 CA LYS A 74 1.044 -9.475 -0.894 1.00 22.38 C ANISOU 840 CA LYS A 74 2962 2800 2743 328 35 403 C ATOM 841 C LYS A 74 0.020 -9.948 -1.898 1.00 21.28 C ANISOU 841 C LYS A 74 2993 2737 2355 325 -76 336 C ATOM 842 O LYS A 74 0.053 -9.433 -3.031 1.00 24.09 O ANISOU 842 O LYS A 74 3553 3261 2339 92 -26 730 O ATOM 843 CB LYS A 74 2.434 -9.880 -1.417 1.00 30.52 C ANISOU 843 CB LYS A 74 3875 3828 3892 232 4 421 C ATOM 844 CG LYS A 74 3.592 -9.359 -0.576 1.00 39.89 C ANISOU 844 CG LYS A 74 5017 5018 5123 140 -21 353 C ATOM 845 CD LYS A 74 3.339 -7.908 -0.170 1.00 48.58 C ANISOU 845 CD LYS A 74 6097 6101 6258 26 -64 320 C ATOM 846 CE LYS A 74 4.509 -7.302 0.665 1.00 55.73 C ANISOU 846 CE LYS A 74 7000 6993 7180 -23 -97 284 C ATOM 847 NZ LYS A 74 5.679 -7.011 -0.249 1.00 62.08 N ANISOU 847 NZ LYS A 74 7799 7773 8014 -49 -128 261 N ATOM 848 H LYS A 74 1.161 -10.885 0.544 1.00 21.00 H ATOM 849 HA LYS A 74 1.000 -8.498 -0.830 1.00 26.88 H ATOM 850 HB2 LYS A 74 2.492 -10.848 -1.430 1.00 36.63 H ATOM 851 HB3 LYS A 74 2.542 -9.532 -2.316 1.00 36.63 H ATOM 852 HG2 LYS A 74 3.675 -9.894 0.228 1.00 47.89 H ATOM 853 HG3 LYS A 74 4.411 -9.395 -1.095 1.00 47.89 H ATOM 854 HD2 LYS A 74 3.231 -7.370 -0.970 1.00 58.30 H ATOM 855 HD3 LYS A 74 2.533 -7.867 0.368 1.00 58.30 H ATOM 856 HE2 LYS A 74 4.221 -6.471 1.076 1.00 66.89 H ATOM 857 HE3 LYS A 74 4.793 -7.938 1.340 1.00 66.89 H ATOM 858 HZ1 LYS A 74 6.405 -6.637 0.256 1.00 74.50 H ATOM 859 HZ2 LYS A 74 5.976 -7.821 -0.670 1.00 74.50 H ATOM 860 HZ3 LYS A 74 5.417 -6.385 -0.929 1.00 74.50 H ATOM 861 N VAL A 75 -0.754 -10.995 -1.648 1.00 19.16 N ANISOU 861 N VAL A 75 2558 2442 2282 362 -212 -89 N ATOM 862 CA VAL A 75 -1.692 -11.610 -2.607 1.00 21.57 C ANISOU 862 CA VAL A 75 2788 2691 2718 319 -499 -340 C ATOM 863 C VAL A 75 -3.086 -11.680 -2.007 1.00 19.21 C ANISOU 863 C VAL A 75 2642 2370 2287 394 -618 -57 C ATOM 864 O VAL A 75 -3.213 -12.112 -0.833 1.00 17.67 O ANISOU 864 O VAL A 75 2664 2183 1867 433 -294 -80 O ATOM 865 CB VAL A 75 -1.255 -13.077 -2.936 1.00 27.13 C ANISOU 865 CB VAL A 75 3436 3378 3494 263 -669 -947 C ATOM 866 CG1 VAL A 75 -2.276 -13.731 -3.876 1.00 31.45 C ANISOU 866 CG1 VAL A 75 3968 3917 4065 345 -619 -1067 C ATOM 867 CG2 VAL A 75 0.169 -13.099 -3.510 1.00 31.02 C ANISOU 867 CG2 VAL A 75 3919 3840 4025 209 -721 -1048 C ATOM 868 H VAL A 75 -0.759 -11.396 -0.887 1.00 23.01 H ATOM 869 HA VAL A 75 -1.722 -11.087 -3.436 1.00 25.90 H ATOM 870 HB VAL A 75 -1.246 -13.594 -2.103 1.00 32.57 H ATOM 871 HG11 VAL A 75 -1.995 -14.628 -4.067 1.00 37.75 H ATOM 872 HG12 VAL A 75 -3.134 -13.741 -3.445 1.00 37.75 H ATOM 873 HG13 VAL A 75 -2.324 -13.221 -4.688 1.00 37.75 H ATOM 874 HG21 VAL A 75 0.413 -14.007 -3.703 1.00 37.23 H ATOM 875 HG22 VAL A 75 0.188 -12.576 -4.315 1.00 37.23 H ATOM 876 HG23 VAL A 75 0.772 -12.727 -2.863 1.00 37.23 H ATOM 877 N LEU A 76 -4.126 -11.302 -2.722 1.00 20.70 N ANISOU 877 N LEU A 76 2746 2662 2457 200 -897 66 N ATOM 878 CA LEU A 76 -5.474 -11.492 -2.275 1.00 23.13 C ANISOU 878 CA LEU A 76 3045 3013 2731 134 -1226 140 C ATOM 879 C LEU A 76 -5.806 -12.971 -2.337 1.00 22.83 C ANISOU 879 C LEU A 76 3213 2992 2468 -231 -1003 -381 C ATOM 880 O LEU A 76 -5.688 -13.628 -3.401 1.00 24.79 O ANISOU 880 O LEU A 76 3739 3243 2435 -580 -714 -709 O ATOM 881 CB LEU A 76 -6.475 -10.621 -3.128 1.00 28.28 C ANISOU 881 CB LEU A 76 3609 3567 3569 409 -1312 449 C ATOM 882 CG LEU A 76 -6.315 -9.069 -2.830 1.00 32.34 C ANISOU 882 CG LEU A 76 4083 4088 4117 540 -1365 408 C ATOM 883 CD1 LEU A 76 -7.334 -8.186 -3.672 1.00 34.53 C ANISOU 883 CD1 LEU A 76 4338 4323 4459 549 -1328 396 C ATOM 884 CD2 LEU A 76 -6.450 -8.637 -1.328 1.00 36.43 C ANISOU 884 CD2 LEU A 76 4586 4557 4698 494 -1360 306 C ATOM 885 H LEU A 76 -4.068 -10.923 -3.492 1.00 24.85 H ATOM 886 HA LEU A 76 -5.544 -11.206 -1.341 1.00 27.77 H ATOM 887 HB2 LEU A 76 -6.302 -10.768 -4.071 1.00 33.95 H ATOM 888 HB3 LEU A 76 -7.385 -10.877 -2.911 1.00 33.95 H ATOM 889 HG LEU A 76 -5.424 -8.809 -3.113 1.00 38.83 H ATOM 890 HD11 LEU A 76 -7.197 -7.261 -3.457 1.00 41.45 H ATOM 891 HD12 LEU A 76 -7.176 -8.333 -4.608 1.00 41.45 H ATOM 892 HD13 LEU A 76 -8.231 -8.446 -3.447 1.00 41.45 H ATOM 893 HD21 LEU A 76 -6.337 -7.686 -1.266 1.00 43.73 H ATOM 894 HD22 LEU A 76 -7.321 -8.885 -1.010 1.00 43.73 H ATOM 895 HD23 LEU A 76 -5.774 -9.083 -0.813 1.00 43.73 H ATOM 896 N GLU A 77 -6.223 -13.539 -1.195 1.00 20.74 N ANISOU 896 N GLU A 77 2817 2584 2479 -260 -1001 -360 N ATOM 897 CA GLU A 77 -6.514 -14.942 -1.042 1.00 21.39 C ANISOU 897 CA GLU A 77 2830 2677 2620 -306 -997 -476 C ATOM 898 C GLU A 77 -7.974 -15.204 -0.812 1.00 21.22 C ANISOU 898 C GLU A 77 2931 2548 2585 -395 -849 -643 C ATOM 899 O GLU A 77 -8.449 -16.337 -0.988 1.00 23.33 O ANISOU 899 O GLU A 77 3329 2682 2852 -290 -543 -636 O ATOM 900 CB GLU A 77 -5.727 -15.485 0.159 1.00 22.65 C ANISOU 900 CB GLU A 77 2930 2782 2894 -260 -1098 -236 C ATOM 901 CG GLU A 77 -4.242 -15.281 0.054 1.00 23.37 C ANISOU 901 CG GLU A 77 3119 2830 2932 -220 -1075 -169 C ATOM 902 CD GLU A 77 -3.591 -15.122 1.470 1.00 21.86 C ANISOU 902 CD GLU A 77 3425 2289 2593 -211 -916 -197 C ATOM 903 OE1 GLU A 77 -3.825 -14.060 2.248 1.00 20.03 O ANISOU 903 OE1 GLU A 77 3437 1707 2464 -192 -864 104 O ATOM 904 OE2 GLU A 77 -2.753 -16.020 1.688 1.00 22.12 O ANISOU 904 OE2 GLU A 77 3596 2247 2561 25 -822 -331 O ATOM 905 H GLU A 77 -6.345 -13.095 -0.469 1.00 24.90 H ATOM 906 HA GLU A 77 -6.232 -15.426 -1.846 1.00 25.68 H ATOM 907 HB2 GLU A 77 -6.032 -15.034 0.962 1.00 27.19 H ATOM 908 HB3 GLU A 77 -5.891 -16.438 0.235 1.00 27.19 H ATOM 909 HG2 GLU A 77 -3.842 -16.050 -0.382 1.00 28.06 H ATOM 910 HG3 GLU A 77 -4.064 -14.475 -0.456 1.00 28.06 H ATOM 911 N GLY A 78 -8.740 -14.160 -0.535 1.00 21.12 N ANISOU 911 N GLY A 78 2806 2644 2576 -255 -723 -499 N ATOM 912 CA GLY A 78 -10.161 -14.284 -0.413 1.00 21.62 C ANISOU 912 CA GLY A 78 2765 2725 2726 -235 -687 -481 C ATOM 913 C GLY A 78 -10.695 -14.393 1.001 1.00 20.64 C ANISOU 913 C GLY A 78 2539 2740 2564 -223 -586 -421 C ATOM 914 O GLY A 78 -11.892 -14.452 1.156 1.00 22.72 O ANISOU 914 O GLY A 78 2780 3251 2601 -283 -390 -318 O ATOM 915 H GLY A 78 -8.446 -13.362 -0.413 1.00 25.36 H ATOM 916 HA2 GLY A 78 -10.577 -13.511 -0.827 1.00 25.96 H ATOM 917 HA3 GLY A 78 -10.448 -15.072 -0.899 1.00 25.96 H ATOM 918 N ASN A 79 -9.844 -14.354 2.008 1.00 19.34 N ANISOU 918 N ASN A 79 2464 2378 2508 -452 -532 -605 N ATOM 919 CA ASN A 79 -10.282 -14.385 3.414 1.00 19.88 C ANISOU 919 CA ASN A 79 2535 2427 2593 -263 -484 -523 C ATOM 920 C ASN A 79 -10.064 -13.092 4.151 1.00 17.93 C ANISOU 920 C ASN A 79 2310 2315 2189 -164 -503 -551 C ATOM 921 O ASN A 79 -10.374 -12.993 5.319 1.00 18.35 O ANISOU 921 O ASN A 79 2359 2504 2110 -96 -355 -304 O ATOM 922 CB ASN A 79 -9.530 -15.519 4.156 1.00 24.81 C ANISOU 922 CB ASN A 79 3209 3004 3215 -263 -301 -519 C ATOM 923 CG ASN A 79 -9.895 -16.880 3.543 1.00 27.92 C ANISOU 923 CG ASN A 79 3751 3268 3588 -210 -133 -404 C ATOM 924 OD1 ASN A 79 -11.073 -17.187 3.411 1.00 28.54 O ANISOU 924 OD1 ASN A 79 4121 3135 3589 -425 -87 -386 O ATOM 925 ND2 ASN A 79 -8.927 -17.594 3.126 1.00 32.01 N ANISOU 925 ND2 ASN A 79 4184 3849 4131 132 28 -375 N ATOM 926 H ASN A 79 -8.991 -14.309 1.913 1.00 23.23 H ATOM 927 HA ASN A 79 -11.240 -14.589 3.443 1.00 23.87 H ATOM 928 HB2 ASN A 79 -8.574 -15.387 4.067 1.00 29.79 H ATOM 929 HB3 ASN A 79 -9.789 -15.522 5.091 1.00 29.79 H ATOM 930 HD21 ASN A 79 -9.101 -18.471 2.726 1.00 38.43 H ATOM 931 HD22 ASN A 79 -8.007 -17.266 3.205 1.00 38.43 H ATOM 932 N GLU A 80 -9.500 -12.106 3.475 1.00 16.60 N ANISOU 932 N GLU A 80 2195 2094 2018 -24 -482 -494 N ATOM 933 CA GLU A 80 -9.108 -10.859 4.102 1.00 16.04 C ANISOU 933 CA GLU A 80 2036 2017 2041 48 -633 -446 C ATOM 934 C GLU A 80 -10.313 -9.958 4.409 1.00 15.71 C ANISOU 934 C GLU A 80 2025 1954 1990 72 -677 -303 C ATOM 935 O GLU A 80 -11.319 -9.946 3.706 1.00 17.31 O ANISOU 935 O GLU A 80 2272 2310 1994 102 -708 -457 O ATOM 936 CB GLU A 80 -8.210 -10.054 3.208 1.00 17.11 C ANISOU 936 CB GLU A 80 2186 2111 2204 -11 -504 -478 C ATOM 937 CG GLU A 80 -6.884 -10.758 2.819 1.00 17.59 C ANISOU 937 CG GLU A 80 2246 2217 2221 -182 -407 -425 C ATOM 938 CD GLU A 80 -6.973 -11.578 1.555 1.00 16.86 C ANISOU 938 CD GLU A 80 2250 2245 1912 -207 -439 -299 C ATOM 939 OE1 GLU A 80 -8.094 -11.870 1.061 1.00 17.34 O ANISOU 939 OE1 GLU A 80 2414 2390 1784 -347 -507 -391 O ATOM 940 OE2 GLU A 80 -5.858 -11.927 1.079 1.00 15.83 O ANISOU 940 OE2 GLU A 80 2141 2110 1764 75 -508 -238 O ATOM 941 H GLU A 80 -9.331 -12.137 2.632 1.00 19.93 H ATOM 942 HA GLU A 80 -8.633 -11.045 4.939 1.00 19.26 H ATOM 943 HB2 GLU A 80 -8.688 -9.855 2.388 1.00 20.55 H ATOM 944 HB3 GLU A 80 -7.981 -9.228 3.662 1.00 20.55 H ATOM 945 HG2 GLU A 80 -6.199 -10.084 2.687 1.00 21.13 H ATOM 946 HG3 GLU A 80 -6.623 -11.353 3.540 1.00 21.13 H ATOM 947 N GLN A 81 -10.138 -9.163 5.457 1.00 14.90 N ANISOU 947 N GLN A 81 1892 1887 1884 96 -758 -123 N ATOM 948 CA GLN A 81 -11.040 -8.070 5.737 1.00 14.49 C ANISOU 948 CA GLN A 81 1822 1746 1937 99 -755 -110 C ATOM 949 C GLN A 81 -10.144 -6.886 6.053 1.00 13.45 C ANISOU 949 C GLN A 81 1744 1615 1753 117 -698 -124 C ATOM 950 O GLN A 81 -9.299 -6.964 6.929 1.00 14.61 O ANISOU 950 O GLN A 81 1886 1718 1947 76 -821 -134 O ATOM 951 CB GLN A 81 -11.933 -8.368 6.948 1.00 16.45 C ANISOU 951 CB GLN A 81 2038 2006 2207 -66 -767 -84 C ATOM 952 CG GLN A 81 -12.892 -9.492 6.768 1.00 19.12 C ANISOU 952 CG GLN A 81 2439 2358 2466 -355 -618 -237 C ATOM 953 CD GLN A 81 -13.651 -9.813 8.056 1.00 19.20 C ANISOU 953 CD GLN A 81 2479 2318 2499 -315 -465 -180 C ATOM 954 OE1 GLN A 81 -14.164 -8.907 8.735 1.00 19.58 O ANISOU 954 OE1 GLN A 81 2560 2390 2489 -229 -366 -306 O ATOM 955 NE2 GLN A 81 -13.679 -11.090 8.434 1.00 20.79 N ANISOU 955 NE2 GLN A 81 2693 2507 2701 -305 -355 -51 N ATOM 956 H GLN A 81 -9.496 -9.241 6.024 1.00 17.90 H ATOM 957 HA GLN A 81 -11.596 -7.868 4.956 1.00 17.40 H ATOM 958 HB2 GLN A 81 -11.365 -8.588 7.703 1.00 19.76 H ATOM 959 HB3 GLN A 81 -12.450 -7.573 7.153 1.00 19.76 H ATOM 960 HG2 GLN A 81 -13.541 -9.250 6.088 1.00 22.95 H ATOM 961 HG3 GLN A 81 -12.405 -10.286 6.498 1.00 22.95 H ATOM 962 HE21 GLN A 81 -14.094 -11.317 9.152 1.00 24.97 H ATOM 963 HE22 GLN A 81 -13.282 -11.687 7.960 1.00 24.97 H ATOM 964 N PHE A 82 -10.373 -5.787 5.377 1.00 13.49 N ANISOU 964 N PHE A 82 1769 1581 1775 138 -361 37 N ATOM 965 CA PHE A 82 -9.578 -4.571 5.549 1.00 13.47 C ANISOU 965 CA PHE A 82 1774 1644 1700 273 -341 68 C ATOM 966 C PHE A 82 -10.510 -3.545 6.195 1.00 13.26 C ANISOU 966 C PHE A 82 1677 1759 1603 326 -393 89 C ATOM 967 O PHE A 82 -11.533 -3.175 5.623 1.00 14.43 O ANISOU 967 O PHE A 82 1854 1938 1690 570 -399 93 O ATOM 968 CB PHE A 82 -9.067 -4.021 4.222 1.00 14.22 C ANISOU 968 CB PHE A 82 1858 1744 1801 220 -396 251 C ATOM 969 CG PHE A 82 -8.044 -4.870 3.490 1.00 14.88 C ANISOU 969 CG PHE A 82 2059 1744 1850 193 -403 210 C ATOM 970 CD1 PHE A 82 -7.576 -4.434 2.247 1.00 17.46 C ANISOU 970 CD1 PHE A 82 2377 2114 2145 393 -184 130 C ATOM 971 CD2 PHE A 82 -7.526 -6.040 3.995 1.00 15.70 C ANISOU 971 CD2 PHE A 82 2027 1846 2093 271 -397 -124 C ATOM 972 CE1 PHE A 82 -6.630 -5.168 1.530 1.00 19.07 C ANISOU 972 CE1 PHE A 82 2552 2393 2302 497 -93 36 C ATOM 973 CE2 PHE A 82 -6.576 -6.807 3.256 1.00 16.74 C ANISOU 973 CE2 PHE A 82 2118 2119 2124 242 -339 -121 C ATOM 974 CZ PHE A 82 -6.141 -6.348 2.004 1.00 18.38 C ANISOU 974 CZ PHE A 82 2418 2254 2312 300 -149 -97 C ATOM 975 H PHE A 82 -10.999 -5.707 4.792 1.00 16.20 H ATOM 976 HA PHE A 82 -8.819 -4.741 6.145 1.00 16.18 H ATOM 977 HB2 PHE A 82 -9.825 -3.908 3.628 1.00 17.08 H ATOM 978 HB3 PHE A 82 -8.658 -3.158 4.389 1.00 17.08 H ATOM 979 HD1 PHE A 82 -7.903 -3.640 1.889 1.00 20.97 H ATOM 980 HD2 PHE A 82 -7.827 -6.356 4.816 1.00 18.86 H ATOM 981 HE1 PHE A 82 -6.349 -4.859 0.699 1.00 22.90 H ATOM 982 HE2 PHE A 82 -6.242 -7.602 3.606 1.00 20.10 H ATOM 983 HZ PHE A 82 -5.506 -6.825 1.520 1.00 22.07 H ATOM 984 N ILE A 83 -10.158 -3.083 7.395 1.00 12.50 N ANISOU 984 N ILE A 83 1562 1636 1553 330 -329 80 N ATOM 985 CA ILE A 83 -11.049 -2.201 8.179 1.00 12.17 C ANISOU 985 CA ILE A 83 1439 1587 1597 214 -243 261 C ATOM 986 C ILE A 83 -10.186 -1.071 8.760 1.00 11.62 C ANISOU 986 C ILE A 83 1458 1379 1577 353 -194 265 C ATOM 987 O ILE A 83 -9.203 -1.341 9.438 1.00 11.79 O ANISOU 987 O ILE A 83 1387 1498 1595 215 -177 230 O ATOM 988 CB ILE A 83 -11.744 -2.971 9.305 1.00 13.02 C ANISOU 988 CB ILE A 83 1563 1661 1723 76 -215 27 C ATOM 989 CG1 ILE A 83 -12.515 -4.177 8.729 1.00 14.42 C ANISOU 989 CG1 ILE A 83 1780 1763 1935 -100 -276 3 C ATOM 990 CG2 ILE A 83 -12.660 -1.987 10.023 1.00 13.89 C ANISOU 990 CG2 ILE A 83 1668 1813 1797 113 -193 -28 C ATOM 991 CD1 ILE A 83 -13.134 -5.036 9.864 1.00 16.91 C ANISOU 991 CD1 ILE A 83 2165 2025 2233 -35 -142 51 C ATOM 992 H ILE A 83 -9.411 -3.261 7.782 1.00 15.02 H ATOM 993 HA ILE A 83 -11.731 -1.810 7.593 1.00 14.62 H ATOM 994 HB ILE A 83 -11.074 -3.293 9.929 1.00 15.64 H ATOM 995 HG12 ILE A 83 -13.233 -3.857 8.161 1.00 17.31 H ATOM 996 HG13 ILE A 83 -11.906 -4.735 8.221 1.00 17.31 H ATOM 997 HG21 ILE A 83 -13.111 -2.444 10.737 1.00 16.68 H ATOM 998 HG22 ILE A 83 -12.130 -1.268 10.376 1.00 16.68 H ATOM 999 HG23 ILE A 83 -13.302 -1.644 9.397 1.00 16.68 H ATOM 1000 HD11 ILE A 83 -13.606 -5.776 9.474 1.00 20.30 H ATOM 1001 HD12 ILE A 83 -12.430 -5.358 10.431 1.00 20.30 H ATOM 1002 HD13 ILE A 83 -13.741 -4.492 10.372 1.00 20.30 H ATOM 1003 N ASN A 84 -10.525 0.167 8.459 1.00 12.62 N ANISOU 1003 N ASN A 84 1534 1529 1731 256 -253 206 N ATOM 1004 CA ASN A 84 -9.757 1.288 8.982 1.00 12.84 C ANISOU 1004 CA ASN A 84 1567 1509 1803 172 -216 268 C ATOM 1005 C ASN A 84 -10.015 1.445 10.477 1.00 12.49 C ANISOU 1005 C ASN A 84 1473 1463 1811 -29 62 291 C ATOM 1006 O ASN A 84 -11.106 1.227 10.993 1.00 13.73 O ANISOU 1006 O ASN A 84 1545 1720 1953 -57 159 130 O ATOM 1007 CB ASN A 84 -10.153 2.568 8.263 1.00 16.28 C ANISOU 1007 CB ASN A 84 2109 1939 2136 202 -252 385 C ATOM 1008 CG ASN A 84 -9.690 2.569 6.827 1.00 18.77 C ANISOU 1008 CG ASN A 84 2564 2288 2281 469 -255 580 C ATOM 1009 OD1 ASN A 84 -8.733 1.874 6.473 1.00 19.44 O ANISOU 1009 OD1 ASN A 84 2822 2489 2077 306 -65 566 O ATOM 1010 ND2 ASN A 84 -10.322 3.382 6.002 1.00 23.51 N ANISOU 1010 ND2 ASN A 84 3027 2961 2944 499 -257 722 N ATOM 1011 H ASN A 84 -11.189 0.389 7.958 1.00 15.15 H ATOM 1012 HA ASN A 84 -8.800 1.129 8.842 1.00 15.42 H ATOM 1013 HB2 ASN A 84 -11.119 2.652 8.271 1.00 19.55 H ATOM 1014 HB3 ASN A 84 -9.746 3.325 8.713 1.00 19.55 H ATOM 1015 HD21 ASN A 84 -10.062 3.423 5.058 1.00 28.22 H ATOM 1016 HD22 ASN A 84 -11.052 3.946 6.333 1.00 28.22 H ATOM 1017 N ALA A 85 -8.982 1.884 11.177 1.00 12.88 N ANISOU 1017 N ALA A 85 1560 1575 1757 79 -44 157 N ATOM 1018 CA ALA A 85 -9.124 2.198 12.583 1.00 13.44 C ANISOU 1018 CA ALA A 85 1725 1561 1820 283 -137 220 C ATOM 1019 C ALA A 85 -9.970 3.493 12.778 1.00 14.18 C ANISOU 1019 C ALA A 85 1904 1557 1925 329 -30 425 C ATOM 1020 O ALA A 85 -9.836 4.465 12.020 1.00 16.49 O ANISOU 1020 O ALA A 85 2417 1743 2105 387 307 568 O ATOM 1021 CB ALA A 85 -7.744 2.449 13.177 1.00 15.41 C ANISOU 1021 CB ALA A 85 1909 1907 2041 279 -267 273 C ATOM 1022 H ALA A 85 -8.192 2.009 10.862 1.00 15.47 H ATOM 1023 HA ALA A 85 -9.552 1.455 13.057 1.00 16.14 H ATOM 1024 HB1 ALA A 85 -7.840 2.657 14.109 1.00 18.51 H ATOM 1025 HB2 ALA A 85 -7.210 1.659 13.071 1.00 18.51 H ATOM 1026 HB3 ALA A 85 -7.335 3.186 12.717 1.00 18.51 H ATOM 1027 N ALA A 86 -10.902 3.428 13.698 1.00 13.87 N ANISOU 1027 N ALA A 86 1762 1629 1878 335 -209 425 N ATOM 1028 CA ALA A 86 -11.698 4.588 14.102 1.00 14.39 C ANISOU 1028 CA ALA A 86 1812 1619 2038 423 -286 206 C ATOM 1029 C ALA A 86 -11.120 5.289 15.304 1.00 14.38 C ANISOU 1029 C ALA A 86 1902 1500 2062 378 -337 137 C ATOM 1030 O ALA A 86 -11.259 6.516 15.431 1.00 16.48 O ANISOU 1030 O ALA A 86 2375 1572 2314 480 -434 14 O ATOM 1031 CB ALA A 86 -13.123 4.208 14.421 1.00 17.69 C ANISOU 1031 CB ALA A 86 2190 2163 2368 471 -205 -29 C ATOM 1032 H ALA A 86 -11.107 2.708 14.121 1.00 16.66 H ATOM 1033 HA ALA A 86 -11.717 5.230 13.362 1.00 17.29 H ATOM 1034 HB1 ALA A 86 -13.606 4.997 14.680 1.00 21.24 H ATOM 1035 HB2 ALA A 86 -13.525 3.820 13.640 1.00 21.24 H ATOM 1036 HB3 ALA A 86 -13.124 3.572 15.140 1.00 21.24 H ATOM 1037 N LYS A 87 -10.460 4.572 16.199 1.00 13.75 N ANISOU 1037 N LYS A 87 1565 1679 1978 391 -372 107 N ATOM 1038 CA LYS A 87 -9.828 5.199 17.378 1.00 15.48 C ANISOU 1038 CA LYS A 87 1931 1876 2074 238 -367 52 C ATOM 1039 C LYS A 87 -8.551 4.440 17.648 1.00 12.62 C ANISOU 1039 C LYS A 87 1692 1391 1714 142 -410 262 C ATOM 1040 O LYS A 87 -8.503 3.221 17.463 1.00 12.86 O ANISOU 1040 O LYS A 87 1562 1366 1958 46 -231 215 O ATOM 1041 CB LYS A 87 -10.669 5.017 18.653 1.00 22.22 C ANISOU 1041 CB LYS A 87 2747 2800 2896 264 -456 -167 C ATOM 1042 CG LYS A 87 -12.005 5.636 18.629 1.00 30.25 C ANISOU 1042 CG LYS A 87 3772 3817 3905 368 -544 -80 C ATOM 1043 CD LYS A 87 -12.712 5.383 20.003 1.00 38.63 C ANISOU 1043 CD LYS A 87 4830 4853 4993 461 -571 -45 C ATOM 1044 CE LYS A 87 -14.235 5.781 20.011 1.00 48.03 C ANISOU 1044 CE LYS A 87 6040 6023 6187 440 -626 -18 C ATOM 1045 NZ LYS A 87 -14.507 7.032 19.250 1.00 55.95 N ANISOU 1045 NZ LYS A 87 7051 6989 7220 449 -674 -3 N ATOM 1046 H LYS A 87 -10.356 3.719 16.158 1.00 16.51 H ATOM 1047 HA LYS A 87 -9.637 6.148 17.223 1.00 18.59 H ATOM 1048 HB2 LYS A 87 -10.793 4.067 18.806 1.00 26.68 H ATOM 1049 HB3 LYS A 87 -10.184 5.404 19.398 1.00 26.68 H ATOM 1050 HG2 LYS A 87 -11.920 6.593 18.494 1.00 36.31 H ATOM 1051 HG3 LYS A 87 -12.539 5.236 17.925 1.00 36.31 H ATOM 1052 HD2 LYS A 87 -12.651 4.438 20.217 1.00 46.36 H ATOM 1053 HD3 LYS A 87 -12.264 5.905 20.687 1.00 46.36 H ATOM 1054 HE2 LYS A 87 -14.751 5.066 19.607 1.00 57.65 H ATOM 1055 HE3 LYS A 87 -14.521 5.920 20.928 1.00 57.65 H ATOM 1056 HZ1 LYS A 87 -15.445 7.238 19.281 1.00 67.16 H ATOM 1057 HZ2 LYS A 87 -14.015 7.762 19.633 1.00 67.16 H ATOM 1058 HZ3 LYS A 87 -14.242 6.923 18.334 1.00 67.16 H ATOM 1059 N ILE A 88 -7.500 5.136 18.080 1.00 12.16 N ANISOU 1059 N ILE A 88 1664 1281 1676 147 -336 263 N ATOM 1060 CA ILE A 88 -6.215 4.546 18.353 1.00 12.14 C ANISOU 1060 CA ILE A 88 1726 1193 1693 206 -383 209 C ATOM 1061 C ILE A 88 -5.757 5.141 19.659 1.00 12.65 C ANISOU 1061 C ILE A 88 1893 1118 1795 270 -400 138 C ATOM 1062 O ILE A 88 -5.488 6.360 19.739 1.00 14.90 O ANISOU 1062 O ILE A 88 2475 1229 1955 -13 -437 67 O ATOM 1063 CB ILE A 88 -5.224 4.842 17.178 1.00 13.60 C ANISOU 1063 CB ILE A 88 1734 1489 1945 237 -153 99 C ATOM 1064 CG1 ILE A 88 -5.810 4.433 15.827 1.00 15.00 C ANISOU 1064 CG1 ILE A 88 1950 1696 2055 174 30 153 C ATOM 1065 CG2 ILE A 88 -3.907 4.153 17.439 1.00 15.68 C ANISOU 1065 CG2 ILE A 88 1963 1839 2155 59 -144 -16 C ATOM 1066 CD1 ILE A 88 -5.075 4.944 14.623 1.00 17.45 C ANISOU 1066 CD1 ILE A 88 2160 2192 2277 178 11 -46 C ATOM 1067 H ILE A 88 -7.520 5.984 18.223 1.00 14.61 H ATOM 1068 HA ILE A 88 -6.306 3.576 18.458 1.00 14.58 H ATOM 1069 HB ILE A 88 -5.063 5.799 17.156 1.00 16.33 H ATOM 1070 HG12 ILE A 88 -5.813 3.464 15.776 1.00 18.02 H ATOM 1071 HG13 ILE A 88 -6.720 4.763 15.775 1.00 18.02 H ATOM 1072 HG21 ILE A 88 -3.307 4.341 16.714 1.00 18.83 H ATOM 1073 HG22 ILE A 88 -3.539 4.483 18.262 1.00 18.83 H ATOM 1074 HG23 ILE A 88 -4.057 3.207 17.504 1.00 18.83 H ATOM 1075 HD11 ILE A 88 -5.520 4.633 13.831 1.00 20.95 H ATOM 1076 HD12 ILE A 88 -5.074 5.904 14.643 1.00 20.95 H ATOM 1077 HD13 ILE A 88 -4.174 4.614 14.644 1.00 20.95 H ATOM 1078 N ILE A 89 -5.621 4.283 20.665 1.00 11.54 N ANISOU 1078 N ILE A 89 1626 1029 1731 257 -406 110 N ATOM 1079 CA ILE A 89 -5.473 4.731 22.047 1.00 11.32 C ANISOU 1079 CA ILE A 89 1593 1040 1669 226 -169 95 C ATOM 1080 C ILE A 89 -4.229 4.075 22.652 1.00 10.67 C ANISOU 1080 C ILE A 89 1480 963 1610 72 -274 -36 C ATOM 1081 O ILE A 89 -4.220 2.890 22.987 1.00 10.34 O ANISOU 1081 O ILE A 89 1402 944 1585 164 -130 2 O ATOM 1082 CB ILE A 89 -6.689 4.369 22.890 1.00 12.38 C ANISOU 1082 CB ILE A 89 1550 1286 1869 613 -48 125 C ATOM 1083 CG1 ILE A 89 -7.919 4.925 22.205 1.00 14.69 C ANISOU 1083 CG1 ILE A 89 1748 1814 2022 365 20 218 C ATOM 1084 CG2 ILE A 89 -6.552 4.808 24.320 1.00 14.09 C ANISOU 1084 CG2 ILE A 89 1785 1560 2010 531 28 114 C ATOM 1085 CD1 ILE A 89 -9.236 4.496 22.912 1.00 16.83 C ANISOU 1085 CD1 ILE A 89 2056 2129 2211 259 106 340 C ATOM 1086 H ILE A 89 -5.612 3.428 20.573 1.00 13.86 H ATOM 1087 HA ILE A 89 -5.356 5.704 22.068 1.00 13.60 H ATOM 1088 HB ILE A 89 -6.767 3.402 22.889 1.00 14.87 H ATOM 1089 HG12 ILE A 89 -7.876 5.894 22.211 1.00 17.65 H ATOM 1090 HG13 ILE A 89 -7.948 4.598 21.292 1.00 17.65 H ATOM 1091 HG21 ILE A 89 -7.344 4.556 24.801 1.00 16.93 H ATOM 1092 HG22 ILE A 89 -5.784 4.381 24.706 1.00 16.93 H ATOM 1093 HG23 ILE A 89 -6.444 5.762 24.345 1.00 16.93 H ATOM 1094 HD11 ILE A 89 -9.981 4.874 22.439 1.00 20.21 H ATOM 1095 HD12 ILE A 89 -9.296 3.538 22.907 1.00 20.21 H ATOM 1096 HD13 ILE A 89 -9.224 4.819 23.816 1.00 20.21 H ATOM 1097 N ARG A 90 -3.175 4.862 22.869 1.00 11.42 N ANISOU 1097 N ARG A 90 1608 1124 1609 159 -336 71 N ATOM 1098 CA ARG A 90 -2.008 4.384 23.522 1.00 11.04 C ANISOU 1098 CA ARG A 90 1467 1125 1602 79 -334 36 C ATOM 1099 C ARG A 90 -2.220 4.351 25.015 1.00 10.45 C ANISOU 1099 C ARG A 90 1377 1023 1571 10 -200 -97 C ATOM 1100 O ARG A 90 -2.931 5.165 25.583 1.00 11.87 O ANISOU 1100 O ARG A 90 1550 1257 1703 211 -74 -120 O ATOM 1101 CB ARG A 90 -0.849 5.327 23.269 1.00 12.58 C ANISOU 1101 CB ARG A 90 1592 1450 1736 54 -113 -4 C ATOM 1102 CG ARG A 90 -0.363 5.364 21.797 1.00 15.36 C ANISOU 1102 CG ARG A 90 1994 1789 2054 17 184 -119 C ATOM 1103 CD ARG A 90 0.832 6.277 21.649 1.00 21.14 C ANISOU 1103 CD ARG A 90 2745 2526 2760 263 699 -58 C ATOM 1104 NE ARG A 90 0.375 7.644 21.774 1.00 27.68 N ANISOU 1104 NE ARG A 90 3560 3327 3629 158 1146 138 N ATOM 1105 CZ ARG A 90 1.019 8.651 21.243 1.00 34.42 C ANISOU 1105 CZ ARG A 90 4421 4215 4443 85 1128 91 C ATOM 1106 NH1 ARG A 90 2.221 8.448 20.724 1.00 37.02 N ANISOU 1106 NH1 ARG A 90 4711 4570 4784 -106 1069 131 N ATOM 1107 NH2 ARG A 90 0.510 9.853 21.391 1.00 40.01 N ANISOU 1107 NH2 ARG A 90 5088 4940 5176 227 1092 116 N ATOM 1108 H ARG A 90 -3.132 5.689 22.636 1.00 13.72 H ATOM 1109 HA ARG A 90 -1.777 3.487 23.203 1.00 13.26 H ATOM 1110 HB2 ARG A 90 -1.121 6.226 23.511 1.00 15.11 H ATOM 1111 HB3 ARG A 90 -0.099 5.053 23.820 1.00 15.11 H ATOM 1112 HG2 ARG A 90 -0.102 4.471 21.521 1.00 18.45 H ATOM 1113 HG3 ARG A 90 -1.076 5.698 21.230 1.00 18.45 H ATOM 1114 HD2 ARG A 90 1.476 6.096 22.352 1.00 25.38 H ATOM 1115 HD3 ARG A 90 1.233 6.159 20.774 1.00 25.38 H ATOM 1116 HE ARG A 90 -0.537 7.792 22.067 1.00 33.22 H ATOM 1117 HH11 ARG A 90 2.526 7.648 20.648 1.00 44.44 H ATOM 1118 HH12 ARG A 90 2.665 9.109 20.398 1.00 44.44 H ATOM 1119 HH21 ARG A 90 -0.257 9.952 21.766 1.00 48.03 H ATOM 1120 HH22 ARG A 90 0.935 10.539 21.094 1.00 48.03 H ATOM 1121 N HIS A 91 -1.550 3.437 25.714 1.00 10.00 N ANISOU 1121 N HIS A 91 1315 1012 1472 152 -235 -75 N ATOM 1122 CA HIS A 91 -1.610 3.435 27.161 1.00 9.04 C ANISOU 1122 CA HIS A 91 1122 883 1431 73 -97 -69 C ATOM 1123 C HIS A 91 -1.137 4.811 27.685 1.00 9.06 C ANISOU 1123 C HIS A 91 1070 824 1550 28 82 -8 C ATOM 1124 O HIS A 91 -0.139 5.341 27.206 1.00 10.09 O ANISOU 1124 O HIS A 91 1126 1021 1686 -80 114 -108 O ATOM 1125 CB HIS A 91 -0.757 2.335 27.751 1.00 10.01 C ANISOU 1125 CB HIS A 91 1306 1071 1425 158 -117 -143 C ATOM 1126 CG HIS A 91 -1.045 2.126 29.193 1.00 9.21 C ANISOU 1126 CG HIS A 91 1100 977 1424 288 -113 -205 C ATOM 1127 ND1 HIS A 91 -0.473 2.877 30.200 1.00 9.88 N ANISOU 1127 ND1 HIS A 91 1229 1091 1432 143 15 -224 N ATOM 1128 CD2 HIS A 91 -1.933 1.285 29.798 1.00 10.41 C ANISOU 1128 CD2 HIS A 91 1228 1120 1607 110 -57 -85 C ATOM 1129 CE1 HIS A 91 -1.018 2.501 31.363 1.00 9.85 C ANISOU 1129 CE1 HIS A 91 1098 1134 1509 115 82 -234 C ATOM 1130 NE2 HIS A 91 -1.895 1.529 31.135 1.00 10.30 N ANISOU 1130 NE2 HIS A 91 1128 1077 1710 227 -77 -54 N ATOM 1131 H HIS A 91 -1.061 2.816 25.374 1.00 12.01 H ATOM 1132 HA HIS A 91 -2.537 3.297 27.449 1.00 10.87 H ATOM 1133 HB2 HIS A 91 -0.939 1.505 27.282 1.00 12.03 H ATOM 1134 HB3 HIS A 91 0.179 2.573 27.660 1.00 12.03 H ATOM 1135 HD2 HIS A 91 -2.480 0.667 29.370 1.00 12.50 H ATOM 1136 HE1 HIS A 91 -0.781 2.829 32.201 1.00 11.83 H ATOM 1137 N PRO A 92 -1.835 5.388 28.663 1.00 9.61 N ANISOU 1137 N PRO A 92 1024 958 1669 135 119 -115 N ATOM 1138 CA PRO A 92 -1.498 6.752 29.092 1.00 10.13 C ANISOU 1138 CA PRO A 92 1189 1006 1655 106 50 -145 C ATOM 1139 C PRO A 92 -0.145 6.861 29.762 1.00 10.67 C ANISOU 1139 C PRO A 92 1290 942 1821 11 -25 -277 C ATOM 1140 O PRO A 92 0.378 7.972 29.899 1.00 12.69 O ANISOU 1140 O PRO A 92 1550 1042 2230 -156 -52 -310 O ATOM 1141 CB PRO A 92 -2.637 7.147 30.016 1.00 11.50 C ANISOU 1141 CB PRO A 92 1364 1312 1693 168 89 -147 C ATOM 1142 CG PRO A 92 -3.193 5.881 30.504 1.00 11.96 C ANISOU 1142 CG PRO A 92 1418 1432 1696 64 322 -146 C ATOM 1143 CD PRO A 92 -3.087 4.944 29.298 1.00 10.83 C ANISOU 1143 CD PRO A 92 1271 1228 1614 108 125 -48 C ATOM 1144 HA PRO A 92 -1.507 7.349 28.315 1.00 12.17 H ATOM 1145 HB2 PRO A 92 -2.292 7.676 30.752 1.00 13.81 H ATOM 1146 HB3 PRO A 92 -3.304 7.645 29.518 1.00 13.81 H ATOM 1147 HG2 PRO A 92 -2.664 5.552 31.247 1.00 14.37 H ATOM 1148 HG3 PRO A 92 -4.119 6.006 30.765 1.00 14.37 H ATOM 1149 HD2 PRO A 92 -3.013 4.021 29.589 1.00 13.01 H ATOM 1150 HD3 PRO A 92 -3.838 5.073 28.698 1.00 13.01 H ATOM 1151 N LYS A 93 0.408 5.735 30.220 1.00 9.88 N ANISOU 1151 N LYS A 93 1079 1054 1620 50 1 -277 N ATOM 1152 CA LYS A 93 1.708 5.755 30.852 1.00 10.75 C ANISOU 1152 CA LYS A 93 1202 1224 1660 37 -5 -279 C ATOM 1153 C LYS A 93 2.818 5.221 29.958 1.00 9.91 C ANISOU 1153 C LYS A 93 1081 994 1688 64 50 -225 C ATOM 1154 O LYS A 93 3.930 4.963 30.422 1.00 10.35 O ANISOU 1154 O LYS A 93 997 1250 1687 24 0 -165 O ATOM 1155 CB LYS A 93 1.686 4.987 32.168 1.00 13.15 C ANISOU 1155 CB LYS A 93 1421 1713 1862 168 47 -465 C ATOM 1156 CG LYS A 93 0.650 5.514 33.207 1.00 19.31 C ANISOU 1156 CG LYS A 93 2254 2445 2639 332 102 -756 C ATOM 1157 CD LYS A 93 0.964 4.998 34.544 1.00 31.27 C ANISOU 1157 CD LYS A 93 3868 3916 4096 443 355 -787 C ATOM 1158 CE LYS A 93 0.139 3.890 34.911 1.00 42.55 C ANISOU 1158 CE LYS A 93 5340 5342 5486 486 276 -785 C ATOM 1159 NZ LYS A 93 -0.234 4.085 36.394 1.00 50.02 N ANISOU 1159 NZ LYS A 93 6288 6262 6455 520 268 -758 N ATOM 1160 H LYS A 93 0.047 4.956 30.173 1.00 11.87 H ATOM 1161 HA LYS A 93 1.930 6.686 31.064 1.00 12.92 H ATOM 1162 HB2 LYS A 93 1.470 4.059 31.982 1.00 15.79 H ATOM 1163 HB3 LYS A 93 2.565 5.043 32.575 1.00 15.79 H ATOM 1164 HG2 LYS A 93 0.684 6.483 33.235 1.00 23.19 H ATOM 1165 HG3 LYS A 93 -0.239 5.212 32.961 1.00 23.19 H ATOM 1166 HD2 LYS A 93 1.888 4.703 34.560 1.00 37.54 H ATOM 1167 HD3 LYS A 93 0.829 5.703 35.196 1.00 37.54 H ATOM 1168 HE2 LYS A 93 -0.670 3.883 34.377 1.00 51.08 H ATOM 1169 HE3 LYS A 93 0.631 3.059 34.813 1.00 51.08 H ATOM 1170 HZ1 LYS A 93 -0.792 3.361 36.690 1.00 60.04 H ATOM 1171 HZ2 LYS A 93 0.560 4.107 36.932 1.00 60.04 H ATOM 1172 HZ3 LYS A 93 -0.710 4.911 36.506 1.00 60.04 H ATOM 1173 N TYR A 94 2.560 5.057 28.678 1.00 9.21 N ANISOU 1173 N TYR A 94 970 994 1536 32 16 -197 N ATOM 1174 CA TYR A 94 3.628 4.704 27.759 1.00 8.94 C ANISOU 1174 CA TYR A 94 1082 895 1419 57 38 -103 C ATOM 1175 C TYR A 94 4.746 5.732 27.856 1.00 9.51 C ANISOU 1175 C TYR A 94 1089 935 1589 2 15 -183 C ATOM 1176 O TYR A 94 4.489 6.923 27.818 1.00 11.24 O ANISOU 1176 O TYR A 94 1193 1045 2034 -81 -24 -27 O ATOM 1177 CB TYR A 94 3.097 4.628 26.347 1.00 9.64 C ANISOU 1177 CB TYR A 94 1228 1070 1365 -158 11 -93 C ATOM 1178 CG TYR A 94 4.167 4.410 25.312 1.00 9.80 C ANISOU 1178 CG TYR A 94 1326 1066 1332 -175 -65 59 C ATOM 1179 CD1 TYR A 94 5.049 3.309 25.382 1.00 9.75 C ANISOU 1179 CD1 TYR A 94 1174 1117 1412 -256 -49 -65 C ATOM 1180 CD2 TYR A 94 4.331 5.286 24.278 1.00 11.45 C ANISOU 1180 CD2 TYR A 94 1603 1234 1514 -223 18 84 C ATOM 1181 CE1 TYR A 94 6.067 3.101 24.476 1.00 10.99 C ANISOU 1181 CE1 TYR A 94 1432 1288 1454 -296 34 -288 C ATOM 1182 CE2 TYR A 94 5.341 5.089 23.331 1.00 12.41 C ANISOU 1182 CE2 TYR A 94 1768 1402 1548 -560 318 -79 C ATOM 1183 CZ TYR A 94 6.192 3.992 23.430 1.00 12.76 C ANISOU 1183 CZ TYR A 94 1636 1646 1566 -465 350 -452 C ATOM 1184 OH TYR A 94 7.225 3.763 22.546 1.00 15.84 O ANISOU 1184 OH TYR A 94 2067 2053 1898 -684 611 -656 O ATOM 1185 H TYR A 94 1.786 5.142 28.315 1.00 11.07 H ATOM 1186 HA TYR A 94 3.991 3.827 28.002 1.00 10.74 H ATOM 1187 HB2 TYR A 94 2.471 3.890 26.288 1.00 11.58 H ATOM 1188 HB3 TYR A 94 2.646 5.460 26.137 1.00 11.58 H ATOM 1189 HD1 TYR A 94 4.959 2.714 26.091 1.00 11.71 H ATOM 1190 HD2 TYR A 94 3.765 6.020 24.203 1.00 13.76 H ATOM 1191 HE1 TYR A 94 6.631 2.365 24.550 1.00 13.20 H ATOM 1192 HE2 TYR A 94 5.445 5.693 22.631 1.00 14.91 H ATOM 1193 HH TYR A 94 7.733 4.407 22.535 1.00 19.02 H ATOM 1194 N ASN A 95 5.970 5.243 27.959 1.00 9.69 N ANISOU 1194 N ASN A 95 1110 1068 1505 -47 8 -98 N ATOM 1195 CA ASN A 95 7.138 6.094 27.967 1.00 9.87 C ANISOU 1195 CA ASN A 95 1113 1101 1535 -72 65 -27 C ATOM 1196 C ASN A 95 8.019 5.707 26.830 1.00 9.74 C ANISOU 1196 C ASN A 95 979 1100 1622 -142 -3 47 C ATOM 1197 O ASN A 95 8.503 4.575 26.777 1.00 9.82 O ANISOU 1197 O ASN A 95 924 1151 1656 15 106 38 O ATOM 1198 CB ASN A 95 7.891 5.937 29.309 1.00 10.80 C ANISOU 1198 CB ASN A 95 1310 1267 1527 32 20 -105 C ATOM 1199 CG ASN A 95 9.015 6.902 29.474 1.00 11.57 C ANISOU 1199 CG ASN A 95 1560 1258 1578 -101 -14 -339 C ATOM 1200 OD1 ASN A 95 9.018 7.741 30.421 1.00 16.47 O ANISOU 1200 OD1 ASN A 95 2198 2020 2038 -258 -86 -671 O ATOM 1201 ND2 ASN A 95 9.905 6.898 28.595 1.00 10.49 N ANISOU 1201 ND2 ASN A 95 1264 1168 1553 -367 -86 -433 N ATOM 1202 H ASN A 95 6.151 4.405 28.027 1.00 11.64 H ATOM 1203 HA ASN A 95 6.871 7.031 27.859 1.00 11.86 H ATOM 1204 HB2 ASN A 95 7.267 6.080 30.038 1.00 12.98 H ATOM 1205 HB3 ASN A 95 8.258 5.041 29.360 1.00 12.98 H ATOM 1206 HD21 ASN A 95 10.663 7.516 28.662 1.00 12.60 H ATOM 1207 HD22 ASN A 95 9.843 6.278 27.839 1.00 12.60 H ATOM 1208 N ARG A 96 8.202 6.602 25.878 1.00 11.59 N ANISOU 1208 N ARG A 96 1312 1404 1689 16 112 126 N ATOM 1209 CA ARG A 96 8.923 6.288 24.655 1.00 13.49 C ANISOU 1209 CA ARG A 96 1562 1725 1840 212 53 239 C ATOM 1210 C ARG A 96 10.424 6.136 24.834 1.00 11.73 C ANISOU 1210 C ARG A 96 1398 1338 1720 230 113 161 C ATOM 1211 O ARG A 96 11.128 5.744 23.885 1.00 13.79 O ANISOU 1211 O ARG A 96 1682 1704 1853 158 224 15 O ATOM 1212 CB ARG A 96 8.601 7.275 23.537 1.00 18.86 C ANISOU 1212 CB ARG A 96 2322 2431 2414 145 -50 510 C ATOM 1213 CG ARG A 96 9.272 8.620 23.869 1.00 24.22 C ANISOU 1213 CG ARG A 96 3085 2966 3150 288 -100 818 C ATOM 1214 CD ARG A 96 9.257 9.610 22.680 1.00 29.90 C ANISOU 1214 CD ARG A 96 3756 3744 3862 210 -139 824 C ATOM 1215 NE ARG A 96 7.883 9.862 22.238 1.00 33.76 N ANISOU 1215 NE ARG A 96 4230 4286 4312 100 -13 667 N ATOM 1216 CZ ARG A 96 7.144 10.824 22.675 0.00 35.74 C ANISOU 1216 CZ ARG A 96 4513 4548 4518 47 -53 549 C ATOM 1217 NH1 ARG A 96 7.688 11.640 23.545 0.00 37.64 N ANISOU 1217 NH1 ARG A 96 4748 4743 4812 31 -102 510 N ATOM 1218 NH2 ARG A 96 5.912 10.929 22.210 0.00 37.58 N ANISOU 1218 NH2 ARG A 96 4741 4736 4804 30 -102 510 N ATOM 1219 H ARG A 96 7.915 7.412 25.915 1.00 13.93 H ATOM 1220 HA ARG A 96 8.598 5.416 24.349 1.00 16.21 H ATOM 1221 HB2 ARG A 96 8.954 6.947 22.696 1.00 22.65 H ATOM 1222 HB3 ARG A 96 7.641 7.408 23.481 1.00 22.65 H ATOM 1223 HG2 ARG A 96 8.800 9.034 24.609 1.00 29.07 H ATOM 1224 HG3 ARG A 96 10.196 8.460 24.114 1.00 29.07 H ATOM 1225 HD2 ARG A 96 9.650 10.452 22.956 1.00 35.90 H ATOM 1226 HD3 ARG A 96 9.754 9.231 21.938 1.00 35.90 H ATOM 1227 HE ARG A 96 7.504 9.266 21.573 1.00 40.53 H ATOM 1228 HH11 ARG A 96 8.496 11.511 23.808 0.00 45.19 H ATOM 1229 HH12 ARG A 96 7.234 12.299 23.859 0.00 45.19 H ATOM 1230 HH21 ARG A 96 5.620 10.362 21.633 0.00 45.12 H ATOM 1231 HH22 ARG A 96 5.405 11.571 22.477 0.00 45.12 H ATOM 1232 N ASP A 97 10.934 6.478 26.001 1.00 11.63 N ANISOU 1232 N ASP A 97 1303 1336 1783 -102 24 120 N ATOM 1233 CA AASP A 97 12.358 6.306 26.245 0.54 12.72 C ANISOU 1233 CA AASP A 97 1516 1496 1819 -137 -32 25 C ATOM 1234 CA BASP A 97 12.343 6.369 26.326 0.46 11.71 C ANISOU 1234 CA BASP A 97 1254 1327 1867 -178 -35 15 C ATOM 1235 C ASP A 97 12.742 5.089 27.074 1.00 11.10 C ANISOU 1235 C ASP A 97 1249 1177 1791 -112 79 -33 C ATOM 1236 O ASP A 97 13.696 4.414 26.730 1.00 13.70 O ANISOU 1236 O ASP A 97 1351 1798 2056 134 141 -8 O ATOM 1237 CB AASP A 97 12.970 7.579 26.809 0.54 15.47 C ANISOU 1237 CB AASP A 97 1923 1881 2076 -311 -27 35 C ATOM 1238 CB BASP A 97 12.799 7.557 27.157 0.46 12.93 C ANISOU 1238 CB BASP A 97 1272 1612 2028 -424 -38 27 C ATOM 1239 CG AASP A 97 13.094 8.604 25.745 0.54 19.71 C ANISOU 1239 CG AASP A 97 2545 2352 2591 -555 98 12 C ATOM 1240 CG BASP A 97 14.241 7.842 26.936 0.46 15.14 C ANISOU 1240 CG BASP A 97 1579 1968 2204 -589 99 118 C ATOM 1241 OD1AASP A 97 13.583 8.336 24.627 0.54 22.54 O ANISOU 1241 OD1AASP A 97 3045 2561 2957 -637 136 49 O ATOM 1242 OD1BASP A 97 14.790 7.485 25.853 0.46 17.37 O ANISOU 1242 OD1BASP A 97 1818 2356 2426 -644 49 -187 O ATOM 1243 OD2AASP A 97 12.547 9.609 26.031 0.54 22.20 O ANISOU 1243 OD2AASP A 97 2831 2728 2875 -361 111 61 O ATOM 1244 OD2BASP A 97 14.772 8.412 27.861 0.46 16.08 O ANISOU 1244 OD2BASP A 97 1671 2188 2250 -552 51 274 O ATOM 1245 H AASP A 97 10.490 6.806 26.660 1.00 13.98 H ATOM 1246 HA AASP A 97 12.778 6.172 25.370 0.54 15.27 H ATOM 1247 HB2AASP A 97 12.399 7.931 27.510 0.54 18.58 H ATOM 1248 HB3AASP A 97 13.855 7.387 27.156 0.54 18.58 H ATOM 1249 N THR A 98 11.942 4.766 28.099 1.00 9.96 N ANISOU 1249 N THR A 98 1130 1097 1557 -176 94 -133 N ATOM 1250 CA THR A 98 12.123 3.540 28.843 1.00 9.80 C ANISOU 1250 CA THR A 98 1082 1126 1517 -138 -42 -48 C ATOM 1251 C THR A 98 11.388 2.359 28.207 1.00 9.00 C ANISOU 1251 C THR A 98 996 947 1475 -33 40 -63 C ATOM 1252 O THR A 98 11.693 1.198 28.506 1.00 10.01 O ANISOU 1252 O THR A 98 1102 979 1722 3 -94 -30 O ATOM 1253 CB THR A 98 11.657 3.657 30.291 1.00 10.55 C ANISOU 1253 CB THR A 98 1210 1213 1587 -147 -116 -141 C ATOM 1254 OG1 THR A 98 10.237 3.858 30.253 1.00 10.60 O ANISOU 1254 OG1 THR A 98 1117 1314 1597 -139 -77 -212 O ATOM 1255 CG2 THR A 98 12.379 4.744 31.037 1.00 12.07 C ANISOU 1255 CG2 THR A 98 1394 1507 1684 -341 -238 -236 C ATOM 1256 H THR A 98 11.287 5.250 28.375 1.00 11.96 H ATOM 1257 HA THR A 98 13.079 3.322 28.856 1.00 11.78 H ATOM 1258 HB THR A 98 11.839 2.820 30.744 1.00 12.68 H ATOM 1259 HG1 THR A 98 9.943 3.927 31.015 1.00 12.74 H ATOM 1260 HG21 THR A 98 12.060 4.788 31.941 1.00 14.50 H ATOM 1261 HG22 THR A 98 13.322 4.564 31.047 1.00 14.50 H ATOM 1262 HG23 THR A 98 12.227 5.591 30.611 1.00 14.50 H ATOM 1263 N LEU A 99 10.420 2.640 27.352 1.00 9.33 N ANISOU 1263 N LEU A 99 1074 1045 1427 -120 -28 -69 N ATOM 1264 CA LEU A 99 9.532 1.667 26.690 1.00 8.77 C ANISOU 1264 CA LEU A 99 1057 981 1295 -35 -93 -114 C ATOM 1265 C LEU A 99 8.536 1.030 27.643 1.00 8.70 C ANISOU 1265 C LEU A 99 972 994 1340 71 -123 -69 C ATOM 1266 O LEU A 99 7.870 0.050 27.287 1.00 9.32 O ANISOU 1266 O LEU A 99 1088 930 1522 -87 -37 -186 O ATOM 1267 CB LEU A 99 10.313 0.643 25.876 1.00 10.56 C ANISOU 1267 CB LEU A 99 1339 1280 1394 -42 88 -104 C ATOM 1268 CG LEU A 99 11.413 1.278 25.050 1.00 11.95 C ANISOU 1268 CG LEU A 99 1620 1381 1540 49 322 15 C ATOM 1269 CD1 LEU A 99 12.109 0.159 24.206 1.00 12.86 C ANISOU 1269 CD1 LEU A 99 1644 1524 1718 -173 465 -179 C ATOM 1270 CD2 LEU A 99 10.887 2.360 24.127 1.00 15.23 C ANISOU 1270 CD2 LEU A 99 2062 1793 1933 199 437 174 C ATOM 1271 H LEU A 99 10.239 3.447 27.118 1.00 11.21 H ATOM 1272 HA LEU A 99 8.995 2.169 26.042 1.00 10.54 H ATOM 1273 HB2 LEU A 99 10.721 0.003 26.479 1.00 12.69 H ATOM 1274 HB3 LEU A 99 9.705 0.190 25.270 1.00 12.69 H ATOM 1275 HG LEU A 99 12.074 1.672 25.640 1.00 14.35 H ATOM 1276 HD11 LEU A 99 12.808 0.554 23.679 1.00 15.44 H ATOM 1277 HD12 LEU A 99 12.478 -0.497 24.801 1.00 15.44 H ATOM 1278 HD13 LEU A 99 11.457 -0.250 23.632 1.00 15.44 H ATOM 1279 HD21 LEU A 99 11.620 2.729 23.628 1.00 18.29 H ATOM 1280 HD22 LEU A 99 10.244 1.974 23.527 1.00 18.29 H ATOM 1281 HD23 LEU A 99 10.472 3.046 24.655 1.00 18.29 H ATOM 1282 N ASP A 100 8.402 1.605 28.825 1.00 8.89 N ANISOU 1282 N ASP A 100 1016 1038 1323 -107 -54 -88 N ATOM 1283 CA ASP A 100 7.426 1.123 29.788 1.00 9.10 C ANISOU 1283 CA ASP A 100 1037 1109 1310 70 1 -134 C ATOM 1284 C ASP A 100 6.006 1.259 29.224 1.00 8.21 C ANISOU 1284 C ASP A 100 981 818 1322 16 -33 -70 C ATOM 1285 O ASP A 100 5.679 2.259 28.574 1.00 9.04 O ANISOU 1285 O ASP A 100 1054 908 1473 -119 -61 -16 O ATOM 1286 CB ASP A 100 7.604 1.965 31.057 1.00 9.45 C ANISOU 1286 CB ASP A 100 1186 1078 1327 -50 -92 -336 C ATOM 1287 CG ASP A 100 7.065 1.333 32.328 1.00 11.56 C ANISOU 1287 CG ASP A 100 1567 1333 1491 116 -30 -401 C ATOM 1288 OD1 ASP A 100 6.960 2.110 33.320 1.00 15.26 O ANISOU 1288 OD1 ASP A 100 2386 1681 1731 56 50 -353 O ATOM 1289 OD2 ASP A 100 6.775 0.134 32.398 1.00 11.31 O ANISOU 1289 OD2 ASP A 100 1415 1390 1492 101 -33 -103 O ATOM 1290 H ASP A 100 8.864 2.277 29.096 1.00 10.68 H ATOM 1291 HA ASP A 100 7.599 0.182 30.001 1.00 10.93 H ATOM 1292 HB2 ASP A 100 8.551 2.127 31.189 1.00 11.35 H ATOM 1293 HB3 ASP A 100 7.145 2.810 30.933 1.00 11.35 H ATOM 1294 N ASN A 101 5.157 0.279 29.537 1.00 8.57 N ANISOU 1294 N ASN A 101 996 945 1315 -158 -10 -132 N ATOM 1295 CA ASN A 101 3.729 0.320 29.139 1.00 8.37 C ANISOU 1295 CA ASN A 101 988 931 1263 -82 94 -172 C ATOM 1296 C ASN A 101 3.540 0.411 27.655 1.00 8.11 C ANISOU 1296 C ASN A 101 967 862 1254 -37 55 -16 C ATOM 1297 O ASN A 101 2.698 1.184 27.166 1.00 8.41 O ANISOU 1297 O ASN A 101 1007 878 1309 19 -96 -149 O ATOM 1298 CB ASN A 101 2.961 1.425 29.880 1.00 10.03 C ANISOU 1298 CB ASN A 101 1201 1212 1400 -14 112 -264 C ATOM 1299 CG ASN A 101 3.143 1.375 31.346 1.00 10.13 C ANISOU 1299 CG ASN A 101 1260 1132 1457 -127 173 -284 C ATOM 1300 OD1 ASN A 101 2.703 0.450 32.016 1.00 10.98 O ANISOU 1300 OD1 ASN A 101 1402 1316 1452 -102 187 -112 O ATOM 1301 ND2 ASN A 101 3.823 2.382 31.889 1.00 10.72 N ANISOU 1301 ND2 ASN A 101 1461 1157 1457 -67 95 -215 N ATOM 1302 H ASN A 101 5.374 -0.426 29.979 1.00 10.30 H ATOM 1303 HA ASN A 101 3.326 -0.529 29.416 1.00 10.06 H ATOM 1304 HB2 ASN A 101 3.274 2.288 29.569 1.00 12.06 H ATOM 1305 HB3 ASN A 101 2.014 1.329 29.693 1.00 12.06 H ATOM 1306 HD21 ASN A 101 3.975 2.404 32.857 1.00 12.88 H ATOM 1307 HD22 ASN A 101 4.170 3.101 31.322 1.00 12.88 H ATOM 1308 N ASP A 102 4.269 -0.411 26.899 1.00 7.94 N ANISOU 1308 N ASP A 102 992 870 1154 16 21 -73 N ATOM 1309 CA ASP A 102 4.202 -0.377 25.470 1.00 7.86 C ANISOU 1309 CA ASP A 102 1019 831 1136 -45 141 -210 C ATOM 1310 C ASP A 102 3.012 -1.198 24.937 1.00 8.18 C ANISOU 1310 C ASP A 102 1016 811 1281 -37 10 -257 C ATOM 1311 O ASP A 102 3.117 -2.360 24.535 1.00 8.50 O ANISOU 1311 O ASP A 102 1046 841 1344 158 53 -87 O ATOM 1312 CB ASP A 102 5.511 -0.868 24.866 1.00 8.20 C ANISOU 1312 CB ASP A 102 1024 865 1228 -53 84 -75 C ATOM 1313 CG ASP A 102 5.587 -0.708 23.355 1.00 8.47 C ANISOU 1313 CG ASP A 102 1138 742 1337 -3 136 -98 C ATOM 1314 OD1 ASP A 102 4.752 0.053 22.788 1.00 8.80 O ANISOU 1314 OD1 ASP A 102 1159 835 1349 -7 41 66 O ATOM 1315 OD2 ASP A 102 6.518 -1.286 22.718 1.00 9.58 O ANISOU 1315 OD2 ASP A 102 1146 1182 1311 205 146 -34 O ATOM 1316 H ASP A 102 4.813 -1.000 27.209 1.00 9.54 H ATOM 1317 HA ASP A 102 4.072 0.552 25.185 1.00 9.45 H ATOM 1318 HB2 ASP A 102 6.243 -0.363 25.255 1.00 9.86 H ATOM 1319 HB3 ASP A 102 5.616 -1.810 25.070 1.00 9.86 H ATOM 1320 N ILE A 103 1.822 -0.603 25.002 1.00 8.07 N ANISOU 1320 N ILE A 103 845 900 1322 63 -88 -101 N ATOM 1321 CA ILE A 103 0.598 -1.276 24.595 1.00 7.57 C ANISOU 1321 CA ILE A 103 922 813 1141 -51 -27 -21 C ATOM 1322 C ILE A 103 -0.386 -0.178 24.118 1.00 7.80 C ANISOU 1322 C ILE A 103 897 809 1256 -59 -8 -117 C ATOM 1323 O ILE A 103 -0.356 0.950 24.597 1.00 8.57 O ANISOU 1323 O ILE A 103 938 860 1458 66 -33 -82 O ATOM 1324 CB ILE A 103 0.014 -2.148 25.740 1.00 8.56 C ANISOU 1324 CB ILE A 103 1079 1024 1150 27 -41 -57 C ATOM 1325 CG1 ILE A 103 -1.081 -3.112 25.237 1.00 8.29 C ANISOU 1325 CG1 ILE A 103 956 1001 1195 -3 -51 22 C ATOM 1326 CG2 ILE A 103 -0.417 -1.327 26.964 1.00 9.20 C ANISOU 1326 CG2 ILE A 103 1215 1092 1190 -54 -43 -62 C ATOM 1327 CD1 ILE A 103 -1.416 -4.182 26.225 1.00 9.86 C ANISOU 1327 CD1 ILE A 103 1231 1183 1333 -211 -29 9 C ATOM 1328 H ILE A 103 1.699 0.201 25.282 1.00 9.70 H ATOM 1329 HA ILE A 103 0.792 -1.863 23.835 1.00 9.10 H ATOM 1330 HB ILE A 103 0.744 -2.711 26.043 1.00 10.29 H ATOM 1331 HG12 ILE A 103 -1.889 -2.606 25.058 1.00 9.97 H ATOM 1332 HG13 ILE A 103 -0.772 -3.543 24.424 1.00 9.97 H ATOM 1333 HG21 ILE A 103 -0.767 -1.922 27.631 1.00 11.06 H ATOM 1334 HG22 ILE A 103 0.346 -0.859 27.311 1.00 11.06 H ATOM 1335 HG23 ILE A 103 -1.093 -0.700 26.697 1.00 11.06 H ATOM 1336 HD11 ILE A 103 -2.099 -4.745 25.855 1.00 11.85 H ATOM 1337 HD12 ILE A 103 -0.627 -4.698 26.406 1.00 11.85 H ATOM 1338 HD13 ILE A 103 -1.732 -3.771 27.034 1.00 11.85 H ATOM 1339 N MET A 104 -1.241 -0.605 23.184 1.00 8.63 N ANISOU 1339 N MET A 104 964 1050 1264 118 -101 -33 N ATOM 1340 CA MET A 104 -2.218 0.282 22.562 1.00 9.45 C ANISOU 1340 CA MET A 104 1095 1092 1402 -27 -133 56 C ATOM 1341 C MET A 104 -3.433 -0.530 22.155 1.00 7.98 C ANISOU 1341 C MET A 104 1006 690 1334 149 -138 -49 C ATOM 1342 O MET A 104 -3.323 -1.696 21.852 1.00 9.12 O ANISOU 1342 O MET A 104 1032 937 1498 134 -69 -196 O ATOM 1343 CB MET A 104 -1.522 0.888 21.333 1.00 13.52 C ANISOU 1343 CB MET A 104 1624 1675 1836 -440 -114 321 C ATOM 1344 CG MET A 104 -2.197 1.711 20.367 1.00 14.69 C ANISOU 1344 CG MET A 104 1766 1979 1838 -65 79 247 C ATOM 1345 SD MET A 104 -1.142 2.350 19.089 1.00 12.72 S ANISOU 1345 SD MET A 104 1372 1900 1559 63 66 336 S ATOM 1346 CE MET A 104 -1.014 1.090 17.852 1.00 12.85 C ANISOU 1346 CE MET A 104 1527 1581 1773 51 -271 311 C ATOM 1347 H MET A 104 -1.273 -1.413 22.892 1.00 10.37 H ATOM 1348 HA MET A 104 -2.474 0.999 23.180 1.00 11.35 H ATOM 1349 HB2 MET A 104 -0.786 1.425 21.666 1.00 16.23 H ATOM 1350 HB3 MET A 104 -1.150 0.146 20.830 1.00 16.23 H ATOM 1351 HG2 MET A 104 -2.892 1.185 19.941 1.00 17.65 H ATOM 1352 HG3 MET A 104 -2.595 2.467 20.827 1.00 17.65 H ATOM 1353 HE1 MET A 104 -0.448 1.405 17.143 1.00 15.43 H ATOM 1354 HE2 MET A 104 -0.637 0.301 18.247 1.00 15.43 H ATOM 1355 HE3 MET A 104 -1.891 0.898 17.510 1.00 15.43 H ATOM 1356 N LEU A 105 -4.552 0.168 22.064 1.00 8.24 N ANISOU 1356 N LEU A 105 1005 834 1293 137 -135 -53 N ATOM 1357 CA LEU A 105 -5.794 -0.372 21.567 1.00 8.30 C ANISOU 1357 CA LEU A 105 916 965 1274 54 -89 -26 C ATOM 1358 C LEU A 105 -6.209 0.340 20.304 1.00 8.17 C ANISOU 1358 C LEU A 105 998 718 1390 59 -42 20 C ATOM 1359 O LEU A 105 -6.080 1.563 20.192 1.00 10.03 O ANISOU 1359 O LEU A 105 1455 817 1537 142 -149 86 O ATOM 1360 CB LEU A 105 -6.919 -0.283 22.589 1.00 9.16 C ANISOU 1360 CB LEU A 105 1078 1070 1332 106 28 28 C ATOM 1361 CG LEU A 105 -6.844 -1.279 23.711 1.00 9.75 C ANISOU 1361 CG LEU A 105 1194 1142 1366 229 178 117 C ATOM 1362 CD1 LEU A 105 -7.720 -0.879 24.859 1.00 11.83 C ANISOU 1362 CD1 LEU A 105 1510 1440 1545 290 176 -25 C ATOM 1363 CD2 LEU A 105 -7.298 -2.697 23.221 1.00 11.44 C ANISOU 1363 CD2 LEU A 105 1496 1359 1493 154 264 148 C ATOM 1364 H LEU A 105 -4.614 0.993 22.296 1.00 9.91 H ATOM 1365 HA LEU A 105 -5.662 -1.319 21.349 1.00 9.98 H ATOM 1366 HB2 LEU A 105 -6.907 0.603 22.983 1.00 11.00 H ATOM 1367 HB3 LEU A 105 -7.763 -0.422 22.130 1.00 11.00 H ATOM 1368 HG LEU A 105 -5.929 -1.341 24.029 1.00 11.71 H ATOM 1369 HD11 LEU A 105 -7.645 -1.538 25.553 1.00 14.21 H ATOM 1370 HD12 LEU A 105 -7.434 -0.023 25.186 1.00 14.21 H ATOM 1371 HD13 LEU A 105 -8.629 -0.827 24.554 1.00 14.21 H ATOM 1372 HD21 LEU A 105 -7.241 -3.314 23.954 1.00 13.75 H ATOM 1373 HD22 LEU A 105 -8.204 -2.644 22.907 1.00 13.75 H ATOM 1374 HD23 LEU A 105 -6.720 -2.981 22.508 1.00 13.75 H ATOM 1375 N ILE A 106 -6.736 -0.412 19.377 1.00 8.76 N ANISOU 1375 N ILE A 106 1090 890 1346 96 -82 71 N ATOM 1376 CA ILE A 106 -7.315 0.111 18.158 1.00 9.30 C ANISOU 1376 CA ILE A 106 1199 1002 1334 143 -66 98 C ATOM 1377 C ILE A 106 -8.767 -0.317 18.078 1.00 9.97 C ANISOU 1377 C ILE A 106 1268 986 1533 200 -95 133 C ATOM 1378 O ILE A 106 -9.054 -1.517 18.139 1.00 10.08 O ANISOU 1378 O ILE A 106 1076 1068 1687 172 -126 28 O ATOM 1379 CB ILE A 106 -6.535 -0.446 16.904 1.00 10.34 C ANISOU 1379 CB ILE A 106 1335 1114 1480 96 -90 77 C ATOM 1380 CG1 ILE A 106 -5.084 0.076 16.903 1.00 11.87 C ANISOU 1380 CG1 ILE A 106 1517 1366 1628 -173 175 -90 C ATOM 1381 CG2 ILE A 106 -7.275 -0.018 15.595 1.00 13.43 C ANISOU 1381 CG2 ILE A 106 1758 1619 1725 278 -135 206 C ATOM 1382 CD1 ILE A 106 -4.173 -0.646 15.918 1.00 13.68 C ANISOU 1382 CD1 ILE A 106 1690 1722 1787 -130 180 -245 C ATOM 1383 H ILE A 106 -6.775 -1.269 19.428 1.00 10.52 H ATOM 1384 HA ILE A 106 -7.269 1.090 18.156 1.00 11.18 H ATOM 1385 HB ILE A 106 -6.519 -1.415 16.951 1.00 12.42 H ATOM 1386 HG12 ILE A 106 -5.090 1.017 16.667 1.00 14.26 H ATOM 1387 HG13 ILE A 106 -4.710 -0.038 17.791 1.00 14.26 H ATOM 1388 HG21 ILE A 106 -6.794 -0.360 14.838 1.00 16.12 H ATOM 1389 HG22 ILE A 106 -8.165 -0.377 15.608 1.00 16.12 H ATOM 1390 HG23 ILE A 106 -7.309 0.941 15.556 1.00 16.12 H ATOM 1391 HD11 ILE A 106 -3.292 -0.269 15.974 1.00 16.44 H ATOM 1392 HD12 ILE A 106 -4.146 -1.579 16.144 1.00 16.44 H ATOM 1393 HD13 ILE A 106 -4.522 -0.534 15.031 1.00 16.44 H ATOM 1394 N LYS A 107 -9.669 0.635 17.899 1.00 10.29 N ANISOU 1394 N LYS A 107 1311 1088 1512 200 -194 109 N ATOM 1395 CA LYS A 107 -11.090 0.350 17.651 1.00 11.50 C ANISOU 1395 CA LYS A 107 1466 1297 1609 240 -153 80 C ATOM 1396 C LYS A 107 -11.290 0.363 16.139 1.00 11.15 C ANISOU 1396 C LYS A 107 1345 1306 1587 135 -26 283 C ATOM 1397 O LYS A 107 -10.949 1.342 15.462 1.00 12.01 O ANISOU 1397 O LYS A 107 1529 1398 1634 23 -87 408 O ATOM 1398 CB LYS A 107 -11.982 1.368 18.289 1.00 13.73 C ANISOU 1398 CB LYS A 107 1693 1724 1800 428 -310 -24 C ATOM 1399 CG LYS A 107 -13.480 0.941 18.162 1.00 16.20 C ANISOU 1399 CG LYS A 107 1943 2137 2074 584 -500 -183 C ATOM 1400 CD LYS A 107 -14.410 1.969 18.771 1.00 18.89 C ANISOU 1400 CD LYS A 107 2254 2497 2425 742 -542 -293 C ATOM 1401 CE LYS A 107 -15.832 1.539 18.601 1.00 22.33 C ANISOU 1401 CE LYS A 107 2694 2953 2837 840 -655 -563 C ATOM 1402 NZ LYS A 107 -16.765 2.643 19.104 1.00 25.77 N ANISOU 1402 NZ LYS A 107 3130 3378 3285 1083 -742 -511 N ATOM 1403 H LYS A 107 -9.486 1.476 17.915 1.00 12.37 H ATOM 1404 HA LYS A 107 -11.320 -0.538 17.996 1.00 13.82 H ATOM 1405 HB2 LYS A 107 -11.764 1.443 19.231 1.00 16.50 H ATOM 1406 HB3 LYS A 107 -11.868 2.222 17.845 1.00 16.50 H ATOM 1407 HG2 LYS A 107 -13.706 0.846 17.223 1.00 19.45 H ATOM 1408 HG3 LYS A 107 -13.613 0.099 18.625 1.00 19.45 H ATOM 1409 HD2 LYS A 107 -14.224 2.052 19.720 1.00 22.68 H ATOM 1410 HD3 LYS A 107 -14.289 2.821 18.324 1.00 22.68 H ATOM 1411 HE2 LYS A 107 -16.015 1.383 17.661 1.00 26.81 H ATOM 1412 HE3 LYS A 107 -15.994 0.735 19.119 1.00 26.81 H ATOM 1413 HZ1 LYS A 107 -17.680 2.373 18.997 1.00 30.94 H ATOM 1414 HZ2 LYS A 107 -16.597 2.815 20.033 1.00 30.94 H ATOM 1415 HZ3 LYS A 107 -16.617 3.450 18.605 1.00 30.94 H ATOM 1416 N LEU A 108 -11.873 -0.692 15.608 1.00 11.18 N ANISOU 1416 N LEU A 108 1356 1360 1530 198 -59 263 N ATOM 1417 CA LEU A 108 -12.197 -0.792 14.187 1.00 11.93 C ANISOU 1417 CA LEU A 108 1441 1519 1571 376 -199 161 C ATOM 1418 C LEU A 108 -13.406 0.051 13.851 1.00 12.29 C ANISOU 1418 C LEU A 108 1437 1609 1623 408 -205 190 C ATOM 1419 O LEU A 108 -14.324 0.188 14.663 1.00 12.81 O ANISOU 1419 O LEU A 108 1426 1751 1691 367 -6 215 O ATOM 1420 CB LEU A 108 -12.489 -2.253 13.851 1.00 12.76 C ANISOU 1420 CB LEU A 108 1635 1557 1657 568 -96 67 C ATOM 1421 CG LEU A 108 -11.347 -3.229 14.130 1.00 13.50 C ANISOU 1421 CG LEU A 108 1729 1546 1854 452 17 -28 C ATOM 1422 CD1 LEU A 108 -11.776 -4.657 13.761 1.00 15.67 C ANISOU 1422 CD1 LEU A 108 2009 1887 2056 404 -19 -66 C ATOM 1423 CD2 LEU A 108 -10.054 -2.879 13.405 1.00 15.88 C ANISOU 1423 CD2 LEU A 108 1982 1919 2133 581 85 128 C ATOM 1424 H LEU A 108 -12.101 -1.388 16.059 1.00 13.43 H ATOM 1425 HA LEU A 108 -11.437 -0.487 13.649 1.00 14.33 H ATOM 1426 HB2 LEU A 108 -13.253 -2.542 14.373 1.00 15.33 H ATOM 1427 HB3 LEU A 108 -12.700 -2.315 12.906 1.00 15.33 H ATOM 1428 HG LEU A 108 -11.159 -3.218 15.082 1.00 16.21 H ATOM 1429 HD11 LEU A 108 -11.049 -5.258 13.941 1.00 18.81 H ATOM 1430 HD12 LEU A 108 -12.540 -4.899 14.288 1.00 18.81 H ATOM 1431 HD13 LEU A 108 -11.999 -4.684 12.828 1.00 18.81 H ATOM 1432 HD21 LEU A 108 -9.385 -3.531 13.627 1.00 19.07 H ATOM 1433 HD22 LEU A 108 -10.215 -2.883 12.459 1.00 19.07 H ATOM 1434 HD23 LEU A 108 -9.766 -2.006 13.684 1.00 19.07 H ATOM 1435 N SER A 109 -13.427 0.611 12.646 1.00 12.59 N ANISOU 1435 N SER A 109 1490 1517 1775 398 -169 303 N ATOM 1436 CA ASER A 109 -14.552 1.443 12.248 0.52 13.42 C ANISOU 1436 CA ASER A 109 1531 1664 1902 420 -228 413 C ATOM 1437 CA BSER A 109 -14.529 1.421 12.159 0.48 13.36 C ANISOU 1437 CA BSER A 109 1377 1620 2078 323 -238 352 C ATOM 1438 C SER A 109 -15.834 0.644 12.058 1.00 14.24 C ANISOU 1438 C SER A 109 1386 1727 2299 353 -196 418 C ATOM 1439 O SER A 109 -16.939 1.255 12.168 1.00 16.82 O ANISOU 1439 O SER A 109 1524 1923 2942 387 -130 347 O ATOM 1440 CB ASER A 109 -14.238 2.238 10.991 0.52 14.29 C ANISOU 1440 CB ASER A 109 1755 1766 1910 472 -190 464 C ATOM 1441 CB BSER A 109 -14.176 1.994 10.786 0.48 14.09 C ANISOU 1441 CB BSER A 109 1446 1665 2244 217 -218 325 C ATOM 1442 OG ASER A 109 -13.794 1.432 9.956 0.52 14.85 O ANISOU 1442 OG ASER A 109 1853 1825 1965 491 -133 515 O ATOM 1443 OG BSER A 109 -13.223 3.028 10.924 0.48 15.12 O ANISOU 1443 OG BSER A 109 1506 1817 2423 89 -144 391 O ATOM 1444 H ASER A 109 -12.813 0.526 12.051 1.00 15.12 H ATOM 1445 HA ASER A 109 -14.719 2.091 12.965 0.52 16.11 H ATOM 1446 HB2ASER A 109 -15.044 2.696 10.704 0.52 17.17 H ATOM 1447 HB3ASER A 109 -13.548 2.888 11.198 0.52 17.17 H ATOM 1448 HG ASER A 109 -13.774 0.649 10.199 0.52 17.84 H ATOM 1449 N SER A 110 -15.720 -0.628 11.772 1.00 14.18 N ANISOU 1449 N SER A 110 1408 1831 2150 179 -297 428 N ATOM 1450 CA SER A 110 -16.888 -1.536 11.717 1.00 15.77 C ANISOU 1450 CA SER A 110 1753 1971 2269 171 -249 491 C ATOM 1451 C SER A 110 -16.427 -2.836 12.331 1.00 14.79 C ANISOU 1451 C SER A 110 1618 1712 2289 117 -168 366 C ATOM 1452 O SER A 110 -15.263 -3.150 12.378 1.00 13.84 O ANISOU 1452 O SER A 110 1447 1577 2232 144 -177 316 O ATOM 1453 CB SER A 110 -17.372 -1.733 10.281 1.00 19.29 C ANISOU 1453 CB SER A 110 2321 2443 2565 45 -326 446 C ATOM 1454 OG SER A 110 -16.385 -2.230 9.476 1.00 22.09 O ANISOU 1454 OG SER A 110 2834 2867 2691 -6 -306 292 O ATOM 1455 H SER A 110 -14.973 -1.017 11.600 1.00 17.03 H ATOM 1456 HA SER A 110 -17.622 -1.171 12.254 1.00 18.94 H ATOM 1457 HB2 SER A 110 -18.116 -2.356 10.284 1.00 23.16 H ATOM 1458 HB3 SER A 110 -17.662 -0.877 9.928 1.00 23.16 H ATOM 1459 HG SER A 110 -16.668 -2.327 8.713 1.00 26.52 H ATOM 1460 N PRO A 111 -17.356 -3.636 12.833 1.00 15.48 N ANISOU 1460 N PRO A 111 1604 1824 2454 307 -180 509 N ATOM 1461 CA PRO A 111 -16.959 -4.889 13.468 1.00 15.71 C ANISOU 1461 CA PRO A 111 1808 1893 2267 -32 -139 500 C ATOM 1462 C PRO A 111 -16.375 -5.838 12.389 1.00 15.14 C ANISOU 1462 C PRO A 111 1818 1772 2164 -147 -305 337 C ATOM 1463 O PRO A 111 -16.830 -5.939 11.230 1.00 17.83 O ANISOU 1463 O PRO A 111 2067 2211 2496 -140 -382 295 O ATOM 1464 CB PRO A 111 -18.284 -5.467 14.003 1.00 18.20 C ANISOU 1464 CB PRO A 111 2205 2199 2511 -40 -9 444 C ATOM 1465 CG PRO A 111 -19.249 -4.277 14.001 1.00 19.29 C ANISOU 1465 CG PRO A 111 2250 2445 2633 220 -185 486 C ATOM 1466 CD PRO A 111 -18.814 -3.333 13.005 1.00 17.48 C ANISOU 1466 CD PRO A 111 1969 2189 2483 337 -225 480 C ATOM 1467 HA PRO A 111 -16.319 -4.745 14.196 1.00 18.86 H ATOM 1468 HB2 PRO A 111 -18.600 -6.168 13.411 1.00 21.85 H ATOM 1469 HB3 PRO A 111 -18.156 -5.806 14.903 1.00 21.85 H ATOM 1470 HG2 PRO A 111 -20.141 -4.593 13.791 1.00 23.16 H ATOM 1471 HG3 PRO A 111 -19.241 -3.862 14.878 1.00 23.16 H ATOM 1472 HD2 PRO A 111 -19.288 -3.480 12.172 1.00 20.99 H ATOM 1473 HD3 PRO A 111 -18.934 -2.425 13.326 1.00 20.99 H ATOM 1474 N ALA A 112 -15.391 -6.599 12.823 1.00 14.40 N ANISOU 1474 N ALA A 112 1634 1775 2062 -187 -417 160 N ATOM 1475 CA ALA A 112 -14.926 -7.698 11.991 1.00 15.71 C ANISOU 1475 CA ALA A 112 1832 1874 2262 -246 -428 -46 C ATOM 1476 C ALA A 112 -15.969 -8.774 11.914 1.00 16.24 C ANISOU 1476 C ALA A 112 1841 1875 2453 -268 -417 122 C ATOM 1477 O ALA A 112 -16.679 -9.013 12.889 1.00 16.90 O ANISOU 1477 O ALA A 112 2070 1786 2566 -318 -233 349 O ATOM 1478 CB ALA A 112 -13.637 -8.289 12.633 1.00 17.54 C ANISOU 1478 CB ALA A 112 2160 2113 2392 -115 -526 -217 C ATOM 1479 H ALA A 112 -14.983 -6.509 13.574 1.00 17.29 H ATOM 1480 HA ALA A 112 -14.722 -7.379 11.087 1.00 18.86 H ATOM 1481 HB1 ALA A 112 -13.322 -9.015 12.090 1.00 21.07 H ATOM 1482 HB2 ALA A 112 -12.968 -7.601 12.679 1.00 21.07 H ATOM 1483 HB3 ALA A 112 -13.844 -8.605 13.515 1.00 21.07 H ATOM 1484 N VAL A 113 -16.029 -9.434 10.780 1.00 16.81 N ANISOU 1484 N VAL A 113 1909 1930 2548 -455 -579 141 N ATOM 1485 CA VAL A 113 -16.900 -10.609 10.668 1.00 19.88 C ANISOU 1485 CA VAL A 113 2367 2318 2866 -641 -902 -21 C ATOM 1486 C VAL A 113 -16.153 -11.814 11.237 1.00 17.87 C ANISOU 1486 C VAL A 113 2105 1925 2760 -342 -639 80 C ATOM 1487 O VAL A 113 -15.089 -12.178 10.746 1.00 19.41 O ANISOU 1487 O VAL A 113 2357 1967 3050 -25 -267 280 O ATOM 1488 CB VAL A 113 -17.203 -10.868 9.214 1.00 25.84 C ANISOU 1488 CB VAL A 113 3228 3106 3482 -913 -1174 -141 C ATOM 1489 CG1 VAL A 113 -18.107 -12.084 9.059 1.00 28.54 C ANISOU 1489 CG1 VAL A 113 3563 3501 3781 -1121 -1187 -159 C ATOM 1490 CG2 VAL A 113 -17.844 -9.612 8.555 1.00 31.69 C ANISOU 1490 CG2 VAL A 113 3977 3938 4125 -888 -1259 -115 C ATOM 1491 H VAL A 113 -15.590 -9.238 10.067 1.00 20.19 H ATOM 1492 HA VAL A 113 -17.735 -10.472 11.162 1.00 23.87 H ATOM 1493 HB VAL A 113 -16.363 -11.057 8.745 1.00 31.02 H ATOM 1494 HG11 VAL A 113 -18.283 -12.225 8.126 1.00 34.26 H ATOM 1495 HG12 VAL A 113 -17.664 -12.851 9.428 1.00 34.26 H ATOM 1496 HG13 VAL A 113 -18.929 -11.923 9.527 1.00 34.26 H ATOM 1497 HG21 VAL A 113 -18.027 -9.802 7.632 1.00 38.04 H ATOM 1498 HG22 VAL A 113 -18.661 -9.401 9.014 1.00 38.04 H ATOM 1499 HG23 VAL A 113 -17.231 -8.876 8.623 1.00 38.04 H ATOM 1500 N ILE A 114 -16.644 -12.361 12.307 1.00 16.75 N ANISOU 1500 N ILE A 114 1832 2032 2500 -329 -751 21 N ATOM 1501 CA ILE A 114 -16.027 -13.461 12.979 1.00 16.86 C ANISOU 1501 CA ILE A 114 1807 2125 2475 -240 -669 -49 C ATOM 1502 C ILE A 114 -16.389 -14.719 12.275 1.00 16.89 C ANISOU 1502 C ILE A 114 1614 2160 2642 -410 -490 -162 C ATOM 1503 O ILE A 114 -17.576 -15.006 12.032 1.00 19.10 O ANISOU 1503 O ILE A 114 1721 2434 3102 -397 -432 -239 O ATOM 1504 CB ILE A 114 -16.463 -13.518 14.435 1.00 18.09 C ANISOU 1504 CB ILE A 114 2104 2293 2478 -291 -767 -16 C ATOM 1505 CG1 ILE A 114 -16.146 -12.201 15.165 1.00 18.94 C ANISOU 1505 CG1 ILE A 114 2229 2404 2563 -43 -887 -174 C ATOM 1506 CG2 ILE A 114 -15.918 -14.745 15.115 1.00 20.09 C ANISOU 1506 CG2 ILE A 114 2413 2555 2666 -433 -681 109 C ATOM 1507 CD1 ILE A 114 -14.659 -11.884 15.251 1.00 19.83 C ANISOU 1507 CD1 ILE A 114 2399 2444 2694 45 -895 -282 C ATOM 1508 H ILE A 114 -17.372 -12.100 12.682 1.00 20.11 H ATOM 1509 HA ILE A 114 -15.052 -13.357 12.951 1.00 20.25 H ATOM 1510 HB ILE A 114 -17.429 -13.609 14.433 1.00 21.73 H ATOM 1511 HG12 ILE A 114 -16.578 -11.471 14.694 1.00 22.74 H ATOM 1512 HG13 ILE A 114 -16.490 -12.256 16.071 1.00 22.74 H ATOM 1513 HG21 ILE A 114 -16.211 -14.751 16.029 1.00 24.12 H ATOM 1514 HG22 ILE A 114 -16.245 -15.525 14.661 1.00 24.12 H ATOM 1515 HG23 ILE A 114 -14.959 -14.722 15.078 1.00 24.12 H ATOM 1516 HD11 ILE A 114 -14.543 -11.053 15.717 1.00 23.82 H ATOM 1517 HD12 ILE A 114 -14.216 -12.591 15.726 1.00 23.82 H ATOM 1518 HD13 ILE A 114 -14.303 -11.814 14.362 1.00 23.82 H ATOM 1519 N ASN A 115 -15.397 -15.515 11.904 1.00 15.71 N ANISOU 1519 N ASN A 115 1659 1940 2371 -532 -538 -159 N ATOM 1520 CA ASN A 115 -15.595 -16.725 11.109 1.00 15.61 C ANISOU 1520 CA ASN A 115 1800 1895 2238 -493 -574 -133 C ATOM 1521 C ASN A 115 -14.409 -17.669 11.397 1.00 16.36 C ANISOU 1521 C ASN A 115 1785 2053 2377 -420 -422 -160 C ATOM 1522 O ASN A 115 -13.574 -17.381 12.233 1.00 17.09 O ANISOU 1522 O ASN A 115 1849 2166 2479 -50 -307 -271 O ATOM 1523 CB ASN A 115 -15.809 -16.397 9.600 1.00 17.45 C ANISOU 1523 CB ASN A 115 2142 2099 2390 -343 -590 -16 C ATOM 1524 CG ASN A 115 -14.627 -15.731 8.989 1.00 19.29 C ANISOU 1524 CG ASN A 115 2461 2253 2614 -379 -463 140 C ATOM 1525 OD1 ASN A 115 -13.503 -15.973 9.353 1.00 20.31 O ANISOU 1525 OD1 ASN A 115 2562 2356 2799 -482 -232 190 O ATOM 1526 ND2 ASN A 115 -14.870 -14.815 8.081 1.00 23.11 N ANISOU 1526 ND2 ASN A 115 2958 2828 2994 -360 -249 152 N ATOM 1527 H ASN A 115 -14.573 -15.372 12.105 1.00 18.87 H ATOM 1528 HA ASN A 115 -16.407 -17.172 11.426 1.00 18.75 H ATOM 1529 HB2 ASN A 115 -15.973 -17.221 9.117 1.00 20.96 H ATOM 1530 HB3 ASN A 115 -16.569 -15.801 9.510 1.00 20.96 H ATOM 1531 HD21 ASN A 115 -14.127 -14.346 7.647 1.00 27.74 H ATOM 1532 HD22 ASN A 115 -15.795 -14.599 7.837 1.00 27.74 H ATOM 1533 N ALA A 116 -14.267 -18.716 10.611 1.00 18.11 N ANISOU 1533 N ALA A 116 2188 2174 2521 -469 -341 -27 N ATOM 1534 CA ALA A 116 -13.214 -19.678 10.876 1.00 19.56 C ANISOU 1534 CA ALA A 116 2404 2326 2701 -379 -385 -117 C ATOM 1535 C ALA A 116 -11.836 -19.079 10.712 1.00 19.61 C ANISOU 1535 C ALA A 116 2361 2396 2693 -262 -340 63 C ATOM 1536 O ALA A 116 -10.892 -19.536 11.394 1.00 21.99 O ANISOU 1536 O ALA A 116 2636 2718 3000 115 -274 483 O ATOM 1537 CB ALA A 116 -13.330 -20.875 9.882 1.00 22.47 C ANISOU 1537 CB ALA A 116 2863 2705 2971 -287 -273 -138 C ATOM 1538 H ALA A 116 -14.757 -18.894 9.927 1.00 21.75 H ATOM 1539 HA ALA A 116 -13.302 -20.019 11.790 1.00 23.49 H ATOM 1540 HB1 ALA A 116 -12.629 -21.504 10.067 1.00 26.98 H ATOM 1541 HB2 ALA A 116 -14.186 -21.295 9.998 1.00 26.98 H ATOM 1542 HB3 ALA A 116 -13.246 -20.545 8.984 1.00 26.98 H ATOM 1543 N ARG A 117 -11.703 -18.037 9.889 1.00 17.28 N ANISOU 1543 N ARG A 117 2102 2043 2420 -659 -339 -174 N ATOM 1544 CA ARG A 117 -10.405 -17.446 9.604 1.00 18.11 C ANISOU 1544 CA ARG A 117 2146 2297 2436 -837 -434 -284 C ATOM 1545 C ARG A 117 -10.091 -16.125 10.255 1.00 15.44 C ANISOU 1545 C ARG A 117 1741 2100 2026 -496 -270 -266 C ATOM 1546 O ARG A 117 -8.976 -15.652 10.216 1.00 14.81 O ANISOU 1546 O ARG A 117 1569 2140 1919 -276 -102 -466 O ATOM 1547 CB ARG A 117 -10.218 -17.314 8.101 1.00 24.36 C ANISOU 1547 CB ARG A 117 3025 3034 3195 -1053 -803 -655 C ATOM 1548 CG ARG A 117 -10.184 -18.770 7.417 1.00 32.94 C ANISOU 1548 CG ARG A 117 4128 4097 4288 -1051 -935 -789 C ATOM 1549 CD ARG A 117 -10.265 -18.755 5.959 1.00 41.12 C ANISOU 1549 CD ARG A 117 5168 5149 5308 -805 -903 -607 C ATOM 1550 NE ARG A 117 -10.149 -20.139 5.418 1.00 43.85 N ANISOU 1550 NE ARG A 117 5532 5473 5656 -723 -924 -595 N ATOM 1551 CZ ARG A 117 -10.738 -20.593 4.315 0.00 46.48 C ANISOU 1551 CZ ARG A 117 5886 5880 5894 -480 -917 -448 C ATOM 1552 NH1 ARG A 117 -11.557 -19.826 3.611 0.00 48.54 N ANISOU 1552 NH1 ARG A 117 6131 6107 6204 -401 -973 -400 N ATOM 1553 NH2 ARG A 117 -10.526 -21.845 3.929 0.00 49.20 N ANISOU 1553 NH2 ARG A 117 6215 6186 6291 -400 -978 -399 N ATOM 1554 H ARG A 117 -12.358 -17.655 9.483 1.00 20.75 H ATOM 1555 HA ARG A 117 -9.723 -18.077 9.916 1.00 21.74 H ATOM 1556 HB2 ARG A 117 -10.959 -16.813 7.724 1.00 29.24 H ATOM 1557 HB3 ARG A 117 -9.377 -16.867 7.917 1.00 29.24 H ATOM 1558 HG2 ARG A 117 -9.354 -19.208 7.661 1.00 39.54 H ATOM 1559 HG3 ARG A 117 -10.936 -19.286 7.748 1.00 39.54 H ATOM 1560 HD2 ARG A 117 -11.121 -18.389 5.687 1.00 49.36 H ATOM 1561 HD3 ARG A 117 -9.538 -18.223 5.600 1.00 49.36 H ATOM 1562 HE ARG A 117 -9.596 -20.764 5.914 1.00 52.63 H ATOM 1563 HH11 ARG A 117 -11.696 -19.012 3.850 0.00 58.26 H ATOM 1564 HH12 ARG A 117 -11.937 -20.137 2.905 0.00 58.26 H ATOM 1565 HH21 ARG A 117 -10.005 -22.353 4.387 0.00 59.05 H ATOM 1566 HH22 ARG A 117 -10.918 -22.151 3.228 0.00 59.05 H ATOM 1567 N VAL A 118 -11.082 -15.542 10.947 1.00 13.58 N ANISOU 1567 N VAL A 118 1500 1825 1835 -410 -336 -229 N ATOM 1568 CA VAL A 118 -10.926 -14.287 11.663 1.00 13.43 C ANISOU 1568 CA VAL A 118 1493 1860 1750 -321 -329 -110 C ATOM 1569 C VAL A 118 -11.695 -14.431 12.975 1.00 12.16 C ANISOU 1569 C VAL A 118 1240 1582 1797 -393 -337 -58 C ATOM 1570 O VAL A 118 -12.906 -14.585 12.977 1.00 13.48 O ANISOU 1570 O VAL A 118 1185 1932 2004 -421 -375 46 O ATOM 1571 CB VAL A 118 -11.513 -13.121 10.866 1.00 13.99 C ANISOU 1571 CB VAL A 118 1680 1800 1836 -306 -368 -121 C ATOM 1572 CG1 VAL A 118 -11.408 -11.802 11.659 1.00 15.67 C ANISOU 1572 CG1 VAL A 118 2008 1876 2069 -83 -380 -30 C ATOM 1573 CG2 VAL A 118 -10.747 -12.932 9.557 1.00 16.41 C ANISOU 1573 CG2 VAL A 118 2052 2082 2100 -546 -354 -12 C ATOM 1574 H VAL A 118 -11.874 -15.872 11.011 1.00 16.31 H ATOM 1575 HA VAL A 118 -9.980 -14.113 11.854 1.00 16.13 H ATOM 1576 HB VAL A 118 -12.456 -13.296 10.661 1.00 16.80 H ATOM 1577 HG11 VAL A 118 -11.784 -11.091 11.135 1.00 18.82 H ATOM 1578 HG12 VAL A 118 -11.893 -11.893 12.483 1.00 18.82 H ATOM 1579 HG13 VAL A 118 -10.483 -11.621 11.842 1.00 18.82 H ATOM 1580 HG21 VAL A 118 -11.132 -12.197 9.074 1.00 19.70 H ATOM 1581 HG22 VAL A 118 -9.827 -12.746 9.758 1.00 19.70 H ATOM 1582 HG23 VAL A 118 -10.813 -13.736 9.037 1.00 19.70 H ATOM 1583 N SER A 119 -10.984 -14.430 14.067 1.00 11.75 N ANISOU 1583 N SER A 119 1314 1429 1721 -237 -251 -45 N ATOM 1584 CA ASER A 119 -11.572 -14.694 15.353 0.34 11.82 C ANISOU 1584 CA ASER A 119 1438 1421 1634 -315 -183 -1 C ATOM 1585 CA BSER A 119 -11.639 -14.633 15.371 0.66 11.51 C ANISOU 1585 CA BSER A 119 1397 1224 1754 -386 -217 -19 C ATOM 1586 C SER A 119 -10.702 -14.145 16.468 1.00 10.94 C ANISOU 1586 C SER A 119 1211 1290 1654 -320 -277 12 C ATOM 1587 O SER A 119 -9.582 -13.769 16.222 1.00 12.19 O ANISOU 1587 O SER A 119 1173 1725 1732 -205 -176 -9 O ATOM 1588 CB ASER A 119 -11.756 -16.190 15.508 0.34 13.36 C ANISOU 1588 CB ASER A 119 1698 1646 1731 -242 -87 -6 C ATOM 1589 CB BSER A 119 -12.171 -16.085 15.607 0.66 12.59 C ANISOU 1589 CB BSER A 119 1542 1226 2014 -171 -227 10 C ATOM 1590 OG ASER A 119 -12.604 -16.442 16.572 0.34 14.29 O ANISOU 1590 OG ASER A 119 1837 1791 1801 -230 34 -11 O ATOM 1591 OG BSER A 119 -11.056 -16.993 15.684 0.66 13.48 O ANISOU 1591 OG BSER A 119 1596 1310 2215 -120 -255 -1 O ATOM 1592 H ASER A 119 -10.139 -14.276 14.095 1.00 14.11 H ATOM 1593 HA ASER A 119 -12.452 -14.265 15.405 0.34 14.20 H ATOM 1594 HB2ASER A 119 -12.146 -16.551 14.696 0.34 16.04 H ATOM 1595 HB3ASER A 119 -10.895 -16.603 15.680 0.34 16.04 H ATOM 1596 HG ASER A 119 -12.709 -17.250 16.663 0.34 17.16 H ATOM 1597 N THR A 120 -11.208 -14.126 17.685 1.00 11.65 N ANISOU 1597 N THR A 120 1304 1508 1617 -335 -265 113 N ATOM 1598 CA THR A 120 -10.543 -13.468 18.759 1.00 11.11 C ANISOU 1598 CA THR A 120 1287 1343 1592 -282 -167 76 C ATOM 1599 C THR A 120 -9.640 -14.378 19.566 1.00 10.99 C ANISOU 1599 C THR A 120 1321 1147 1708 -333 -92 57 C ATOM 1600 O THR A 120 -9.809 -15.611 19.597 1.00 13.00 O ANISOU 1600 O THR A 120 1570 1441 1930 -329 -386 208 O ATOM 1601 CB THR A 120 -11.579 -12.834 19.733 1.00 12.83 C ANISOU 1601 CB THR A 120 1444 1612 1819 -103 -133 312 C ATOM 1602 OG1 THR A 120 -12.357 -13.855 20.337 1.00 14.52 O ANISOU 1602 OG1 THR A 120 1521 1839 2155 -204 136 270 O ATOM 1603 CG2 THR A 120 -12.462 -11.825 19.054 1.00 14.17 C ANISOU 1603 CG2 THR A 120 1689 1748 1946 23 -248 439 C ATOM 1604 H THR A 120 -11.952 -14.496 17.908 1.00 14.00 H ATOM 1605 HA THR A 120 -9.991 -12.745 18.394 1.00 13.35 H ATOM 1606 HB THR A 120 -11.093 -12.368 20.432 1.00 15.41 H ATOM 1607 HG1 THR A 120 -12.757 -14.280 19.762 1.00 17.43 H ATOM 1608 HG21 THR A 120 -13.085 -11.457 19.684 1.00 17.01 H ATOM 1609 HG22 THR A 120 -11.928 -11.114 18.691 1.00 17.01 H ATOM 1610 HG23 THR A 120 -12.950 -12.243 18.341 1.00 17.01 H ATOM 1611 N ILE A 121 -8.711 -13.754 20.291 1.00 9.59 N ANISOU 1611 N ILE A 121 1174 999 1472 -96 -109 86 N ATOM 1612 CA ILE A 121 -7.897 -14.468 21.255 1.00 9.28 C ANISOU 1612 CA ILE A 121 1145 1028 1354 -26 -60 174 C ATOM 1613 C ILE A 121 -8.245 -13.960 22.642 1.00 9.49 C ANISOU 1613 C ILE A 121 1234 1038 1335 -29 -37 74 C ATOM 1614 O ILE A 121 -8.404 -12.768 22.853 1.00 10.21 O ANISOU 1614 O ILE A 121 1330 1055 1495 97 138 74 O ATOM 1615 CB ILE A 121 -6.390 -14.258 20.938 1.00 9.91 C ANISOU 1615 CB ILE A 121 1191 1182 1394 -98 8 199 C ATOM 1616 CG1 ILE A 121 -5.497 -15.079 21.904 1.00 11.04 C ANISOU 1616 CG1 ILE A 121 1330 1321 1544 225 -72 92 C ATOM 1617 CG2 ILE A 121 -5.946 -12.798 20.939 1.00 10.54 C ANISOU 1617 CG2 ILE A 121 1223 1305 1477 -158 -66 140 C ATOM 1618 CD1 ILE A 121 -5.572 -16.562 21.710 1.00 13.22 C ANISOU 1618 CD1 ILE A 121 1610 1605 1806 172 31 163 C ATOM 1619 H ILE A 121 -8.537 -12.913 20.238 1.00 11.53 H ATOM 1620 HA ILE A 121 -8.097 -15.427 21.211 1.00 11.16 H ATOM 1621 HB ILE A 121 -6.236 -14.601 20.044 1.00 11.91 H ATOM 1622 HG12 ILE A 121 -4.574 -14.812 21.775 1.00 13.27 H ATOM 1623 HG13 ILE A 121 -5.769 -14.888 22.815 1.00 13.27 H ATOM 1624 HG21 ILE A 121 -5.009 -12.756 20.736 1.00 12.66 H ATOM 1625 HG22 ILE A 121 -6.447 -12.319 20.275 1.00 12.66 H ATOM 1626 HG23 ILE A 121 -6.111 -12.423 21.807 1.00 12.66 H ATOM 1627 HD11 ILE A 121 -4.993 -16.989 22.345 1.00 15.87 H ATOM 1628 HD12 ILE A 121 -6.478 -16.849 21.847 1.00 15.87 H ATOM 1629 HD13 ILE A 121 -5.293 -16.774 20.816 1.00 15.87 H ATOM 1630 N SER A 122 -8.364 -14.874 23.603 1.00 9.97 N ANISOU 1630 N SER A 122 1255 1161 1373 33 -36 170 N ATOM 1631 CA ASER A 122 -8.757 -14.523 24.962 0.69 10.18 C ANISOU 1631 CA ASER A 122 1215 1223 1431 -276 -35 188 C ATOM 1632 CA BSER A 122 -8.782 -14.497 24.938 0.31 10.14 C ANISOU 1632 CA BSER A 122 1243 1150 1460 -58 48 126 C ATOM 1633 C SER A 122 -7.708 -13.721 25.676 1.00 9.16 C ANISOU 1633 C SER A 122 1043 1014 1423 -64 92 53 C ATOM 1634 O SER A 122 -6.509 -13.990 25.546 1.00 9.88 O ANISOU 1634 O SER A 122 994 1094 1667 33 53 12 O ATOM 1635 CB ASER A 122 -8.920 -15.824 25.790 0.69 12.35 C ANISOU 1635 CB ASER A 122 1598 1461 1635 -683 -54 200 C ATOM 1636 CB BSER A 122 -9.089 -15.770 25.719 0.31 11.98 C ANISOU 1636 CB BSER A 122 1598 1326 1625 -118 141 75 C ATOM 1637 OG ASER A 122 -10.029 -16.601 25.295 0.69 14.51 O ANISOU 1637 OG ASER A 122 1895 1798 1822 -883 -84 210 O ATOM 1638 OG BSER A 122 -9.381 -15.495 27.051 0.31 13.85 O ANISOU 1638 OG BSER A 122 1860 1662 1739 -153 191 76 O ATOM 1639 H ASER A 122 -8.219 -15.714 23.490 1.00 11.98 H ATOM 1640 HA ASER A 122 -9.603 -14.029 24.960 0.69 12.23 H ATOM 1641 HB2ASER A 122 -8.108 -16.349 25.719 0.69 14.84 H ATOM 1642 HB3ASER A 122 -9.085 -15.591 26.717 0.69 14.84 H ATOM 1643 HG ASER A 122 -10.379 -16.217 24.661 0.69 17.43 H ATOM 1644 N LEU A 123 -8.162 -12.766 26.494 1.00 9.55 N ANISOU 1644 N LEU A 123 1149 1112 1367 107 62 104 N ATOM 1645 CA LEU A 123 -7.301 -12.117 27.451 1.00 9.47 C ANISOU 1645 CA LEU A 123 1178 1102 1318 -76 4 65 C ATOM 1646 C LEU A 123 -6.944 -13.105 28.554 1.00 9.34 C ANISOU 1646 C LEU A 123 1197 948 1405 -101 118 84 C ATOM 1647 O LEU A 123 -7.672 -14.044 28.851 1.00 10.81 O ANISOU 1647 O LEU A 123 1254 1167 1688 -153 -97 183 O ATOM 1648 CB LEU A 123 -7.996 -10.872 28.027 1.00 10.04 C ANISOU 1648 CB LEU A 123 1361 1122 1330 97 -22 -12 C ATOM 1649 CG LEU A 123 -8.212 -9.744 27.017 1.00 11.84 C ANISOU 1649 CG LEU A 123 1572 1325 1603 273 15 59 C ATOM 1650 CD1 LEU A 123 -8.938 -8.589 27.700 1.00 13.93 C ANISOU 1650 CD1 LEU A 123 1834 1576 1881 485 30 151 C ATOM 1651 CD2 LEU A 123 -6.910 -9.288 26.363 1.00 13.80 C ANISOU 1651 CD2 LEU A 123 1846 1577 1819 -34 158 346 C ATOM 1652 H LEU A 123 -8.974 -12.483 26.505 1.00 11.47 H ATOM 1653 HA LEU A 123 -6.474 -11.834 27.007 1.00 11.38 H ATOM 1654 HB2 LEU A 123 -8.866 -11.132 28.368 1.00 12.06 H ATOM 1655 HB3 LEU A 123 -7.453 -10.520 28.750 1.00 12.06 H ATOM 1656 HG LEU A 123 -8.790 -10.073 26.311 1.00 14.23 H ATOM 1657 HD11 LEU A 123 -9.072 -7.884 27.062 1.00 16.73 H ATOM 1658 HD12 LEU A 123 -9.786 -8.901 28.025 1.00 16.73 H ATOM 1659 HD13 LEU A 123 -8.403 -8.272 28.431 1.00 16.73 H ATOM 1660 HD21 LEU A 123 -7.103 -8.583 25.742 1.00 16.57 H ATOM 1661 HD22 LEU A 123 -6.313 -8.970 27.045 1.00 16.57 H ATOM 1662 HD23 LEU A 123 -6.515 -10.032 25.903 1.00 16.57 H ATOM 1663 N PRO A 124 -5.787 -12.904 29.189 1.00 8.16 N ANISOU 1663 N PRO A 124 1041 832 1226 -35 107 116 N ATOM 1664 CA PRO A 124 -5.310 -13.904 30.165 1.00 8.77 C ANISOU 1664 CA PRO A 124 1026 997 1310 150 60 101 C ATOM 1665 C PRO A 124 -5.921 -13.714 31.524 1.00 8.90 C ANISOU 1665 C PRO A 124 1163 792 1427 56 160 22 C ATOM 1666 O PRO A 124 -6.157 -12.577 31.972 1.00 10.10 O ANISOU 1666 O PRO A 124 1348 966 1524 84 373 5 O ATOM 1667 CB PRO A 124 -3.788 -13.585 30.182 1.00 9.43 C ANISOU 1667 CB PRO A 124 1108 1124 1352 15 204 234 C ATOM 1668 CG PRO A 124 -3.699 -12.122 29.903 1.00 9.98 C ANISOU 1668 CG PRO A 124 1252 1184 1356 20 96 196 C ATOM 1669 CD PRO A 124 -4.781 -11.849 28.908 1.00 8.67 C ANISOU 1669 CD PRO A 124 1078 1002 1214 -67 98 113 C ATOM 1670 HA PRO A 124 -5.463 -14.817 29.845 1.00 10.54 H ATOM 1671 HB2 PRO A 124 -3.420 -13.791 31.056 1.00 11.33 H ATOM 1672 HB3 PRO A 124 -3.339 -14.095 29.490 1.00 11.33 H ATOM 1673 HG2 PRO A 124 -3.851 -11.623 30.721 1.00 11.99 H ATOM 1674 HG3 PRO A 124 -2.829 -11.913 29.529 1.00 11.99 H ATOM 1675 HD2 PRO A 124 -5.163 -10.970 29.057 1.00 10.42 H ATOM 1676 HD3 PRO A 124 -4.440 -11.940 28.004 1.00 10.42 H ATOM 1677 N THR A 125 -6.047 -14.823 32.255 1.00 8.74 N ANISOU 1677 N THR A 125 1184 842 1296 -84 131 77 N ATOM 1678 CA THR A 125 -6.466 -14.800 33.638 1.00 8.41 C ANISOU 1678 CA THR A 125 976 910 1311 -104 145 127 C ATOM 1679 C THR A 125 -5.349 -14.932 34.655 1.00 8.53 C ANISOU 1679 C THR A 125 976 892 1371 18 237 92 C ATOM 1680 O THR A 125 -5.586 -14.786 35.855 1.00 9.26 O ANISOU 1680 O THR A 125 1001 1127 1391 45 145 18 O ATOM 1681 CB THR A 125 -7.578 -15.845 33.884 1.00 9.80 C ANISOU 1681 CB THR A 125 1119 1145 1458 65 89 104 C ATOM 1682 OG1 THR A 125 -7.088 -17.106 33.456 1.00 11.10 O ANISOU 1682 OG1 THR A 125 1328 1159 1729 -50 205 38 O ATOM 1683 CG2 THR A 125 -8.859 -15.479 33.161 1.00 11.94 C ANISOU 1683 CG2 THR A 125 1439 1514 1582 -137 47 158 C ATOM 1684 H THR A 125 -5.889 -15.614 31.957 1.00 10.51 H ATOM 1685 HA THR A 125 -6.875 -13.924 33.799 1.00 10.11 H ATOM 1686 HB THR A 125 -7.770 -15.886 34.834 1.00 11.77 H ATOM 1687 HG1 THR A 125 -6.416 -17.305 33.881 1.00 13.33 H ATOM 1688 HG21 THR A 125 -9.532 -16.142 33.330 1.00 14.34 H ATOM 1689 HG22 THR A 125 -9.177 -14.627 33.469 1.00 14.34 H ATOM 1690 HG23 THR A 125 -8.700 -15.429 32.216 1.00 14.34 H ATOM 1691 N ALA A 127 -4.145 -15.219 34.163 1.00 9.13 N ANISOU 1691 N ALA A 127 1121 1022 1328 -56 211 158 N ATOM 1692 CA ALA A 127 -2.954 -15.245 34.994 1.00 8.87 C ANISOU 1692 CA ALA A 127 1015 1005 1350 116 79 131 C ATOM 1693 C ALA A 127 -1.792 -15.073 34.017 1.00 10.04 C ANISOU 1693 C ALA A 127 1070 1235 1509 249 137 102 C ATOM 1694 O ALA A 127 -1.856 -15.550 32.897 1.00 11.03 O ANISOU 1694 O ALA A 127 1049 1641 1500 61 241 61 O ATOM 1695 CB ALA A 127 -2.795 -16.564 35.740 1.00 10.24 C ANISOU 1695 CB ALA A 127 1195 1265 1432 117 119 32 C ATOM 1696 H ALA A 127 -3.994 -15.404 33.336 1.00 10.98 H ATOM 1697 HA ALA A 127 -2.960 -14.502 35.633 1.00 10.66 H ATOM 1698 HB1 ALA A 127 -1.996 -16.528 36.271 1.00 12.31 H ATOM 1699 HB2 ALA A 127 -3.559 -16.697 36.306 1.00 12.31 H ATOM 1700 HB3 ALA A 127 -2.732 -17.278 35.101 1.00 12.31 H ATOM 1701 N PRO A 128 -0.690 -14.459 34.471 1.00 10.60 N ANISOU 1701 N PRO A 128 1235 1114 1677 215 323 211 N ATOM 1702 CA PRO A 128 0.458 -14.324 33.541 1.00 10.75 C ANISOU 1702 CA PRO A 128 1158 1305 1622 110 237 199 C ATOM 1703 C PRO A 128 1.177 -15.685 33.427 1.00 10.03 C ANISOU 1703 C PRO A 128 978 1284 1550 140 110 228 C ATOM 1704 O PRO A 128 1.028 -16.539 34.268 1.00 10.16 O ANISOU 1704 O PRO A 128 1117 1165 1579 155 180 241 O ATOM 1705 CB PRO A 128 1.309 -13.274 34.242 1.00 12.95 C ANISOU 1705 CB PRO A 128 1482 1576 1863 6 56 15 C ATOM 1706 CG PRO A 128 1.068 -13.489 35.692 1.00 12.64 C ANISOU 1706 CG PRO A 128 1469 1470 1865 -130 -162 25 C ATOM 1707 CD PRO A 128 -0.439 -13.913 35.780 1.00 11.52 C ANISOU 1707 CD PRO A 128 1285 1324 1769 86 81 7 C ATOM 1708 HA PRO A 128 0.172 -14.006 32.659 1.00 12.91 H ATOM 1709 HB2 PRO A 128 2.245 -13.413 34.025 1.00 15.56 H ATOM 1710 HB3 PRO A 128 1.022 -12.387 33.973 1.00 15.56 H ATOM 1711 HG2 PRO A 128 1.645 -14.196 36.020 1.00 15.18 H ATOM 1712 HG3 PRO A 128 1.223 -12.664 36.177 1.00 15.18 H ATOM 1713 HD2 PRO A 128 -0.563 -14.592 36.461 1.00 13.84 H ATOM 1714 HD3 PRO A 128 -1.002 -13.139 35.940 1.00 13.84 H ATOM 1715 N PRO A 129 2.014 -15.869 32.364 1.00 10.26 N ANISOU 1715 N PRO A 129 1065 1284 1548 203 -21 398 N ATOM 1716 CA PRO A 129 2.511 -17.225 32.071 1.00 11.02 C ANISOU 1716 CA PRO A 129 1203 1402 1583 347 -13 318 C ATOM 1717 C PRO A 129 3.760 -17.511 32.898 1.00 10.07 C ANISOU 1717 C PRO A 129 1060 1163 1604 362 33 252 C ATOM 1718 O PRO A 129 4.657 -16.666 33.063 1.00 11.75 O ANISOU 1718 O PRO A 129 1294 1306 1864 38 -83 443 O ATOM 1719 CB PRO A 129 2.856 -17.163 30.599 1.00 11.74 C ANISOU 1719 CB PRO A 129 1352 1480 1627 144 -5 313 C ATOM 1720 CG PRO A 129 3.276 -15.708 30.392 1.00 11.39 C ANISOU 1720 CG PRO A 129 1301 1428 1596 135 80 358 C ATOM 1721 CD PRO A 129 2.357 -14.895 31.328 1.00 11.48 C ANISOU 1721 CD PRO A 129 1305 1465 1591 67 34 467 C ATOM 1722 HA PRO A 129 1.824 -17.904 32.236 1.00 13.24 H ATOM 1723 HB2 PRO A 129 3.589 -17.768 30.405 1.00 14.10 H ATOM 1724 HB3 PRO A 129 2.075 -17.379 30.066 1.00 14.10 H ATOM 1725 HG2 PRO A 129 4.207 -15.596 30.641 1.00 13.68 H ATOM 1726 HG3 PRO A 129 3.135 -15.454 29.466 1.00 13.68 H ATOM 1727 HD2 PRO A 129 2.839 -14.145 31.711 1.00 13.79 H ATOM 1728 HD3 PRO A 129 1.560 -14.605 30.856 1.00 13.79 H ATOM 1729 N ALA A 130 3.846 -18.705 33.418 1.00 10.97 N ANISOU 1729 N ALA A 130 1361 1232 1575 427 16 129 N ATOM 1730 CA ALA A 130 4.978 -19.125 34.188 1.00 10.25 C ANISOU 1730 CA ALA A 130 1291 1218 1387 333 42 132 C ATOM 1731 C ALA A 130 6.222 -19.214 33.314 1.00 9.90 C ANISOU 1731 C ALA A 130 1185 1269 1309 153 58 177 C ATOM 1732 O ALA A 130 6.168 -19.605 32.155 1.00 9.92 O ANISOU 1732 O ALA A 130 1259 1116 1393 162 -2 216 O ATOM 1733 CB ALA A 130 4.700 -20.484 34.849 1.00 12.05 C ANISOU 1733 CB ALA A 130 1561 1457 1560 127 145 225 C ATOM 1734 H ALA A 130 3.240 -19.309 33.336 1.00 13.18 H ATOM 1735 HA ALA A 130 5.147 -18.469 34.896 1.00 12.32 H ATOM 1736 HB1 ALA A 130 5.470 -20.746 35.359 1.00 14.47 H ATOM 1737 HB2 ALA A 130 3.938 -20.400 35.426 1.00 14.47 H ATOM 1738 HB3 ALA A 130 4.523 -21.133 34.165 1.00 14.47 H ATOM 1739 N ALA A 132 7.384 -18.987 33.933 1.00 9.73 N ANISOU 1739 N ALA A 132 1268 1128 1302 189 17 172 N ATOM 1740 CA ALA A 132 8.634 -19.282 33.284 1.00 11.04 C ANISOU 1740 CA ALA A 132 1300 1377 1517 217 71 264 C ATOM 1741 C ALA A 132 8.622 -20.723 32.752 1.00 10.02 C ANISOU 1741 C ALA A 132 1101 1137 1568 221 145 427 C ATOM 1742 O ALA A 132 8.138 -21.641 33.399 1.00 10.74 O ANISOU 1742 O ALA A 132 1242 1182 1656 223 103 446 O ATOM 1743 CB ALA A 132 9.787 -19.083 34.242 1.00 12.93 C ANISOU 1743 CB ALA A 132 1518 1656 1740 144 30 219 C ATOM 1744 H ALA A 132 7.463 -18.664 34.726 1.00 11.70 H ATOM 1745 HA ALA A 132 8.756 -18.674 32.525 1.00 13.26 H ATOM 1746 HB1 ALA A 132 10.608 -19.285 33.787 1.00 15.53 H ATOM 1747 HB2 ALA A 132 9.792 -18.169 34.538 1.00 15.53 H ATOM 1748 HB3 ALA A 132 9.674 -19.670 34.992 1.00 15.53 H ATOM 1749 N GLY A 133 9.209 -20.895 31.565 1.00 10.67 N ANISOU 1749 N GLY A 133 1325 1232 1497 270 120 402 N ATOM 1750 CA GLY A 133 9.250 -22.174 30.904 1.00 11.96 C ANISOU 1750 CA GLY A 133 1610 1300 1635 369 192 315 C ATOM 1751 C GLY A 133 8.055 -22.512 30.047 1.00 11.90 C ANISOU 1751 C GLY A 133 1704 1206 1612 373 174 181 C ATOM 1752 O GLY A 133 8.071 -23.468 29.268 1.00 13.87 O ANISOU 1752 O GLY A 133 2032 1357 1880 477 239 70 O ATOM 1753 H GLY A 133 9.594 -20.265 31.123 1.00 12.82 H ATOM 1754 HA2 GLY A 133 10.037 -22.207 30.339 1.00 14.37 H ATOM 1755 HA3 GLY A 133 9.337 -22.868 31.576 1.00 14.37 H ATOM 1756 N THR A 134 6.965 -21.741 30.178 1.00 11.15 N ANISOU 1756 N THR A 134 1559 1164 1514 157 0 212 N ATOM 1757 CA THR A 134 5.775 -22.022 29.378 1.00 11.24 C ANISOU 1757 CA THR A 134 1495 1210 1566 36 150 116 C ATOM 1758 C THR A 134 6.113 -21.830 27.916 1.00 10.85 C ANISOU 1758 C THR A 134 1570 1030 1521 170 78 122 C ATOM 1759 O THR A 134 6.747 -20.820 27.541 1.00 10.57 O ANISOU 1759 O THR A 134 1462 1020 1535 73 184 106 O ATOM 1760 CB THR A 134 4.648 -21.025 29.747 1.00 11.69 C ANISOU 1760 CB THR A 134 1448 1453 1540 36 110 148 C ATOM 1761 OG1 THR A 134 4.265 -21.193 31.118 1.00 12.81 O ANISOU 1761 OG1 THR A 134 1631 1737 1499 -53 220 254 O ATOM 1762 CG2 THR A 134 3.454 -21.242 28.900 1.00 13.42 C ANISOU 1762 CG2 THR A 134 1555 1824 1721 -26 64 49 C ATOM 1763 H THR A 134 6.895 -21.068 30.709 1.00 13.40 H ATOM 1764 HA THR A 134 5.466 -22.940 29.527 1.00 13.51 H ATOM 1765 HB THR A 134 4.962 -20.118 29.608 1.00 14.04 H ATOM 1766 HG1 THR A 134 4.908 -21.057 31.608 1.00 15.39 H ATOM 1767 HG21 THR A 134 2.765 -20.619 29.139 1.00 16.12 H ATOM 1768 HG22 THR A 134 3.681 -21.118 27.975 1.00 16.12 H ATOM 1769 HG23 THR A 134 3.123 -22.135 29.022 1.00 16.12 H ATOM 1770 N GLU A 135 5.659 -22.737 27.067 1.00 11.83 N ANISOU 1770 N GLU A 135 1782 1160 1551 51 19 130 N ATOM 1771 CA AGLU A 135 5.837 -22.648 25.608 0.49 12.16 C ANISOU 1771 CA AGLU A 135 1698 1304 1620 192 7 41 C ATOM 1772 CA BGLU A 135 5.931 -22.572 25.639 0.51 12.03 C ANISOU 1772 CA BGLU A 135 1934 1036 1600 180 79 -10 C ATOM 1773 C GLU A 135 4.777 -21.750 25.032 1.00 11.67 C ANISOU 1773 C GLU A 135 1560 1287 1588 80 -30 155 C ATOM 1774 O GLU A 135 3.587 -21.967 25.336 1.00 14.09 O ANISOU 1774 O GLU A 135 1674 1773 1907 -157 -109 402 O ATOM 1775 CB AGLU A 135 5.601 -24.035 25.001 0.49 14.72 C ANISOU 1775 CB AGLU A 135 1982 1741 1868 236 -71 -111 C ATOM 1776 CB BGLU A 135 6.162 -23.920 24.941 0.51 14.45 C ANISOU 1776 CB BGLU A 135 2499 1253 1738 266 168 -208 C ATOM 1777 CG AGLU A 135 6.573 -25.063 25.526 0.49 18.28 C ANISOU 1777 CG AGLU A 135 2414 2222 2309 427 -99 -217 C ATOM 1778 CG BGLU A 135 6.529 -23.732 23.502 0.51 17.33 C ANISOU 1778 CG BGLU A 135 2848 1657 2080 396 211 -269 C ATOM 1779 CD AGLU A 135 6.106 -26.528 25.237 0.49 22.41 C ANISOU 1779 CD AGLU A 135 3103 2767 2645 331 -213 -179 C ATOM 1780 CD BGLU A 135 6.842 -25.024 22.829 0.51 20.47 C ANISOU 1780 CD BGLU A 135 3227 2093 2459 331 243 -310 C ATOM 1781 OE1AGLU A 135 6.471 -27.474 26.002 0.49 24.85 O ANISOU 1781 OE1AGLU A 135 3492 3033 2915 340 -133 -114 O ATOM 1782 OE1BGLU A 135 5.917 -25.880 22.791 0.51 21.96 O ANISOU 1782 OE1BGLU A 135 3475 2225 2645 172 150 -602 O ATOM 1783 OE2AGLU A 135 5.437 -26.727 24.211 0.49 24.67 O ANISOU 1783 OE2AGLU A 135 3424 3082 2868 269 -149 -306 O ATOM 1784 OE2BGLU A 135 7.996 -25.159 22.370 0.51 21.23 O ANISOU 1784 OE2BGLU A 135 3332 2211 2523 614 414 -283 O ATOM 1785 H AGLU A 135 5.229 -23.440 27.312 1.00 14.20 H ATOM 1786 HA AGLU A 135 6.729 -22.318 25.374 0.49 14.61 H ATOM 1787 HB2AGLU A 135 4.704 -24.329 25.221 0.49 17.67 H ATOM 1788 HB3AGLU A 135 5.708 -23.983 24.039 0.49 17.67 H ATOM 1789 HG2AGLU A 135 7.434 -24.932 25.099 0.49 21.95 H ATOM 1790 HG3AGLU A 135 6.658 -24.958 26.486 0.49 21.95 H ATOM 1791 N CYS A 136 5.169 -20.775 24.248 1.00 10.40 N ANISOU 1791 N CYS A 136 1314 1187 1451 251 33 207 N ATOM 1792 CA CYS A 136 4.269 -19.818 23.629 1.00 9.85 C ANISOU 1792 CA CYS A 136 1227 1145 1369 -43 -19 17 C ATOM 1793 C CYS A 136 4.480 -19.781 22.142 1.00 9.79 C ANISOU 1793 C CYS A 136 1061 1272 1389 62 79 16 C ATOM 1794 O CYS A 136 5.500 -20.247 21.637 1.00 12.76 O ANISOU 1794 O CYS A 136 1184 2150 1513 381 94 62 O ATOM 1795 CB CYS A 136 4.493 -18.423 24.211 1.00 11.08 C ANISOU 1795 CB CYS A 136 1305 1434 1472 111 73 -92 C ATOM 1796 SG CYS A 136 4.367 -18.345 26.022 1.00 12.50 S ANISOU 1796 SG CYS A 136 1517 1641 1591 214 -32 -82 S ATOM 1797 H CYS A 136 5.993 -20.637 24.046 1.00 12.50 H ATOM 1798 HA CYS A 136 3.342 -20.082 23.804 1.00 11.83 H ATOM 1799 HB2 CYS A 136 5.381 -18.121 23.963 1.00 13.31 H ATOM 1800 HB3 CYS A 136 3.827 -17.821 23.842 1.00 13.31 H ATOM 1801 N LEU A 137 3.510 -19.200 21.451 1.00 8.55 N ANISOU 1801 N LEU A 137 1058 921 1268 77 65 83 N ATOM 1802 CA LEU A 137 3.541 -19.030 20.006 1.00 9.10 C ANISOU 1802 CA LEU A 137 1188 986 1284 22 73 3 C ATOM 1803 C LEU A 137 3.607 -17.544 19.691 1.00 8.33 C ANISOU 1803 C LEU A 137 1124 880 1160 49 238 -7 C ATOM 1804 O LEU A 137 2.686 -16.789 20.040 1.00 9.10 O ANISOU 1804 O LEU A 137 1029 1076 1354 9 165 17 O ATOM 1805 CB LEU A 137 2.300 -19.658 19.389 1.00 10.91 C ANISOU 1805 CB LEU A 137 1362 1286 1496 -161 69 -65 C ATOM 1806 CG LEU A 137 2.223 -19.596 17.870 1.00 12.04 C ANISOU 1806 CG LEU A 137 1551 1416 1609 -257 8 -77 C ATOM 1807 CD1 LEU A 137 3.334 -20.392 17.208 1.00 13.91 C ANISOU 1807 CD1 LEU A 137 1730 1794 1760 -222 173 -122 C ATOM 1808 CD2 LEU A 137 0.885 -20.083 17.380 1.00 13.82 C ANISOU 1808 CD2 LEU A 137 1766 1713 1770 -221 -51 -186 C ATOM 1809 H LEU A 137 2.796 -18.884 21.812 1.00 10.27 H ATOM 1810 HA LEU A 137 4.336 -19.468 19.636 1.00 10.94 H ATOM 1811 HB2 LEU A 137 2.270 -20.593 19.645 1.00 13.10 H ATOM 1812 HB3 LEU A 137 1.519 -19.201 19.739 1.00 13.10 H ATOM 1813 HG LEU A 137 2.318 -18.672 17.592 1.00 14.47 H ATOM 1814 HD11 LEU A 137 3.242 -20.323 16.255 1.00 16.70 H ATOM 1815 HD12 LEU A 137 4.181 -20.033 17.483 1.00 16.70 H ATOM 1816 HD13 LEU A 137 3.263 -21.310 17.478 1.00 16.70 H ATOM 1817 HD21 LEU A 137 0.867 -20.033 16.421 1.00 16.59 H ATOM 1818 HD22 LEU A 137 0.761 -20.992 17.663 1.00 16.59 H ATOM 1819 HD23 LEU A 137 0.196 -19.527 17.751 1.00 16.59 H ATOM 1820 N ILE A 138 4.684 -17.168 19.009 1.00 8.72 N ANISOU 1820 N ILE A 138 1154 904 1256 151 163 78 N ATOM 1821 CA ILE A 138 4.933 -15.784 18.580 1.00 9.21 C ANISOU 1821 CA ILE A 138 1187 1007 1304 -2 99 73 C ATOM 1822 C ILE A 138 4.799 -15.734 17.074 1.00 8.56 C ANISOU 1822 C ILE A 138 1061 850 1342 158 112 117 C ATOM 1823 O ILE A 138 5.246 -16.674 16.398 1.00 9.45 O ANISOU 1823 O ILE A 138 1231 1039 1321 281 100 -7 O ATOM 1824 CB ILE A 138 6.332 -15.303 19.019 1.00 10.02 C ANISOU 1824 CB ILE A 138 1315 1078 1414 -131 66 -3 C ATOM 1825 CG1 ILE A 138 6.603 -15.686 20.483 1.00 11.44 C ANISOU 1825 CG1 ILE A 138 1453 1338 1557 -47 -176 3 C ATOM 1826 CG2 ILE A 138 6.502 -13.824 18.708 1.00 10.98 C ANISOU 1826 CG2 ILE A 138 1384 1273 1514 -176 20 53 C ATOM 1827 CD1 ILE A 138 8.021 -15.303 20.921 1.00 14.73 C ANISOU 1827 CD1 ILE A 138 1927 1745 1925 -213 -426 241 C ATOM 1828 H ILE A 138 5.308 -17.711 18.774 1.00 10.48 H ATOM 1829 HA ILE A 138 4.260 -15.191 18.974 1.00 11.07 H ATOM 1830 HB ILE A 138 6.979 -15.782 18.477 1.00 12.04 H ATOM 1831 HG12 ILE A 138 5.973 -15.221 21.056 1.00 13.75 H ATOM 1832 HG13 ILE A 138 6.503 -16.646 20.586 1.00 13.75 H ATOM 1833 HG21 ILE A 138 7.377 -13.545 18.988 1.00 13.19 H ATOM 1834 HG22 ILE A 138 6.403 -13.690 17.763 1.00 13.19 H ATOM 1835 HG23 ILE A 138 5.832 -13.326 19.182 1.00 13.19 H ATOM 1836 HD11 ILE A 138 8.144 -15.560 21.838 1.00 17.69 H ATOM 1837 HD12 ILE A 138 8.654 -15.762 20.364 1.00 17.69 H ATOM 1838 HD13 ILE A 138 8.130 -14.354 20.829 1.00 17.69 H ATOM 1839 N SER A 139 4.191 -14.703 16.512 1.00 8.50 N ANISOU 1839 N SER A 139 1106 873 1251 36 26 -62 N ATOM 1840 CA SER A 139 3.910 -14.705 15.066 1.00 9.06 C ANISOU 1840 CA SER A 139 1180 962 1301 75 -28 -5 C ATOM 1841 C SER A 139 3.960 -13.325 14.483 1.00 8.24 C ANISOU 1841 C SER A 139 1095 855 1182 104 34 -14 C ATOM 1842 O SER A 139 3.790 -12.305 15.199 1.00 9.22 O ANISOU 1842 O SER A 139 1221 881 1400 29 23 12 O ATOM 1843 CB SER A 139 2.559 -15.373 14.844 1.00 9.31 C ANISOU 1843 CB SER A 139 1169 1049 1318 102 57 -46 C ATOM 1844 OG SER A 139 1.556 -14.808 15.658 1.00 9.66 O ANISOU 1844 OG SER A 139 1054 1178 1440 -11 73 -18 O ATOM 1845 H SER A 139 3.930 -13.997 16.928 1.00 10.22 H ATOM 1846 HA SER A 139 4.590 -15.246 14.613 1.00 10.89 H ATOM 1847 HB2 SER A 139 2.306 -15.264 13.914 1.00 11.18 H ATOM 1848 HB3 SER A 139 2.638 -16.317 15.054 1.00 11.18 H ATOM 1849 HG SER A 139 0.840 -15.183 15.521 1.00 11.61 H ATOM 1850 N GLY A 140 4.224 -13.260 13.186 1.00 8.50 N ANISOU 1850 N GLY A 140 1184 940 1104 26 44 42 N ATOM 1851 CA GLY A 140 4.194 -12.002 12.494 1.00 8.47 C ANISOU 1851 CA GLY A 140 1194 885 1140 53 49 69 C ATOM 1852 C GLY A 140 4.888 -12.049 11.121 1.00 9.19 C ANISOU 1852 C GLY A 140 1288 925 1278 -84 -3 -117 C ATOM 1853 O GLY A 140 5.375 -13.118 10.689 1.00 9.75 O ANISOU 1853 O GLY A 140 1404 971 1329 -14 93 -99 O ATOM 1854 H GLY A 140 4.422 -13.935 12.691 1.00 10.21 H ATOM 1855 HA2 GLY A 140 3.272 -11.732 12.359 1.00 10.18 H ATOM 1856 HA3 GLY A 140 4.633 -11.328 13.035 1.00 10.18 H ATOM 1857 N TRP A 141 4.841 -10.912 10.444 1.00 10.21 N ANISOU 1857 N TRP A 141 1430 1065 1384 37 253 60 N ATOM 1858 CA TRP A 141 5.449 -10.730 9.119 1.00 10.75 C ANISOU 1858 CA TRP A 141 1484 1221 1379 24 225 167 C ATOM 1859 C TRP A 141 6.754 -9.930 9.218 1.00 11.21 C ANISOU 1859 C TRP A 141 1658 1118 1482 74 422 54 C ATOM 1860 O TRP A 141 7.189 -9.278 8.263 1.00 12.17 O ANISOU 1860 O TRP A 141 1757 1294 1571 -65 417 223 O ATOM 1861 CB TRP A 141 4.482 -10.052 8.161 1.00 11.70 C ANISOU 1861 CB TRP A 141 1577 1435 1435 99 132 235 C ATOM 1862 CG TRP A 141 3.286 -10.887 7.797 1.00 11.03 C ANISOU 1862 CG TRP A 141 1531 1308 1352 282 50 97 C ATOM 1863 CD1 TRP A 141 3.191 -11.767 6.728 1.00 12.13 C ANISOU 1863 CD1 TRP A 141 1641 1456 1511 286 32 -19 C ATOM 1864 CD2 TRP A 141 1.995 -10.914 8.424 1.00 10.63 C ANISOU 1864 CD2 TRP A 141 1526 1231 1281 84 86 193 C ATOM 1865 NE1 TRP A 141 1.948 -12.300 6.672 1.00 12.06 N ANISOU 1865 NE1 TRP A 141 1689 1457 1435 335 -35 -11 N ATOM 1866 CE2 TRP A 141 1.174 -11.822 7.687 1.00 10.93 C ANISOU 1866 CE2 TRP A 141 1587 1210 1356 293 72 93 C ATOM 1867 CE3 TRP A 141 1.451 -10.256 9.539 1.00 10.16 C ANISOU 1867 CE3 TRP A 141 1418 1125 1316 178 66 219 C ATOM 1868 CZ2 TRP A 141 -0.165 -12.062 8.002 1.00 11.14 C ANISOU 1868 CZ2 TRP A 141 1545 1297 1390 247 -160 18 C ATOM 1869 CZ3 TRP A 141 0.114 -10.491 9.834 1.00 10.29 C ANISOU 1869 CZ3 TRP A 141 1428 1184 1298 76 -33 169 C ATOM 1870 CH2 TRP A 141 -0.692 -11.401 9.086 1.00 11.19 C ANISOU 1870 CH2 TRP A 141 1487 1405 1361 144 -161 144 C ATOM 1871 H TRP A 141 4.450 -10.204 10.736 1.00 12.26 H ATOM 1872 HA TRP A 141 5.667 -11.611 8.749 1.00 12.91 H ATOM 1873 HB2 TRP A 141 4.157 -9.236 8.573 1.00 14.06 H ATOM 1874 HB3 TRP A 141 4.954 -9.839 7.341 1.00 14.06 H ATOM 1875 HD1 TRP A 141 3.881 -11.962 6.135 1.00 14.57 H ATOM 1876 HE1 TRP A 141 1.687 -12.874 6.087 1.00 14.48 H ATOM 1877 HE3 TRP A 141 1.946 -9.631 10.017 1.00 12.20 H ATOM 1878 HZ2 TRP A 141 -0.682 -12.649 7.497 1.00 13.38 H ATOM 1879 HZ3 TRP A 141 -0.260 -10.067 10.572 1.00 12.36 H ATOM 1880 HH2 TRP A 141 -1.569 -11.566 9.349 1.00 13.45 H ATOM 1881 N GLY A 142 7.394 -10.030 10.361 1.00 11.29 N ANISOU 1881 N GLY A 142 1440 1280 1570 -93 265 -23 N ATOM 1882 CA GLY A 142 8.651 -9.348 10.569 1.00 12.86 C ANISOU 1882 CA GLY A 142 1568 1644 1673 -154 291 -221 C ATOM 1883 C GLY A 142 9.827 -9.953 9.806 1.00 11.13 C ANISOU 1883 C GLY A 142 1408 1298 1522 -146 271 -140 C ATOM 1884 O GLY A 142 9.752 -11.033 9.194 1.00 11.92 O ANISOU 1884 O GLY A 142 1515 1376 1638 -87 248 -158 O ATOM 1885 H GLY A 142 7.122 -10.489 11.035 1.00 13.56 H ATOM 1886 HA2 GLY A 142 8.559 -8.423 10.294 1.00 15.44 H ATOM 1887 HA3 GLY A 142 8.866 -9.363 11.515 1.00 15.44 H ATOM 1888 N ASN A 143 10.951 -9.251 9.897 1.00 11.34 N ANISOU 1888 N ASN A 143 1438 1322 1547 -85 305 -22 N ATOM 1889 CA ASN A 143 12.172 -9.715 9.235 1.00 11.59 C ANISOU 1889 CA ASN A 143 1360 1448 1597 -102 300 -236 C ATOM 1890 C ASN A 143 12.526 -11.111 9.704 1.00 11.48 C ANISOU 1890 C ASN A 143 1351 1517 1495 -88 320 -133 C ATOM 1891 O ASN A 143 12.349 -11.484 10.880 1.00 11.39 O ANISOU 1891 O ASN A 143 1345 1487 1495 -189 188 -178 O ATOM 1892 CB ASN A 143 13.298 -8.759 9.610 1.00 13.39 C ANISOU 1892 CB ASN A 143 1625 1601 1862 -273 435 -262 C ATOM 1893 CG ASN A 143 14.502 -8.846 8.748 1.00 14.23 C ANISOU 1893 CG ASN A 143 1801 1583 2024 -345 709 -354 C ATOM 1894 OD1 ASN A 143 14.665 -9.683 7.876 1.00 15.06 O ANISOU 1894 OD1 ASN A 143 1934 1605 2181 -299 900 -204 O ATOM 1895 ND2 ASN A 143 15.389 -7.904 8.989 1.00 16.96 N ANISOU 1895 ND2 ASN A 143 2064 2085 2296 -405 751 -433 N ATOM 1896 H ASN A 143 11.036 -8.512 10.328 1.00 13.62 H ATOM 1897 HA ASN A 143 12.055 -9.716 8.262 1.00 13.92 H ATOM 1898 HB2 ASN A 143 12.964 -7.850 9.554 1.00 16.08 H ATOM 1899 HB3 ASN A 143 13.575 -8.948 10.520 1.00 16.08 H ATOM 1900 HD21 ASN A 143 16.222 -7.872 8.474 1.00 20.37 H ATOM 1901 HD22 ASN A 143 15.217 -7.235 9.684 1.00 20.37 H ATOM 1902 N THR A 144 12.956 -11.920 8.751 1.00 11.80 N ANISOU 1902 N THR A 144 1537 1395 1551 40 420 -124 N ATOM 1903 CA THR A 144 13.331 -13.290 8.954 1.00 12.36 C ANISOU 1903 CA THR A 144 1572 1389 1735 43 389 -166 C ATOM 1904 C THR A 144 14.840 -13.509 9.072 1.00 13.61 C ANISOU 1904 C THR A 144 1553 1607 2009 87 460 -217 C ATOM 1905 O THR A 144 15.307 -14.635 9.278 1.00 14.67 O ANISOU 1905 O THR A 144 1596 1796 2181 137 407 -213 O ATOM 1906 CB THR A 144 12.777 -14.237 7.882 1.00 12.94 C ANISOU 1906 CB THR A 144 1725 1493 1697 -240 464 -103 C ATOM 1907 OG1 THR A 144 13.301 -13.848 6.610 1.00 14.87 O ANISOU 1907 OG1 THR A 144 2177 1695 1778 -21 621 -112 O ATOM 1908 CG2 THR A 144 11.256 -14.205 7.840 1.00 14.10 C ANISOU 1908 CG2 THR A 144 1827 1722 1809 -347 267 -150 C ATOM 1909 H THR A 144 13.041 -11.673 7.931 1.00 14.17 H ATOM 1910 HA THR A 144 12.941 -13.576 9.807 1.00 14.84 H ATOM 1911 HB THR A 144 13.057 -15.144 8.080 1.00 15.54 H ATOM 1912 HG1 THR A 144 13.077 -13.078 6.438 1.00 17.86 H ATOM 1913 HG21 THR A 144 10.934 -14.805 7.163 1.00 16.94 H ATOM 1914 HG22 THR A 144 10.899 -14.474 8.690 1.00 16.94 H ATOM 1915 HG23 THR A 144 10.952 -13.317 7.640 1.00 16.94 H ATOM 1916 N LEU A 145 15.622 -12.443 9.037 1.00 14.86 N ANISOU 1916 N LEU A 145 1752 1717 2176 32 524 -161 N ATOM 1917 CA LEU A 145 17.068 -12.493 9.233 1.00 17.24 C ANISOU 1917 CA LEU A 145 2094 2069 2390 -235 665 -382 C ATOM 1918 C LEU A 145 17.526 -11.586 10.368 1.00 19.63 C ANISOU 1918 C LEU A 145 2378 2448 2632 -280 905 -553 C ATOM 1919 O LEU A 145 16.898 -10.584 10.627 1.00 20.99 O ANISOU 1919 O LEU A 145 2709 2540 2725 -487 877 -633 O ATOM 1920 CB LEU A 145 17.745 -12.047 7.938 1.00 19.53 C ANISOU 1920 CB LEU A 145 2412 2397 2613 -491 718 -385 C ATOM 1921 CG LEU A 145 17.579 -12.988 6.716 1.00 21.94 C ANISOU 1921 CG LEU A 145 2679 2801 2856 -650 869 -524 C ATOM 1922 CD1 LEU A 145 18.204 -12.366 5.467 1.00 24.10 C ANISOU 1922 CD1 LEU A 145 2965 3061 3129 -702 952 -477 C ATOM 1923 CD2 LEU A 145 18.197 -14.389 7.055 1.00 24.61 C ANISOU 1923 CD2 LEU A 145 3066 3090 3195 -625 799 -682 C ATOM 1924 H LEU A 145 15.328 -11.647 8.896 1.00 17.84 H ATOM 1925 HA LEU A 145 17.344 -13.411 9.432 1.00 20.71 H ATOM 1926 HB2 LEU A 145 17.382 -11.183 7.687 1.00 23.45 H ATOM 1927 HB3 LEU A 145 18.696 -11.958 8.107 1.00 23.45 H ATOM 1928 HG LEU A 145 16.633 -13.114 6.543 1.00 26.34 H ATOM 1929 HD11 LEU A 145 18.088 -12.968 4.728 1.00 28.93 H ATOM 1930 HD12 LEU A 145 17.768 -11.532 5.282 1.00 28.93 H ATOM 1931 HD13 LEU A 145 19.140 -12.219 5.626 1.00 28.93 H ATOM 1932 HD21 LEU A 145 18.093 -14.968 6.296 1.00 29.55 H ATOM 1933 HD22 LEU A 145 19.129 -14.278 7.257 1.00 29.55 H ATOM 1934 HD23 LEU A 145 17.739 -14.757 7.814 1.00 29.55 H ATOM 1935 N SER A 146 18.554 -12.086 11.072 1.00 22.17 N ANISOU 1935 N SER A 146 2514 3012 2898 -269 968 -668 N ATOM 1936 CA SER A 146 19.270 -11.364 12.172 1.00 25.16 C ANISOU 1936 CA SER A 146 2954 3272 3333 -430 867 -635 C ATOM 1937 C SER A 146 20.201 -10.315 11.639 1.00 27.05 C ANISOU 1937 C SER A 146 2964 3670 3643 -550 852 -711 C ATOM 1938 O SER A 146 20.522 -9.375 12.354 1.00 26.77 O ANISOU 1938 O SER A 146 2599 3882 3688 -717 622 -684 O ATOM 1939 CB SER A 146 20.132 -12.307 13.024 1.00 27.32 C ANISOU 1939 CB SER A 146 3335 3491 3556 -266 817 -434 C ATOM 1940 OG SER A 146 19.370 -13.183 13.829 1.00 27.98 O ANISOU 1940 OG SER A 146 3512 3531 3589 -27 831 -231 O ATOM 1941 H SER A 146 18.874 -12.872 10.933 1.00 26.62 H ATOM 1942 HA SER A 146 18.615 -10.929 12.757 1.00 30.21 H ATOM 1943 HB2 SER A 146 20.687 -12.837 12.430 1.00 32.80 H ATOM 1944 HB3 SER A 146 20.697 -11.770 13.602 1.00 32.80 H ATOM 1945 HG SER A 146 19.868 -13.667 14.265 1.00 33.60 H ATOM 1946 N PHE A 147 20.549 -10.435 10.352 1.00 30.93 N ANISOU 1946 N PHE A 147 3653 4045 4054 -543 950 -520 N ATOM 1947 CA PHE A 147 21.403 -9.430 9.660 1.00 35.08 C ANISOU 1947 CA PHE A 147 4330 4492 4505 -326 1008 -415 C ATOM 1948 C PHE A 147 20.856 -9.528 8.220 1.00 35.73 C ANISOU 1948 C PHE A 147 4458 4597 4520 -254 1468 -483 C ATOM 1949 O PHE A 147 20.891 -10.622 7.600 1.00 37.23 O ANISOU 1949 O PHE A 147 4773 4811 4560 -292 1504 -356 O ATOM 1950 CB PHE A 147 22.928 -9.793 9.778 1.00 37.57 C ANISOU 1950 CB PHE A 147 4686 4764 4824 -213 741 -241 C ATOM 1951 CG PHE A 147 23.453 -10.093 11.262 1.00 35.67 C ANISOU 1951 CG PHE A 147 4419 4589 4543 -94 500 -137 C ATOM 1952 CD1 PHE A 147 23.564 -11.439 11.752 1.00 35.22 C ANISOU 1952 CD1 PHE A 147 4368 4499 4514 -47 375 -55 C ATOM 1953 CD2 PHE A 147 23.905 -9.018 12.130 1.00 35.62 C ANISOU 1953 CD2 PHE A 147 4424 4566 4545 -3 406 -75 C ATOM 1954 CE1 PHE A 147 24.066 -11.716 13.125 1.00 33.94 C ANISOU 1954 CE1 PHE A 147 4213 4305 4377 36 225 62 C ATOM 1955 CE2 PHE A 147 24.418 -9.288 13.494 1.00 34.17 C ANISOU 1955 CE2 PHE A 147 4233 4361 4391 102 303 -26 C ATOM 1956 CZ PHE A 147 24.479 -10.618 13.972 1.00 33.82 C ANISOU 1956 CZ PHE A 147 4183 4354 4315 172 280 61 C ATOM 1957 H PHE A 147 20.307 -11.088 9.847 1.00 37.13 H ATOM 1958 HA PHE A 147 21.244 -8.532 10.017 1.00 42.11 H ATOM 1959 HB2 PHE A 147 23.096 -10.586 9.245 1.00 45.10 H ATOM 1960 HB3 PHE A 147 23.447 -9.052 9.430 1.00 45.10 H ATOM 1961 HD1 PHE A 147 23.286 -12.146 11.215 1.00 42.27 H ATOM 1962 HD2 PHE A 147 23.857 -8.140 11.828 1.00 42.76 H ATOM 1963 HE1 PHE A 147 24.114 -12.591 13.438 1.00 40.74 H ATOM 1964 HE2 PHE A 147 24.682 -8.583 14.041 1.00 41.02 H ATOM 1965 HZ PHE A 147 24.804 -10.788 14.826 1.00 40.60 H ATOM 1966 N GLY A 148 20.277 -8.457 7.704 1.00 36.06 N ANISOU 1966 N GLY A 148 4434 4629 4638 -196 1573 -752 N ATOM 1967 CA GLY A 148 19.691 -8.474 6.361 1.00 35.63 C ANISOU 1967 CA GLY A 148 4378 4554 4607 -287 1572 -1073 C ATOM 1968 C GLY A 148 18.246 -8.001 6.394 1.00 31.15 C ANISOU 1968 C GLY A 148 3701 4073 4060 -624 1630 -1342 C ATOM 1969 O GLY A 148 17.862 -7.527 7.458 1.00 30.30 O ANISOU 1969 O GLY A 148 3440 4203 3871 -1012 1720 -1611 O ATOM 1970 H GLY A 148 20.207 -7.700 8.107 1.00 43.29 H ATOM 1971 HA2 GLY A 148 20.197 -7.891 5.775 1.00 42.77 H ATOM 1972 HA3 GLY A 148 19.716 -9.376 6.004 1.00 42.77 H ATOM 1973 N ALA A 149 17.478 -8.087 5.302 1.00 29.17 N ANISOU 1973 N ALA A 149 3594 3668 3820 -724 1674 -1212 N ATOM 1974 CA ALA A 149 16.119 -7.558 5.184 1.00 29.33 C ANISOU 1974 CA ALA A 149 3819 3601 3725 -905 1480 -1042 C ATOM 1975 C ALA A 149 15.244 -8.493 4.377 1.00 26.38 C ANISOU 1975 C ALA A 149 3679 3200 3143 -820 1307 -626 C ATOM 1976 O ALA A 149 15.040 -8.319 3.166 1.00 28.45 O ANISOU 1976 O ALA A 149 4311 3350 3148 -1040 1377 -456 O ATOM 1977 CB ALA A 149 16.116 -6.224 4.520 1.00 34.01 C ANISOU 1977 CB ALA A 149 4341 4206 4374 -862 1514 -1019 C ATOM 1978 H ALA A 149 17.743 -8.470 4.579 1.00 35.01 H ATOM 1979 HA ALA A 149 15.728 -7.461 6.078 1.00 35.21 H ATOM 1980 HB1 ALA A 149 15.212 -5.908 4.459 1.00 40.82 H ATOM 1981 HB2 ALA A 149 16.642 -5.615 5.043 1.00 40.82 H ATOM 1982 HB3 ALA A 149 16.493 -6.313 3.642 1.00 40.82 H ATOM 1983 N ASP A 150 14.846 -9.565 5.009 1.00 21.73 N ANISOU 1983 N ASP A 150 2858 2688 2712 -379 954 -160 N ATOM 1984 CA ASP A 150 14.084 -10.573 4.274 1.00 18.07 C ANISOU 1984 CA ASP A 150 2403 2218 2246 -76 798 -5 C ATOM 1985 C ASP A 150 12.700 -10.560 4.921 1.00 15.22 C ANISOU 1985 C ASP A 150 2080 1762 1940 -62 705 95 C ATOM 1986 O ASP A 150 12.437 -11.267 5.886 1.00 15.35 O ANISOU 1986 O ASP A 150 2184 1770 1877 -107 550 189 O ATOM 1987 CB ASP A 150 14.732 -11.941 4.344 1.00 19.12 C ANISOU 1987 CB ASP A 150 2610 2273 2383 131 775 18 C ATOM 1988 CG ASP A 150 14.012 -12.979 3.528 1.00 21.38 C ANISOU 1988 CG ASP A 150 3345 2271 2505 454 686 -125 C ATOM 1989 OD1 ASP A 150 12.866 -12.775 3.162 1.00 21.93 O ANISOU 1989 OD1 ASP A 150 3596 2173 2562 116 601 -318 O ATOM 1990 OD2 ASP A 150 14.568 -14.070 3.320 1.00 23.88 O ANISOU 1990 OD2 ASP A 150 3945 2424 2704 543 642 -67 O ATOM 1991 H ASP A 150 14.992 -9.744 5.837 1.00 26.10 H ATOM 1992 HA ASP A 150 13.999 -10.309 3.334 1.00 21.70 H ATOM 1993 HB2 ASP A 150 15.640 -11.876 4.010 1.00 22.96 H ATOM 1994 HB3 ASP A 150 14.739 -12.239 5.267 1.00 22.96 H ATOM 1995 N TYR A 151 11.843 -9.682 4.426 1.00 16.13 N ANISOU 1995 N TYR A 151 2157 1992 1978 56 580 226 N ATOM 1996 CA TYR A 151 10.493 -9.523 4.971 1.00 18.10 C ANISOU 1996 CA TYR A 151 2324 2414 2140 153 585 374 C ATOM 1997 C TYR A 151 9.610 -10.491 4.196 1.00 18.18 C ANISOU 1997 C TYR A 151 2226 2768 1912 38 433 368 C ATOM 1998 O TYR A 151 9.516 -10.399 2.945 1.00 21.02 O ANISOU 1998 O TYR A 151 2685 3482 1821 -91 339 429 O ATOM 1999 CB TYR A 151 10.026 -8.056 4.880 1.00 20.12 C ANISOU 1999 CB TYR A 151 2561 2587 2497 471 705 515 C ATOM 2000 CG TYR A 151 10.821 -7.166 5.793 1.00 20.78 C ANISOU 2000 CG TYR A 151 2751 2536 2608 400 799 452 C ATOM 2001 CD1 TYR A 151 10.472 -7.079 7.136 1.00 20.94 C ANISOU 2001 CD1 TYR A 151 2729 2560 2665 305 912 468 C ATOM 2002 CD2 TYR A 151 11.984 -6.505 5.372 1.00 22.84 C ANISOU 2002 CD2 TYR A 151 2982 2830 2866 49 869 135 C ATOM 2003 CE1 TYR A 151 11.225 -6.332 7.996 1.00 22.23 C ANISOU 2003 CE1 TYR A 151 2947 2662 2839 199 934 227 C ATOM 2004 CE2 TYR A 151 12.785 -5.753 6.301 1.00 23.65 C ANISOU 2004 CE2 TYR A 151 3115 2894 2977 -157 976 62 C ATOM 2005 CZ TYR A 151 12.338 -5.638 7.636 1.00 23.13 C ANISOU 2005 CZ TYR A 151 3196 2708 2886 -2 917 -15 C ATOM 2006 OH TYR A 151 13.066 -4.965 8.638 1.00 24.57 O ANISOU 2006 OH TYR A 151 3516 2671 3147 -200 873 -228 O ATOM 2007 H TYR A 151 12.016 -9.157 3.767 1.00 19.37 H ATOM 2008 HA TYR A 151 10.490 -9.789 5.914 1.00 21.73 H ATOM 2009 HB2 TYR A 151 10.142 -7.740 3.970 1.00 24.16 H ATOM 2010 HB3 TYR A 151 9.093 -8.001 5.138 1.00 24.16 H ATOM 2011 HD1 TYR A 151 9.714 -7.519 7.446 1.00 25.14 H ATOM 2012 HD2 TYR A 151 12.260 -6.581 4.487 1.00 27.42 H ATOM 2013 HE1 TYR A 151 10.954 -6.287 8.884 1.00 26.70 H ATOM 2014 HE2 TYR A 151 13.542 -5.297 6.013 1.00 28.40 H ATOM 2015 HH TYR A 151 13.090 -4.161 8.476 1.00 29.49 H ATOM 2016 N PRO A 152 8.976 -11.412 4.867 1.00 15.56 N ANISOU 2016 N PRO A 152 1857 2287 1766 317 271 344 N ATOM 2017 CA PRO A 152 8.256 -12.482 4.191 1.00 16.09 C ANISOU 2017 CA PRO A 152 1942 2281 1891 386 305 202 C ATOM 2018 C PRO A 152 6.873 -12.028 3.741 1.00 16.75 C ANISOU 2018 C PRO A 152 2056 2376 1933 484 363 267 C ATOM 2019 O PRO A 152 6.226 -11.186 4.350 1.00 18.61 O ANISOU 2019 O PRO A 152 2219 2787 2067 542 206 279 O ATOM 2020 CB PRO A 152 8.074 -13.533 5.293 1.00 15.89 C ANISOU 2020 CB PRO A 152 1970 2076 1993 413 208 108 C ATOM 2021 CG PRO A 152 7.975 -12.637 6.551 1.00 15.87 C ANISOU 2021 CG PRO A 152 2026 2024 1979 299 277 87 C ATOM 2022 CD PRO A 152 8.938 -11.533 6.353 1.00 15.83 C ANISOU 2022 CD PRO A 152 1965 2117 1932 318 323 180 C ATOM 2023 HA PRO A 152 8.766 -12.849 3.440 1.00 19.32 H ATOM 2024 HB2 PRO A 152 7.256 -14.034 5.150 1.00 19.09 H ATOM 2025 HB3 PRO A 152 8.847 -14.117 5.334 1.00 19.09 H ATOM 2026 HG2 PRO A 152 7.072 -12.290 6.631 1.00 19.06 H ATOM 2027 HG3 PRO A 152 8.210 -13.156 7.336 1.00 19.06 H ATOM 2028 HD2 PRO A 152 8.606 -10.714 6.754 1.00 19.01 H ATOM 2029 HD3 PRO A 152 9.811 -11.775 6.699 1.00 19.01 H ATOM 2030 N ASP A 153 6.371 -12.702 2.735 1.00 18.27 N ANISOU 2030 N ASP A 153 2258 2536 2150 152 375 375 N ATOM 2031 CA AASP A 153 5.008 -12.511 2.353 0.88 18.26 C ANISOU 2031 CA AASP A 153 2272 2504 2162 155 275 386 C ATOM 2032 CA BASP A 153 4.998 -12.474 2.341 0.12 17.57 C ANISOU 2032 CA BASP A 153 2264 2401 2011 185 321 263 C ATOM 2033 C ASP A 153 4.038 -13.294 3.193 1.00 16.32 C ANISOU 2033 C ASP A 153 2146 2180 1876 292 232 272 C ATOM 2034 O ASP A 153 2.966 -12.836 3.492 1.00 15.80 O ANISOU 2034 O ASP A 153 2185 1896 1920 307 11 318 O ATOM 2035 CB AASP A 153 4.774 -12.891 0.866 0.88 20.26 C ANISOU 2035 CB AASP A 153 2525 2780 2393 66 319 523 C ATOM 2036 CB BASP A 153 4.766 -12.744 0.848 0.12 18.15 C ANISOU 2036 CB BASP A 153 2400 2451 2043 126 350 125 C ATOM 2037 CG AASP A 153 5.632 -12.064 -0.090 0.88 23.77 C ANISOU 2037 CG AASP A 153 3084 3405 2544 -155 414 549 C ATOM 2038 CG BASP A 153 4.868 -14.219 0.493 0.12 18.66 C ANISOU 2038 CG BASP A 153 2511 2470 2109 49 376 -23 C ATOM 2039 OD1AASP A 153 6.026 -10.931 0.232 0.88 25.04 O ANISOU 2039 OD1AASP A 153 3292 3623 2601 -85 381 812 O ATOM 2040 OD1BASP A 153 5.509 -14.993 1.229 0.12 19.21 O ANISOU 2040 OD1BASP A 153 2588 2530 2180 7 404 -123 O ATOM 2041 OD2AASP A 153 5.742 -12.487 -1.226 0.88 26.95 O ANISOU 2041 OD2AASP A 153 3449 3980 2810 -117 579 370 O ATOM 2042 OD2BASP A 153 4.323 -14.618 -0.557 0.12 19.18 O ANISOU 2042 OD2BASP A 153 2555 2554 2178 33 399 -72 O ATOM 2043 H AASP A 153 6.802 -13.274 2.259 1.00 21.94 H ATOM 2044 HA AASP A 153 4.786 -11.562 2.454 0.88 21.92 H ATOM 2045 HB2AASP A 153 4.997 -13.826 0.739 0.88 24.33 H ATOM 2046 HB3AASP A 153 3.842 -12.738 0.643 0.88 24.33 H ATOM 2047 N GLU A 154 4.456 -14.491 3.629 1.00 15.06 N ANISOU 2047 N GLU A 154 1969 1998 1755 416 421 29 N ATOM 2048 CA GLU A 154 3.575 -15.367 4.421 1.00 13.83 C ANISOU 2048 CA GLU A 154 1833 1808 1613 292 107 -230 C ATOM 2049 C GLU A 154 3.871 -15.254 5.942 1.00 12.24 C ANISOU 2049 C GLU A 154 1593 1680 1378 421 0 -47 C ATOM 2050 O GLU A 154 4.998 -15.077 6.353 1.00 13.15 O ANISOU 2050 O GLU A 154 1663 1866 1468 265 128 58 O ATOM 2051 CB GLU A 154 3.746 -16.850 4.067 1.00 17.14 C ANISOU 2051 CB GLU A 154 2284 2189 2038 472 91 -397 C ATOM 2052 CG GLU A 154 3.362 -17.116 2.552 1.00 20.99 C ANISOU 2052 CG GLU A 154 2814 2650 2511 451 189 -449 C ATOM 2053 CD GLU A 154 3.672 -18.555 2.260 1.00 25.27 C ANISOU 2053 CD GLU A 154 3413 3215 2973 470 499 -501 C ATOM 2054 OE1 GLU A 154 4.732 -18.880 1.718 1.00 28.61 O ANISOU 2054 OE1 GLU A 154 3919 3537 3416 527 566 -592 O ATOM 2055 OE2 GLU A 154 2.879 -19.390 2.652 1.00 27.14 O ANISOU 2055 OE2 GLU A 154 3643 3545 3125 525 467 -591 O ATOM 2056 H GLU A 154 5.238 -14.818 3.482 1.00 18.08 H ATOM 2057 HA GLU A 154 2.640 -15.116 4.267 1.00 16.61 H ATOM 2058 HB2 GLU A 154 4.671 -17.108 4.199 1.00 20.58 H ATOM 2059 HB3 GLU A 154 3.163 -17.385 4.629 1.00 20.58 H ATOM 2060 HG2 GLU A 154 2.414 -16.962 2.416 1.00 25.20 H ATOM 2061 HG3 GLU A 154 3.895 -16.552 1.970 1.00 25.20 H ATOM 2062 N LEU A 155 2.804 -15.401 6.707 1.00 10.84 N ANISOU 2062 N LEU A 155 1449 1347 1323 203 34 -192 N ATOM 2063 CA LEU A 155 2.866 -15.276 8.184 1.00 10.50 C ANISOU 2063 CA LEU A 155 1473 1196 1322 270 69 -250 C ATOM 2064 C LEU A 155 3.797 -16.338 8.774 1.00 9.75 C ANISOU 2064 C LEU A 155 1380 1023 1301 108 -6 -169 C ATOM 2065 O LEU A 155 3.686 -17.530 8.432 1.00 10.99 O ANISOU 2065 O LEU A 155 1552 1126 1499 129 -59 -178 O ATOM 2066 CB LEU A 155 1.467 -15.476 8.756 1.00 10.36 C ANISOU 2066 CB LEU A 155 1345 1209 1382 172 -19 -226 C ATOM 2067 CG LEU A 155 1.370 -15.284 10.240 1.00 9.61 C ANISOU 2067 CG LEU A 155 1235 1084 1334 31 -60 -113 C ATOM 2068 CD1 LEU A 155 1.764 -13.901 10.703 1.00 10.53 C ANISOU 2068 CD1 LEU A 155 1424 1203 1374 154 -69 19 C ATOM 2069 CD2 LEU A 155 -0.039 -15.611 10.729 1.00 11.46 C ANISOU 2069 CD2 LEU A 155 1398 1398 1559 -51 65 -178 C ATOM 2070 H LEU A 155 2.017 -15.575 6.407 1.00 13.02 H ATOM 2071 HA LEU A 155 3.192 -14.386 8.435 1.00 12.62 H ATOM 2072 HB2 LEU A 155 0.867 -14.840 8.337 1.00 12.44 H ATOM 2073 HB3 LEU A 155 1.177 -16.380 8.556 1.00 12.44 H ATOM 2074 HG LEU A 155 1.975 -15.912 10.667 1.00 11.55 H ATOM 2075 HD11 LEU A 155 1.677 -13.855 11.658 1.00 12.65 H ATOM 2076 HD12 LEU A 155 2.675 -13.735 10.448 1.00 12.65 H ATOM 2077 HD13 LEU A 155 1.185 -13.257 10.289 1.00 12.65 H ATOM 2078 HD21 LEU A 155 -0.078 -15.482 11.679 1.00 13.77 H ATOM 2079 HD22 LEU A 155 -0.664 -15.028 10.293 1.00 13.77 H ATOM 2080 HD23 LEU A 155 -0.240 -16.525 10.514 1.00 13.77 H ATOM 2081 N LYS A 156 4.721 -15.902 9.656 1.00 9.77 N ANISOU 2081 N LYS A 156 1437 1020 1256 146 15 -69 N ATOM 2082 CA LYS A 156 5.663 -16.788 10.304 1.00 9.60 C ANISOU 2082 CA LYS A 156 1286 1019 1345 46 59 -12 C ATOM 2083 C LYS A 156 5.312 -16.949 11.776 1.00 8.96 C ANISOU 2083 C LYS A 156 1175 950 1279 124 68 -93 C ATOM 2084 O LYS A 156 4.693 -16.091 12.429 1.00 9.44 O ANISOU 2084 O LYS A 156 1264 1021 1301 79 38 -70 O ATOM 2085 CB LYS A 156 7.077 -16.236 10.188 1.00 11.64 C ANISOU 2085 CB LYS A 156 1492 1356 1573 -77 233 79 C ATOM 2086 CG LYS A 156 7.555 -16.025 8.739 1.00 13.84 C ANISOU 2086 CG LYS A 156 1789 1601 1867 -315 354 -282 C ATOM 2087 CD LYS A 156 7.598 -17.326 7.990 1.00 19.59 C ANISOU 2087 CD LYS A 156 2527 2386 2530 -705 939 -673 C ATOM 2088 CE LYS A 156 8.194 -17.124 6.623 1.00 25.23 C ANISOU 2088 CE LYS A 156 3221 3095 3272 -805 1289 -1073 C ATOM 2089 NZ LYS A 156 8.634 -18.564 6.161 1.00 32.05 N ANISOU 2089 NZ LYS A 156 4026 4028 4123 -814 1350 -1307 N ATOM 2090 H LYS A 156 4.810 -15.079 9.887 1.00 11.74 H ATOM 2091 HA LYS A 156 5.634 -17.669 9.876 1.00 11.54 H ATOM 2092 HB2 LYS A 156 7.114 -15.378 10.640 1.00 13.98 H ATOM 2093 HB3 LYS A 156 7.689 -16.857 10.613 1.00 13.98 H ATOM 2094 HG2 LYS A 156 6.942 -15.428 8.282 1.00 16.62 H ATOM 2095 HG3 LYS A 156 8.449 -15.648 8.748 1.00 16.62 H ATOM 2096 HD2 LYS A 156 8.148 -17.961 8.475 1.00 23.52 H ATOM 2097 HD3 LYS A 156 6.696 -17.668 7.884 1.00 23.52 H ATOM 2098 HE2 LYS A 156 7.529 -16.775 6.009 1.00 30.30 H ATOM 2099 HE3 LYS A 156 8.973 -16.547 6.673 1.00 30.30 H ATOM 2100 HZ1 LYS A 156 9.029 -18.522 5.287 1.00 38.47 H ATOM 2101 HZ2 LYS A 156 9.277 -18.924 6.776 1.00 38.47 H ATOM 2102 HZ3 LYS A 156 7.871 -19.146 6.130 1.00 38.47 H ATOM 2103 N CYS A 157 5.748 -18.083 12.311 1.00 9.42 N ANISOU 2103 N CYS A 157 1277 975 1328 218 51 -78 N ATOM 2104 CA CYS A 157 5.474 -18.599 13.620 1.00 10.21 C ANISOU 2104 CA CYS A 157 1317 1181 1379 216 -12 76 C ATOM 2105 C CYS A 157 6.750 -19.050 14.290 1.00 9.59 C ANISOU 2105 C CYS A 157 1235 1054 1355 137 51 -43 C ATOM 2106 O CYS A 157 7.663 -19.551 13.637 1.00 10.41 O ANISOU 2106 O CYS A 157 1256 1332 1368 215 139 -77 O ATOM 2107 CB CYS A 157 4.525 -19.871 13.491 1.00 11.83 C ANISOU 2107 CB CYS A 157 1561 1412 1521 396 41 55 C ATOM 2108 SG CYS A 157 2.760 -19.446 13.435 1.00 12.77 S ANISOU 2108 SG CYS A 157 1622 1483 1745 21 5 -4 S ATOM 2109 H CYS A 157 6.260 -18.616 11.871 1.00 11.32 H ATOM 2110 HA CYS A 157 5.036 -17.918 14.173 1.00 12.26 H ATOM 2111 HB2 CYS A 157 4.744 -20.345 12.673 1.00 14.21 H ATOM 2112 HB3 CYS A 157 4.669 -20.449 14.256 1.00 14.21 H ATOM 2113 N LEU A 158 6.778 -18.914 15.624 1.00 9.13 N ANISOU 2113 N LEU A 158 1167 1034 1268 130 -63 -18 N ATOM 2114 CA LEU A 158 7.876 -19.357 16.421 1.00 9.93 C ANISOU 2114 CA LEU A 158 1317 1126 1328 122 98 -77 C ATOM 2115 C LEU A 158 7.348 -19.900 17.723 1.00 9.35 C ANISOU 2115 C LEU A 158 1149 1077 1325 156 18 -45 C ATOM 2116 O LEU A 158 6.625 -19.201 18.440 1.00 9.97 O ANISOU 2116 O LEU A 158 1355 1077 1356 179 209 -57 O ATOM 2117 CB LEU A 158 8.868 -18.217 16.669 1.00 10.43 C ANISOU 2117 CB LEU A 158 1328 1212 1424 131 131 -37 C ATOM 2118 CG LEU A 158 10.079 -18.545 17.565 1.00 12.30 C ANISOU 2118 CG LEU A 158 1489 1532 1650 -32 92 -72 C ATOM 2119 CD1 LEU A 158 11.051 -19.475 16.919 1.00 14.58 C ANISOU 2119 CD1 LEU A 158 1745 1863 1931 240 -119 -215 C ATOM 2120 CD2 LEU A 158 10.828 -17.217 17.904 1.00 14.04 C ANISOU 2120 CD2 LEU A 158 1801 1695 1840 -189 199 -125 C ATOM 2121 H LEU A 158 6.145 -18.554 16.082 1.00 10.97 H ATOM 2122 HA LEU A 158 8.346 -20.078 15.954 1.00 11.93 H ATOM 2123 HB2 LEU A 158 9.215 -17.925 15.811 1.00 12.53 H ATOM 2124 HB3 LEU A 158 8.390 -17.484 17.088 1.00 12.53 H ATOM 2125 HG LEU A 158 9.771 -18.945 18.393 1.00 14.77 H ATOM 2126 HD11 LEU A 158 11.777 -19.637 17.526 1.00 17.51 H ATOM 2127 HD12 LEU A 158 10.605 -20.299 16.713 1.00 17.51 H ATOM 2128 HD13 LEU A 158 11.381 -19.071 16.113 1.00 17.51 H ATOM 2129 HD21 LEU A 158 11.583 -17.418 18.462 1.00 16.87 H ATOM 2130 HD22 LEU A 158 11.124 -16.808 17.087 1.00 16.87 H ATOM 2131 HD23 LEU A 158 10.227 -16.628 18.365 1.00 16.87 H ATOM 2132 N ASP A 159 7.803 -21.084 18.112 1.00 10.00 N ANISOU 2132 N ASP A 159 1400 1051 1350 168 49 -23 N ATOM 2133 CA ASP A 159 7.524 -21.615 19.446 1.00 10.89 C ANISOU 2133 CA ASP A 159 1564 1050 1523 -82 61 -96 C ATOM 2134 C ASP A 159 8.690 -21.279 20.360 1.00 10.39 C ANISOU 2134 C ASP A 159 1434 1064 1451 258 33 -133 C ATOM 2135 O ASP A 159 9.834 -21.587 20.029 1.00 12.25 O ANISOU 2135 O ASP A 159 1495 1618 1543 476 75 -234 O ATOM 2136 CB ASP A 159 7.277 -23.122 19.313 1.00 14.05 C ANISOU 2136 CB ASP A 159 1911 1499 1930 -282 118 -14 C ATOM 2137 CG ASP A 159 5.965 -23.350 18.470 1.00 18.66 C ANISOU 2137 CG ASP A 159 2374 2146 2568 -863 275 -151 C ATOM 2138 OD1 ASP A 159 4.802 -23.112 19.022 1.00 21.47 O ANISOU 2138 OD1 ASP A 159 2605 2716 2839 -662 134 73 O ATOM 2139 OD2 ASP A 159 6.106 -23.752 17.435 1.00 22.69 O ANISOU 2139 OD2 ASP A 159 2819 2955 2848 -1212 203 -19 O ATOM 2140 H ASP A 159 8.280 -21.604 17.621 1.00 12.02 H ATOM 2141 HA ASP A 159 6.714 -21.196 19.804 1.00 13.08 H ATOM 2142 HB2 ASP A 159 8.021 -23.537 18.851 1.00 16.88 H ATOM 2143 HB3 ASP A 159 7.155 -23.513 20.192 1.00 16.88 H ATOM 2144 N ALA A 160 8.419 -20.629 21.469 1.00 10.52 N ANISOU 2144 N ALA A 160 1435 1117 1445 189 207 90 N ATOM 2145 CA ALA A 160 9.466 -20.178 22.308 1.00 10.90 C ANISOU 2145 CA ALA A 160 1356 1261 1524 -28 211 -81 C ATOM 2146 C ALA A 160 9.006 -20.120 23.755 1.00 10.21 C ANISOU 2146 C ALA A 160 1229 1145 1504 211 189 -60 C ATOM 2147 O ALA A 160 7.836 -19.860 24.036 1.00 10.66 O ANISOU 2147 O ALA A 160 1181 1220 1650 190 299 44 O ATOM 2148 CB ALA A 160 9.866 -18.769 21.905 1.00 12.58 C ANISOU 2148 CB ALA A 160 1641 1526 1614 -303 136 -105 C ATOM 2149 H ALA A 160 7.628 -20.441 21.749 1.00 12.64 H ATOM 2150 HA ALA A 160 10.242 -20.771 22.236 1.00 13.09 H ATOM 2151 HB1 ALA A 160 10.576 -18.470 22.479 1.00 15.11 H ATOM 2152 HB2 ALA A 160 10.163 -18.778 20.993 1.00 15.11 H ATOM 2153 HB3 ALA A 160 9.105 -18.190 21.997 1.00 15.11 H ATOM 2154 N PRO A 161 9.950 -20.301 24.703 1.00 9.61 N ANISOU 2154 N PRO A 161 1168 1050 1431 213 264 144 N ATOM 2155 CA PRO A 161 9.558 -20.340 26.106 1.00 9.10 C ANISOU 2155 CA PRO A 161 1198 939 1322 130 206 181 C ATOM 2156 C PRO A 161 9.686 -18.961 26.787 1.00 8.80 C ANISOU 2156 C PRO A 161 1155 915 1273 121 78 288 C ATOM 2157 O PRO A 161 10.600 -18.186 26.525 1.00 9.89 O ANISOU 2157 O PRO A 161 1192 1103 1462 146 238 252 O ATOM 2158 CB PRO A 161 10.572 -21.311 26.710 1.00 11.92 C ANISOU 2158 CB PRO A 161 1632 1284 1615 390 253 110 C ATOM 2159 CG PRO A 161 11.830 -21.053 25.886 1.00 12.35 C ANISOU 2159 CG PRO A 161 1567 1506 1620 412 77 -19 C ATOM 2160 CD PRO A 161 11.335 -20.762 24.465 1.00 11.20 C ANISOU 2160 CD PRO A 161 1333 1393 1530 178 223 -42 C ATOM 2161 HA PRO A 161 8.648 -20.690 26.212 1.00 10.94 H ATOM 2162 HB2 PRO A 161 10.718 -21.101 27.645 1.00 14.32 H ATOM 2163 HB3 PRO A 161 10.264 -22.224 26.600 1.00 14.32 H ATOM 2164 HG2 PRO A 161 12.304 -20.287 26.247 1.00 14.84 H ATOM 2165 HG3 PRO A 161 12.395 -21.841 25.898 1.00 14.84 H ATOM 2166 HD2 PRO A 161 11.864 -20.059 24.056 1.00 13.46 H ATOM 2167 HD3 PRO A 161 11.338 -21.572 23.931 1.00 13.46 H ATOM 2168 N VAL A 162 8.846 -18.791 27.802 1.00 8.99 N ANISOU 2168 N VAL A 162 1275 890 1252 196 126 152 N ATOM 2169 CA VAL A 162 8.962 -17.644 28.703 1.00 8.79 C ANISOU 2169 CA VAL A 162 1211 885 1244 252 145 211 C ATOM 2170 C VAL A 162 10.195 -17.794 29.533 1.00 9.22 C ANISOU 2170 C VAL A 162 1232 976 1297 339 108 348 C ATOM 2171 O VAL A 162 10.466 -18.865 30.095 1.00 9.88 O ANISOU 2171 O VAL A 162 1174 996 1583 253 51 279 O ATOM 2172 CB VAL A 162 7.697 -17.572 29.593 1.00 9.05 C ANISOU 2172 CB VAL A 162 1171 1038 1231 126 49 160 C ATOM 2173 CG1 VAL A 162 7.806 -16.466 30.632 1.00 10.07 C ANISOU 2173 CG1 VAL A 162 1269 1198 1360 170 80 -7 C ATOM 2174 CG2 VAL A 162 6.476 -17.436 28.735 1.00 10.19 C ANISOU 2174 CG2 VAL A 162 1209 1205 1458 135 59 171 C ATOM 2175 H VAL A 162 8.198 -19.325 27.992 1.00 10.81 H ATOM 2176 HA VAL A 162 9.031 -16.817 28.181 1.00 10.56 H ATOM 2177 HB VAL A 162 7.617 -18.418 30.079 1.00 10.88 H ATOM 2178 HG11 VAL A 162 7.005 -16.455 31.160 1.00 12.10 H ATOM 2179 HG12 VAL A 162 8.567 -16.638 31.192 1.00 12.10 H ATOM 2180 HG13 VAL A 162 7.914 -15.625 30.182 1.00 12.10 H ATOM 2181 HG21 VAL A 162 5.701 -17.392 29.300 1.00 12.24 H ATOM 2182 HG22 VAL A 162 6.548 -16.633 28.214 1.00 12.24 H ATOM 2183 HG23 VAL A 162 6.416 -18.198 28.155 1.00 12.24 H ATOM 2184 N LEU A 163 10.956 -16.716 29.677 1.00 9.94 N ANISOU 2184 N LEU A 163 1236 1168 1373 297 -6 351 N ATOM 2185 CA LEU A 163 12.147 -16.711 30.557 1.00 10.05 C ANISOU 2185 CA LEU A 163 1182 1254 1381 139 48 350 C ATOM 2186 C LEU A 163 11.763 -16.260 31.941 1.00 9.90 C ANISOU 2186 C LEU A 163 1118 1228 1416 36 -161 148 C ATOM 2187 O LEU A 163 10.781 -15.510 32.125 1.00 10.31 O ANISOU 2187 O LEU A 163 1124 1266 1528 157 -74 52 O ATOM 2188 CB LEU A 163 13.219 -15.799 29.982 1.00 12.22 C ANISOU 2188 CB LEU A 163 1424 1496 1723 245 6 615 C ATOM 2189 CG LEU A 163 13.713 -16.147 28.552 1.00 16.16 C ANISOU 2189 CG LEU A 163 1909 1937 2293 169 395 757 C ATOM 2190 CD1 LEU A 163 14.984 -15.265 28.276 1.00 20.50 C ANISOU 2190 CD1 LEU A 163 2491 2539 2758 112 621 921 C ATOM 2191 CD2 LEU A 163 13.954 -17.625 28.286 1.00 19.60 C ANISOU 2191 CD2 LEU A 163 2436 2504 2508 216 145 601 C ATOM 2192 H LEU A 163 10.814 -15.967 29.279 1.00 11.95 H ATOM 2193 HA LEU A 163 12.512 -17.618 30.617 1.00 12.07 H ATOM 2194 HB2 LEU A 163 12.867 -14.895 29.954 1.00 14.68 H ATOM 2195 HB3 LEU A 163 13.990 -15.826 30.569 1.00 14.68 H ATOM 2196 HG LEU A 163 13.031 -15.859 27.926 1.00 19.40 H ATOM 2197 HD11 LEU A 163 15.314 -15.459 27.396 1.00 24.61 H ATOM 2198 HD12 LEU A 163 14.741 -14.338 28.338 1.00 24.61 H ATOM 2199 HD13 LEU A 163 15.656 -15.472 28.931 1.00 24.61 H ATOM 2200 HD21 LEU A 163 14.255 -17.734 27.381 1.00 23.54 H ATOM 2201 HD22 LEU A 163 14.623 -17.947 28.895 1.00 23.54 H ATOM 2202 HD23 LEU A 163 13.133 -18.104 28.418 1.00 23.54 H ATOM 2203 N THR A 164 12.565 -16.649 32.919 1.00 10.19 N ANISOU 2203 N THR A 164 1249 1179 1442 12 -231 236 N ATOM 2204 CA THR A 164 12.385 -16.056 34.233 1.00 10.84 C ANISOU 2204 CA THR A 164 1226 1376 1517 129 -205 318 C ATOM 2205 C THR A 164 12.611 -14.563 34.169 1.00 10.89 C ANISOU 2205 C THR A 164 1170 1485 1485 85 -169 234 C ATOM 2206 O THR A 164 13.418 -14.054 33.370 1.00 10.45 O ANISOU 2206 O THR A 164 1254 1275 1440 143 -115 195 O ATOM 2207 CB THR A 164 13.312 -16.647 35.282 1.00 11.38 C ANISOU 2207 CB THR A 164 1273 1469 1582 -60 -170 501 C ATOM 2208 OG1 THR A 164 14.664 -16.369 34.888 1.00 11.94 O ANISOU 2208 OG1 THR A 164 1246 1544 1747 68 -271 569 O ATOM 2209 CG2 THR A 164 13.130 -18.146 35.449 1.00 13.15 C ANISOU 2209 CG2 THR A 164 1576 1676 1744 -152 -225 664 C ATOM 2210 H THR A 164 13.196 -17.229 32.855 1.00 12.24 H ATOM 2211 HA THR A 164 11.463 -16.209 34.526 1.00 13.03 H ATOM 2212 HB THR A 164 13.137 -16.225 36.137 1.00 13.67 H ATOM 2213 HG1 THR A 164 15.186 -16.679 35.439 1.00 14.34 H ATOM 2214 HG21 THR A 164 13.733 -18.477 36.119 1.00 15.79 H ATOM 2215 HG22 THR A 164 12.229 -18.339 35.718 1.00 15.79 H ATOM 2216 HG23 THR A 164 13.310 -18.593 34.618 1.00 15.79 H ATOM 2217 N GLN A 165 11.988 -13.848 35.076 1.00 11.91 N ANISOU 2217 N GLN A 165 1300 1567 1657 263 -240 152 N ATOM 2218 CA GLN A 165 12.248 -12.433 35.160 1.00 12.34 C ANISOU 2218 CA GLN A 165 1397 1586 1705 311 -104 -13 C ATOM 2219 C GLN A 165 13.708 -12.164 35.515 1.00 11.45 C ANISOU 2219 C GLN A 165 1333 1370 1649 234 -212 48 C ATOM 2220 O GLN A 165 14.290 -11.213 34.999 1.00 11.65 O ANISOU 2220 O GLN A 165 1380 1375 1673 266 -211 26 O ATOM 2221 CB GLN A 165 11.316 -11.747 36.135 1.00 14.51 C ANISOU 2221 CB GLN A 165 1680 1943 1892 428 -11 -66 C ATOM 2222 CG GLN A 165 11.107 -10.286 35.830 1.00 16.94 C ANISOU 2222 CG GLN A 165 2097 2198 2141 714 -48 15 C ATOM 2223 CD GLN A 165 10.286 -9.970 34.532 1.00 16.44 C ANISOU 2223 CD GLN A 165 2018 2136 2092 806 -98 178 C ATOM 2224 OE1 GLN A 165 10.084 -8.785 34.252 1.00 18.28 O ANISOU 2224 OE1 GLN A 165 2268 2443 2234 373 -69 390 O ATOM 2225 NE2 GLN A 165 9.825 -11.009 33.788 1.00 15.41 N ANISOU 2225 NE2 GLN A 165 1874 2084 1898 996 -193 203 N ATOM 2226 H GLN A 165 11.420 -14.150 35.646 1.00 14.30 H ATOM 2227 HA GLN A 165 12.086 -12.038 34.277 1.00 14.82 H ATOM 2228 HB2 GLN A 165 10.452 -12.185 36.105 1.00 17.43 H ATOM 2229 HB3 GLN A 165 11.690 -11.815 37.028 1.00 17.43 H ATOM 2230 HG2 GLN A 165 10.637 -9.883 36.576 1.00 20.34 H ATOM 2231 HG3 GLN A 165 11.976 -9.867 35.732 1.00 20.34 H ATOM 2232 HE21 GLN A 165 9.372 -10.859 33.073 1.00 18.51 H ATOM 2233 HE22 GLN A 165 9.985 -11.818 34.033 1.00 18.51 H ATOM 2234 N ALA A 166 14.302 -12.992 36.365 1.00 10.75 N ANISOU 2234 N ALA A 166 1160 1365 1560 168 -253 127 N ATOM 2235 CA ALA A 166 15.702 -12.813 36.700 1.00 11.00 C ANISOU 2235 CA ALA A 166 1326 1328 1526 69 -368 221 C ATOM 2236 C ALA A 166 16.578 -12.913 35.436 1.00 10.72 C ANISOU 2236 C ALA A 166 1266 1182 1623 68 -335 216 C ATOM 2237 O ALA A 166 17.496 -12.121 35.255 1.00 11.26 O ANISOU 2237 O ALA A 166 1341 1159 1776 55 -274 157 O ATOM 2238 CB ALA A 166 16.120 -13.819 37.768 1.00 12.18 C ANISOU 2238 CB ALA A 166 1473 1548 1606 177 -377 292 C ATOM 2239 H ALA A 166 13.920 -13.656 36.756 1.00 12.92 H ATOM 2240 HA ALA A 166 15.823 -11.915 37.074 1.00 13.22 H ATOM 2241 HB1 ALA A 166 17.047 -13.686 37.976 1.00 14.62 H ATOM 2242 HB2 ALA A 166 15.584 -13.681 38.552 1.00 14.62 H ATOM 2243 HB3 ALA A 166 15.984 -14.707 37.430 1.00 14.62 H ATOM 2244 N GLU A 167 16.333 -13.902 34.565 1.00 10.10 N ANISOU 2244 N GLU A 167 1197 1108 1533 109 -290 309 N ATOM 2245 CA GLU A 167 17.192 -14.026 33.404 1.00 10.47 C ANISOU 2245 CA GLU A 167 1202 1131 1645 133 -258 -54 C ATOM 2246 C GLU A 167 16.905 -12.920 32.394 1.00 10.05 C ANISOU 2246 C GLU A 167 1107 1150 1563 70 -270 44 C ATOM 2247 O GLU A 167 17.810 -12.430 31.712 1.00 10.68 O ANISOU 2247 O GLU A 167 1118 1144 1796 -59 -203 158 O ATOM 2248 CB GLU A 167 16.922 -15.364 32.703 1.00 12.68 C ANISOU 2248 CB GLU A 167 1651 1323 1845 181 -120 -108 C ATOM 2249 CG GLU A 167 17.847 -15.634 31.616 1.00 18.09 C ANISOU 2249 CG GLU A 167 2397 2035 2440 55 203 -203 C ATOM 2250 CD GLU A 167 17.941 -17.169 31.369 1.00 21.14 C ANISOU 2250 CD GLU A 167 2688 2296 3046 205 240 -420 C ATOM 2251 OE1 GLU A 167 16.953 -17.714 30.821 1.00 21.91 O ANISOU 2251 OE1 GLU A 167 2563 2578 3182 10 352 -355 O ATOM 2252 OE2 GLU A 167 19.029 -17.777 31.783 1.00 24.40 O ANISOU 2252 OE2 GLU A 167 3205 2586 3479 266 186 -455 O ATOM 2253 H GLU A 167 15.704 -14.485 34.627 1.00 12.14 H ATOM 2254 HA GLU A 167 18.134 -13.985 33.671 1.00 12.58 H ATOM 2255 HB2 GLU A 167 17.004 -16.081 33.351 1.00 15.23 H ATOM 2256 HB3 GLU A 167 16.024 -15.352 32.336 1.00 15.23 H ATOM 2257 HG2 GLU A 167 17.528 -15.209 30.805 1.00 21.72 H ATOM 2258 HG3 GLU A 167 18.729 -15.304 31.850 1.00 21.72 H ATOM 2259 N CYS A 168 15.662 -12.458 32.300 1.00 9.51 N ANISOU 2259 N CYS A 168 1091 1048 1472 121 -300 63 N ATOM 2260 CA CYS A 168 15.303 -11.316 31.454 1.00 9.72 C ANISOU 2260 CA CYS A 168 1000 1184 1511 308 -318 1 C ATOM 2261 C CYS A 168 16.089 -10.062 31.891 1.00 10.47 C ANISOU 2261 C CYS A 168 1304 1173 1499 163 -289 -46 C ATOM 2262 O CYS A 168 16.763 -9.418 31.072 1.00 11.02 O ANISOU 2262 O CYS A 168 1355 1289 1543 231 -244 32 O ATOM 2263 CB CYS A 168 13.799 -11.097 31.533 1.00 10.70 C ANISOU 2263 CB CYS A 168 1162 1359 1545 336 -259 -38 C ATOM 2264 SG CYS A 168 13.076 -9.920 30.432 1.00 11.10 S ANISOU 2264 SG CYS A 168 1306 1156 1755 177 -235 7 S ATOM 2265 H CYS A 168 14.994 -12.794 32.724 1.00 11.42 H ATOM 2266 HA CYS A 168 15.536 -11.517 30.523 1.00 11.68 H ATOM 2267 HB2 CYS A 168 13.364 -11.947 31.362 1.00 12.86 H ATOM 2268 HB3 CYS A 168 13.587 -10.808 32.434 1.00 12.86 H ATOM 2269 N LYS A 169 16.047 -9.802 33.210 1.00 10.39 N ANISOU 2269 N LYS A 169 1472 951 1526 104 -347 -83 N ATOM 2270 CA LYS A 169 16.775 -8.657 33.741 1.00 12.41 C ANISOU 2270 CA LYS A 169 1810 1188 1718 63 -371 -187 C ATOM 2271 C LYS A 169 18.277 -8.798 33.536 1.00 13.24 C ANISOU 2271 C LYS A 169 1998 1191 1841 -197 -403 -96 C ATOM 2272 O LYS A 169 18.997 -7.829 33.281 1.00 14.44 O ANISOU 2272 O LYS A 169 2181 1233 2072 -360 -357 26 O ATOM 2273 CB LYS A 169 16.395 -8.432 35.226 1.00 14.48 C ANISOU 2273 CB LYS A 169 1991 1536 1974 230 -467 -147 C ATOM 2274 CG LYS A 169 14.932 -8.031 35.349 1.00 19.50 C ANISOU 2274 CG LYS A 169 2538 2255 2615 514 -435 -167 C ATOM 2275 CD LYS A 169 14.461 -7.830 36.831 1.00 30.11 C ANISOU 2275 CD LYS A 169 3795 3696 3951 490 -416 -242 C ATOM 2276 CE LYS A 169 14.701 -9.009 37.701 1.00 42.94 C ANISOU 2276 CE LYS A 169 5398 5372 5546 353 -405 -356 C ATOM 2277 NZ LYS A 169 16.045 -8.976 38.404 1.00 52.74 N ANISOU 2277 NZ LYS A 169 6638 6603 6797 204 -443 -404 N ATOM 2278 H LYS A 169 15.616 -10.263 33.794 1.00 12.49 H ATOM 2279 HA LYS A 169 16.492 -7.859 33.247 1.00 14.91 H ATOM 2280 HB2 LYS A 169 16.531 -9.254 35.722 1.00 17.39 H ATOM 2281 HB3 LYS A 169 16.941 -7.720 35.595 1.00 17.39 H ATOM 2282 HG2 LYS A 169 14.795 -7.195 34.878 1.00 23.41 H ATOM 2283 HG3 LYS A 169 14.382 -8.726 34.954 1.00 23.41 H ATOM 2284 HD2 LYS A 169 14.940 -7.078 37.212 1.00 36.15 H ATOM 2285 HD3 LYS A 169 13.508 -7.649 36.834 1.00 36.15 H ATOM 2286 HE2 LYS A 169 14.010 -9.043 38.381 1.00 51.54 H ATOM 2287 HE3 LYS A 169 14.669 -9.812 37.158 1.00 51.54 H ATOM 2288 HZ1 LYS A 169 16.149 -9.757 38.951 1.00 63.30 H ATOM 2289 HZ2 LYS A 169 16.753 -8.952 37.756 1.00 63.30 H ATOM 2290 HZ3 LYS A 169 16.105 -8.195 38.960 1.00 63.30 H ATOM 2291 N ALA A 170 18.801 -10.006 33.729 1.00 12.16 N ANISOU 2291 N ALA A 170 1600 1206 1815 -178 -473 4 N ATOM 2292 CA ALA A 170 20.243 -10.241 33.557 1.00 13.05 C ANISOU 2292 CA ALA A 170 1605 1425 1927 -66 -484 151 C ATOM 2293 C ALA A 170 20.656 -9.992 32.127 1.00 12.23 C ANISOU 2293 C ALA A 170 1463 1225 1960 -170 -502 -34 C ATOM 2294 O ALA A 170 21.811 -9.588 31.872 1.00 13.21 O ANISOU 2294 O ALA A 170 1404 1371 2244 -310 -622 108 O ATOM 2295 CB ALA A 170 20.606 -11.604 34.054 1.00 14.90 C ANISOU 2295 CB ALA A 170 1808 1800 2054 -109 -616 201 C ATOM 2296 H ALA A 170 18.352 -10.703 33.957 1.00 14.61 H ATOM 2297 HA ALA A 170 20.725 -9.594 34.113 1.00 15.67 H ATOM 2298 HB1 ALA A 170 21.549 -11.739 33.933 1.00 17.90 H ATOM 2299 HB2 ALA A 170 20.382 -11.667 34.985 1.00 17.90 H ATOM 2300 HB3 ALA A 170 20.115 -12.260 33.553 1.00 17.90 H ATOM 2301 N SER A 171 19.761 -10.230 31.185 1.00 10.98 N ANISOU 2301 N SER A 171 1359 1116 1697 -82 -336 -32 N ATOM 2302 CA SER A 171 20.058 -10.056 29.793 1.00 10.98 C ANISOU 2302 CA SER A 171 1323 1179 1670 106 -163 -123 C ATOM 2303 C SER A 171 20.079 -8.597 29.369 1.00 10.86 C ANISOU 2303 C SER A 171 1296 1129 1700 18 -30 -67 C ATOM 2304 O SER A 171 20.808 -8.187 28.449 1.00 11.89 O ANISOU 2304 O SER A 171 1396 1224 1900 -49 84 21 O ATOM 2305 CB SER A 171 19.058 -10.806 28.914 1.00 12.36 C ANISOU 2305 CB SER A 171 1601 1264 1831 57 -158 -131 C ATOM 2306 OG SER A 171 19.072 -12.226 29.164 1.00 13.76 O ANISOU 2306 OG SER A 171 1794 1285 2151 51 -146 -188 O ATOM 2307 H SER A 171 18.959 -10.500 31.338 1.00 13.19 H ATOM 2308 HA SER A 171 20.946 -10.428 29.615 1.00 13.19 H ATOM 2309 HB2 SER A 171 18.167 -10.467 29.096 1.00 14.84 H ATOM 2310 HB3 SER A 171 19.284 -10.652 27.983 1.00 14.84 H ATOM 2311 HG SER A 171 19.623 -12.402 29.746 1.00 16.53 H ATOM 2312 N TYR A 172 19.265 -7.797 30.041 1.00 9.31 N ANISOU 2312 N TYR A 172 1133 932 1472 -84 -91 -133 N ATOM 2313 CA TYR A 172 19.100 -6.358 29.767 1.00 9.61 C ANISOU 2313 CA TYR A 172 1121 1008 1523 -13 -140 -55 C ATOM 2314 C TYR A 172 19.166 -5.567 31.046 1.00 9.56 C ANISOU 2314 C TYR A 172 1111 964 1558 -1 -131 -192 C ATOM 2315 O TYR A 172 18.148 -5.059 31.555 1.00 9.87 O ANISOU 2315 O TYR A 172 1137 1083 1529 -91 -184 -169 O ATOM 2316 CB TYR A 172 17.771 -6.101 29.050 1.00 9.98 C ANISOU 2316 CB TYR A 172 1140 1233 1421 96 -189 -143 C ATOM 2317 CG TYR A 172 17.664 -6.743 27.709 1.00 8.69 C ANISOU 2317 CG TYR A 172 979 1016 1306 82 -242 -72 C ATOM 2318 CD1 TYR A 172 18.369 -6.253 26.621 1.00 10.13 C ANISOU 2318 CD1 TYR A 172 1308 1094 1449 -125 73 -4 C ATOM 2319 CD2 TYR A 172 16.839 -7.831 27.470 1.00 8.77 C ANISOU 2319 CD2 TYR A 172 997 959 1375 -52 -139 -71 C ATOM 2320 CE1 TYR A 172 18.221 -6.797 25.361 1.00 10.15 C ANISOU 2320 CE1 TYR A 172 1305 1127 1426 -187 -41 37 C ATOM 2321 CE2 TYR A 172 16.680 -8.400 26.206 1.00 9.16 C ANISOU 2321 CE2 TYR A 172 961 1130 1389 -37 -55 -56 C ATOM 2322 CZ TYR A 172 17.359 -7.854 25.152 1.00 8.97 C ANISOU 2322 CZ TYR A 172 981 1065 1361 -83 -103 -62 C ATOM 2323 OH TYR A 172 17.233 -8.332 23.886 1.00 9.80 O ANISOU 2323 OH TYR A 172 1157 1143 1423 30 -102 -47 O ATOM 2324 H TYR A 172 18.773 -8.070 30.691 1.00 11.19 H ATOM 2325 HA TYR A 172 19.826 -6.056 29.182 1.00 11.55 H ATOM 2326 HB2 TYR A 172 17.050 -6.444 29.600 1.00 11.99 H ATOM 2327 HB3 TYR A 172 17.664 -5.144 28.928 1.00 11.99 H ATOM 2328 HD1 TYR A 172 18.918 -5.510 26.733 1.00 12.18 H ATOM 2329 HD2 TYR A 172 16.342 -8.175 28.177 1.00 10.53 H ATOM 2330 HE1 TYR A 172 18.682 -6.429 24.642 1.00 12.20 H ATOM 2331 HE2 TYR A 172 16.095 -9.111 26.076 1.00 11.00 H ATOM 2332 HH TYR A 172 16.455 -8.265 23.636 1.00 11.77 H ATOM 2333 N PRO A 173 20.344 -5.488 31.682 1.00 10.44 N ANISOU 2333 N PRO A 173 1132 1199 1634 -125 -202 -193 N ATOM 2334 CA PRO A 173 20.401 -4.893 33.016 1.00 10.55 C ANISOU 2334 CA PRO A 173 1284 1104 1620 -16 -415 -152 C ATOM 2335 C PRO A 173 19.887 -3.479 33.082 1.00 10.86 C ANISOU 2335 C PRO A 173 1383 1133 1609 -267 -427 -193 C ATOM 2336 O PRO A 173 20.183 -2.621 32.277 1.00 11.71 O ANISOU 2336 O PRO A 173 1460 1214 1776 -130 -235 7 O ATOM 2337 CB PRO A 173 21.907 -4.989 33.391 1.00 11.93 C ANISOU 2337 CB PRO A 173 1496 1364 1674 -99 -473 -278 C ATOM 2338 CG PRO A 173 22.454 -6.110 32.521 1.00 12.78 C ANISOU 2338 CG PRO A 173 1580 1465 1810 -95 -328 -275 C ATOM 2339 CD PRO A 173 21.658 -6.025 31.263 1.00 12.13 C ANISOU 2339 CD PRO A 173 1455 1442 1714 -107 -270 -251 C ATOM 2340 HA PRO A 173 19.886 -5.442 33.644 1.00 12.67 H ATOM 2341 HB2 PRO A 173 22.349 -4.150 33.190 1.00 14.33 H ATOM 2342 HB3 PRO A 173 21.997 -5.209 34.332 1.00 14.33 H ATOM 2343 HG2 PRO A 173 23.396 -5.959 32.345 1.00 15.35 H ATOM 2344 HG3 PRO A 173 22.317 -6.964 32.960 1.00 15.35 H ATOM 2345 HD2 PRO A 173 22.084 -5.418 30.638 1.00 14.58 H ATOM 2346 HD3 PRO A 173 21.550 -6.908 30.876 1.00 14.58 H ATOM 2347 N GLY A 174 18.984 -3.273 34.051 1.00 11.38 N ANISOU 2347 N GLY A 174 1449 1260 1616 -234 -371 -234 N ATOM 2348 CA GLY A 174 18.388 -1.971 34.274 1.00 11.81 C ANISOU 2348 CA GLY A 174 1512 1352 1623 -6 -300 -195 C ATOM 2349 C GLY A 174 17.192 -1.643 33.362 1.00 10.62 C ANISOU 2349 C GLY A 174 1306 1159 1569 -92 -300 -227 C ATOM 2350 O GLY A 174 16.513 -0.628 33.618 1.00 12.03 O ANISOU 2350 O GLY A 174 1520 1283 1768 -20 -279 -326 O ATOM 2351 H GLY A 174 18.706 -3.883 34.590 1.00 13.67 H ATOM 2352 HA2 GLY A 174 18.086 -1.916 35.194 1.00 14.19 H ATOM 2353 HA3 GLY A 174 19.063 -1.288 34.138 1.00 14.19 H ATOM 2354 N LYS A 175 16.938 -2.428 32.319 1.00 9.79 N ANISOU 2354 N LYS A 175 1153 1051 1518 -78 -276 -117 N ATOM 2355 CA LYS A 175 16.016 -2.030 31.286 1.00 10.33 C ANISOU 2355 CA LYS A 175 1194 1200 1529 54 -190 -46 C ATOM 2356 C LYS A 175 14.614 -2.666 31.373 1.00 10.38 C ANISOU 2356 C LYS A 175 1226 1102 1615 54 -233 59 C ATOM 2357 O LYS A 175 13.723 -2.239 30.637 1.00 11.51 O ANISOU 2357 O LYS A 175 1339 1125 1910 -25 -283 134 O ATOM 2358 CB LYS A 175 16.615 -2.321 29.933 1.00 10.86 C ANISOU 2358 CB LYS A 175 1304 1304 1519 -23 -189 -113 C ATOM 2359 CG LYS A 175 17.842 -1.462 29.647 1.00 12.67 C ANISOU 2359 CG LYS A 175 1461 1588 1763 126 -143 -57 C ATOM 2360 CD LYS A 175 18.517 -1.836 28.365 1.00 15.52 C ANISOU 2360 CD LYS A 175 1842 1976 2079 153 -117 -23 C ATOM 2361 CE LYS A 175 19.606 -0.789 28.099 1.00 18.37 C ANISOU 2361 CE LYS A 175 2245 2253 2482 337 91 158 C ATOM 2362 NZ LYS A 175 18.972 0.379 27.453 1.00 22.79 N ANISOU 2362 NZ LYS A 175 2873 2774 3014 326 273 81 N ATOM 2363 H LYS A 175 17.295 -3.200 32.194 1.00 11.77 H ATOM 2364 HA LYS A 175 15.895 -1.060 31.346 1.00 12.40 H ATOM 2365 HB2 LYS A 175 16.885 -3.252 29.899 1.00 13.05 H ATOM 2366 HB3 LYS A 175 15.954 -2.140 29.247 1.00 13.05 H ATOM 2367 HG2 LYS A 175 17.570 -0.533 29.585 1.00 15.21 H ATOM 2368 HG3 LYS A 175 18.481 -1.574 30.368 1.00 15.21 H ATOM 2369 HD2 LYS A 175 18.930 -2.709 28.449 1.00 18.64 H ATOM 2370 HD3 LYS A 175 17.878 -1.820 27.635 1.00 18.64 H ATOM 2371 HE2 LYS A 175 20.005 -0.507 28.937 1.00 22.06 H ATOM 2372 HE3 LYS A 175 20.277 -1.154 27.501 1.00 22.06 H ATOM 2373 HZ1 LYS A 175 19.632 1.053 27.274 1.00 27.37 H ATOM 2374 HZ2 LYS A 175 18.564 0.115 26.625 1.00 27.37 H ATOM 2375 HZ3 LYS A 175 18.299 0.748 28.029 1.00 27.37 H ATOM 2376 N ILE A 176 14.465 -3.687 32.196 1.00 10.04 N ANISOU 2376 N ILE A 176 1167 1069 1576 20 -224 -1 N ATOM 2377 CA ILE A 176 13.223 -4.440 32.194 1.00 9.73 C ANISOU 2377 CA ILE A 176 1228 1090 1380 -45 -225 -43 C ATOM 2378 C ILE A 176 12.308 -3.884 33.270 1.00 10.69 C ANISOU 2378 C ILE A 176 1331 1350 1380 53 -156 -72 C ATOM 2379 O ILE A 176 12.582 -4.043 34.468 1.00 13.62 O ANISOU 2379 O ILE A 176 1479 2233 1462 276 -172 -31 O ATOM 2380 CB ILE A 176 13.508 -5.949 32.423 1.00 10.07 C ANISOU 2380 CB ILE A 176 1252 1105 1467 -126 -86 68 C ATOM 2381 CG1 ILE A 176 14.438 -6.500 31.331 1.00 10.26 C ANISOU 2381 CG1 ILE A 176 1208 1178 1514 -59 -78 -72 C ATOM 2382 CG2 ILE A 176 12.233 -6.707 32.502 1.00 11.37 C ANISOU 2382 CG2 ILE A 176 1396 1371 1552 -4 -42 211 C ATOM 2383 CD1 ILE A 176 13.951 -6.313 29.923 1.00 11.68 C ANISOU 2383 CD1 ILE A 176 1376 1453 1611 200 -14 -118 C ATOM 2384 H ILE A 176 15.055 -3.962 32.758 1.00 12.06 H ATOM 2385 HA ILE A 176 12.780 -4.337 31.326 1.00 11.69 H ATOM 2386 HB ILE A 176 13.963 -6.041 33.275 1.00 12.09 H ATOM 2387 HG12 ILE A 176 15.297 -6.056 31.404 1.00 12.33 H ATOM 2388 HG13 ILE A 176 14.552 -7.453 31.476 1.00 12.33 H ATOM 2389 HG21 ILE A 176 12.431 -7.636 32.643 1.00 13.66 H ATOM 2390 HG22 ILE A 176 11.713 -6.367 33.233 1.00 13.66 H ATOM 2391 HG23 ILE A 176 11.753 -6.596 31.678 1.00 13.66 H ATOM 2392 HD11 ILE A 176 14.595 -6.688 29.317 1.00 14.04 H ATOM 2393 HD12 ILE A 176 13.108 -6.761 29.822 1.00 14.04 H ATOM 2394 HD13 ILE A 176 13.847 -5.374 29.751 1.00 14.04 H ATOM 2395 N THR A 177 11.236 -3.258 32.853 1.00 10.25 N ANISOU 2395 N THR A 177 1254 1263 1378 72 -151 -121 N ATOM 2396 CA THR A 177 10.278 -2.664 33.784 1.00 10.47 C ANISOU 2396 CA THR A 177 1299 1278 1401 108 -236 -230 C ATOM 2397 C THR A 177 9.251 -3.731 34.152 1.00 10.58 C ANISOU 2397 C THR A 177 1308 1320 1393 31 -138 -228 C ATOM 2398 O THR A 177 9.166 -4.809 33.577 1.00 10.84 O ANISOU 2398 O THR A 177 1165 1393 1561 16 -7 -88 O ATOM 2399 CB THR A 177 9.566 -1.456 33.213 1.00 11.01 C ANISOU 2399 CB THR A 177 1356 1294 1533 -15 -118 -148 C ATOM 2400 OG1 THR A 177 8.673 -1.933 32.208 1.00 11.26 O ANISOU 2400 OG1 THR A 177 1308 1383 1585 -16 -266 -226 O ATOM 2401 CG2 THR A 177 10.555 -0.439 32.619 1.00 12.61 C ANISOU 2401 CG2 THR A 177 1537 1528 1727 -37 -190 -104 C ATOM 2402 H THR A 177 11.027 -3.155 32.026 1.00 12.31 H ATOM 2403 HA THR A 177 10.745 -2.390 34.601 1.00 12.58 H ATOM 2404 HB THR A 177 9.059 -1.018 33.914 1.00 13.23 H ATOM 2405 HG1 THR A 177 8.267 -1.305 31.872 1.00 13.52 H ATOM 2406 HG21 THR A 177 10.077 0.314 32.265 1.00 15.15 H ATOM 2407 HG22 THR A 177 11.159 -0.134 33.299 1.00 15.15 H ATOM 2408 HG23 THR A 177 11.060 -0.848 31.913 1.00 15.15 H ATOM 2409 N ASN A 178 8.324 -3.337 35.027 1.00 11.80 N ANISOU 2409 N ASN A 178 1408 1564 1513 129 -127 -205 N ATOM 2410 CA ASN A 178 7.237 -4.217 35.420 1.00 13.36 C ANISOU 2410 CA ASN A 178 1436 1868 1772 5 -3 -154 C ATOM 2411 C ASN A 178 6.248 -4.523 34.318 1.00 10.67 C ANISOU 2411 C ASN A 178 1073 1525 1458 -74 8 -13 C ATOM 2412 O ASN A 178 5.495 -5.479 34.433 1.00 11.52 O ANISOU 2412 O ASN A 178 1261 1565 1551 -180 122 -19 O ATOM 2413 CB ASN A 178 6.460 -3.670 36.632 1.00 20.90 C ANISOU 2413 CB ASN A 178 2491 2826 2623 -97 -14 -422 C ATOM 2414 CG ASN A 178 7.277 -3.720 37.919 1.00 28.42 C ANISOU 2414 CG ASN A 178 3554 3840 3406 16 132 -547 C ATOM 2415 OD1 ASN A 178 6.997 -2.932 38.855 1.00 32.29 O ANISOU 2415 OD1 ASN A 178 4096 4559 3616 -6 280 -485 O ATOM 2416 ND2 ASN A 178 8.185 -4.661 38.007 1.00 33.99 N ANISOU 2416 ND2 ASN A 178 4283 4396 4237 25 -1 -466 N ATOM 2417 H ASN A 178 8.307 -2.565 35.404 1.00 14.18 H ATOM 2418 HA ASN A 178 7.629 -5.072 35.695 1.00 16.05 H ATOM 2419 HB2 ASN A 178 6.221 -2.745 36.464 1.00 25.09 H ATOM 2420 HB3 ASN A 178 5.660 -4.203 36.763 1.00 25.09 H ATOM 2421 HD21 ASN A 178 8.736 -4.736 38.814 1.00 40.80 H ATOM 2422 HD22 ASN A 178 8.313 -5.289 37.266 1.00 40.80 H ATOM 2423 N SER A 179 6.273 -3.768 33.209 1.00 9.40 N ANISOU 2423 N SER A 179 1187 1152 1232 68 58 -116 N ATOM 2424 CA SER A 179 5.400 -4.063 32.092 1.00 8.88 C ANISOU 2424 CA SER A 179 1103 1038 1233 -36 106 -151 C ATOM 2425 C SER A 179 5.948 -5.107 31.130 1.00 8.01 C ANISOU 2425 C SER A 179 882 952 1209 -74 -50 -18 C ATOM 2426 O SER A 179 5.272 -5.437 30.173 1.00 9.32 O ANISOU 2426 O SER A 179 984 1202 1356 -43 -131 -183 O ATOM 2427 CB SER A 179 5.075 -2.793 31.299 1.00 8.96 C ANISOU 2427 CB SER A 179 1023 1077 1305 176 54 -55 C ATOM 2428 OG SER A 179 6.208 -2.331 30.568 1.00 9.59 O ANISOU 2428 OG SER A 179 1251 1015 1377 -21 -3 117 O ATOM 2429 H SER A 179 6.786 -3.087 33.091 1.00 11.29 H ATOM 2430 HA SER A 179 4.555 -4.410 32.448 1.00 10.67 H ATOM 2431 HB2 SER A 179 4.357 -2.987 30.676 1.00 10.77 H ATOM 2432 HB3 SER A 179 4.796 -2.099 31.917 1.00 10.77 H ATOM 2433 HG SER A 179 6.014 -1.652 30.151 1.00 11.52 H ATOM 2434 N MET A 180 7.181 -5.575 31.354 1.00 8.06 N ANISOU 2434 N MET A 180 882 1063 1116 97 -10 5 N ATOM 2435 CA MET A 180 7.918 -6.323 30.341 1.00 8.57 C ANISOU 2435 CA MET A 180 1047 987 1221 33 46 -18 C ATOM 2436 C MET A 180 8.228 -7.731 30.831 1.00 8.69 C ANISOU 2436 C MET A 180 1194 946 1161 145 -114 -38 C ATOM 2437 O MET A 180 8.421 -7.970 32.031 1.00 10.25 O ANISOU 2437 O MET A 180 1500 1163 1233 161 -70 -17 O ATOM 2438 CB MET A 180 9.281 -5.628 30.088 1.00 8.35 C ANISOU 2438 CB MET A 180 946 982 1246 105 -60 0 C ATOM 2439 CG MET A 180 9.095 -4.267 29.500 1.00 8.91 C ANISOU 2439 CG MET A 180 1078 1001 1305 5 -128 -48 C ATOM 2440 SD MET A 180 10.725 -3.453 29.409 1.00 9.20 S ANISOU 2440 SD MET A 180 1070 1019 1407 -8 -20 1 S ATOM 2441 CE MET A 180 10.230 -1.784 29.104 1.00 10.18 C ANISOU 2441 CE MET A 180 1272 1168 1428 -152 -2 -24 C ATOM 2442 H MET A 180 7.612 -5.468 32.091 1.00 9.68 H ATOM 2443 HA MET A 180 7.410 -6.357 29.504 1.00 10.30 H ATOM 2444 HB2 MET A 180 9.753 -5.534 30.930 1.00 10.04 H ATOM 2445 HB3 MET A 180 9.802 -6.160 29.467 1.00 10.04 H ATOM 2446 HG2 MET A 180 8.732 -4.342 28.604 1.00 10.70 H ATOM 2447 HG3 MET A 180 8.512 -3.739 30.067 1.00 10.70 H ATOM 2448 HE1 MET A 180 11.014 -1.234 29.034 1.00 12.23 H ATOM 2449 HE2 MET A 180 9.732 -1.751 28.285 1.00 12.23 H ATOM 2450 HE3 MET A 180 9.684 -1.482 29.833 1.00 12.23 H ATOM 2451 N PHE A 181 8.338 -8.669 29.895 1.00 8.24 N ANISOU 2451 N PHE A 181 987 1001 1143 127 -195 5 N ATOM 2452 CA PHE A 181 8.876 -9.993 30.174 1.00 7.48 C ANISOU 2452 CA PHE A 181 897 783 1161 198 -169 87 C ATOM 2453 C PHE A 181 9.578 -10.502 28.898 1.00 7.66 C ANISOU 2453 C PHE A 181 856 843 1212 82 -110 148 C ATOM 2454 O PHE A 181 9.345 -9.954 27.824 1.00 9.01 O ANISOU 2454 O PHE A 181 1075 1029 1319 214 24 242 O ATOM 2455 CB PHE A 181 7.807 -10.960 30.685 1.00 8.84 C ANISOU 2455 CB PHE A 181 1050 1069 1241 131 39 92 C ATOM 2456 CG PHE A 181 6.796 -11.432 29.665 1.00 7.79 C ANISOU 2456 CG PHE A 181 895 769 1296 141 233 154 C ATOM 2457 CD1 PHE A 181 5.889 -10.588 29.054 1.00 7.97 C ANISOU 2457 CD1 PHE A 181 1002 780 1247 37 105 53 C ATOM 2458 CD2 PHE A 181 6.715 -12.767 29.354 1.00 9.45 C ANISOU 2458 CD2 PHE A 181 1123 981 1485 119 18 41 C ATOM 2459 CE1 PHE A 181 4.931 -11.047 28.199 1.00 8.65 C ANISOU 2459 CE1 PHE A 181 1113 881 1293 -23 90 -30 C ATOM 2460 CE2 PHE A 181 5.747 -13.252 28.467 1.00 10.14 C ANISOU 2460 CE2 PHE A 181 1316 969 1566 38 -132 -13 C ATOM 2461 CZ PHE A 181 4.854 -12.352 27.874 1.00 9.05 C ANISOU 2461 CZ PHE A 181 1092 888 1459 -42 -51 61 C ATOM 2462 H PHE A 181 8.102 -8.558 29.076 1.00 9.90 H ATOM 2463 HA PHE A 181 9.558 -9.912 30.874 1.00 8.99 H ATOM 2464 HB2 PHE A 181 8.251 -11.747 31.037 1.00 10.63 H ATOM 2465 HB3 PHE A 181 7.316 -10.522 31.397 1.00 10.63 H ATOM 2466 HD1 PHE A 181 5.904 -9.683 29.267 1.00 9.58 H ATOM 2467 HD2 PHE A 181 7.301 -13.365 29.759 1.00 11.35 H ATOM 2468 HE1 PHE A 181 4.350 -10.442 27.798 1.00 10.40 H ATOM 2469 HE2 PHE A 181 5.713 -14.157 28.255 1.00 12.18 H ATOM 2470 HZ PHE A 181 4.217 -12.651 27.266 1.00 10.87 H ATOM 2471 N CYS A 182 10.427 -11.500 29.068 1.00 8.20 N ANISOU 2471 N CYS A 182 1079 848 1187 192 -68 22 N ATOM 2472 CA CYS A 182 11.185 -12.015 27.964 1.00 8.72 C ANISOU 2472 CA CYS A 182 1032 992 1288 157 53 45 C ATOM 2473 C CYS A 182 10.691 -13.387 27.534 1.00 8.37 C ANISOU 2473 C CYS A 182 1052 869 1260 172 50 43 C ATOM 2474 O CYS A 182 10.315 -14.189 28.402 1.00 8.39 O ANISOU 2474 O CYS A 182 1058 901 1228 89 98 49 O ATOM 2475 CB CYS A 182 12.679 -12.132 28.309 1.00 9.58 C ANISOU 2475 CB CYS A 182 1139 1057 1443 89 -158 -25 C ATOM 2476 SG CYS A 182 13.595 -10.599 28.545 1.00 10.50 S ANISOU 2476 SG CYS A 182 1220 1171 1597 -33 -112 49 S ATOM 2477 H CYS A 182 10.577 -11.893 29.818 1.00 9.85 H ATOM 2478 HA CYS A 182 11.095 -11.406 27.202 1.00 10.47 H ATOM 2479 HB2 CYS A 182 12.759 -12.640 29.131 1.00 11.51 H ATOM 2480 HB3 CYS A 182 13.116 -12.617 27.591 1.00 11.51 H ATOM 2481 N VAL A 183 10.758 -13.653 26.237 1.00 8.55 N ANISOU 2481 N VAL A 183 1128 893 1226 68 -6 42 N ATOM 2482 CA VAL A 183 10.383 -14.924 25.677 1.00 8.82 C ANISOU 2482 CA VAL A 183 1196 924 1233 50 -44 53 C ATOM 2483 C VAL A 183 11.415 -15.204 24.579 1.00 9.32 C ANISOU 2483 C VAL A 183 1337 835 1370 96 94 86 C ATOM 2484 O VAL A 183 11.744 -14.303 23.819 1.00 10.72 O ANISOU 2484 O VAL A 183 1593 1119 1364 151 235 100 O ATOM 2485 CB VAL A 183 8.951 -14.899 25.070 1.00 9.53 C ANISOU 2485 CB VAL A 183 1280 1049 1292 -136 -176 -120 C ATOM 2486 CG1 VAL A 183 8.511 -16.269 24.666 1.00 11.69 C ANISOU 2486 CG1 VAL A 183 1508 1407 1526 2 -328 13 C ATOM 2487 CG2 VAL A 183 7.943 -14.306 26.051 1.00 10.22 C ANISOU 2487 CG2 VAL A 183 1180 1311 1395 -47 -187 108 C ATOM 2488 H VAL A 183 11.029 -13.088 25.648 1.00 10.27 H ATOM 2489 HA VAL A 183 10.435 -15.626 26.359 1.00 10.60 H ATOM 2490 HB VAL A 183 8.956 -14.337 24.267 1.00 11.45 H ATOM 2491 HG11 VAL A 183 7.626 -16.216 24.297 1.00 14.04 H ATOM 2492 HG12 VAL A 183 9.121 -16.612 24.009 1.00 14.04 H ATOM 2493 HG13 VAL A 183 8.510 -16.837 25.440 1.00 14.04 H ATOM 2494 HG21 VAL A 183 7.074 -14.307 25.644 1.00 12.28 H ATOM 2495 HG22 VAL A 183 7.933 -14.841 26.848 1.00 12.28 H ATOM 2496 HG23 VAL A 183 8.206 -13.408 26.263 1.00 12.28 H ATOM 2497 N GLY A 184 11.933 -16.433 24.531 1.00 9.75 N ANISOU 2497 N GLY A 184 1330 954 1422 104 216 131 N ATOM 2498 CA GLY A 184 12.904 -16.710 23.496 1.00 10.40 C ANISOU 2498 CA GLY A 184 1301 1218 1432 144 170 167 C ATOM 2499 C GLY A 184 14.021 -17.589 24.013 1.00 10.77 C ANISOU 2499 C GLY A 184 1391 1187 1515 87 267 153 C ATOM 2500 O GLY A 184 13.832 -18.450 24.869 1.00 11.34 O ANISOU 2500 O GLY A 184 1389 1293 1628 260 339 173 O ATOM 2501 H GLY A 184 11.747 -17.086 25.059 1.00 11.72 H ATOM 2502 HA2 GLY A 184 12.472 -17.162 22.755 1.00 12.49 H ATOM 2503 HA3 GLY A 184 13.286 -15.879 23.175 1.00 12.49 H ATOM 2504 N PHE A 184A 15.206 -17.338 23.460 1.00 12.14 N ANISOU 2504 N PHE A 184A 1400 1420 1794 83 75 310 N ATOM 2505 CA PHE A 184A 16.369 -18.255 23.602 1.00 13.91 C ANISOU 2505 CA PHE A 184A 1536 1782 1969 72 -101 354 C ATOM 2506 C PHE A 184A 17.643 -17.466 23.776 1.00 15.76 C ANISOU 2506 C PHE A 184A 1869 1872 2248 34 -312 629 C ATOM 2507 O PHE A 184A 17.959 -16.706 22.914 1.00 20.33 O ANISOU 2507 O PHE A 184A 2383 2793 2549 -425 -566 1064 O ATOM 2508 CB PHE A 184A 16.496 -19.054 22.301 1.00 15.43 C ANISOU 2508 CB PHE A 184A 1751 1971 2142 147 185 9 C ATOM 2509 CG PHE A 184A 15.300 -19.896 22.008 1.00 15.67 C ANISOU 2509 CG PHE A 184A 1779 2042 2135 191 247 -224 C ATOM 2510 CD1 PHE A 184A 14.252 -19.392 21.251 1.00 15.48 C ANISOU 2510 CD1 PHE A 184A 1857 2008 2017 329 350 -210 C ATOM 2511 CD2 PHE A 184A 15.223 -21.154 22.511 1.00 17.09 C ANISOU 2511 CD2 PHE A 184A 2040 2179 2275 210 187 -117 C ATOM 2512 CE1 PHE A 184A 13.157 -20.196 20.982 1.00 15.36 C ANISOU 2512 CE1 PHE A 184A 1883 1954 1999 393 315 -304 C ATOM 2513 CE2 PHE A 184A 14.092 -21.967 22.227 1.00 17.08 C ANISOU 2513 CE2 PHE A 184A 2069 2190 2232 157 228 -228 C ATOM 2514 CZ PHE A 184A 13.073 -21.473 21.489 1.00 15.47 C ANISOU 2514 CZ PHE A 184A 1845 1974 2060 337 290 -409 C ATOM 2515 H PHE A 184A 15.377 -16.639 22.989 1.00 14.59 H ATOM 2516 HA PHE A 184A 16.246 -18.865 24.359 1.00 16.71 H ATOM 2517 HB2 PHE A 184A 16.613 -18.436 21.563 1.00 18.53 H ATOM 2518 HB3 PHE A 184A 17.265 -19.642 22.366 1.00 18.53 H ATOM 2519 HD1 PHE A 184A 14.297 -18.530 20.904 1.00 18.59 H ATOM 2520 HD2 PHE A 184A 15.923 -21.494 23.020 1.00 20.53 H ATOM 2521 HE1 PHE A 184A 12.456 -19.859 20.473 1.00 18.45 H ATOM 2522 HE2 PHE A 184A 14.042 -22.830 22.570 1.00 20.51 H ATOM 2523 HZ PHE A 184A 12.331 -22.001 21.304 1.00 18.58 H ATOM 2524 N LEU A 185 18.416 -17.776 24.765 1.00 15.68 N ANISOU 2524 N LEU A 185 1847 1731 2380 284 -460 299 N ATOM 2525 CA LEU A 185 19.683 -17.077 24.934 1.00 17.09 C ANISOU 2525 CA LEU A 185 2035 1927 2530 1 -580 111 C ATOM 2526 C LEU A 185 20.756 -17.533 23.908 1.00 15.86 C ANISOU 2526 C LEU A 185 1777 1725 2524 52 -573 120 C ATOM 2527 O LEU A 185 21.722 -16.815 23.649 1.00 16.57 O ANISOU 2527 O LEU A 185 1946 1603 2746 -19 -416 340 O ATOM 2528 CB LEU A 185 20.216 -17.333 26.328 1.00 21.53 C ANISOU 2528 CB LEU A 185 2679 2568 2935 82 -692 80 C ATOM 2529 CG LEU A 185 19.306 -16.810 27.447 1.00 26.56 C ANISOU 2529 CG LEU A 185 3359 3247 3485 96 -624 66 C ATOM 2530 CD1 LEU A 185 20.008 -16.967 28.838 1.00 33.43 C ANISOU 2530 CD1 LEU A 185 4234 4157 4310 -12 -591 75 C ATOM 2531 CD2 LEU A 185 18.967 -15.347 27.286 1.00 27.29 C ANISOU 2531 CD2 LEU A 185 3441 3348 3581 151 -518 33 C ATOM 2532 H LEU A 185 18.250 -18.377 25.357 1.00 18.83 H ATOM 2533 HA LEU A 185 19.541 -16.113 24.828 1.00 20.52 H ATOM 2534 HB2 LEU A 185 20.318 -18.290 26.452 1.00 25.86 H ATOM 2535 HB3 LEU A 185 21.077 -16.896 26.418 1.00 25.86 H ATOM 2536 HG LEU A 185 18.480 -17.319 27.459 1.00 31.88 H ATOM 2537 HD11 LEU A 185 19.422 -16.635 29.522 1.00 40.13 H ATOM 2538 HD12 LEU A 185 20.195 -17.896 28.990 1.00 40.13 H ATOM 2539 HD13 LEU A 185 20.826 -16.464 28.833 1.00 40.13 H ATOM 2540 HD21 LEU A 185 18.399 -15.077 28.011 1.00 32.76 H ATOM 2541 HD22 LEU A 185 19.780 -14.835 27.299 1.00 32.76 H ATOM 2542 HD23 LEU A 185 18.514 -15.222 26.450 1.00 32.76 H ATOM 2543 N GLU A 186 20.595 -18.673 23.312 1.00 16.85 N ANISOU 2543 N GLU A 186 1929 1859 2613 -66 -412 130 N ATOM 2544 CA GLU A 186 21.606 -19.126 22.325 1.00 20.60 C ANISOU 2544 CA GLU A 186 2515 2408 2903 -22 -173 107 C ATOM 2545 C GLU A 186 21.556 -18.432 21.018 1.00 20.93 C ANISOU 2545 C GLU A 186 2471 2509 2973 -98 -296 319 C ATOM 2546 O GLU A 186 22.427 -18.611 20.201 1.00 22.38 O ANISOU 2546 O GLU A 186 2516 2894 3094 -157 -31 626 O ATOM 2547 CB GLU A 186 21.401 -20.670 22.060 1.00 25.94 C ANISOU 2547 CB GLU A 186 3283 3116 3458 39 153 -30 C ATOM 2548 CG GLU A 186 20.138 -20.966 21.249 1.00 32.45 C ANISOU 2548 CG GLU A 186 4138 4013 4179 -93 521 -91 C ATOM 2549 CD GLU A 186 19.552 -22.478 21.203 1.00 35.53 C ANISOU 2549 CD GLU A 186 4582 4490 4429 -11 848 -157 C ATOM 2550 OE1 GLU A 186 20.095 -23.356 20.425 1.00 37.65 O ANISOU 2550 OE1 GLU A 186 4887 4857 4563 0 972 -193 O ATOM 2551 OE2 GLU A 186 18.512 -22.732 21.919 1.00 36.05 O ANISOU 2551 OE2 GLU A 186 4590 4568 4539 -87 979 -149 O ATOM 2552 H GLU A 186 19.937 -19.212 23.436 1.00 20.23 H ATOM 2553 HA GLU A 186 22.502 -18.998 22.703 1.00 24.73 H ATOM 2554 HB2 GLU A 186 22.163 -21.010 21.565 1.00 31.15 H ATOM 2555 HB3 GLU A 186 21.326 -21.130 22.911 1.00 31.15 H ATOM 2556 HG2 GLU A 186 19.428 -20.405 21.599 1.00 38.96 H ATOM 2557 HG3 GLU A 186 20.314 -20.710 20.330 1.00 38.96 H ATOM 2558 N GLY A 187 20.518 -17.632 20.811 1.00 20.30 N ANISOU 2558 N GLY A 187 2553 2301 2857 -138 -833 327 N ATOM 2559 CA GLY A 187 20.386 -16.895 19.541 1.00 21.82 C ANISOU 2559 CA GLY A 187 2814 2533 2945 -139 -969 15 C ATOM 2560 C GLY A 187 19.746 -17.678 18.427 1.00 19.05 C ANISOU 2560 C GLY A 187 2497 1843 2897 14 -936 -216 C ATOM 2561 O GLY A 187 19.531 -18.921 18.556 1.00 21.52 O ANISOU 2561 O GLY A 187 2971 1855 3351 -32 -849 -110 O ATOM 2562 H GLY A 187 19.882 -17.495 21.373 1.00 24.37 H ATOM 2563 HA2 GLY A 187 19.852 -16.099 19.693 1.00 26.20 H ATOM 2564 HA3 GLY A 187 21.266 -16.616 19.245 1.00 26.20 H ATOM 2565 N GLY A 188 19.389 -17.006 17.356 1.00 16.13 N ANISOU 2565 N GLY A 188 1850 1804 2475 406 -577 -439 N ATOM 2566 CA GLY A 188 18.849 -17.663 16.178 1.00 15.68 C ANISOU 2566 CA GLY A 188 1798 1915 2245 355 -236 -589 C ATOM 2567 C GLY A 188 17.350 -17.728 16.079 1.00 13.12 C ANISOU 2567 C GLY A 188 1437 1603 1946 396 -82 -429 C ATOM 2568 O GLY A 188 16.854 -18.046 14.989 1.00 13.84 O ANISOU 2568 O GLY A 188 1557 1798 1902 295 57 -355 O ATOM 2569 H GLY A 188 19.450 -16.152 17.281 1.00 19.37 H ATOM 2570 HA2 GLY A 188 19.175 -17.202 15.390 1.00 18.83 H ATOM 2571 HA3 GLY A 188 19.185 -18.572 16.149 1.00 18.83 H ATOM 2572 N LYS A 188A 16.637 -17.477 17.163 1.00 12.51 N ANISOU 2572 N LYS A 188A 1493 1418 1841 450 4 -263 N ATOM 2573 CA LYS A 188A 15.162 -17.584 17.164 1.00 12.20 C ANISOU 2573 CA LYS A 188A 1516 1416 1705 254 155 -112 C ATOM 2574 C LYS A 188A 14.586 -16.412 17.951 1.00 10.82 C ANISOU 2574 C LYS A 188A 1404 1172 1534 165 1 -112 C ATOM 2575 O LYS A 188A 14.820 -16.278 19.134 1.00 11.74 O ANISOU 2575 O LYS A 188A 1649 1237 1576 265 -101 -105 O ATOM 2576 CB LYS A 188A 14.754 -18.898 17.844 1.00 13.37 C ANISOU 2576 CB LYS A 188A 1687 1566 1829 319 289 -117 C ATOM 2577 CG LYS A 188A 15.095 -20.096 16.985 1.00 17.97 C ANISOU 2577 CG LYS A 188A 2343 2091 2394 322 482 -104 C ATOM 2578 CD LYS A 188A 14.329 -21.306 17.577 1.00 25.79 C ANISOU 2578 CD LYS A 188A 3292 3089 3416 249 576 -262 C ATOM 2579 CE LYS A 188A 15.113 -22.114 18.434 1.00 34.30 C ANISOU 2579 CE LYS A 188A 4317 4274 4442 115 649 -238 C ATOM 2580 NZ LYS A 188A 14.341 -23.553 18.284 1.00 37.98 N ANISOU 2580 NZ LYS A 188A 4782 4684 4967 66 653 -147 N ATOM 2581 H LYS A 188A 16.971 -17.241 17.919 1.00 15.02 H ATOM 2582 HA LYS A 188A 14.814 -17.566 16.248 1.00 14.66 H ATOM 2583 HB2 LYS A 188A 15.228 -18.984 18.686 1.00 16.06 H ATOM 2584 HB3 LYS A 188A 13.796 -18.896 17.997 1.00 16.06 H ATOM 2585 HG2 LYS A 188A 14.799 -19.948 16.073 1.00 21.58 H ATOM 2586 HG3 LYS A 188A 16.048 -20.273 17.021 1.00 21.58 H ATOM 2587 HD2 LYS A 188A 13.573 -20.978 18.090 1.00 30.96 H ATOM 2588 HD3 LYS A 188A 14.015 -21.865 16.849 1.00 30.96 H ATOM 2589 HE2 LYS A 188A 16.025 -22.187 18.111 1.00 41.18 H ATOM 2590 HE3 LYS A 188A 15.067 -21.802 19.351 1.00 41.18 H ATOM 2591 HZ1 LYS A 188A 14.776 -24.216 18.826 1.00 45.60 H ATOM 2592 HZ2 LYS A 188A 13.428 -23.466 18.569 1.00 45.60 H ATOM 2593 HZ3 LYS A 188A 14.356 -23.839 17.368 1.00 45.60 H ATOM 2594 N ASP A 189 13.836 -15.551 17.276 1.00 10.02 N ANISOU 2594 N ASP A 189 1279 1102 1427 14 38 -152 N ATOM 2595 CA ASP A 189 13.286 -14.344 17.910 1.00 9.36 C ANISOU 2595 CA ASP A 189 1235 934 1386 97 19 -252 C ATOM 2596 C ASP A 189 12.284 -13.662 17.013 1.00 9.05 C ANISOU 2596 C ASP A 189 1180 986 1273 51 -32 -157 C ATOM 2597 O ASP A 189 12.169 -14.013 15.864 1.00 10.65 O ANISOU 2597 O ASP A 189 1376 1174 1496 164 11 -199 O ATOM 2598 CB ASP A 189 14.470 -13.402 18.148 1.00 10.04 C ANISOU 2598 CB ASP A 189 1267 1123 1423 103 3 -172 C ATOM 2599 CG ASP A 189 14.265 -12.287 19.175 1.00 9.94 C ANISOU 2599 CG ASP A 189 1182 1161 1433 -83 106 -32 C ATOM 2600 OD1 ASP A 189 13.171 -12.188 19.825 1.00 9.45 O ANISOU 2600 OD1 ASP A 189 1185 987 1418 64 242 20 O ATOM 2601 OD2 ASP A 189 15.265 -11.499 19.355 1.00 10.87 O ANISOU 2601 OD2 ASP A 189 1279 1285 1565 66 -2 -70 O ATOM 2602 H ASP A 189 13.626 -15.636 16.447 1.00 12.04 H ATOM 2603 HA ASP A 189 12.864 -14.566 18.767 1.00 11.24 H ATOM 2604 HB2 ASP A 189 15.224 -13.934 18.448 1.00 12.06 H ATOM 2605 HB3 ASP A 189 14.693 -12.978 17.305 1.00 12.06 H ATOM 2606 N SER A 190 11.579 -12.670 17.535 1.00 8.62 N ANISOU 2606 N SER A 190 1118 962 1195 147 122 43 N ATOM 2607 CA SER A 190 10.824 -11.731 16.713 1.00 8.48 C ANISOU 2607 CA SER A 190 1082 899 1240 54 97 -127 C ATOM 2608 C SER A 190 11.793 -10.651 16.219 1.00 8.87 C ANISOU 2608 C SER A 190 1116 930 1324 8 9 -169 C ATOM 2609 O SER A 190 12.962 -10.578 16.658 1.00 10.11 O ANISOU 2609 O SER A 190 1307 1136 1396 -46 -8 -31 O ATOM 2610 CB SER A 190 9.632 -11.197 17.472 1.00 9.46 C ANISOU 2610 CB SER A 190 1246 988 1360 218 -21 -96 C ATOM 2611 OG SER A 190 10.028 -10.613 18.685 1.00 10.44 O ANISOU 2611 OG SER A 190 1317 1176 1472 164 93 -176 O ATOM 2612 H SER A 190 11.521 -12.514 18.379 1.00 10.36 H ATOM 2613 HA SER A 190 10.484 -12.206 15.926 1.00 10.19 H ATOM 2614 HB2 SER A 190 9.188 -10.526 16.930 1.00 11.37 H ATOM 2615 HB3 SER A 190 9.023 -11.928 17.659 1.00 11.37 H ATOM 2616 HG SER A 190 9.373 -10.328 19.086 1.00 12.54 H ATOM 2617 N CYS A 191 11.317 -9.775 15.332 1.00 9.04 N ANISOU 2617 N CYS A 191 1037 1000 1400 95 32 1 N ATOM 2618 CA CYS A 191 12.188 -8.801 14.724 1.00 9.24 C ANISOU 2618 CA CYS A 191 1092 1048 1369 -108 169 21 C ATOM 2619 C CYS A 191 11.373 -7.644 14.141 1.00 9.41 C ANISOU 2619 C CYS A 191 1088 1134 1355 -145 155 32 C ATOM 2620 O CYS A 191 10.146 -7.585 14.344 1.00 9.75 O ANISOU 2620 O CYS A 191 1185 1053 1465 -49 185 18 O ATOM 2621 CB CYS A 191 13.056 -9.487 13.638 1.00 10.35 C ANISOU 2621 CB CYS A 191 1138 1278 1515 -117 56 85 C ATOM 2622 SG CYS A 191 14.534 -8.579 13.129 1.00 12.17 S ANISOU 2622 SG CYS A 191 1359 1489 1776 -17 346 -39 S ATOM 2623 H CYS A 191 10.497 -9.733 15.074 1.00 10.87 H ATOM 2624 HA CYS A 191 12.788 -8.436 15.407 1.00 11.10 H ATOM 2625 HB2 CYS A 191 13.347 -10.348 13.976 1.00 12.43 H ATOM 2626 HB3 CYS A 191 12.510 -9.618 12.847 1.00 12.43 H ATOM 2627 N GLN A 192 12.015 -6.681 13.473 1.00 9.36 N ANISOU 2627 N GLN A 192 1100 1009 1448 26 192 161 N ATOM 2628 CA GLN A 192 11.275 -5.537 12.953 1.00 10.22 C ANISOU 2628 CA GLN A 192 1257 1146 1480 -95 214 178 C ATOM 2629 C GLN A 192 10.144 -5.964 12.030 1.00 9.84 C ANISOU 2629 C GLN A 192 1296 1003 1438 -25 177 148 C ATOM 2630 O GLN A 192 10.300 -6.822 11.193 1.00 10.92 O ANISOU 2630 O GLN A 192 1479 1148 1520 -46 227 76 O ATOM 2631 CB GLN A 192 12.199 -4.524 12.227 1.00 10.47 C ANISOU 2631 CB GLN A 192 1355 1195 1426 -155 201 155 C ATOM 2632 CG GLN A 192 12.992 -3.624 13.194 1.00 11.32 C ANISOU 2632 CG GLN A 192 1402 1299 1602 -185 168 110 C ATOM 2633 CD GLN A 192 14.012 -4.369 14.049 1.00 11.20 C ANISOU 2633 CD GLN A 192 1394 1142 1718 -16 213 25 C ATOM 2634 OE1 GLN A 192 14.727 -5.258 13.583 1.00 12.19 O ANISOU 2634 OE1 GLN A 192 1383 1315 1935 71 208 -181 O ATOM 2635 NE2 GLN A 192 14.068 -4.004 15.325 1.00 11.41 N ANISOU 2635 NE2 GLN A 192 1413 1280 1641 -96 117 108 N ATOM 2636 H GLN A 192 12.859 -6.668 13.312 1.00 11.25 H ATOM 2637 HA GLN A 192 10.868 -5.067 13.711 1.00 12.28 H ATOM 2638 HB2 GLN A 192 12.837 -5.013 11.685 1.00 12.57 H ATOM 2639 HB3 GLN A 192 11.656 -3.951 11.663 1.00 12.57 H ATOM 2640 HG2 GLN A 192 13.470 -2.957 12.677 1.00 13.60 H ATOM 2641 HG3 GLN A 192 12.367 -3.186 13.795 1.00 13.60 H ATOM 2642 HE21 GLN A 192 14.623 -4.387 15.858 1.00 13.70 H ATOM 2643 HE22 GLN A 192 13.549 -3.384 15.617 1.00 13.70 H ATOM 2644 N ARG A 193 9.015 -5.279 12.207 1.00 10.77 N ANISOU 2644 N ARG A 193 1350 1133 1611 -89 101 196 N ATOM 2645 CA ARG A 193 7.703 -5.523 11.589 1.00 12.31 C ANISOU 2645 CA ARG A 193 1533 1384 1759 -10 90 -105 C ATOM 2646 C ARG A 193 6.886 -6.537 12.341 1.00 10.19 C ANISOU 2646 C ARG A 193 1256 1061 1554 -162 -47 14 C ATOM 2647 O ARG A 193 5.716 -6.728 12.029 1.00 11.26 O ANISOU 2647 O ARG A 193 1432 1171 1674 -226 -260 255 O ATOM 2648 CB ARG A 193 7.757 -5.922 10.097 1.00 19.39 C ANISOU 2648 CB ARG A 193 2373 2473 2522 -2 126 -131 C ATOM 2649 CG ARG A 193 7.927 -4.973 9.087 1.00 26.52 C ANISOU 2649 CG ARG A 193 3355 3311 3409 254 278 -258 C ATOM 2650 CD ARG A 193 7.639 -5.657 7.697 1.00 28.80 C ANISOU 2650 CD ARG A 193 3673 3585 3687 116 405 -172 C ATOM 2651 NE ARG A 193 7.738 -4.636 6.728 1.00 29.41 N ANISOU 2651 NE ARG A 193 3824 3629 3720 102 507 -86 N ATOM 2652 CZ ARG A 193 7.216 -4.730 5.486 1.00 29.70 C ANISOU 2652 CZ ARG A 193 3900 3714 3673 15 519 199 C ATOM 2653 NH1 ARG A 193 6.695 -5.878 5.066 1.00 27.83 N ANISOU 2653 NH1 ARG A 193 3588 3472 3515 162 470 241 N ATOM 2654 NH2 ARG A 193 7.234 -3.631 4.697 1.00 33.67 N ANISOU 2654 NH2 ARG A 193 4376 4180 4237 -57 493 282 N ATOM 2655 H ARG A 193 8.983 -4.601 12.735 1.00 12.94 H ATOM 2656 HA ARG A 193 7.204 -4.681 11.630 1.00 14.78 H ATOM 2657 HB2 ARG A 193 8.488 -6.552 9.998 1.00 23.28 H ATOM 2658 HB3 ARG A 193 6.927 -6.382 9.896 1.00 23.28 H ATOM 2659 HG2 ARG A 193 7.300 -4.243 9.212 1.00 31.83 H ATOM 2660 HG3 ARG A 193 8.841 -4.647 9.091 1.00 31.83 H ATOM 2661 HD2 ARG A 193 8.304 -6.338 7.513 1.00 34.58 H ATOM 2662 HD3 ARG A 193 6.742 -6.025 7.683 1.00 34.58 H ATOM 2663 HE ARG A 193 8.091 -3.777 7.008 1.00 35.30 H ATOM 2664 HH11 ARG A 193 6.657 -6.553 5.597 1.00 33.41 H ATOM 2665 HH12 ARG A 193 6.381 -5.941 4.268 1.00 33.41 H ATOM 2666 HH21 ARG A 193 7.605 -2.908 4.979 1.00 40.42 H ATOM 2667 HH22 ARG A 193 6.966 -3.686 3.882 1.00 40.42 H ATOM 2668 N ASP A 194 7.447 -7.189 13.363 1.00 8.98 N ANISOU 2668 N ASP A 194 981 1127 1304 15 53 7 N ATOM 2669 CA ASP A 194 6.626 -8.052 14.274 1.00 8.52 C ANISOU 2669 CA ASP A 194 1009 1002 1226 64 62 45 C ATOM 2670 C ASP A 194 5.990 -7.289 15.402 1.00 8.47 C ANISOU 2670 C ASP A 194 948 1002 1268 44 182 172 C ATOM 2671 O ASP A 194 5.059 -7.808 16.033 1.00 8.28 O ANISOU 2671 O ASP A 194 997 808 1340 -111 124 28 O ATOM 2672 CB ASP A 194 7.485 -9.160 14.866 1.00 8.52 C ANISOU 2672 CB ASP A 194 1032 984 1224 30 56 -113 C ATOM 2673 CG ASP A 194 7.843 -10.222 13.853 1.00 9.18 C ANISOU 2673 CG ASP A 194 1121 1045 1321 -23 68 -185 C ATOM 2674 OD1 ASP A 194 7.017 -10.605 13.010 1.00 9.87 O ANISOU 2674 OD1 ASP A 194 1278 1045 1427 -40 104 -228 O ATOM 2675 OD2 ASP A 194 9.008 -10.713 13.920 1.00 9.76 O ANISOU 2675 OD2 ASP A 194 1240 1006 1462 -8 201 -177 O ATOM 2676 H ASP A 194 8.283 -7.159 13.562 1.00 10.79 H ATOM 2677 HA ASP A 194 5.910 -8.472 13.752 1.00 10.24 H ATOM 2678 HB2 ASP A 194 8.309 -8.775 15.202 1.00 10.24 H ATOM 2679 HB3 ASP A 194 6.998 -9.586 15.588 1.00 10.24 H ATOM 2680 N ALA A 195 6.477 -6.065 15.719 1.00 8.76 N ANISOU 2680 N ALA A 195 1048 991 1290 34 163 124 N ATOM 2681 CA ALA A 195 5.979 -5.358 16.898 1.00 8.12 C ANISOU 2681 CA ALA A 195 999 785 1300 -42 61 6 C ATOM 2682 C ALA A 195 4.485 -5.252 16.878 1.00 7.70 C ANISOU 2682 C ALA A 195 995 723 1207 20 55 47 C ATOM 2683 O ALA A 195 3.868 -5.063 15.831 1.00 8.77 O ANISOU 2683 O ALA A 195 1105 1028 1201 55 52 40 O ATOM 2684 CB ALA A 195 6.561 -3.954 17.027 1.00 9.91 C ANISOU 2684 CB ALA A 195 1212 1109 1443 -165 32 -145 C ATOM 2685 H ALA A 195 7.079 -5.642 15.274 1.00 10.53 H ATOM 2686 HA ALA A 195 6.233 -5.863 17.698 1.00 9.75 H ATOM 2687 HB1 ALA A 195 6.201 -3.539 17.814 1.00 11.90 H ATOM 2688 HB2 ALA A 195 7.516 -4.018 17.097 1.00 11.90 H ATOM 2689 HB3 ALA A 195 6.322 -3.445 16.249 1.00 11.90 H ATOM 2690 N GLY A 196 3.886 -5.326 18.060 1.00 7.83 N ANISOU 2690 N GLY A 196 1061 805 1107 -3 -30 50 N ATOM 2691 CA GLY A 196 2.466 -5.200 18.227 1.00 8.03 C ANISOU 2691 CA GLY A 196 988 931 1132 29 51 57 C ATOM 2692 C GLY A 196 1.754 -6.543 18.121 1.00 7.91 C ANISOU 2692 C GLY A 196 1009 831 1166 148 34 144 C ATOM 2693 O GLY A 196 0.613 -6.652 18.581 1.00 8.64 O ANISOU 2693 O GLY A 196 978 1020 1285 -57 17 65 O ATOM 2694 H GLY A 196 4.306 -5.453 18.799 1.00 9.40 H ATOM 2695 HA2 GLY A 196 2.275 -4.818 19.098 1.00 9.65 H ATOM 2696 HA3 GLY A 196 2.111 -4.608 17.546 1.00 9.65 H ATOM 2697 N GLY A 197 2.409 -7.546 17.558 1.00 8.29 N ANISOU 2697 N GLY A 197 1023 878 1247 -59 47 78 N ATOM 2698 CA GLY A 197 1.806 -8.842 17.364 1.00 8.07 C ANISOU 2698 CA GLY A 197 1043 810 1213 -16 -19 61 C ATOM 2699 C GLY A 197 1.792 -9.685 18.632 1.00 7.92 C ANISOU 2699 C GLY A 197 927 867 1214 -126 -58 -76 C ATOM 2700 O GLY A 197 2.278 -9.296 19.704 1.00 8.78 O ANISOU 2700 O GLY A 197 1013 1010 1314 -102 -61 -85 O ATOM 2701 H GLY A 197 3.220 -7.494 17.276 1.00 9.96 H ATOM 2702 HA2 GLY A 197 0.892 -8.729 17.062 1.00 9.70 H ATOM 2703 HA3 GLY A 197 2.297 -9.326 16.681 1.00 9.70 H ATOM 2704 N PRO A 198 1.172 -10.858 18.508 1.00 8.54 N ANISOU 2704 N PRO A 198 1242 811 1193 -64 16 64 N ATOM 2705 CA PRO A 198 0.892 -11.709 19.650 1.00 8.81 C ANISOU 2705 CA PRO A 198 1274 829 1246 -62 36 145 C ATOM 2706 C PRO A 198 1.989 -12.637 20.122 1.00 8.23 C ANISOU 2706 C PRO A 198 1080 842 1204 8 104 5 C ATOM 2707 O PRO A 198 2.719 -13.216 19.308 1.00 9.49 O ANISOU 2707 O PRO A 198 1334 1047 1225 90 134 -27 O ATOM 2708 CB PRO A 198 -0.267 -12.572 19.144 1.00 9.62 C ANISOU 2708 CB PRO A 198 1257 1020 1380 -131 157 106 C ATOM 2709 CG PRO A 198 -0.005 -12.653 17.662 1.00 10.49 C ANISOU 2709 CG PRO A 198 1388 1168 1429 -139 122 101 C ATOM 2710 CD PRO A 198 0.563 -11.346 17.281 1.00 9.43 C ANISOU 2710 CD PRO A 198 1304 1005 1275 -111 63 51 C ATOM 2711 HA PRO A 198 0.583 -11.167 20.406 1.00 10.59 H ATOM 2712 HB2 PRO A 198 -0.233 -13.450 19.553 1.00 11.56 H ATOM 2713 HB3 PRO A 198 -1.113 -12.133 19.325 1.00 11.56 H ATOM 2714 HG2 PRO A 198 0.628 -13.365 17.483 1.00 12.60 H ATOM 2715 HG3 PRO A 198 -0.839 -12.812 17.193 1.00 12.60 H ATOM 2716 HD2 PRO A 198 1.236 -11.459 16.592 1.00 11.33 H ATOM 2717 HD3 PRO A 198 -0.141 -10.744 16.993 1.00 11.33 H ATOM 2718 N VAL A 199 1.973 -12.842 21.434 1.00 8.17 N ANISOU 2718 N VAL A 199 1018 909 1176 62 115 26 N ATOM 2719 CA VAL A 199 2.579 -14.017 22.069 1.00 8.00 C ANISOU 2719 CA VAL A 199 979 876 1183 -106 33 53 C ATOM 2720 C VAL A 199 1.417 -14.721 22.782 1.00 8.09 C ANISOU 2720 C VAL A 199 959 926 1190 135 88 32 C ATOM 2721 O VAL A 199 0.806 -14.152 23.684 1.00 8.37 O ANISOU 2721 O VAL A 199 1052 870 1259 30 154 36 O ATOM 2722 CB VAL A 199 3.660 -13.623 23.139 1.00 9.97 C ANISOU 2722 CB VAL A 199 1124 1277 1385 -118 -7 86 C ATOM 2723 CG1 VAL A 199 4.202 -14.856 23.810 1.00 10.53 C ANISOU 2723 CG1 VAL A 199 1249 1282 1471 81 -70 183 C ATOM 2724 CG2 VAL A 199 4.701 -12.729 22.544 1.00 11.00 C ANISOU 2724 CG2 VAL A 199 1393 1275 1513 -310 174 -101 C ATOM 2725 H VAL A 199 1.608 -12.303 21.996 1.00 9.81 H ATOM 2726 HA VAL A 199 2.972 -14.615 21.399 1.00 9.61 H ATOM 2727 HB VAL A 199 3.210 -13.101 23.837 1.00 11.97 H ATOM 2728 HG11 VAL A 199 4.859 -14.595 24.459 1.00 12.65 H ATOM 2729 HG12 VAL A 199 3.481 -15.320 24.241 1.00 12.65 H ATOM 2730 HG13 VAL A 199 4.604 -15.421 23.145 1.00 12.65 H ATOM 2731 HG21 VAL A 199 5.345 -12.506 23.220 1.00 13.22 H ATOM 2732 HG22 VAL A 199 5.132 -13.190 21.821 1.00 13.22 H ATOM 2733 HG23 VAL A 199 4.279 -11.931 22.218 1.00 13.22 H ATOM 2734 N VAL A 200 1.087 -15.921 22.334 1.00 8.22 N ANISOU 2734 N VAL A 200 1037 915 1172 8 179 -2 N ATOM 2735 CA VAL A 200 -0.038 -16.690 22.865 1.00 8.30 C ANISOU 2735 CA VAL A 200 1082 843 1227 -8 195 7 C ATOM 2736 C VAL A 200 0.506 -17.888 23.630 1.00 8.65 C ANISOU 2736 C VAL A 200 1020 853 1413 -41 164 19 C ATOM 2737 O VAL A 200 1.337 -18.636 23.129 1.00 9.55 O ANISOU 2737 O VAL A 200 1152 878 1597 98 284 190 O ATOM 2738 CB VAL A 200 -0.971 -17.124 21.738 1.00 9.38 C ANISOU 2738 CB VAL A 200 1165 1047 1352 -30 53 29 C ATOM 2739 CG1 VAL A 200 -2.011 -18.161 22.238 1.00 10.53 C ANISOU 2739 CG1 VAL A 200 1277 1260 1463 -86 -2 66 C ATOM 2740 CG2 VAL A 200 -1.659 -15.893 21.180 1.00 10.76 C ANISOU 2740 CG2 VAL A 200 1409 1242 1438 -89 -42 -4 C ATOM 2741 H VAL A 200 1.510 -16.327 21.704 1.00 9.88 H ATOM 2742 HA VAL A 200 -0.547 -16.131 23.489 1.00 9.97 H ATOM 2743 HB VAL A 200 -0.445 -17.535 21.021 1.00 11.27 H ATOM 2744 HG11 VAL A 200 -2.580 -18.410 21.506 1.00 12.65 H ATOM 2745 HG12 VAL A 200 -1.548 -18.932 22.571 1.00 12.65 H ATOM 2746 HG13 VAL A 200 -2.534 -17.765 22.939 1.00 12.65 H ATOM 2747 HG21 VAL A 200 -2.248 -16.159 20.471 1.00 12.93 H ATOM 2748 HG22 VAL A 200 -2.160 -15.471 21.882 1.00 12.93 H ATOM 2749 HG23 VAL A 200 -0.993 -15.289 20.844 1.00 12.93 H ATOM 2750 N CYS A 201 -0.008 -18.079 24.840 1.00 9.03 N ANISOU 2750 N CYS A 201 1022 994 1415 48 100 131 N ATOM 2751 CA CYS A 201 0.401 -19.193 25.652 1.00 10.17 C ANISOU 2751 CA CYS A 201 1144 1185 1536 222 91 327 C ATOM 2752 C CYS A 201 -0.821 -19.762 26.287 1.00 10.09 C ANISOU 2752 C CYS A 201 1206 968 1659 41 114 281 C ATOM 2753 O CYS A 201 -1.651 -19.045 26.845 1.00 10.29 O ANISOU 2753 O CYS A 201 1084 1124 1702 -27 146 335 O ATOM 2754 CB CYS A 201 1.339 -18.719 26.821 1.00 11.75 C ANISOU 2754 CB CYS A 201 1314 1476 1674 260 80 323 C ATOM 2755 SG CYS A 201 2.569 -17.464 26.424 1.00 11.68 S ANISOU 2755 SG CYS A 201 1345 1295 1797 96 212 23 S ATOM 2756 H CYS A 201 -0.596 -17.570 25.207 1.00 10.85 H ATOM 2757 HA CYS A 201 0.851 -19.877 25.113 1.00 12.22 H ATOM 2758 HB2 CYS A 201 0.781 -18.359 27.528 1.00 14.11 H ATOM 2759 HB3 CYS A 201 1.818 -19.493 27.155 1.00 14.11 H ATOM 2760 N ASN A 202 -0.990 -21.070 26.208 1.00 11.78 N ANISOU 2760 N ASN A 202 1447 1168 1861 133 243 214 N ATOM 2761 CA ASN A 202 -2.143 -21.752 26.851 1.00 12.10 C ANISOU 2761 CA ASN A 202 1504 1194 1899 65 137 177 C ATOM 2762 C ASN A 202 -3.443 -21.073 26.410 1.00 11.66 C ANISOU 2762 C ASN A 202 1526 1017 1886 7 103 129 C ATOM 2763 O ASN A 202 -4.327 -20.854 27.239 1.00 12.85 O ANISOU 2763 O ASN A 202 1582 1290 2009 -2 242 405 O ATOM 2764 CB ASN A 202 -2.010 -21.761 28.374 1.00 14.87 C ANISOU 2764 CB ASN A 202 1793 1743 2114 -64 90 389 C ATOM 2765 CG ASN A 202 -0.736 -22.340 28.907 1.00 15.77 C ANISOU 2765 CG ASN A 202 1977 1736 2279 10 70 153 C ATOM 2766 OD1 ASN A 202 0.070 -21.647 29.513 1.00 16.45 O ANISOU 2766 OD1 ASN A 202 2096 1870 2282 1 7 32 O ATOM 2767 ND2 ASN A 202 -0.480 -23.534 28.633 1.00 18.03 N ANISOU 2767 ND2 ASN A 202 2309 1982 2560 483 -25 139 N ATOM 2768 H ASN A 202 -0.459 -21.603 25.791 1.00 14.15 H ATOM 2769 HA ASN A 202 -2.171 -22.683 26.546 1.00 14.53 H ATOM 2770 HB2 ASN A 202 -2.069 -20.847 28.692 1.00 17.86 H ATOM 2771 HB3 ASN A 202 -2.742 -22.280 28.743 1.00 17.86 H ATOM 2772 HD21 ASN A 202 0.345 -23.946 28.966 1.00 21.65 H ATOM 2773 HD22 ASN A 202 -1.103 -24.056 28.087 1.00 21.65 H ATOM 2774 N GLY A 203 -3.562 -20.740 25.131 1.00 11.21 N ANISOU 2774 N GLY A 203 1450 1029 1781 -121 -91 88 N ATOM 2775 CA GLY A 203 -4.800 -20.204 24.622 1.00 12.02 C ANISOU 2775 CA GLY A 203 1571 1256 1739 -164 -111 41 C ATOM 2776 C GLY A 203 -5.140 -18.786 25.026 1.00 11.05 C ANISOU 2776 C GLY A 203 1418 1013 1768 -35 -68 38 C ATOM 2777 O GLY A 203 -6.290 -18.357 24.858 1.00 12.83 O ANISOU 2777 O GLY A 203 1561 1196 2119 -142 -368 41 O ATOM 2778 H GLY A 203 -2.938 -20.817 24.544 1.00 13.47 H ATOM 2779 HA2 GLY A 203 -4.774 -20.234 23.653 1.00 14.43 H ATOM 2780 HA3 GLY A 203 -5.528 -20.774 24.916 1.00 14.43 H ATOM 2781 N GLN A 204 -4.158 -18.046 25.516 1.00 9.47 N ANISOU 2781 N GLN A 204 1207 948 1443 -105 41 140 N ATOM 2782 CA GLN A 204 -4.382 -16.690 26.002 1.00 9.45 C ANISOU 2782 CA GLN A 204 1172 1066 1353 -73 31 63 C ATOM 2783 C GLN A 204 -3.334 -15.748 25.433 1.00 8.50 C ANISOU 2783 C GLN A 204 940 911 1380 -38 52 31 C ATOM 2784 O GLN A 204 -2.181 -16.126 25.238 1.00 8.94 O ANISOU 2784 O GLN A 204 971 944 1482 9 79 15 O ATOM 2785 CB GLN A 204 -4.211 -16.617 27.530 1.00 10.59 C ANISOU 2785 CB GLN A 204 1434 1158 1433 -153 94 85 C ATOM 2786 CG GLN A 204 -5.183 -17.501 28.289 1.00 11.73 C ANISOU 2786 CG GLN A 204 1550 1374 1532 -73 82 161 C ATOM 2787 CD GLN A 204 -4.651 -17.705 29.742 1.00 12.39 C ANISOU 2787 CD GLN A 204 1866 1216 1624 63 297 196 C ATOM 2788 OE1 GLN A 204 -3.719 -18.554 29.950 1.00 16.71 O ANISOU 2788 OE1 GLN A 204 2473 1936 1941 791 116 277 O ATOM 2789 NE2 GLN A 204 -5.146 -17.054 30.618 1.00 11.64 N ANISOU 2789 NE2 GLN A 204 1806 1023 1592 490 302 415 N ATOM 2790 H GLN A 204 -3.342 -18.308 25.580 1.00 11.38 H ATOM 2791 HA GLN A 204 -5.277 -16.376 25.754 1.00 11.36 H ATOM 2792 HB2 GLN A 204 -3.312 -16.899 27.759 1.00 12.73 H ATOM 2793 HB3 GLN A 204 -4.354 -15.702 27.819 1.00 12.73 H ATOM 2794 HG2 GLN A 204 -6.052 -17.072 28.332 1.00 14.09 H ATOM 2795 HG3 GLN A 204 -5.247 -18.366 27.856 1.00 14.09 H ATOM 2796 HE21 GLN A 204 -4.873 -17.145 31.429 1.00 13.98 H ATOM 2797 HE22 GLN A 204 -5.774 -16.496 30.436 1.00 13.98 H ATOM 2798 N LEU A 209 -3.745 -14.526 25.133 1.00 8.52 N ANISOU 2798 N LEU A 209 954 939 1346 -17 5 81 N ATOM 2799 CA LEU A 209 -2.810 -13.497 24.711 1.00 8.13 C ANISOU 2799 CA LEU A 209 955 890 1245 -121 31 43 C ATOM 2800 C LEU A 209 -2.009 -12.993 25.907 1.00 8.30 C ANISOU 2800 C LEU A 209 974 912 1266 1 140 13 C ATOM 2801 O LEU A 209 -2.551 -12.283 26.759 1.00 9.99 O ANISOU 2801 O LEU A 209 1045 1379 1372 274 -33 -126 O ATOM 2802 CB LEU A 209 -3.578 -12.337 24.087 1.00 8.31 C ANISOU 2802 CB LEU A 209 1032 896 1231 -45 -33 149 C ATOM 2803 CG LEU A 209 -2.684 -11.204 23.577 1.00 9.08 C ANISOU 2803 CG LEU A 209 1132 1041 1276 -4 -7 106 C ATOM 2804 CD1 LEU A 209 -1.840 -11.649 22.387 1.00 10.23 C ANISOU 2804 CD1 LEU A 209 1225 1266 1397 172 111 22 C ATOM 2805 CD2 LEU A 209 -3.544 -9.992 23.208 1.00 9.82 C ANISOU 2805 CD2 LEU A 209 1280 1140 1309 6 -157 224 C ATOM 2806 H LEU A 209 -4.564 -14.266 25.166 1.00 10.24 H ATOM 2807 HA LEU A 209 -2.191 -13.863 24.046 1.00 9.77 H ATOM 2808 HB2 LEU A 209 -4.091 -12.671 23.335 1.00 9.99 H ATOM 2809 HB3 LEU A 209 -4.177 -11.965 24.753 1.00 9.99 H ATOM 2810 HG LEU A 209 -2.080 -10.936 24.287 1.00 10.91 H ATOM 2811 HD11 LEU A 209 -1.296 -10.913 22.098 1.00 12.29 H ATOM 2812 HD12 LEU A 209 -1.283 -12.383 22.656 1.00 12.29 H ATOM 2813 HD13 LEU A 209 -2.424 -11.924 21.676 1.00 12.29 H ATOM 2814 HD21 LEU A 209 -2.973 -9.290 22.890 1.00 11.79 H ATOM 2815 HD22 LEU A 209 -4.164 -10.248 22.521 1.00 11.79 H ATOM 2816 HD23 LEU A 209 -4.021 -9.699 23.988 1.00 11.79 H ATOM 2817 N GLN A 210 -0.742 -13.394 25.955 1.00 8.24 N ANISOU 2817 N GLN A 210 1126 837 1167 -29 200 0 N ATOM 2818 CA GLN A 210 0.097 -13.036 27.104 1.00 7.80 C ANISOU 2818 CA GLN A 210 1006 865 1091 -18 117 81 C ATOM 2819 C GLN A 210 1.059 -11.917 26.813 1.00 7.41 C ANISOU 2819 C GLN A 210 1021 653 1140 9 48 58 C ATOM 2820 O GLN A 210 1.509 -11.224 27.736 1.00 7.82 O ANISOU 2820 O GLN A 210 1029 834 1109 -67 108 -32 O ATOM 2821 CB GLN A 210 0.900 -14.251 27.590 1.00 8.37 C ANISOU 2821 CB GLN A 210 1015 1005 1159 -27 60 246 C ATOM 2822 CG GLN A 210 0.007 -15.383 28.129 1.00 9.13 C ANISOU 2822 CG GLN A 210 1128 1045 1295 35 183 188 C ATOM 2823 CD GLN A 210 -0.570 -15.091 29.487 1.00 9.47 C ANISOU 2823 CD GLN A 210 1131 1044 1424 36 295 226 C ATOM 2824 OE1 GLN A 210 -0.639 -13.940 29.916 1.00 9.87 O ANISOU 2824 OE1 GLN A 210 1177 1100 1472 44 238 141 O ATOM 2825 NE2 GLN A 210 -0.993 -16.147 30.189 1.00 10.91 N ANISOU 2825 NE2 GLN A 210 1491 1198 1456 -49 343 379 N ATOM 2826 H GLN A 210 -0.349 -13.864 25.351 1.00 9.90 H ATOM 2827 HA GLN A 210 -0.483 -12.747 27.839 1.00 9.37 H ATOM 2828 HB2 GLN A 210 1.417 -14.605 26.850 1.00 10.05 H ATOM 2829 HB3 GLN A 210 1.493 -13.972 28.305 1.00 10.05 H ATOM 2830 HG2 GLN A 210 -0.731 -15.520 27.515 1.00 10.97 H ATOM 2831 HG3 GLN A 210 0.535 -16.194 28.198 1.00 10.97 H ATOM 2832 HE21 GLN A 210 -1.332 -16.036 30.972 1.00 13.11 H ATOM 2833 HE22 GLN A 210 -0.927 -16.938 29.857 1.00 13.11 H ATOM 2834 N GLY A 211 1.446 -11.724 25.549 1.00 7.81 N ANISOU 2834 N GLY A 211 996 813 1159 -151 107 3 N ATOM 2835 CA GLY A 211 2.444 -10.737 25.240 1.00 8.09 C ANISOU 2835 CA GLY A 211 973 998 1104 48 15 104 C ATOM 2836 C GLY A 211 2.149 -9.954 23.968 1.00 7.20 C ANISOU 2836 C GLY A 211 789 825 1120 50 11 -78 C ATOM 2837 O GLY A 211 1.448 -10.434 23.073 1.00 8.51 O ANISOU 2837 O GLY A 211 1024 1029 1179 -24 5 -71 O ATOM 2838 H GLY A 211 1.142 -12.153 24.868 1.00 9.39 H ATOM 2839 HA2 GLY A 211 2.510 -10.108 25.975 1.00 9.73 H ATOM 2840 HA3 GLY A 211 3.304 -11.173 25.135 1.00 9.73 H ATOM 2841 N VAL A 212 2.746 -8.771 23.923 1.00 7.60 N ANISOU 2841 N VAL A 212 926 804 1159 -84 -42 -18 N ATOM 2842 CA VAL A 212 2.784 -7.936 22.736 1.00 7.41 C ANISOU 2842 CA VAL A 212 945 761 1110 -41 1 94 C ATOM 2843 C VAL A 212 4.244 -7.783 22.348 1.00 7.30 C ANISOU 2843 C VAL A 212 914 766 1093 13 3 56 C ATOM 2844 O VAL A 212 5.073 -7.365 23.166 1.00 7.74 O ANISOU 2844 O VAL A 212 885 868 1188 -44 7 -85 O ATOM 2845 CB VAL A 212 2.179 -6.537 22.982 1.00 8.52 C ANISOU 2845 CB VAL A 212 1018 970 1247 116 33 112 C ATOM 2846 CG1 VAL A 212 2.254 -5.682 21.736 1.00 9.24 C ANISOU 2846 CG1 VAL A 212 1110 1078 1323 89 60 112 C ATOM 2847 CG2 VAL A 212 0.752 -6.635 23.499 1.00 10.67 C ANISOU 2847 CG2 VAL A 212 1226 1322 1505 357 182 232 C ATOM 2848 H VAL A 212 3.151 -8.419 24.595 1.00 9.14 H ATOM 2849 HA VAL A 212 2.301 -8.370 22.002 1.00 8.91 H ATOM 2850 HB VAL A 212 2.709 -6.091 23.675 1.00 10.23 H ATOM 2851 HG11 VAL A 212 1.871 -4.822 21.924 1.00 11.10 H ATOM 2852 HG12 VAL A 212 3.174 -5.582 21.482 1.00 11.10 H ATOM 2853 HG13 VAL A 212 1.764 -6.112 21.032 1.00 11.10 H ATOM 2854 HG21 VAL A 212 0.410 -5.749 23.640 1.00 12.81 H ATOM 2855 HG22 VAL A 212 0.216 -7.094 22.848 1.00 12.81 H ATOM 2856 HG23 VAL A 212 0.753 -7.122 24.326 1.00 12.81 H ATOM 2857 N VAL A 213 4.595 -8.106 21.110 1.00 7.38 N ANISOU 2857 N VAL A 213 895 839 1071 1 -3 -5 N ATOM 2858 CA VAL A 213 5.985 -7.939 20.636 1.00 7.31 C ANISOU 2858 CA VAL A 213 872 728 1179 -13 93 22 C ATOM 2859 C VAL A 213 6.366 -6.468 20.802 1.00 7.01 C ANISOU 2859 C VAL A 213 804 701 1160 -16 -8 158 C ATOM 2860 O VAL A 213 5.654 -5.564 20.332 1.00 7.62 O ANISOU 2860 O VAL A 213 984 753 1157 49 -65 86 O ATOM 2861 CB VAL A 213 6.102 -8.327 19.163 1.00 8.07 C ANISOU 2861 CB VAL A 213 972 853 1241 17 67 -60 C ATOM 2862 CG1 VAL A 213 7.526 -8.088 18.633 1.00 8.85 C ANISOU 2862 CG1 VAL A 213 1047 1073 1242 103 196 34 C ATOM 2863 CG2 VAL A 213 5.657 -9.743 18.843 1.00 9.22 C ANISOU 2863 CG2 VAL A 213 1172 1002 1328 67 7 -108 C ATOM 2864 H VAL A 213 4.057 -8.424 20.519 1.00 8.87 H ATOM 2865 HA VAL A 213 6.594 -8.493 21.167 1.00 8.79 H ATOM 2866 HB VAL A 213 5.513 -7.730 18.656 1.00 9.70 H ATOM 2867 HG11 VAL A 213 7.561 -8.342 17.708 1.00 10.63 H ATOM 2868 HG12 VAL A 213 7.742 -7.157 18.726 1.00 10.63 H ATOM 2869 HG13 VAL A 213 8.142 -8.619 19.142 1.00 10.63 H ATOM 2870 HG21 VAL A 213 5.765 -9.899 17.902 1.00 11.07 H ATOM 2871 HG22 VAL A 213 6.198 -10.360 19.341 1.00 11.07 H ATOM 2872 HG23 VAL A 213 4.734 -9.843 19.088 1.00 11.07 H ATOM 2873 N SER A 214 7.508 -6.220 21.472 1.00 8.01 N ANISOU 2873 N SER A 214 826 884 1334 0 6 -65 N ATOM 2874 CA SER A 214 7.934 -4.863 21.823 1.00 7.82 C ANISOU 2874 CA SER A 214 826 871 1276 123 70 -97 C ATOM 2875 C SER A 214 9.351 -4.548 21.295 1.00 7.87 C ANISOU 2875 C SER A 214 878 939 1173 23 88 105 C ATOM 2876 O SER A 214 9.473 -3.808 20.300 1.00 8.68 O ANISOU 2876 O SER A 214 990 1034 1274 -76 17 183 O ATOM 2877 CB SER A 214 7.726 -4.597 23.296 1.00 8.25 C ANISOU 2877 CB SER A 214 980 885 1271 1 62 -112 C ATOM 2878 OG SER A 214 8.065 -3.262 23.654 1.00 8.84 O ANISOU 2878 OG SER A 214 1130 994 1234 -15 13 -140 O ATOM 2879 H SER A 214 8.054 -6.831 21.734 1.00 9.63 H ATOM 2880 HA SER A 214 7.334 -4.247 21.354 1.00 9.40 H ATOM 2881 HB2 SER A 214 6.793 -4.750 23.512 1.00 9.92 H ATOM 2882 HB3 SER A 214 8.284 -5.207 23.805 1.00 9.92 H ATOM 2883 HG SER A 214 8.321 -2.850 22.993 1.00 10.62 H ATOM 2884 N TRP A 215 10.379 -5.100 21.896 1.00 7.82 N ANISOU 2884 N TRP A 215 833 884 1253 -15 95 122 N ATOM 2885 CA TRP A 215 11.726 -4.686 21.557 1.00 7.66 C ANISOU 2885 CA TRP A 215 825 908 1180 -85 49 29 C ATOM 2886 C TRP A 215 12.738 -5.765 21.820 1.00 7.75 C ANISOU 2886 C TRP A 215 884 807 1252 6 152 79 C ATOM 2887 O TRP A 215 12.444 -6.788 22.428 1.00 8.56 O ANISOU 2887 O TRP A 215 963 879 1410 10 147 205 O ATOM 2888 CB TRP A 215 12.111 -3.399 22.280 1.00 7.99 C ANISOU 2888 CB TRP A 215 836 990 1211 -70 40 -10 C ATOM 2889 CG TRP A 215 12.186 -3.449 23.780 1.00 7.93 C ANISOU 2889 CG TRP A 215 851 912 1251 -94 -72 20 C ATOM 2890 CD1 TRP A 215 11.159 -3.269 24.655 1.00 8.51 C ANISOU 2890 CD1 TRP A 215 989 1041 1202 -8 63 87 C ATOM 2891 CD2 TRP A 215 13.363 -3.654 24.597 1.00 8.25 C ANISOU 2891 CD2 TRP A 215 919 945 1271 -36 5 -51 C ATOM 2892 NE1 TRP A 215 11.621 -3.354 25.949 1.00 8.76 N ANISOU 2892 NE1 TRP A 215 1026 1070 1233 -73 99 -30 N ATOM 2893 CE2 TRP A 215 12.970 -3.555 25.933 1.00 8.41 C ANISOU 2893 CE2 TRP A 215 1001 944 1248 -66 11 10 C ATOM 2894 CE3 TRP A 215 14.708 -3.905 24.306 1.00 9.15 C ANISOU 2894 CE3 TRP A 215 971 1239 1268 -3 -32 70 C ATOM 2895 CZ2 TRP A 215 13.882 -3.730 26.986 1.00 9.47 C ANISOU 2895 CZ2 TRP A 215 1125 1168 1306 -19 -76 -82 C ATOM 2896 CZ3 TRP A 215 15.580 -4.077 25.348 1.00 10.05 C ANISOU 2896 CZ3 TRP A 215 1068 1377 1373 50 -104 -70 C ATOM 2897 CH2 TRP A 215 15.162 -3.977 26.658 1.00 10.04 C ANISOU 2897 CH2 TRP A 215 1186 1276 1353 85 -219 -51 C ATOM 2898 H TRP A 215 10.329 -5.711 22.499 1.00 9.39 H ATOM 2899 HA TRP A 215 11.753 -4.496 20.596 1.00 9.21 H ATOM 2900 HB2 TRP A 215 12.985 -3.124 21.960 1.00 9.61 H ATOM 2901 HB3 TRP A 215 11.460 -2.718 22.049 1.00 9.61 H ATOM 2902 HD1 TRP A 215 10.279 -3.091 24.414 1.00 10.22 H ATOM 2903 HE1 TRP A 215 11.142 -3.249 26.656 1.00 10.53 H ATOM 2904 HE3 TRP A 215 15.003 -3.951 23.426 1.00 11.00 H ATOM 2905 HZ2 TRP A 215 13.627 -3.603 27.871 1.00 11.38 H ATOM 2906 HZ3 TRP A 215 16.481 -4.221 25.167 1.00 12.07 H ATOM 2907 HH2 TRP A 215 15.785 -4.095 27.338 1.00 12.06 H ATOM 2908 N GLY A 216 13.974 -5.503 21.422 1.00 8.29 N ANISOU 2908 N GLY A 216 949 883 1318 29 88 128 N ATOM 2909 CA GLY A 216 15.105 -6.343 21.777 1.00 8.77 C ANISOU 2909 CA GLY A 216 979 996 1356 45 -16 133 C ATOM 2910 C GLY A 216 16.356 -5.640 21.257 1.00 9.45 C ANISOU 2910 C GLY A 216 985 1087 1519 81 9 271 C ATOM 2911 O GLY A 216 16.273 -4.661 20.523 1.00 10.97 O ANISOU 2911 O GLY A 216 1007 1302 1859 47 139 351 O ATOM 2912 H GLY A 216 14.187 -4.828 20.934 1.00 9.96 H ATOM 2913 HA2 GLY A 216 15.166 -6.444 22.740 1.00 10.53 H ATOM 2914 HA3 GLY A 216 15.027 -7.216 21.362 1.00 10.53 H ATOM 2915 N HIS A 217 17.534 -6.126 21.661 1.00 9.46 N ANISOU 2915 N HIS A 217 944 1130 1522 133 176 233 N ATOM 2916 CA HIS A 217 18.793 -5.611 21.082 1.00 9.71 C ANISOU 2916 CA HIS A 217 1029 1143 1518 -32 146 70 C ATOM 2917 C HIS A 217 19.181 -6.476 19.937 1.00 10.28 C ANISOU 2917 C HIS A 217 1079 1207 1619 -197 99 66 C ATOM 2918 O HIS A 217 19.524 -7.663 20.129 1.00 11.11 O ANISOU 2918 O HIS A 217 1137 1248 1835 -86 187 30 O ATOM 2919 CB HIS A 217 19.865 -5.514 22.148 1.00 11.90 C ANISOU 2919 CB HIS A 217 1405 1415 1703 -67 5 -76 C ATOM 2920 CG HIS A 217 19.647 -4.427 23.127 1.00 15.04 C ANISOU 2920 CG HIS A 217 1659 1896 2159 -81 99 -65 C ATOM 2921 ND1 HIS A 217 18.601 -3.496 23.125 1.00 18.08 N ANISOU 2921 ND1 HIS A 217 2274 2255 2340 92 116 -99 N ATOM 2922 CD2 HIS A 217 20.371 -4.176 24.215 1.00 16.78 C ANISOU 2922 CD2 HIS A 217 2009 2162 2204 -214 -83 -182 C ATOM 2923 CE1 HIS A 217 18.746 -2.696 24.189 1.00 17.22 C ANISOU 2923 CE1 HIS A 217 2155 2090 2298 127 -123 -220 C ATOM 2924 NE2 HIS A 217 19.808 -3.121 24.880 1.00 19.16 N ANISOU 2924 NE2 HIS A 217 2442 2395 2442 -137 151 -228 N ATOM 2925 H HIS A 217 17.637 -6.740 22.255 1.00 11.37 H ATOM 2926 HA HIS A 217 18.634 -4.709 20.734 1.00 11.67 H ATOM 2927 HB2 HIS A 217 19.895 -6.351 22.637 1.00 14.30 H ATOM 2928 HB3 HIS A 217 20.720 -5.356 21.717 1.00 14.30 H ATOM 2929 HD2 HIS A 217 21.123 -4.650 24.488 1.00 20.15 H ATOM 2930 HE1 HIS A 217 18.188 -1.990 24.422 1.00 20.68 H ATOM 2931 N GLY A 219 19.077 -5.930 18.721 1.00 11.41 N ANISOU 2931 N GLY A 219 1291 1395 1649 -149 107 91 N ATOM 2932 CA GLY A 219 19.171 -6.785 17.534 1.00 12.23 C ANISOU 2932 CA GLY A 219 1517 1464 1665 -121 73 140 C ATOM 2933 C GLY A 219 17.963 -7.677 17.463 1.00 11.29 C ANISOU 2933 C GLY A 219 1179 1413 1697 -143 130 74 C ATOM 2934 O GLY A 219 16.920 -7.412 18.062 1.00 11.61 O ANISOU 2934 O GLY A 219 1176 1268 1967 32 236 2 O ATOM 2935 H GLY A 219 18.955 -5.094 18.559 1.00 13.70 H ATOM 2936 HA2 GLY A 219 19.209 -6.239 16.733 1.00 14.69 H ATOM 2937 HA3 GLY A 219 19.969 -7.334 17.582 1.00 14.69 H ATOM 2938 N CYS A 220 18.087 -8.735 16.653 1.00 12.09 N ANISOU 2938 N CYS A 220 1337 1525 1732 -224 74 -22 N ATOM 2939 CA CYS A 220 17.033 -9.764 16.527 1.00 12.46 C ANISOU 2939 CA CYS A 220 1427 1523 1786 -56 32 142 C ATOM 2940 C CYS A 220 17.748 -11.084 16.545 1.00 11.35 C ANISOU 2940 C CYS A 220 1265 1361 1688 109 41 90 C ATOM 2941 O CYS A 220 18.629 -11.322 15.722 1.00 12.92 O ANISOU 2941 O CYS A 220 1296 1850 1761 86 241 62 O ATOM 2942 CB CYS A 220 16.229 -9.682 15.163 1.00 15.03 C ANISOU 2942 CB CYS A 220 1647 1873 2192 1 -199 145 C ATOM 2943 SG CYS A 220 15.479 -8.145 14.932 1.00 14.18 S ANISOU 2943 SG CYS A 220 1555 1692 2143 57 55 24 S ATOM 2944 H CYS A 220 18.776 -8.884 16.161 1.00 14.53 H ATOM 2945 HA CYS A 220 16.409 -9.716 17.281 1.00 14.97 H ATOM 2946 HB2 CYS A 220 16.841 -9.833 14.425 1.00 18.06 H ATOM 2947 HB3 CYS A 220 15.535 -10.359 15.163 1.00 18.06 H ATOM 2948 N ALA A 221 17.380 -11.950 17.477 1.00 10.85 N ANISOU 2948 N ALA A 221 1171 1332 1620 79 54 49 N ATOM 2949 CA ALA A 221 17.958 -13.272 17.557 1.00 11.60 C ANISOU 2949 CA ALA A 221 1274 1448 1685 154 -31 -109 C ATOM 2950 C ALA A 221 19.453 -13.286 17.839 1.00 11.39 C ANISOU 2950 C ALA A 221 1075 1494 1759 98 114 -88 C ATOM 2951 O ALA A 221 20.147 -14.270 17.551 1.00 12.29 O ANISOU 2951 O ALA A 221 1004 1648 2016 80 71 -137 O ATOM 2952 CB ALA A 221 17.606 -14.136 16.284 1.00 13.03 C ANISOU 2952 CB ALA A 221 1585 1603 1762 209 17 -171 C ATOM 2953 H ALA A 221 16.789 -11.790 18.080 1.00 13.04 H ATOM 2954 HA ALA A 221 17.536 -13.723 18.317 1.00 13.94 H ATOM 2955 HB1 ALA A 221 18.007 -15.003 16.376 1.00 15.65 H ATOM 2956 HB2 ALA A 221 16.652 -14.220 16.219 1.00 15.65 H ATOM 2957 HB3 ALA A 221 17.950 -13.696 15.504 1.00 15.65 H ATOM 2958 N TRP A 221A 19.957 -12.243 18.476 1.00 11.40 N ANISOU 2958 N TRP A 221A 1127 1613 1591 87 66 -88 N ATOM 2959 CA TRP A 221A 21.340 -12.192 18.904 1.00 12.12 C ANISOU 2959 CA TRP A 221A 1315 1598 1690 2 -35 9 C ATOM 2960 C TRP A 221A 21.520 -13.034 20.161 1.00 11.76 C ANISOU 2960 C TRP A 221A 1246 1418 1805 202 69 50 C ATOM 2961 O TRP A 221A 20.639 -13.110 21.044 1.00 12.44 O ANISOU 2961 O TRP A 221A 1320 1415 1991 107 232 118 O ATOM 2962 CB TRP A 221A 21.812 -10.785 19.164 1.00 13.83 C ANISOU 2962 CB TRP A 221A 1502 1813 1939 -74 76 251 C ATOM 2963 CG TRP A 221A 21.922 -9.938 17.939 1.00 15.12 C ANISOU 2963 CG TRP A 221A 1415 2114 2216 105 146 475 C ATOM 2964 CD1 TRP A 221A 21.483 -10.203 16.659 1.00 17.63 C ANISOU 2964 CD1 TRP A 221A 1912 2430 2357 -82 365 663 C ATOM 2965 CD2 TRP A 221A 22.487 -8.616 17.890 1.00 16.54 C ANISOU 2965 CD2 TRP A 221A 1577 2230 2478 206 449 539 C ATOM 2966 NE1 TRP A 221A 21.788 -9.109 15.809 1.00 18.54 N ANISOU 2966 NE1 TRP A 221A 1959 2611 2473 94 448 705 N ATOM 2967 CE2 TRP A 221A 22.390 -8.143 16.587 1.00 17.68 C ANISOU 2967 CE2 TRP A 221A 1829 2278 2611 266 584 686 C ATOM 2968 CE3 TRP A 221A 23.082 -7.826 18.848 1.00 19.85 C ANISOU 2968 CE3 TRP A 221A 2349 2432 2760 -52 600 612 C ATOM 2969 CZ2 TRP A 221A 22.881 -6.877 16.223 1.00 19.41 C ANISOU 2969 CZ2 TRP A 221A 2211 2418 2744 239 649 657 C ATOM 2970 CZ3 TRP A 221A 23.561 -6.577 18.471 1.00 21.78 C ANISOU 2970 CZ3 TRP A 221A 2702 2609 2963 -212 615 418 C ATOM 2971 CH2 TRP A 221A 23.418 -6.137 17.228 1.00 21.18 C ANISOU 2971 CH2 TRP A 221A 2575 2548 2925 130 630 570 C ATOM 2972 H TRP A 221A 19.507 -11.538 18.676 1.00 13.69 H ATOM 2973 HA TRP A 221A 21.905 -12.574 18.200 1.00 14.55 H ATOM 2974 HB2 TRP A 221A 21.185 -10.354 19.766 1.00 16.61 H ATOM 2975 HB3 TRP A 221A 22.689 -10.823 19.577 1.00 16.61 H ATOM 2976 HD1 TRP A 221A 21.072 -10.992 16.388 1.00 21.17 H ATOM 2977 HE1 TRP A 221A 21.605 -9.048 14.971 1.00 22.26 H ATOM 2978 HE3 TRP A 221A 23.153 -8.117 19.728 1.00 23.83 H ATOM 2979 HZ2 TRP A 221A 22.667 -6.494 15.403 1.00 23.30 H ATOM 2980 HZ3 TRP A 221A 23.944 -6.021 19.111 1.00 26.14 H ATOM 2981 HH2 TRP A 221A 23.768 -5.301 17.017 1.00 25.43 H ATOM 2982 N LYS A 222 22.698 -13.621 20.338 1.00 12.60 N ANISOU 2982 N LYS A 222 1312 1561 1914 360 -87 5 N ATOM 2983 CA LYS A 222 22.993 -14.372 21.512 1.00 14.67 C ANISOU 2983 CA LYS A 222 1537 1874 2165 488 -168 39 C ATOM 2984 C LYS A 222 22.839 -13.520 22.764 1.00 13.10 C ANISOU 2984 C LYS A 222 1351 1585 2043 317 -97 119 C ATOM 2985 O LYS A 222 23.230 -12.349 22.819 1.00 13.36 O ANISOU 2985 O LYS A 222 1371 1610 2095 70 39 279 O ATOM 2986 CB LYS A 222 24.468 -14.903 21.472 1.00 20.49 C ANISOU 2986 CB LYS A 222 2375 2609 2801 810 -175 44 C ATOM 2987 CG LYS A 222 24.756 -15.849 22.598 1.00 28.07 C ANISOU 2987 CG LYS A 222 3428 3555 3681 813 -293 38 C ATOM 2988 CD LYS A 222 26.247 -16.337 22.550 1.00 33.39 C ANISOU 2988 CD LYS A 222 4142 4209 4335 892 -355 75 C ATOM 2989 CE LYS A 222 26.399 -17.737 23.120 0.00 35.51 C ANISOU 2989 CE LYS A 222 4441 4460 4591 758 -383 39 C ATOM 2990 NZ LYS A 222 25.834 -17.855 24.491 0.00 36.85 N ANISOU 2990 NZ LYS A 222 4613 4613 4777 689 -395 22 N ATOM 2991 H LYS A 222 23.345 -13.589 19.772 1.00 15.13 H ATOM 2992 HA LYS A 222 22.385 -15.138 21.576 1.00 17.62 H ATOM 2993 HB2 LYS A 222 24.615 -15.374 20.637 1.00 24.60 H ATOM 2994 HB3 LYS A 222 25.079 -14.153 21.544 1.00 24.60 H ATOM 2995 HG2 LYS A 222 24.609 -15.397 23.444 1.00 33.70 H ATOM 2996 HG3 LYS A 222 24.177 -16.624 22.524 1.00 33.70 H ATOM 2997 HD2 LYS A 222 26.548 -16.351 21.628 1.00 40.08 H ATOM 2998 HD3 LYS A 222 26.797 -15.735 23.074 1.00 40.08 H ATOM 2999 HE2 LYS A 222 25.932 -18.365 22.547 0.00 42.63 H ATOM 3000 HE3 LYS A 222 27.341 -17.962 23.162 0.00 42.63 H ATOM 3001 HZ1 LYS A 222 25.949 -18.751 24.816 0.00 44.24 H ATOM 3002 HZ2 LYS A 222 26.283 -17.248 25.083 0.00 44.24 H ATOM 3003 HZ3 LYS A 222 24.898 -17.644 24.479 0.00 44.24 H ATOM 3004 N ASN A 223 22.217 -14.081 23.770 1.00 12.39 N ANISOU 3004 N ASN A 223 1402 1434 1871 226 -154 180 N ATOM 3005 CA ASN A 223 22.033 -13.454 25.072 1.00 13.37 C ANISOU 3005 CA ASN A 223 1536 1628 1918 24 -264 143 C ATOM 3006 C ASN A 223 21.113 -12.247 25.081 1.00 12.21 C ANISOU 3006 C ASN A 223 1263 1567 1810 59 68 218 C ATOM 3007 O ASN A 223 21.028 -11.547 26.084 1.00 13.35 O ANISOU 3007 O ASN A 223 1334 1888 1852 121 -47 44 O ATOM 3008 CB ASN A 223 23.367 -13.093 25.763 1.00 17.54 C ANISOU 3008 CB ASN A 223 2104 2182 2380 298 -769 161 C ATOM 3009 CG ASN A 223 24.184 -14.342 25.989 1.00 23.83 C ANISOU 3009 CG ASN A 223 2895 2991 3167 314 -834 175 C ATOM 3010 OD1 ASN A 223 23.653 -15.335 26.435 1.00 25.73 O ANISOU 3010 OD1 ASN A 223 3222 3205 3348 498 -873 336 O ATOM 3011 ND2 ASN A 223 25.452 -14.288 25.716 1.00 29.69 N ANISOU 3011 ND2 ASN A 223 3679 3720 3883 591 -733 78 N ATOM 3012 H ASN A 223 21.871 -14.868 23.729 1.00 14.88 H ATOM 3013 HA ASN A 223 21.604 -14.121 25.648 1.00 16.06 H ATOM 3014 HB2 ASN A 223 23.874 -12.491 25.197 1.00 21.07 H ATOM 3015 HB3 ASN A 223 23.187 -12.682 26.623 1.00 21.07 H ATOM 3016 HD21 ASN A 223 26.016 -15.079 25.850 1.00 35.65 H ATOM 3017 HD22 ASN A 223 25.845 -13.458 25.375 1.00 35.65 H ATOM 3018 N ARG A 224 20.374 -12.037 24.017 1.00 10.56 N ANISOU 3018 N ARG A 224 1007 1338 1666 91 63 96 N ATOM 3019 CA AARG A 224 19.509 -10.853 23.847 0.48 10.36 C ANISOU 3019 CA AARG A 224 1146 1264 1527 96 13 133 C ATOM 3020 CA BARG A 224 19.493 -10.857 23.875 0.52 12.35 C ANISOU 3020 CA BARG A 224 1238 1582 1874 47 240 218 C ATOM 3021 C ARG A 224 18.152 -11.349 23.386 1.00 10.67 C ANISOU 3021 C ARG A 224 1182 1299 1572 56 23 60 C ATOM 3022 O ARG A 224 17.775 -11.211 22.232 1.00 10.73 O ANISOU 3022 O ARG A 224 1280 1280 1516 -111 111 -4 O ATOM 3023 CB AARG A 224 20.125 -9.885 22.821 0.48 11.69 C ANISOU 3023 CB AARG A 224 1349 1436 1657 165 98 102 C ATOM 3024 CB BARG A 224 20.128 -9.843 22.914 0.52 14.22 C ANISOU 3024 CB BARG A 224 1323 1844 2236 -105 288 385 C ATOM 3025 CG AARG A 224 21.548 -9.417 23.229 0.48 17.19 C ANISOU 3025 CG AARG A 224 2125 2137 2269 57 167 -28 C ATOM 3026 CG BARG A 224 21.319 -9.093 23.600 0.52 15.72 C ANISOU 3026 CG BARG A 224 1450 1948 2575 -200 306 491 C ATOM 3027 CD AARG A 224 22.135 -8.294 22.379 0.48 21.84 C ANISOU 3027 CD AARG A 224 2796 2733 2768 69 143 12 C ATOM 3028 CD BARG A 224 22.344 -8.554 22.735 0.52 17.24 C ANISOU 3028 CD BARG A 224 1642 2097 2813 214 549 353 C ATOM 3029 NE AARG A 224 23.606 -8.448 22.208 0.48 21.72 N ANISOU 3029 NE AARG A 224 2885 2649 2718 21 -6 57 N ATOM 3030 NE BARG A 224 23.210 -9.666 22.421 0.52 18.15 N ANISOU 3030 NE BARG A 224 1635 2306 2956 -30 763 182 N ATOM 3031 CZ AARG A 224 24.528 -7.538 22.492 0.48 20.56 C ANISOU 3031 CZ AARG A 224 2704 2591 2514 -57 -121 -130 C ATOM 3032 CZ BARG A 224 24.350 -9.553 21.761 0.52 18.12 C ANISOU 3032 CZ BARG A 224 1544 2399 2942 -380 676 40 C ATOM 3033 NH1AARG A 224 24.192 -6.334 22.985 0.48 24.80 N ANISOU 3033 NH1AARG A 224 3162 3173 3088 28 109 54 N ATOM 3034 NH1BARG A 224 24.834 -8.322 21.343 0.52 19.19 N ANISOU 3034 NH1BARG A 224 1818 2621 2853 -156 559 -41 N ATOM 3035 NH2AARG A 224 25.771 -7.797 22.157 0.48 17.79 N ANISOU 3035 NH2AARG A 224 2338 2210 2212 -255 -137 -253 N ATOM 3036 NH2BARG A 224 24.988 -10.675 21.596 0.52 16.24 N ANISOU 3036 NH2BARG A 224 1011 2159 3001 -570 532 -70 N ATOM 3037 H AARG A 224 20.344 -12.576 23.347 1.00 12.68 H ATOM 3038 HA AARG A 224 19.405 -10.388 24.703 0.48 12.45 H ATOM 3039 HB2AARG A 224 20.190 -10.332 21.963 0.48 14.05 H ATOM 3040 HB3AARG A 224 19.560 -9.100 22.746 0.48 14.05 H ATOM 3041 HG2AARG A 224 21.517 -9.103 24.146 0.48 20.64 H ATOM 3042 HG3AARG A 224 22.150 -10.175 23.166 0.48 20.64 H ATOM 3043 HD2AARG A 224 21.724 -8.309 21.500 0.48 26.22 H ATOM 3044 HD3AARG A 224 21.967 -7.443 22.813 0.48 26.22 H ATOM 3045 HE AARG A 224 23.920 -9.295 21.856 0.48 26.08 H ATOM 3046 HH11AARG A 224 23.369 -6.155 23.161 0.48 29.77 H ATOM 3047 HH12AARG A 224 24.804 -5.755 23.161 0.48 29.77 H ATOM 3048 HH21AARG A 224 25.977 -8.573 21.847 0.48 21.36 H ATOM 3049 HH22AARG A 224 26.393 -7.238 22.356 0.48 21.36 H ATOM 3050 N PRO A 225 17.348 -11.917 24.309 1.00 10.41 N ANISOU 3050 N PRO A 225 1028 1463 1466 154 62 89 N ATOM 3051 CA PRO A 225 16.024 -12.427 23.933 1.00 10.08 C ANISOU 3051 CA PRO A 225 1173 1239 1416 -25 52 45 C ATOM 3052 C PRO A 225 15.029 -11.324 23.621 1.00 8.51 C ANISOU 3052 C PRO A 225 948 909 1375 -221 52 -77 C ATOM 3053 O PRO A 225 15.263 -10.165 23.903 1.00 9.81 O ANISOU 3053 O PRO A 225 990 1089 1649 84 -10 -168 O ATOM 3054 CB PRO A 225 15.630 -13.205 25.188 1.00 11.03 C ANISOU 3054 CB PRO A 225 1323 1346 1523 167 77 132 C ATOM 3055 CG PRO A 225 16.277 -12.444 26.272 1.00 11.76 C ANISOU 3055 CG PRO A 225 1393 1558 1517 146 132 209 C ATOM 3056 CD PRO A 225 17.588 -12.005 25.745 1.00 11.54 C ANISOU 3056 CD PRO A 225 1267 1556 1561 107 12 355 C ATOM 3057 HA PRO A 225 16.092 -13.039 23.171 1.00 12.11 H ATOM 3058 HB2 PRO A 225 14.665 -13.205 25.290 1.00 13.25 H ATOM 3059 HB3 PRO A 225 15.977 -14.110 25.142 1.00 13.25 H ATOM 3060 HG2 PRO A 225 15.729 -11.677 26.501 1.00 14.13 H ATOM 3061 HG3 PRO A 225 16.396 -13.018 27.045 1.00 14.13 H ATOM 3062 HD2 PRO A 225 17.825 -11.135 26.104 1.00 13.86 H ATOM 3063 HD3 PRO A 225 18.270 -12.668 25.936 1.00 13.86 H ATOM 3064 N GLY A 226 13.889 -11.671 23.072 1.00 8.96 N ANISOU 3064 N GLY A 226 1080 955 1371 -100 17 -50 N ATOM 3065 CA GLY A 226 12.850 -10.695 22.822 1.00 8.61 C ANISOU 3065 CA GLY A 226 997 1030 1245 127 -55 35 C ATOM 3066 C GLY A 226 12.208 -10.229 24.110 1.00 7.55 C ANISOU 3066 C GLY A 226 828 842 1200 30 -57 144 C ATOM 3067 O GLY A 226 12.042 -11.001 25.066 1.00 8.64 O ANISOU 3067 O GLY A 226 1053 969 1260 -6 27 93 O ATOM 3068 H GLY A 226 13.687 -12.472 22.832 1.00 10.77 H ATOM 3069 HA2 GLY A 226 13.228 -9.925 22.367 1.00 10.35 H ATOM 3070 HA3 GLY A 226 12.166 -11.084 22.256 1.00 10.35 H ATOM 3071 N VAL A 227 11.799 -8.956 24.105 1.00 7.99 N ANISOU 3071 N VAL A 227 923 877 1238 88 20 124 N ATOM 3072 CA VAL A 227 11.127 -8.334 25.233 1.00 7.68 C ANISOU 3072 CA VAL A 227 956 813 1149 51 -62 44 C ATOM 3073 C VAL A 227 9.697 -8.003 24.775 1.00 7.16 C ANISOU 3073 C VAL A 227 918 639 1164 13 -67 174 C ATOM 3074 O VAL A 227 9.479 -7.398 23.721 1.00 8.05 O ANISOU 3074 O VAL A 227 858 874 1326 78 60 212 O ATOM 3075 CB VAL A 227 11.856 -7.092 25.768 1.00 8.18 C ANISOU 3075 CB VAL A 227 952 937 1218 11 -98 69 C ATOM 3076 CG1 VAL A 227 11.183 -6.602 27.041 1.00 9.28 C ANISOU 3076 CG1 VAL A 227 1109 1101 1316 -74 18 -102 C ATOM 3077 CG2 VAL A 227 13.318 -7.408 26.018 1.00 9.61 C ANISOU 3077 CG2 VAL A 227 1120 1161 1371 111 -138 141 C ATOM 3078 H VAL A 227 11.905 -8.425 23.437 1.00 9.61 H ATOM 3079 HA VAL A 227 11.067 -8.984 25.964 1.00 9.23 H ATOM 3080 HB VAL A 227 11.807 -6.376 25.100 1.00 9.83 H ATOM 3081 HG11 VAL A 227 11.650 -5.826 27.362 1.00 11.15 H ATOM 3082 HG12 VAL A 227 10.271 -6.377 26.845 1.00 11.15 H ATOM 3083 HG13 VAL A 227 11.215 -7.299 27.700 1.00 11.15 H ATOM 3084 HG21 VAL A 227 13.755 -6.621 26.351 1.00 11.55 H ATOM 3085 HG22 VAL A 227 13.378 -8.115 26.665 1.00 11.55 H ATOM 3086 HG23 VAL A 227 13.723 -7.684 25.192 1.00 11.55 H ATOM 3087 N TYR A 228 8.731 -8.333 25.621 1.00 7.45 N ANISOU 3087 N TYR A 228 884 847 1101 -40 -24 79 N ATOM 3088 CA TYR A 228 7.303 -8.297 25.294 1.00 7.17 C ANISOU 3088 CA TYR A 228 801 792 1131 1 36 -9 C ATOM 3089 C TYR A 228 6.542 -7.589 26.416 1.00 7.25 C ANISOU 3089 C TYR A 228 853 818 1083 4 17 123 C ATOM 3090 O TYR A 228 6.922 -7.650 27.606 1.00 8.25 O ANISOU 3090 O TYR A 228 979 991 1164 203 -36 36 O ATOM 3091 CB TYR A 228 6.803 -9.748 25.178 1.00 7.66 C ANISOU 3091 CB TYR A 228 901 858 1150 -85 -50 64 C ATOM 3092 CG TYR A 228 7.498 -10.492 24.042 1.00 7.27 C ANISOU 3092 CG TYR A 228 1019 601 1142 103 24 14 C ATOM 3093 CD1 TYR A 228 8.711 -11.147 24.244 1.00 7.65 C ANISOU 3093 CD1 TYR A 228 1020 748 1137 43 -45 -48 C ATOM 3094 CD2 TYR A 228 6.968 -10.481 22.778 1.00 8.27 C ANISOU 3094 CD2 TYR A 228 1137 847 1159 -5 -58 -5 C ATOM 3095 CE1 TYR A 228 9.397 -11.767 23.204 1.00 8.68 C ANISOU 3095 CE1 TYR A 228 1146 922 1230 52 23 -59 C ATOM 3096 CE2 TYR A 228 7.643 -11.063 21.739 1.00 8.76 C ANISOU 3096 CE2 TYR A 228 1223 1003 1104 82 -103 -80 C ATOM 3097 CZ TYR A 228 8.823 -11.697 21.915 1.00 9.00 C ANISOU 3097 CZ TYR A 228 1253 1002 1164 70 251 -59 C ATOM 3098 OH TYR A 228 9.461 -12.254 20.848 1.00 9.98 O ANISOU 3098 OH TYR A 228 1402 1161 1227 221 213 13 O ATOM 3099 H TYR A 228 8.882 -8.593 26.427 1.00 8.96 H ATOM 3100 HA TYR A 228 7.153 -7.827 24.446 1.00 8.61 H ATOM 3101 HB2 TYR A 228 6.988 -10.218 26.006 1.00 9.20 H ATOM 3102 HB3 TYR A 228 5.849 -9.745 25.000 1.00 9.20 H ATOM 3103 HD1 TYR A 228 9.084 -11.151 25.095 1.00 9.19 H ATOM 3104 HD2 TYR A 228 6.178 -10.018 22.614 1.00 9.94 H ATOM 3105 HE1 TYR A 228 10.214 -12.187 23.347 1.00 10.43 H ATOM 3106 HE2 TYR A 228 7.272 -11.030 20.886 1.00 10.53 H ATOM 3107 HH TYR A 228 9.561 -13.059 20.970 1.00 11.98 H ATOM 3108 N THR A 229 5.460 -6.929 26.051 1.00 7.29 N ANISOU 3108 N THR A 229 894 767 1111 27 -107 -7 N ATOM 3109 CA THR A 229 4.606 -6.311 27.060 1.00 7.23 C ANISOU 3109 CA THR A 229 845 754 1149 132 5 10 C ATOM 3110 C THR A 229 3.691 -7.386 27.657 1.00 7.29 C ANISOU 3110 C THR A 229 823 742 1207 106 -25 -50 C ATOM 3111 O THR A 229 3.082 -8.189 26.927 1.00 7.97 O ANISOU 3111 O THR A 229 919 825 1283 -105 -30 -94 O ATOM 3112 CB THR A 229 3.761 -5.195 26.465 1.00 7.78 C ANISOU 3112 CB THR A 229 972 797 1187 36 20 3 C ATOM 3113 OG1 THR A 229 4.617 -4.279 25.860 1.00 9.07 O ANISOU 3113 OG1 THR A 229 1057 913 1477 -24 -13 128 O ATOM 3114 CG2 THR A 229 2.892 -4.517 27.501 1.00 9.32 C ANISOU 3114 CG2 THR A 229 1202 1020 1318 186 -26 -48 C ATOM 3115 H THR A 229 5.195 -6.823 25.239 1.00 8.77 H ATOM 3116 HA THR A 229 5.161 -5.937 27.776 1.00 8.70 H ATOM 3117 HB THR A 229 3.177 -5.571 25.788 1.00 9.35 H ATOM 3118 HG1 THR A 229 4.184 -3.665 25.531 1.00 10.90 H ATOM 3119 HG21 THR A 229 2.375 -3.821 27.090 1.00 11.19 H ATOM 3120 HG22 THR A 229 2.296 -5.157 27.898 1.00 11.19 H ATOM 3121 HG23 THR A 229 3.441 -4.134 28.189 1.00 11.19 H ATOM 3122 N LYS A 230 3.616 -7.398 28.987 1.00 7.84 N ANISOU 3122 N LYS A 230 938 867 1176 -7 50 -74 N ATOM 3123 CA LYS A 230 2.819 -8.343 29.766 1.00 8.52 C ANISOU 3123 CA LYS A 230 989 1014 1234 40 50 -68 C ATOM 3124 C LYS A 230 1.353 -7.948 29.759 1.00 7.71 C ANISOU 3124 C LYS A 230 930 791 1208 203 142 75 C ATOM 3125 O LYS A 230 0.884 -7.110 30.544 1.00 8.76 O ANISOU 3125 O LYS A 230 919 1000 1408 100 112 -29 O ATOM 3126 CB LYS A 230 3.385 -8.397 31.186 1.00 10.21 C ANISOU 3126 CB LYS A 230 1190 1301 1389 -34 142 143 C ATOM 3127 CG LYS A 230 2.735 -9.487 32.041 1.00 13.22 C ANISOU 3127 CG LYS A 230 1602 1694 1728 -134 -31 431 C ATOM 3128 CD LYS A 230 3.425 -9.637 33.403 1.00 16.93 C ANISOU 3128 CD LYS A 230 2133 2101 2199 158 -169 611 C ATOM 3129 CE LYS A 230 4.593 -10.507 33.272 1.00 20.14 C ANISOU 3129 CE LYS A 230 2479 2583 2590 183 -504 571 C ATOM 3130 NZ LYS A 230 5.376 -10.538 34.597 1.00 22.79 N ANISOU 3130 NZ LYS A 230 2795 2925 2939 173 -797 584 N ATOM 3131 H LYS A 230 4.041 -6.839 29.483 1.00 9.43 H ATOM 3132 HA LYS A 230 2.898 -9.236 29.370 1.00 10.24 H ATOM 3133 HB2 LYS A 230 4.337 -8.578 31.140 1.00 12.27 H ATOM 3134 HB3 LYS A 230 3.230 -7.543 31.620 1.00 12.27 H ATOM 3135 HG2 LYS A 230 1.805 -9.258 32.197 1.00 15.88 H ATOM 3136 HG3 LYS A 230 2.797 -10.336 31.575 1.00 15.88 H ATOM 3137 HD2 LYS A 230 3.720 -8.768 33.716 1.00 20.33 H ATOM 3138 HD3 LYS A 230 2.810 -10.038 34.037 1.00 20.33 H ATOM 3139 HE2 LYS A 230 4.304 -11.409 33.063 1.00 24.18 H ATOM 3140 HE3 LYS A 230 5.176 -10.165 32.576 1.00 24.18 H ATOM 3141 HZ1 LYS A 230 6.143 -11.109 34.512 1.00 27.37 H ATOM 3142 HZ2 LYS A 230 5.670 -9.653 34.825 1.00 27.37 H ATOM 3143 HZ3 LYS A 230 4.816 -10.871 35.302 1.00 27.37 H ATOM 3144 N VAL A 231 0.595 -8.596 28.887 1.00 7.63 N ANISOU 3144 N VAL A 231 855 847 1196 15 63 -45 N ATOM 3145 CA VAL A 231 -0.819 -8.241 28.650 1.00 7.18 C ANISOU 3145 CA VAL A 231 852 753 1125 119 32 37 C ATOM 3146 C VAL A 231 -1.644 -8.386 29.915 1.00 7.26 C ANISOU 3146 C VAL A 231 784 751 1224 49 -9 24 C ATOM 3147 O VAL A 231 -2.579 -7.607 30.155 1.00 7.93 O ANISOU 3147 O VAL A 231 927 834 1251 119 23 28 O ATOM 3148 CB VAL A 231 -1.385 -9.075 27.497 1.00 7.91 C ANISOU 3148 CB VAL A 231 981 865 1159 89 -17 -138 C ATOM 3149 CG1 VAL A 231 -2.889 -8.891 27.357 1.00 9.48 C ANISOU 3149 CG1 VAL A 231 1179 1150 1271 -32 -34 -48 C ATOM 3150 CG2 VAL A 231 -0.691 -8.649 26.195 1.00 8.52 C ANISOU 3150 CG2 VAL A 231 1027 1016 1196 254 7 -106 C ATOM 3151 H VAL A 231 0.870 -9.255 28.408 1.00 9.17 H ATOM 3152 HA VAL A 231 -0.860 -7.300 28.379 1.00 8.64 H ATOM 3153 HB VAL A 231 -1.199 -10.024 27.655 1.00 9.51 H ATOM 3154 HG11 VAL A 231 -3.202 -9.429 26.626 1.00 11.38 H ATOM 3155 HG12 VAL A 231 -3.314 -9.166 28.172 1.00 11.38 H ATOM 3156 HG13 VAL A 231 -3.075 -7.965 27.186 1.00 11.38 H ATOM 3157 HG21 VAL A 231 -1.043 -9.169 25.469 1.00 10.24 H ATOM 3158 HG22 VAL A 231 -0.859 -7.717 26.042 1.00 10.24 H ATOM 3159 HG23 VAL A 231 0.253 -8.802 26.280 1.00 10.24 H ATOM 3160 N TYR A 232 -1.299 -9.371 30.764 1.00 7.85 N ANISOU 3160 N TYR A 232 916 859 1208 109 86 140 N ATOM 3161 CA TYR A 232 -2.073 -9.586 31.991 1.00 7.99 C ANISOU 3161 CA TYR A 232 976 819 1239 -17 110 148 C ATOM 3162 C TYR A 232 -2.160 -8.304 32.800 1.00 7.96 C ANISOU 3162 C TYR A 232 971 797 1256 -56 140 188 C ATOM 3163 O TYR A 232 -3.183 -8.046 33.457 1.00 9.21 O ANISOU 3163 O TYR A 232 1135 1031 1335 -17 317 41 O ATOM 3164 CB TYR A 232 -1.409 -10.723 32.814 1.00 8.47 C ANISOU 3164 CB TYR A 232 1109 871 1236 13 156 183 C ATOM 3165 CG TYR A 232 -2.054 -10.917 34.137 1.00 9.19 C ANISOU 3165 CG TYR A 232 1203 892 1398 21 231 127 C ATOM 3166 CD1 TYR A 232 -3.259 -11.588 34.288 1.00 10.58 C ANISOU 3166 CD1 TYR A 232 1408 1066 1545 29 347 157 C ATOM 3167 CD2 TYR A 232 -1.436 -10.382 35.269 1.00 11.06 C ANISOU 3167 CD2 TYR A 232 1439 1212 1549 9 211 142 C ATOM 3168 CE1 TYR A 232 -3.867 -11.702 35.509 1.00 12.51 C ANISOU 3168 CE1 TYR A 232 1667 1318 1767 104 503 374 C ATOM 3169 CE2 TYR A 232 -2.051 -10.457 36.514 1.00 13.27 C ANISOU 3169 CE2 TYR A 232 1827 1554 1663 289 446 324 C ATOM 3170 CZ TYR A 232 -3.231 -11.132 36.636 1.00 13.39 C ANISOU 3170 CZ TYR A 232 1874 1528 1685 451 753 534 C ATOM 3171 OH TYR A 232 -3.842 -11.227 37.849 1.00 18.25 O ANISOU 3171 OH TYR A 232 2661 2245 2028 673 1047 527 O ATOM 3172 H TYR A 232 -0.639 -9.912 30.653 1.00 9.43 H ATOM 3173 HA TYR A 232 -2.983 -9.865 31.757 1.00 9.60 H ATOM 3174 HB2 TYR A 232 -1.479 -11.555 32.319 1.00 10.17 H ATOM 3175 HB3 TYR A 232 -0.476 -10.503 32.963 1.00 10.17 H ATOM 3176 HD1 TYR A 232 -3.677 -11.945 33.537 1.00 12.71 H ATOM 3177 HD2 TYR A 232 -0.645 -9.903 35.176 1.00 13.28 H ATOM 3178 HE1 TYR A 232 -4.679 -12.147 35.596 1.00 15.02 H ATOM 3179 HE2 TYR A 232 -1.638 -10.095 37.264 1.00 15.94 H ATOM 3180 HH TYR A 232 -3.944 -12.016 38.050 1.00 21.91 H ATOM 3181 N ASN A 233 -1.106 -7.488 32.844 1.00 7.93 N ANISOU 3181 N ASN A 233 912 893 1209 59 7 -17 N ATOM 3182 CA ASN A 233 -1.110 -6.276 33.655 1.00 8.24 C ANISOU 3182 CA ASN A 233 1060 865 1207 -161 -153 2 C ATOM 3183 C ASN A 233 -2.113 -5.241 33.181 1.00 8.34 C ANISOU 3183 C ASN A 233 1058 852 1260 109 -81 31 C ATOM 3184 O ASN A 233 -2.365 -4.288 33.914 1.00 11.03 O ANISOU 3184 O ASN A 233 1534 1219 1436 392 53 -232 O ATOM 3185 CB ASN A 233 0.302 -5.682 33.714 1.00 10.32 C ANISOU 3185 CB ASN A 233 1267 1223 1432 26 91 -72 C ATOM 3186 CG ASN A 233 1.261 -6.533 34.474 1.00 11.83 C ANISOU 3186 CG ASN A 233 1274 1520 1702 -173 -49 55 C ATOM 3187 OD1 ASN A 233 0.918 -7.588 35.023 1.00 14.28 O ANISOU 3187 OD1 ASN A 233 1504 1747 2175 57 -479 258 O ATOM 3188 ND2 ASN A 233 2.455 -6.015 34.642 1.00 13.79 N ANISOU 3188 ND2 ASN A 233 1612 1780 1849 -28 2 -84 N ATOM 3189 H ASN A 233 -0.374 -7.617 32.411 1.00 9.53 H ATOM 3190 HA ASN A 233 -1.359 -6.522 34.570 1.00 9.90 H ATOM 3191 HB2 ASN A 233 0.641 -5.585 32.810 1.00 12.40 H ATOM 3192 HB3 ASN A 233 0.262 -4.816 34.147 1.00 12.40 H ATOM 3193 HD21 ASN A 233 3.141 -6.514 35.132 1.00 16.57 H ATOM 3194 HD22 ASN A 233 2.661 -5.129 34.277 1.00 16.57 H ATOM 3195 N TYR A 234 -2.679 -5.417 31.989 1.00 7.87 N ANISOU 3195 N TYR A 234 885 892 1213 89 16 53 N ATOM 3196 CA TYR A 234 -3.518 -4.435 31.323 1.00 8.24 C ANISOU 3196 CA TYR A 234 996 913 1224 11 90 93 C ATOM 3197 C TYR A 234 -4.936 -4.967 31.122 1.00 7.94 C ANISOU 3197 C TYR A 234 1058 655 1305 80 35 133 C ATOM 3198 O TYR A 234 -5.704 -4.297 30.458 1.00 8.87 O ANISOU 3198 O TYR A 234 1081 846 1444 171 -6 107 O ATOM 3199 CB TYR A 234 -2.902 -4.024 29.978 1.00 8.82 C ANISOU 3199 CB TYR A 234 1048 989 1313 3 58 173 C ATOM 3200 CG TYR A 234 -1.560 -3.416 30.192 1.00 8.34 C ANISOU 3200 CG TYR A 234 1035 821 1312 38 57 33 C ATOM 3201 CD1 TYR A 234 -1.424 -2.114 30.602 1.00 8.90 C ANISOU 3201 CD1 TYR A 234 1106 915 1362 28 61 -29 C ATOM 3202 CD2 TYR A 234 -0.420 -4.196 30.106 1.00 8.72 C ANISOU 3202 CD2 TYR A 234 1087 871 1357 130 170 59 C ATOM 3203 CE1 TYR A 234 -0.175 -1.545 30.933 1.00 9.57 C ANISOU 3203 CE1 TYR A 234 1145 963 1528 -41 124 47 C ATOM 3204 CE2 TYR A 234 0.823 -3.676 30.409 1.00 9.65 C ANISOU 3204 CE2 TYR A 234 1057 1074 1536 90 301 123 C ATOM 3205 CZ TYR A 234 0.948 -2.386 30.855 1.00 9.34 C ANISOU 3205 CZ TYR A 234 898 1037 1613 -12 165 -15 C ATOM 3206 OH TYR A 234 2.179 -1.942 31.183 1.00 11.19 O ANISOU 3206 OH TYR A 234 1059 1330 1865 -40 42 16 O ATOM 3207 H TYR A 234 -2.583 -6.137 31.528 1.00 9.46 H ATOM 3208 HA TYR A 234 -3.574 -3.634 31.885 1.00 9.91 H ATOM 3209 HB2 TYR A 234 -2.799 -4.807 29.415 1.00 10.59 H ATOM 3210 HB3 TYR A 234 -3.472 -3.368 29.547 1.00 10.59 H ATOM 3211 HD1 TYR A 234 -2.189 -1.595 30.700 1.00 10.70 H ATOM 3212 HD2 TYR A 234 -0.495 -5.090 29.861 1.00 10.48 H ATOM 3213 HE1 TYR A 234 -0.104 -0.666 31.228 1.00 11.50 H ATOM 3214 HE2 TYR A 234 1.573 -4.224 30.368 1.00 11.60 H ATOM 3215 HH TYR A 234 2.188 -1.695 31.965 1.00 13.45 H ATOM 3216 N VAL A 235 -5.295 -6.088 31.721 1.00 8.93 N ANISOU 3216 N VAL A 235 1110 851 1430 80 17 26 N ATOM 3217 CA VAL A 235 -6.658 -6.603 31.481 1.00 9.32 C ANISOU 3217 CA VAL A 235 1097 987 1456 62 107 15 C ATOM 3218 C VAL A 235 -7.723 -5.569 31.863 1.00 8.97 C ANISOU 3218 C VAL A 235 947 1026 1433 105 37 92 C ATOM 3219 O VAL A 235 -8.652 -5.320 31.097 1.00 9.22 O ANISOU 3219 O VAL A 235 942 1075 1487 100 -35 17 O ATOM 3220 CB VAL A 235 -6.856 -7.943 32.189 1.00 10.66 C ANISOU 3220 CB VAL A 235 1165 1253 1633 41 66 130 C ATOM 3221 CG1 VAL A 235 -8.315 -8.349 32.183 1.00 12.90 C ANISOU 3221 CG1 VAL A 235 1494 1548 1859 -161 72 175 C ATOM 3222 CG2 VAL A 235 -6.014 -9.015 31.491 1.00 11.82 C ANISOU 3222 CG2 VAL A 235 1448 1273 1771 176 -91 -30 C ATOM 3223 H VAL A 235 -4.805 -6.559 32.248 1.00 10.73 H ATOM 3224 HA VAL A 235 -6.753 -6.770 30.520 1.00 11.19 H ATOM 3225 HB VAL A 235 -6.557 -7.869 33.119 1.00 12.81 H ATOM 3226 HG11 VAL A 235 -8.405 -9.192 32.634 1.00 15.50 H ATOM 3227 HG12 VAL A 235 -8.827 -7.677 32.638 1.00 15.50 H ATOM 3228 HG13 VAL A 235 -8.613 -8.430 31.274 1.00 15.50 H ATOM 3229 HG21 VAL A 235 -6.142 -9.854 31.939 1.00 14.20 H ATOM 3230 HG22 VAL A 235 -6.295 -9.087 30.576 1.00 14.20 H ATOM 3231 HG23 VAL A 235 -5.089 -8.761 31.530 1.00 14.20 H ATOM 3232 N ASP A 236 -7.607 -4.979 33.049 1.00 8.72 N ANISOU 3232 N ASP A 236 1029 945 1341 177 63 -4 N ATOM 3233 CA ASP A 236 -8.587 -3.986 33.471 1.00 9.60 C ANISOU 3233 CA ASP A 236 1244 1003 1399 186 184 27 C ATOM 3234 C ASP A 236 -8.569 -2.748 32.594 1.00 8.61 C ANISOU 3234 C ASP A 236 1050 823 1398 161 45 -48 C ATOM 3235 O ASP A 236 -9.620 -2.212 32.211 1.00 9.35 O ANISOU 3235 O ASP A 236 1061 1006 1485 136 8 -17 O ATOM 3236 CB ASP A 236 -8.391 -3.600 34.916 1.00 11.41 C ANISOU 3236 CB ASP A 236 1635 1159 1543 247 246 54 C ATOM 3237 CG ASP A 236 -8.663 -4.700 35.926 1.00 13.18 C ANISOU 3237 CG ASP A 236 1913 1474 1621 103 142 6 C ATOM 3238 OD1 ASP A 236 -9.409 -5.643 35.613 1.00 14.12 O ANISOU 3238 OD1 ASP A 236 2164 1369 1831 -38 334 18 O ATOM 3239 OD2 ASP A 236 -8.103 -4.573 37.052 1.00 15.37 O ANISOU 3239 OD2 ASP A 236 2247 1959 1633 65 159 68 O ATOM 3240 H ASP A 236 -6.982 -5.133 33.619 1.00 10.48 H ATOM 3241 HA ASP A 236 -9.479 -4.383 33.394 1.00 11.53 H ATOM 3242 HB2 ASP A 236 -7.471 -3.317 35.036 1.00 13.71 H ATOM 3243 HB3 ASP A 236 -8.986 -2.863 35.121 1.00 13.71 H ATOM 3244 N TRP A 237 -7.370 -2.281 32.258 1.00 8.10 N ANISOU 3244 N TRP A 237 961 872 1247 28 63 -39 N ATOM 3245 CA TRP A 237 -7.270 -1.125 31.355 1.00 8.78 C ANISOU 3245 CA TRP A 237 1040 1000 1295 101 27 -101 C ATOM 3246 C TRP A 237 -7.937 -1.410 30.043 1.00 8.17 C ANISOU 3246 C TRP A 237 962 820 1321 145 125 30 C ATOM 3247 O TRP A 237 -8.663 -0.566 29.486 1.00 8.79 O ANISOU 3247 O TRP A 237 916 952 1472 129 35 -40 O ATOM 3248 CB TRP A 237 -5.774 -0.744 31.144 1.00 9.29 C ANISOU 3248 CB TRP A 237 1056 1112 1363 18 -66 -132 C ATOM 3249 CG TRP A 237 -5.638 0.397 30.205 1.00 9.32 C ANISOU 3249 CG TRP A 237 1157 962 1422 -9 64 -133 C ATOM 3250 CD1 TRP A 237 -5.900 1.738 30.513 1.00 10.29 C ANISOU 3250 CD1 TRP A 237 1196 1174 1538 98 151 -294 C ATOM 3251 CD2 TRP A 237 -5.199 0.398 28.830 1.00 9.48 C ANISOU 3251 CD2 TRP A 237 1178 954 1469 -91 20 -152 C ATOM 3252 NE1 TRP A 237 -5.692 2.508 29.407 1.00 10.84 N ANISOU 3252 NE1 TRP A 237 1261 1173 1685 49 67 -90 N ATOM 3253 CE2 TRP A 237 -5.318 1.724 28.345 1.00 9.99 C ANISOU 3253 CE2 TRP A 237 1154 1144 1498 -10 -40 -1 C ATOM 3254 CE3 TRP A 237 -4.811 -0.613 27.948 1.00 10.32 C ANISOU 3254 CE3 TRP A 237 1312 1135 1474 -68 94 -202 C ATOM 3255 CZ2 TRP A 237 -4.978 2.068 27.015 1.00 11.14 C ANISOU 3255 CZ2 TRP A 237 1269 1381 1584 -206 -107 72 C ATOM 3256 CZ3 TRP A 237 -4.476 -0.258 26.652 1.00 11.49 C ANISOU 3256 CZ3 TRP A 237 1494 1343 1529 -282 114 -190 C ATOM 3257 CH2 TRP A 237 -4.584 1.068 26.200 1.00 11.93 C ANISOU 3257 CH2 TRP A 237 1502 1515 1517 -402 -40 -10 C ATOM 3258 H TRP A 237 -6.618 -2.601 32.526 1.00 9.74 H ATOM 3259 HA TRP A 237 -7.723 -0.359 31.765 1.00 10.55 H ATOM 3260 HB2 TRP A 237 -5.385 -0.487 31.995 1.00 11.17 H ATOM 3261 HB3 TRP A 237 -5.298 -1.504 30.772 1.00 11.17 H ATOM 3262 HD1 TRP A 237 -6.209 2.050 31.333 1.00 12.36 H ATOM 3263 HE1 TRP A 237 -5.830 3.356 29.366 1.00 13.03 H ATOM 3264 HE3 TRP A 237 -4.772 -1.500 28.226 1.00 12.39 H ATOM 3265 HZ2 TRP A 237 -5.097 2.933 26.695 1.00 13.39 H ATOM 3266 HZ3 TRP A 237 -4.225 -0.922 26.052 1.00 13.80 H ATOM 3267 HH2 TRP A 237 -4.341 1.268 25.325 1.00 14.34 H ATOM 3268 N ILE A 238 -7.735 -2.602 29.493 1.00 8.52 N ANISOU 3268 N ILE A 238 1171 839 1228 12 103 -44 N ATOM 3269 CA ILE A 238 -8.323 -2.957 28.177 1.00 9.13 C ANISOU 3269 CA ILE A 238 1180 993 1297 74 253 -151 C ATOM 3270 C ILE A 238 -9.850 -2.985 28.297 1.00 8.43 C ANISOU 3270 C ILE A 238 1063 832 1310 86 139 -125 C ATOM 3271 O ILE A 238 -10.554 -2.366 27.516 1.00 9.68 O ANISOU 3271 O ILE A 238 1181 946 1552 222 -68 -72 O ATOM 3272 CB ILE A 238 -7.775 -4.290 27.693 1.00 8.66 C ANISOU 3272 CB ILE A 238 1107 905 1278 160 229 -146 C ATOM 3273 CG1 ILE A 238 -6.305 -4.143 27.294 1.00 9.62 C ANISOU 3273 CG1 ILE A 238 1171 1091 1391 346 236 -43 C ATOM 3274 CG2 ILE A 238 -8.610 -4.828 26.545 1.00 9.75 C ANISOU 3274 CG2 ILE A 238 1256 1109 1341 38 129 -285 C ATOM 3275 CD1 ILE A 238 -5.582 -5.469 27.113 1.00 10.25 C ANISOU 3275 CD1 ILE A 238 1234 1241 1420 239 93 -77 C ATOM 3276 H ILE A 238 -7.265 -3.229 29.848 1.00 10.24 H ATOM 3277 HA ILE A 238 -8.081 -2.271 27.520 1.00 10.97 H ATOM 3278 HB ILE A 238 -7.827 -4.923 28.426 1.00 10.41 H ATOM 3279 HG12 ILE A 238 -6.256 -3.661 26.454 1.00 11.55 H ATOM 3280 HG13 ILE A 238 -5.842 -3.644 27.986 1.00 11.55 H ATOM 3281 HG21 ILE A 238 -8.243 -5.668 26.259 1.00 11.72 H ATOM 3282 HG22 ILE A 238 -9.513 -4.950 26.846 1.00 11.72 H ATOM 3283 HG23 ILE A 238 -8.588 -4.198 25.821 1.00 11.72 H ATOM 3284 HD11 ILE A 238 -4.671 -5.297 26.865 1.00 12.32 H ATOM 3285 HD12 ILE A 238 -5.611 -5.955 27.940 1.00 12.32 H ATOM 3286 HD13 ILE A 238 -6.021 -5.972 26.422 1.00 12.32 H ATOM 3287 N LYS A 239 -10.365 -3.705 29.291 1.00 9.05 N ANISOU 3287 N LYS A 239 1078 970 1391 67 143 -74 N ATOM 3288 CA LYS A 239 -11.821 -3.836 29.427 1.00 9.87 C ANISOU 3288 CA LYS A 239 1119 1221 1411 -53 147 -126 C ATOM 3289 C LYS A 239 -12.481 -2.515 29.671 1.00 8.69 C ANISOU 3289 C LYS A 239 881 1145 1278 133 71 -92 C ATOM 3290 O LYS A 239 -13.507 -2.163 29.099 1.00 9.93 O ANISOU 3290 O LYS A 239 1040 1273 1461 92 -76 -61 O ATOM 3291 CB LYS A 239 -12.183 -4.837 30.505 1.00 11.68 C ANISOU 3291 CB LYS A 239 1392 1399 1647 -37 91 -174 C ATOM 3292 CG LYS A 239 -11.757 -6.268 30.095 1.00 14.93 C ANISOU 3292 CG LYS A 239 1841 1720 2112 -20 -85 5 C ATOM 3293 CD LYS A 239 -12.103 -7.230 31.270 1.00 23.33 C ANISOU 3293 CD LYS A 239 2968 2723 3173 -110 33 140 C ATOM 3294 CE LYS A 239 -11.886 -8.669 30.968 1.00 33.04 C ANISOU 3294 CE LYS A 239 4165 4080 4309 -291 188 193 C ATOM 3295 NZ LYS A 239 -12.404 -9.438 32.210 1.00 40.54 N ANISOU 3295 NZ LYS A 239 5113 5052 5238 -463 256 229 N ATOM 3296 H LYS A 239 -9.908 -4.120 29.889 1.00 10.88 H ATOM 3297 HA LYS A 239 -12.175 -4.182 28.581 1.00 11.86 H ATOM 3298 HB2 LYS A 239 -11.724 -4.604 31.327 1.00 14.03 H ATOM 3299 HB3 LYS A 239 -13.143 -4.831 30.640 1.00 14.03 H ATOM 3300 HG2 LYS A 239 -12.247 -6.545 29.305 1.00 17.93 H ATOM 3301 HG3 LYS A 239 -10.800 -6.296 29.938 1.00 17.93 H ATOM 3302 HD2 LYS A 239 -11.549 -7.002 32.032 1.00 28.01 H ATOM 3303 HD3 LYS A 239 -13.039 -7.116 31.499 1.00 28.01 H ATOM 3304 HE2 LYS A 239 -12.400 -8.932 30.189 1.00 39.66 H ATOM 3305 HE3 LYS A 239 -10.941 -8.850 30.849 1.00 39.66 H ATOM 3306 HZ1 LYS A 239 -12.292 -10.383 32.080 1.00 48.66 H ATOM 3307 HZ2 LYS A 239 -11.914 -9.170 32.990 1.00 48.66 H ATOM 3308 HZ3 LYS A 239 -13.336 -9.250 32.347 1.00 48.66 H ATOM 3309 N ASP A 240 -11.881 -1.668 30.544 1.00 9.08 N ANISOU 3309 N ASP A 240 1025 1050 1374 -29 -7 -208 N ATOM 3310 CA ASP A 240 -12.447 -0.351 30.841 1.00 8.79 C ANISOU 3310 CA ASP A 240 997 1006 1336 112 48 -163 C ATOM 3311 C ASP A 240 -12.343 0.584 29.635 1.00 8.56 C ANISOU 3311 C ASP A 240 882 1002 1369 156 50 -73 C ATOM 3312 O ASP A 240 -13.261 1.374 29.360 1.00 9.80 O ANISOU 3312 O ASP A 240 1075 1190 1457 313 139 -33 O ATOM 3313 CB ASP A 240 -11.784 0.248 32.059 1.00 9.18 C ANISOU 3313 CB ASP A 240 1152 1031 1306 135 81 -85 C ATOM 3314 CG ASP A 240 -12.323 -0.311 33.385 1.00 11.35 C ANISOU 3314 CG ASP A 240 1452 1345 1516 34 -36 99 C ATOM 3315 OD1 ASP A 240 -13.453 -0.846 33.385 1.00 12.69 O ANISOU 3315 OD1 ASP A 240 1563 1485 1775 -81 111 -65 O ATOM 3316 OD2 ASP A 240 -11.641 -0.174 34.419 1.00 12.61 O ANISOU 3316 OD2 ASP A 240 1529 1750 1513 85 22 -124 O ATOM 3317 H ASP A 240 -11.153 -1.842 30.968 1.00 10.91 H ATOM 3318 HA ASP A 240 -13.398 -0.460 31.047 1.00 10.56 H ATOM 3319 HB2 ASP A 240 -10.833 0.061 32.022 1.00 11.03 H ATOM 3320 HB3 ASP A 240 -11.932 1.206 32.057 1.00 11.03 H ATOM 3321 N THR A 241 -11.253 0.499 28.881 1.00 8.94 N ANISOU 3321 N THR A 241 1003 976 1418 187 137 18 N ATOM 3322 CA THR A 241 -11.121 1.344 27.698 1.00 9.42 C ANISOU 3322 CA THR A 241 1156 974 1450 218 196 8 C ATOM 3323 C THR A 241 -12.137 0.948 26.635 1.00 9.54 C ANISOU 3323 C THR A 241 1144 1027 1452 229 89 117 C ATOM 3324 O THR A 241 -12.779 1.828 26.032 1.00 10.66 O ANISOU 3324 O THR A 241 1197 1116 1738 304 -24 123 O ATOM 3325 CB THR A 241 -9.676 1.297 27.138 1.00 9.78 C ANISOU 3325 CB THR A 241 1228 1022 1465 220 165 40 C ATOM 3326 OG1 THR A 241 -8.787 1.825 28.124 1.00 10.40 O ANISOU 3326 OG1 THR A 241 1184 1112 1655 139 159 81 O ATOM 3327 CG2 THR A 241 -9.556 2.103 25.879 1.00 10.86 C ANISOU 3327 CG2 THR A 241 1366 1263 1495 213 183 213 C ATOM 3328 H THR A 241 -10.588 -0.026 29.027 1.00 10.74 H ATOM 3329 HA THR A 241 -11.308 2.271 27.955 1.00 11.32 H ATOM 3330 HB THR A 241 -9.433 0.378 26.941 1.00 11.75 H ATOM 3331 HG1 THR A 241 -8.832 1.378 28.810 1.00 12.50 H ATOM 3332 HG21 THR A 241 -8.656 2.062 25.547 1.00 13.04 H ATOM 3333 HG22 THR A 241 -10.151 1.757 25.210 1.00 13.04 H ATOM 3334 HG23 THR A 241 -9.783 3.020 26.054 1.00 13.04 H ATOM 3335 N ILE A 242 -12.347 -0.341 26.424 1.00 9.98 N ANISOU 3335 N ILE A 242 1195 1219 1377 234 -81 -9 N ATOM 3336 CA ILE A 242 -13.339 -0.788 25.477 1.00 10.47 C ANISOU 3336 CA ILE A 242 1388 1214 1377 103 0 -80 C ATOM 3337 C ILE A 242 -14.729 -0.227 25.897 1.00 11.02 C ANISOU 3337 C ILE A 242 1375 1356 1456 291 -15 -52 C ATOM 3338 O ILE A 242 -15.456 0.348 25.106 1.00 12.67 O ANISOU 3338 O ILE A 242 1488 1698 1628 527 -123 -4 O ATOM 3339 CB ILE A 242 -13.344 -2.309 25.378 1.00 11.49 C ANISOU 3339 CB ILE A 242 1472 1351 1541 163 -122 -205 C ATOM 3340 CG1 ILE A 242 -12.107 -2.783 24.611 1.00 12.62 C ANISOU 3340 CG1 ILE A 242 1619 1502 1675 400 -175 -388 C ATOM 3341 CG2 ILE A 242 -14.663 -2.845 24.759 1.00 12.97 C ANISOU 3341 CG2 ILE A 242 1680 1523 1725 -22 -178 -8 C ATOM 3342 CD1 ILE A 242 -11.925 -4.302 24.639 1.00 14.34 C ANISOU 3342 CD1 ILE A 242 1803 1694 1950 512 -213 -454 C ATOM 3343 H ILE A 242 -11.925 -0.976 26.821 1.00 11.99 H ATOM 3344 HA ILE A 242 -13.122 -0.428 24.592 1.00 12.58 H ATOM 3345 HB ILE A 242 -13.281 -2.660 26.280 1.00 13.80 H ATOM 3346 HG12 ILE A 242 -12.188 -2.509 23.684 1.00 15.16 H ATOM 3347 HG13 ILE A 242 -11.318 -2.381 25.007 1.00 15.16 H ATOM 3348 HG21 ILE A 242 -14.621 -3.803 24.717 1.00 15.58 H ATOM 3349 HG22 ILE A 242 -15.400 -2.573 25.311 1.00 15.58 H ATOM 3350 HG23 ILE A 242 -14.764 -2.482 23.876 1.00 15.58 H ATOM 3351 HD11 ILE A 242 -11.136 -4.531 24.142 1.00 17.22 H ATOM 3352 HD12 ILE A 242 -11.834 -4.589 25.550 1.00 17.22 H ATOM 3353 HD13 ILE A 242 -12.695 -4.716 24.241 1.00 17.22 H ATOM 3354 N ALA A 243 -15.059 -0.355 27.184 1.00 10.62 N ANISOU 3354 N ALA A 243 1223 1382 1429 103 2 -39 N ATOM 3355 CA ALA A 243 -16.380 0.076 27.647 1.00 11.81 C ANISOU 3355 CA ALA A 243 1254 1640 1595 100 -4 -228 C ATOM 3356 C ALA A 243 -16.574 1.543 27.469 1.00 12.96 C ANISOU 3356 C ALA A 243 1289 1896 1740 493 9 -99 C ATOM 3357 O ALA A 243 -17.670 2.012 27.171 1.00 14.96 O ANISOU 3357 O ALA A 243 1430 2158 2096 480 -75 -65 O ATOM 3358 CB ALA A 243 -16.543 -0.298 29.115 1.00 12.62 C ANISOU 3358 CB ALA A 243 1429 1657 1708 31 -30 -263 C ATOM 3359 H ALA A 243 -14.549 -0.681 27.796 1.00 12.75 H ATOM 3360 HA ALA A 243 -17.072 -0.390 27.132 1.00 14.19 H ATOM 3361 HB1 ALA A 243 -17.410 -0.014 29.415 1.00 15.16 H ATOM 3362 HB2 ALA A 243 -16.460 -1.250 29.205 1.00 15.16 H ATOM 3363 HB3 ALA A 243 -15.859 0.140 29.626 1.00 15.16 H ATOM 3364 N ALA A 244 -15.519 2.335 27.716 1.00 12.20 N ANISOU 3364 N ALA A 244 1316 1600 1718 575 61 -105 N ATOM 3365 CA ALA A 244 -15.581 3.795 27.619 1.00 13.80 C ANISOU 3365 CA ALA A 244 1698 1698 1846 544 185 -27 C ATOM 3366 C ALA A 244 -15.649 4.334 26.219 1.00 14.23 C ANISOU 3366 C ALA A 244 1856 1642 1907 633 48 76 C ATOM 3367 O ALA A 244 -15.965 5.480 26.056 1.00 16.93 O ANISOU 3367 O ALA A 244 2601 1760 2072 987 143 207 O ATOM 3368 CB ALA A 244 -14.406 4.423 28.314 1.00 14.91 C ANISOU 3368 CB ALA A 244 1946 1744 1973 466 113 -20 C ATOM 3369 H ALA A 244 -14.744 2.040 27.945 1.00 14.65 H ATOM 3370 HA ALA A 244 -16.389 4.097 28.084 1.00 16.57 H ATOM 3371 HB1 ALA A 244 -14.470 5.377 28.236 1.00 17.90 H ATOM 3372 HB2 ALA A 244 -14.418 4.168 29.240 1.00 17.90 H ATOM 3373 HB3 ALA A 244 -13.597 4.114 27.899 1.00 17.90 H ATOM 3374 N ASN A 245 -15.396 3.503 25.239 1.00 13.80 N ANISOU 3374 N ASN A 245 1785 1625 1835 567 47 156 N ATOM 3375 CA ASN A 245 -15.341 3.906 23.854 1.00 15.00 C ANISOU 3375 CA ASN A 245 1792 1878 2031 766 -117 192 C ATOM 3376 C ASN A 245 -16.260 3.085 23.012 1.00 19.03 C ANISOU 3376 C ASN A 245 2152 2635 2445 750 -527 88 C ATOM 3377 O ASN A 245 -16.044 2.931 21.804 1.00 18.62 O ANISOU 3377 O ASN A 245 1961 2733 2380 718 -341 5 O ATOM 3378 CB ASN A 245 -13.900 3.792 23.323 1.00 14.48 C ANISOU 3378 CB ASN A 245 1776 1733 1991 703 -82 205 C ATOM 3379 CG ASN A 245 -13.002 4.828 23.947 1.00 14.50 C ANISOU 3379 CG ASN A 245 1813 1572 2124 533 115 261 C ATOM 3380 OD1 ASN A 245 -13.027 5.969 23.469 1.00 17.18 O ANISOU 3380 OD1 ASN A 245 2405 1653 2470 463 156 503 O ATOM 3381 ND2 ASN A 245 -12.293 4.498 24.999 1.00 13.27 N ANISOU 3381 ND2 ASN A 245 1598 1375 2067 347 32 199 N ATOM 3382 H ASN A 245 -15.246 2.665 25.354 1.00 16.58 H ATOM 3383 HA ASN A 245 -15.619 4.843 23.782 1.00 18.02 H ATOM 3384 HB2 ASN A 245 -13.548 2.914 23.539 1.00 17.39 H ATOM 3385 HB3 ASN A 245 -13.901 3.928 22.363 1.00 17.39 H ATOM 3386 HD21 ASN A 245 -11.703 5.159 25.419 1.00 15.93 H ATOM 3387 HD22 ASN A 245 -12.353 3.591 25.366 1.00 15.93 H ATOM 3388 N SER A 246 -17.370 2.675 23.609 1.00 26.24 N ANISOU 3388 N SER A 246 3149 3472 3351 396 -692 6 N ATOM 3389 CA SER A 246 -18.497 2.104 22.890 1.00 34.80 C ANISOU 3389 CA SER A 246 4305 4470 4446 183 -647 -110 C ATOM 3390 C SER A 246 -19.814 2.429 23.584 1.00 36.26 C ANISOU 3390 C SER A 246 4435 4762 4581 181 -466 -219 C ATOM 3391 O SER A 246 -19.978 3.599 24.029 1.00 37.68 O ANISOU 3391 O SER A 246 4592 5032 4692 195 -406 -248 O ATOM 3392 CB SER A 246 -18.371 0.606 22.771 1.00 41.59 C ANISOU 3392 CB SER A 246 5229 5257 5316 -12 -802 -2 C ATOM 3393 OG SER A 246 -17.805 -0.064 23.892 1.00 42.19 O ANISOU 3393 OG SER A 246 5314 5333 5383 -154 -932 70 O ATOM 3394 OXT SER A 246 -20.729 1.605 23.708 0.00 36.32 O ANISOU 3394 OXT SER A 246 4467 4761 4572 193 -438 -209 O ATOM 3395 H SER A 246 -17.497 2.720 24.459 1.00 31.51 H ATOM 3396 HA SER A 246 -18.526 2.481 21.986 1.00 41.77 H ATOM 3397 HB2 SER A 246 -19.258 0.243 22.623 1.00 49.92 H ATOM 3398 HB3 SER A 246 -17.818 0.413 21.998 1.00 49.92 H ATOM 3399 HG SER A 246 -17.616 0.479 24.477 1.00 50.64 H TER 3400 SER A 246 ATOM 3401 N ARG E 1 24.305 20.130 7.134 1.00 59.48 N ANISOU 3401 N ARG E 1 7492 7420 7687 -1030 -917 96 N ATOM 3402 CA ARG E 1 25.750 19.817 7.234 1.00 52.81 C ANISOU 3402 CA ARG E 1 6661 6537 6866 -1126 -920 54 C ATOM 3403 C ARG E 1 26.250 19.579 8.687 1.00 39.69 C ANISOU 3403 C ARG E 1 5067 4571 5445 -1483 -1133 -146 C ATOM 3404 O ARG E 1 27.450 19.576 8.910 1.00 35.49 O ANISOU 3404 O ARG E 1 4571 3738 5176 -1758 -1407 -257 O ATOM 3405 CB ARG E 1 26.548 20.959 6.571 1.00 61.10 C ANISOU 3405 CB ARG E 1 7674 7636 7907 -947 -775 143 C ATOM 3406 CG ARG E 1 26.518 22.288 7.310 1.00 70.25 C ANISOU 3406 CG ARG E 1 8840 8827 9023 -799 -681 225 C ATOM 3407 CD ARG E 1 25.480 23.304 6.879 1.00 77.22 C ANISOU 3407 CD ARG E 1 9737 9702 9899 -685 -609 267 C ATOM 3408 NE ARG E 1 24.155 23.092 7.486 1.00 81.25 N ANISOU 3408 NE ARG E 1 10268 10246 10356 -637 -410 301 N ATOM 3409 CZ ARG E 1 23.839 23.275 8.774 1.00 84.81 C ANISOU 3409 CZ ARG E 1 10752 10743 10729 -620 -336 315 C ATOM 3410 NH1 ARG E 1 24.759 23.641 9.644 1.00 87.58 N ANISOU 3410 NH1 ARG E 1 11051 11012 11214 -617 -431 313 N ATOM 3411 NH2 ARG E 1 22.582 23.066 9.193 1.00 89.62 N ANISOU 3411 NH2 ARG E 1 11320 11259 11473 -600 -407 329 N ATOM 3412 H1 ARG E 1 24.107 20.448 6.250 1.00 71.39 H ATOM 3413 H2 ARG E 1 23.793 19.338 7.311 1.00 71.39 H ATOM 3414 H3 ARG E 1 24.079 20.807 7.775 1.00 71.39 H ATOM 3415 HA ARG E 1 25.927 18.999 6.725 1.00 63.38 H ATOM 3416 HB2 ARG E 1 27.476 20.686 6.501 1.00 73.34 H ATOM 3417 HB3 ARG E 1 26.187 21.111 5.683 1.00 73.34 H ATOM 3418 HG2 ARG E 1 26.363 22.105 8.250 1.00 84.31 H ATOM 3419 HG3 ARG E 1 27.386 22.709 7.207 1.00 84.31 H ATOM 3420 HD2 ARG E 1 25.784 24.189 7.132 1.00 92.67 H ATOM 3421 HD3 ARG E 1 25.376 23.255 5.916 1.00 92.67 H ATOM 3422 HE ARG E 1 23.444 22.792 6.897 1.00 97.51 H ATOM 3423 HH11 ARG E 1 25.566 23.782 9.383 1.00105.11 H ATOM 3424 HH12 ARG E 1 24.550 23.751 10.471 1.00105.11 H ATOM 3425 HH21 ARG E 1 21.978 22.818 8.634 1.00107.56 H ATOM 3426 HH22 ARG E 1 22.383 23.170 10.023 1.00107.56 H ATOM 3427 N PRO E 2 25.342 19.410 9.656 1.00 32.71 N ANISOU 3427 N PRO E 2 4102 3840 4484 -1549 -1085 -210 N ATOM 3428 CA PRO E 2 25.778 19.104 11.019 1.00 29.63 C ANISOU 3428 CA PRO E 2 3622 3591 4044 -1470 -718 -12 C ATOM 3429 C PRO E 2 26.440 17.761 11.124 1.00 25.47 C ANISOU 3429 C PRO E 2 2988 3036 3652 -1498 -488 77 C ATOM 3430 O PRO E 2 26.233 16.861 10.304 1.00 22.94 O ANISOU 3430 O PRO E 2 2591 2671 3455 -1187 -453 159 O ATOM 3431 CB PRO E 2 24.485 19.037 11.851 1.00 32.10 C ANISOU 3431 CB PRO E 2 3980 3980 4237 -1275 -692 50 C ATOM 3432 CG PRO E 2 23.415 19.315 10.960 1.00 34.15 C ANISOU 3432 CG PRO E 2 4260 4288 4429 -1242 -778 2 C ATOM 3433 CD PRO E 2 23.872 19.394 9.555 1.00 33.82 C ANISOU 3433 CD PRO E 2 4220 4165 4466 -1304 -910 -29 C ATOM 3434 HA PRO E 2 26.369 19.803 11.369 1.00 35.57 H ATOM 3435 HB2 PRO E 2 24.389 18.148 12.228 1.00 38.54 H ATOM 3436 HB3 PRO E 2 24.520 19.702 12.556 1.00 38.54 H ATOM 3437 HG2 PRO E 2 22.755 18.610 11.044 1.00 41.00 H ATOM 3438 HG3 PRO E 2 23.016 20.162 11.216 1.00 41.00 H ATOM 3439 HD2 PRO E 2 23.578 18.612 9.062 1.00 40.60 H ATOM 3440 HD3 PRO E 2 23.554 20.212 9.143 1.00 40.60 H ATOM 3441 N ASP E 3 27.252 17.650 12.151 1.00 26.17 N ANISOU 3441 N ASP E 3 3171 3189 3583 -1355 -419 106 N ATOM 3442 CA ASP E 3 28.022 16.423 12.428 1.00 27.90 C ANISOU 3442 CA ASP E 3 3387 3495 3721 -1129 -311 150 C ATOM 3443 C ASP E 3 27.176 15.133 12.454 1.00 24.58 C ANISOU 3443 C ASP E 3 2776 3179 3385 -935 -153 143 C ATOM 3444 O ASP E 3 27.595 14.082 11.958 1.00 23.76 O ANISOU 3444 O ASP E 3 2563 3042 3421 -744 -82 149 O ATOM 3445 CB ASP E 3 28.770 16.573 13.783 1.00 32.98 C ANISOU 3445 CB ASP E 3 4110 4196 4224 -1104 -383 126 C ATOM 3446 CG ASP E 3 27.797 16.951 15.051 1.00 35.44 C ANISOU 3446 CG ASP E 3 4498 4710 4258 -957 -339 82 C ATOM 3447 OD1 ASP E 3 26.510 16.973 15.021 1.00 36.26 O ANISOU 3447 OD1 ASP E 3 4615 4844 4317 -1091 -254 121 O ATOM 3448 OD2 ASP E 3 28.388 17.248 16.144 1.00 37.09 O ANISOU 3448 OD2 ASP E 3 4770 4982 4339 -780 -274 78 O ATOM 3449 H ASP E 3 27.387 18.276 12.724 1.00 31.42 H ATOM 3450 HA ASP E 3 28.699 16.317 11.727 1.00 33.50 H ATOM 3451 HB2 ASP E 3 29.212 15.735 13.989 1.00 39.59 H ATOM 3452 HB3 ASP E 3 29.430 17.279 13.697 1.00 39.59 H ATOM 3453 N PHE E 4 25.925 15.201 12.972 1.00 23.29 N ANISOU 3453 N PHE E 4 2709 3001 3139 -793 -93 229 N ATOM 3454 CA PHE E 4 25.175 13.978 13.081 1.00 22.41 C ANISOU 3454 CA PHE E 4 2662 2833 3020 -552 27 291 C ATOM 3455 C PHE E 4 24.724 13.441 11.747 1.00 20.20 C ANISOU 3455 C PHE E 4 2297 2469 2909 -379 89 296 C ATOM 3456 O PHE E 4 24.359 12.267 11.699 1.00 20.39 O ANISOU 3456 O PHE E 4 2222 2396 3129 -310 192 237 O ATOM 3457 CB PHE E 4 23.985 14.187 14.040 1.00 24.13 C ANISOU 3457 CB PHE E 4 2994 3055 3119 -570 177 460 C ATOM 3458 CG PHE E 4 22.960 15.137 13.541 1.00 23.67 C ANISOU 3458 CG PHE E 4 2926 2999 3067 -836 278 500 C ATOM 3459 CD1 PHE E 4 22.099 14.744 12.549 1.00 23.32 C ANISOU 3459 CD1 PHE E 4 2890 2960 3012 -901 309 552 C ATOM 3460 CD2 PHE E 4 22.845 16.389 14.126 1.00 25.38 C ANISOU 3460 CD2 PHE E 4 3153 3212 3277 -770 147 465 C ATOM 3461 CE1 PHE E 4 21.188 15.612 12.075 1.00 24.26 C ANISOU 3461 CE1 PHE E 4 3065 3054 3099 -918 171 517 C ATOM 3462 CE2 PHE E 4 21.899 17.284 13.695 1.00 26.37 C ANISOU 3462 CE2 PHE E 4 3316 3349 3353 -880 74 416 C ATOM 3463 CZ PHE E 4 21.021 16.864 12.667 1.00 25.60 C ANISOU 3463 CZ PHE E 4 3229 3256 3242 -950 32 415 C ATOM 3464 H PHE E 4 25.527 15.912 13.247 1.00 27.96 H ATOM 3465 HA PHE E 4 25.756 13.299 13.484 1.00 26.91 H ATOM 3466 HB2 PHE E 4 23.550 13.333 14.187 1.00 28.97 H ATOM 3467 HB3 PHE E 4 24.322 14.532 14.882 1.00 28.97 H ATOM 3468 HD1 PHE E 4 22.193 13.906 12.156 1.00 28.00 H ATOM 3469 HD2 PHE E 4 23.423 16.628 14.814 1.00 30.47 H ATOM 3470 HE1 PHE E 4 20.603 15.341 11.406 1.00 29.13 H ATOM 3471 HE2 PHE E 4 21.819 18.125 14.083 1.00 31.65 H ATOM 3472 HZ PHE E 4 20.380 17.451 12.335 1.00 30.73 H ATOM 3473 N CYS E 5 24.806 14.220 10.676 1.00 19.22 N ANISOU 3473 N CYS E 5 2280 2322 2700 -235 105 229 N ATOM 3474 CA CYS E 5 24.562 13.708 9.337 1.00 18.67 C ANISOU 3474 CA CYS E 5 2378 2055 2661 -144 211 238 C ATOM 3475 C CYS E 5 25.526 12.632 8.918 1.00 19.39 C ANISOU 3475 C CYS E 5 2452 2073 2843 -120 300 258 C ATOM 3476 O CYS E 5 25.231 11.874 7.987 1.00 18.68 O ANISOU 3476 O CYS E 5 2347 1792 2959 -13 467 295 O ATOM 3477 CB CYS E 5 24.637 14.874 8.317 1.00 18.65 C ANISOU 3477 CB CYS E 5 2407 2081 2600 -127 211 48 C ATOM 3478 SG CYS E 5 23.406 16.156 8.544 1.00 18.57 S ANISOU 3478 SG CYS E 5 2409 1839 2809 -110 263 -87 S ATOM 3479 H CYS E 5 25.004 15.057 10.699 1.00 23.08 H ATOM 3480 HA CYS E 5 23.657 13.333 9.301 1.00 22.42 H ATOM 3481 HB2 CYS E 5 25.510 15.290 8.389 1.00 22.40 H ATOM 3482 HB3 CYS E 5 24.521 14.511 7.425 1.00 22.40 H ATOM 3483 N LEU E 6 26.654 12.558 9.626 1.00 21.48 N ANISOU 3483 N LEU E 6 2620 2471 3070 -256 302 246 N ATOM 3484 CA LEU E 6 27.638 11.574 9.332 1.00 25.47 C ANISOU 3484 CA LEU E 6 3138 3044 3494 -82 312 340 C ATOM 3485 C LEU E 6 27.510 10.333 10.186 1.00 24.19 C ANISOU 3485 C LEU E 6 2937 2745 3508 266 327 479 C ATOM 3486 O LEU E 6 28.341 9.385 10.065 1.00 24.75 O ANISOU 3486 O LEU E 6 2768 2893 3742 441 305 414 O ATOM 3487 CB LEU E 6 29.024 12.210 9.532 1.00 30.77 C ANISOU 3487 CB LEU E 6 3824 3816 4051 -413 266 398 C ATOM 3488 CG LEU E 6 29.214 13.557 8.835 1.00 35.33 C ANISOU 3488 CG LEU E 6 4410 4438 4577 -748 199 389 C ATOM 3489 CD1 LEU E 6 30.597 14.138 9.154 1.00 38.71 C ANISOU 3489 CD1 LEU E 6 4837 4846 5024 -845 147 424 C ATOM 3490 CD2 LEU E 6 28.978 13.326 7.375 1.00 38.56 C ANISOU 3490 CD2 LEU E 6 4822 4821 5010 -830 215 377 C ATOM 3491 H LEU E 6 26.856 13.077 10.281 1.00 25.79 H ATOM 3492 HA LEU E 6 27.556 11.307 8.393 1.00 30.57 H ATOM 3493 HB2 LEU E 6 29.168 12.348 10.481 1.00 36.94 H ATOM 3494 HB3 LEU E 6 29.696 11.603 9.185 1.00 36.94 H ATOM 3495 HG LEU E 6 28.542 14.180 9.155 1.00 42.41 H ATOM 3496 HD11 LEU E 6 30.692 14.982 8.706 1.00 46.46 H ATOM 3497 HD12 LEU E 6 30.673 14.260 10.103 1.00 46.46 H ATOM 3498 HD13 LEU E 6 31.270 13.526 8.847 1.00 46.46 H ATOM 3499 HD21 LEU E 6 29.089 14.155 6.905 1.00 46.29 H ATOM 3500 HD22 LEU E 6 29.612 12.680 7.055 1.00 46.29 H ATOM 3501 HD23 LEU E 6 28.084 12.997 7.251 1.00 46.29 H ATOM 3502 N GLU E 7 26.554 10.291 11.081 1.00 24.60 N ANISOU 3502 N GLU E 7 3025 2832 3491 358 384 656 N ATOM 3503 CA GLU E 7 26.319 9.092 11.913 1.00 26.58 C ANISOU 3503 CA GLU E 7 3318 3099 3684 326 526 779 C ATOM 3504 C GLU E 7 25.730 7.965 11.057 1.00 22.36 C ANISOU 3504 C GLU E 7 2659 2472 3363 385 610 892 C ATOM 3505 O GLU E 7 24.816 8.218 10.230 1.00 20.67 O ANISOU 3505 O GLU E 7 2431 2075 3349 320 633 916 O ATOM 3506 CB GLU E 7 25.180 9.322 12.950 1.00 34.16 C ANISOU 3506 CB GLU E 7 4340 4171 4466 186 578 566 C ATOM 3507 CG GLU E 7 25.391 10.236 14.103 1.00 39.14 C ANISOU 3507 CG GLU E 7 4951 4875 5046 8 560 328 C ATOM 3508 CD GLU E 7 24.011 10.497 14.901 1.00 38.45 C ANISOU 3508 CD GLU E 7 4911 4819 4882 -233 581 84 C ATOM 3509 OE1 GLU E 7 24.145 11.198 15.956 1.00 39.96 O ANISOU 3509 OE1 GLU E 7 5153 5153 4877 -246 569 31 O ATOM 3510 OE2 GLU E 7 22.845 10.173 14.402 1.00 36.22 O ANISOU 3510 OE2 GLU E 7 4579 4383 4802 -448 610 -19 O ATOM 3511 H GLU E 7 26.012 10.940 11.242 1.00 29.54 H ATOM 3512 HA GLU E 7 27.138 8.793 12.361 1.00 31.92 H ATOM 3513 HB2 GLU E 7 24.413 9.665 12.466 1.00 41.00 H ATOM 3514 HB3 GLU E 7 24.950 8.458 13.324 1.00 41.00 H ATOM 3515 HG2 GLU E 7 26.027 9.837 14.717 1.00 46.99 H ATOM 3516 HG3 GLU E 7 25.723 11.088 13.781 1.00 46.99 H ATOM 3517 N PRO E 8 26.100 6.715 11.362 1.00 22.29 N ANISOU 3517 N PRO E 8 2581 2666 3223 679 474 781 N ATOM 3518 CA PRO E 8 25.372 5.633 10.682 1.00 21.43 C ANISOU 3518 CA PRO E 8 2596 2496 3050 664 558 740 C ATOM 3519 C PRO E 8 23.867 5.615 11.138 1.00 18.97 C ANISOU 3519 C PRO E 8 2345 2050 2813 420 787 586 C ATOM 3520 O PRO E 8 23.530 6.022 12.244 1.00 18.10 O ANISOU 3520 O PRO E 8 2308 1730 2837 238 857 332 O ATOM 3521 CB PRO E 8 26.062 4.355 11.234 1.00 24.73 C ANISOU 3521 CB PRO E 8 3071 2972 3353 787 357 617 C ATOM 3522 CG PRO E 8 27.273 4.779 11.962 1.00 26.80 C ANISOU 3522 CG PRO E 8 3372 3269 3544 863 305 564 C ATOM 3523 CD PRO E 8 27.175 6.264 12.273 1.00 25.85 C ANISOU 3523 CD PRO E 8 3207 3122 3491 791 318 660 C ATOM 3524 HA PRO E 8 25.451 5.686 9.706 1.00 25.73 H ATOM 3525 HB2 PRO E 8 25.453 3.898 11.834 1.00 29.69 H ATOM 3526 HB3 PRO E 8 26.301 3.776 10.494 1.00 29.69 H ATOM 3527 HG2 PRO E 8 27.339 4.272 12.786 1.00 32.18 H ATOM 3528 HG3 PRO E 8 28.050 4.609 11.406 1.00 32.18 H ATOM 3529 HD2 PRO E 8 26.917 6.402 13.198 1.00 31.03 H ATOM 3530 HD3 PRO E 8 28.010 6.712 12.063 1.00 31.03 H ATOM 3531 N PRO E 9 23.005 5.125 10.288 1.00 16.99 N ANISOU 3531 N PRO E 9 1978 1877 2602 192 671 791 N ATOM 3532 CA PRO E 9 21.580 5.082 10.673 1.00 17.97 C ANISOU 3532 CA PRO E 9 2211 2077 2541 15 653 613 C ATOM 3533 C PRO E 9 21.372 4.042 11.783 1.00 16.84 C ANISOU 3533 C PRO E 9 2167 1799 2433 156 559 459 C ATOM 3534 O PRO E 9 22.148 3.113 11.935 1.00 18.28 O ANISOU 3534 O PRO E 9 2542 1822 2581 116 727 466 O ATOM 3535 CB PRO E 9 20.911 4.547 9.386 1.00 19.66 C ANISOU 3535 CB PRO E 9 2466 2410 2593 -157 504 721 C ATOM 3536 CG PRO E 9 22.035 3.942 8.553 1.00 20.71 C ANISOU 3536 CG PRO E 9 2583 2557 2728 -134 465 661 C ATOM 3537 CD PRO E 9 23.333 4.523 8.990 1.00 20.06 C ANISOU 3537 CD PRO E 9 2502 2407 2714 89 551 599 C ATOM 3538 HA PRO E 9 21.229 5.961 10.925 1.00 21.58 H ATOM 3539 HB2 PRO E 9 20.256 3.871 9.617 1.00 23.60 H ATOM 3540 HB3 PRO E 9 20.491 5.281 8.910 1.00 23.60 H ATOM 3541 HG2 PRO E 9 22.042 2.981 8.684 1.00 24.87 H ATOM 3542 HG3 PRO E 9 21.879 4.147 7.617 1.00 24.87 H ATOM 3543 HD2 PRO E 9 23.998 3.825 9.098 1.00 24.09 H ATOM 3544 HD3 PRO E 9 23.627 5.204 8.365 1.00 24.09 H ATOM 3545 N TYR E 10 20.328 4.245 12.523 1.00 14.45 N ANISOU 3545 N TYR E 10 1785 1599 2106 -93 430 232 N ATOM 3546 CA TYR E 10 20.034 3.473 13.720 1.00 13.44 C ANISOU 3546 CA TYR E 10 1553 1599 1957 -145 172 349 C ATOM 3547 C TYR E 10 18.570 2.989 13.768 1.00 12.12 C ANISOU 3547 C TYR E 10 1487 1174 1945 -77 243 272 C ATOM 3548 O TYR E 10 17.652 3.736 14.023 1.00 12.18 O ANISOU 3548 O TYR E 10 1509 1131 1986 50 201 223 O ATOM 3549 CB TYR E 10 20.324 4.376 14.931 1.00 14.55 C ANISOU 3549 CB TYR E 10 1753 1730 2046 -164 55 393 C ATOM 3550 CG TYR E 10 20.225 3.674 16.234 1.00 13.97 C ANISOU 3550 CG TYR E 10 1563 1697 2048 -241 -84 373 C ATOM 3551 CD1 TYR E 10 19.229 4.025 17.119 1.00 14.34 C ANISOU 3551 CD1 TYR E 10 1669 1766 2014 -617 -43 109 C ATOM 3552 CD2 TYR E 10 21.110 2.600 16.592 1.00 15.93 C ANISOU 3552 CD2 TYR E 10 1852 2048 2152 -150 -74 519 C ATOM 3553 CE1 TYR E 10 19.140 3.412 18.328 1.00 15.19 C ANISOU 3553 CE1 TYR E 10 1766 1937 2068 -672 -39 117 C ATOM 3554 CE2 TYR E 10 20.998 2.013 17.770 1.00 16.92 C ANISOU 3554 CE2 TYR E 10 2027 2162 2239 -82 47 518 C ATOM 3555 CZ TYR E 10 20.009 2.388 18.659 1.00 16.75 C ANISOU 3555 CZ TYR E 10 2003 2209 2153 -476 -20 401 C ATOM 3556 OH TYR E 10 19.912 1.762 19.863 1.00 19.93 O ANISOU 3556 OH TYR E 10 2542 2616 2413 -526 -37 594 O ATOM 3557 H TYR E 10 19.739 4.850 12.358 1.00 17.36 H ATOM 3558 HA TYR E 10 20.624 2.691 13.762 1.00 16.15 H ATOM 3559 HB2 TYR E 10 21.225 4.728 14.850 1.00 17.48 H ATOM 3560 HB3 TYR E 10 19.685 5.106 14.937 1.00 17.48 H ATOM 3561 HD1 TYR E 10 18.648 4.721 16.910 1.00 17.22 H ATOM 3562 HD2 TYR E 10 21.787 2.344 16.009 1.00 19.13 H ATOM 3563 HE1 TYR E 10 18.472 3.662 18.925 1.00 18.24 H ATOM 3564 HE2 TYR E 10 21.583 1.327 17.998 1.00 20.32 H ATOM 3565 HH TYR E 10 19.173 1.416 19.941 1.00 23.93 H ATOM 3566 N THR E 11 18.376 1.706 13.514 1.00 12.38 N ANISOU 3566 N THR E 11 1580 1221 1902 50 400 376 N ATOM 3567 CA THR E 11 17.056 1.138 13.576 1.00 11.67 C ANISOU 3567 CA THR E 11 1539 1150 1744 -58 317 280 C ATOM 3568 C THR E 11 16.541 1.201 14.999 1.00 10.68 C ANISOU 3568 C THR E 11 1392 1033 1633 -109 168 223 C ATOM 3569 O THR E 11 15.325 1.459 15.231 1.00 10.85 O ANISOU 3569 O THR E 11 1322 1183 1616 43 266 132 O ATOM 3570 CB THR E 11 17.097 -0.355 13.077 1.00 13.28 C ANISOU 3570 CB THR E 11 1681 1487 1879 174 363 266 C ATOM 3571 OG1 THR E 11 17.376 -0.334 11.671 1.00 14.92 O ANISOU 3571 OG1 THR E 11 2010 1636 2024 107 416 227 O ATOM 3572 CG2 THR E 11 15.779 -1.103 13.360 1.00 14.06 C ANISOU 3572 CG2 THR E 11 1821 1556 1964 81 264 328 C ATOM 3573 H THR E 11 18.995 1.148 13.303 1.00 14.87 H ATOM 3574 HA THR E 11 16.449 1.646 12.999 1.00 14.02 H ATOM 3575 HB THR E 11 17.812 -0.823 13.535 1.00 15.95 H ATOM 3576 HG1 THR E 11 16.789 0.081 11.275 1.00 17.92 H ATOM 3577 HG21 THR E 11 15.840 -2.007 13.043 1.00 16.88 H ATOM 3578 HG22 THR E 11 15.605 -1.115 14.304 1.00 16.88 H ATOM 3579 HG23 THR E 11 15.051 -0.665 12.914 1.00 16.88 H ATOM 3580 N GLY E 12 17.401 0.934 15.984 1.00 11.65 N ANISOU 3580 N GLY E 12 1338 1411 1676 -279 135 536 N ATOM 3581 CA GLY E 12 16.990 0.939 17.377 1.00 12.07 C ANISOU 3581 CA GLY E 12 1410 1519 1656 -416 96 369 C ATOM 3582 C GLY E 12 16.324 -0.355 17.772 1.00 10.69 C ANISOU 3582 C GLY E 12 1321 1123 1619 -277 88 77 C ATOM 3583 O GLY E 12 16.172 -1.286 16.961 1.00 11.55 O ANISOU 3583 O GLY E 12 1501 1134 1754 -16 231 83 O ATOM 3584 H GLY E 12 18.232 0.746 15.865 1.00 13.99 H ATOM 3585 HA2 GLY E 12 17.766 1.072 17.944 1.00 14.50 H ATOM 3586 HA3 GLY E 12 16.367 1.666 17.530 1.00 14.50 H ATOM 3587 N PRO E 13 15.900 -0.443 19.029 1.00 10.24 N ANISOU 3587 N PRO E 13 1202 1131 1558 -200 -3 131 N ATOM 3588 CA PRO E 13 15.499 -1.715 19.621 1.00 10.36 C ANISOU 3588 CA PRO E 13 1168 1218 1550 -100 -12 289 C ATOM 3589 C PRO E 13 14.071 -2.094 19.339 1.00 9.23 C ANISOU 3589 C PRO E 13 1079 1089 1340 -132 -54 126 C ATOM 3590 O PRO E 13 13.693 -3.260 19.462 1.00 9.24 O ANISOU 3590 O PRO E 13 1037 1062 1411 -35 18 130 O ATOM 3591 CB PRO E 13 15.759 -1.480 21.115 1.00 11.87 C ANISOU 3591 CB PRO E 13 1436 1451 1625 -354 -138 260 C ATOM 3592 CG PRO E 13 15.494 -0.015 21.313 1.00 11.96 C ANISOU 3592 CG PRO E 13 1545 1444 1554 -101 -108 204 C ATOM 3593 CD PRO E 13 16.113 0.606 20.045 1.00 11.71 C ANISOU 3593 CD PRO E 13 1460 1373 1617 -142 -81 176 C ATOM 3594 HA PRO E 13 16.087 -2.432 19.304 1.00 12.44 H ATOM 3595 HB2 PRO E 13 15.148 -2.017 21.644 1.00 14.26 H ATOM 3596 HB3 PRO E 13 16.681 -1.696 21.326 1.00 14.26 H ATOM 3597 HG2 PRO E 13 14.538 0.149 21.354 1.00 14.36 H ATOM 3598 HG3 PRO E 13 15.941 0.301 22.113 1.00 14.36 H ATOM 3599 HD2 PRO E 13 15.641 1.418 19.799 1.00 14.07 H ATOM 3600 HD3 PRO E 13 17.061 0.768 20.173 1.00 14.07 H ATOM 3601 N CYS E 14 13.224 -1.115 19.010 1.00 9.00 N ANISOU 3601 N CYS E 14 991 1030 1398 -48 -109 12 N ATOM 3602 CA CYS E 14 11.804 -1.423 18.824 1.00 9.31 C ANISOU 3602 CA CYS E 14 1098 1025 1413 79 3 84 C ATOM 3603 C CYS E 14 11.585 -2.158 17.518 1.00 9.09 C ANISOU 3603 C CYS E 14 1037 978 1437 -18 105 72 C ATOM 3604 O CYS E 14 12.410 -2.103 16.611 1.00 9.48 O ANISOU 3604 O CYS E 14 1121 1024 1458 -118 121 35 O ATOM 3605 CB CYS E 14 10.931 -0.213 18.940 1.00 10.15 C ANISOU 3605 CB CYS E 14 1195 1260 1403 -156 38 -120 C ATOM 3606 SG CYS E 14 10.793 0.406 20.664 1.00 11.61 S ANISOU 3606 SG CYS E 14 1445 1422 1544 -126 192 -120 S ATOM 3607 H CYS E 14 13.437 -0.291 18.892 1.00 10.81 H ATOM 3608 HA CYS E 14 11.535 -2.034 19.541 1.00 11.18 H ATOM 3609 HB2 CYS E 14 11.304 0.498 18.395 1.00 12.20 H ATOM 3610 HB3 CYS E 14 10.040 -0.436 18.629 1.00 12.20 H ATOM 3611 N ARG E 15 10.493 -2.886 17.461 1.00 9.82 N ANISOU 3611 N ARG E 15 1168 1103 1459 -123 96 -100 N ATOM 3612 CA ARG E 15 10.238 -3.851 16.419 1.00 9.88 C ANISOU 3612 CA ARG E 15 1336 992 1427 -152 97 16 C ATOM 3613 C ARG E 15 9.154 -3.531 15.425 1.00 10.42 C ANISOU 3613 C ARG E 15 1247 1041 1670 -141 29 -2 C ATOM 3614 O ARG E 15 8.634 -4.389 14.733 1.00 10.40 O ANISOU 3614 O ARG E 15 1266 1043 1644 -126 118 25 O ATOM 3615 CB ARG E 15 10.176 -5.257 16.998 1.00 10.34 C ANISOU 3615 CB ARG E 15 1340 1139 1448 -55 156 -14 C ATOM 3616 CG ARG E 15 11.527 -5.731 17.492 1.00 10.18 C ANISOU 3616 CG ARG E 15 1387 1087 1394 -159 140 34 C ATOM 3617 CD ARG E 15 11.553 -7.018 18.270 1.00 10.53 C ANISOU 3617 CD ARG E 15 1349 1182 1471 -188 14 63 C ATOM 3618 NE ARG E 15 12.965 -7.390 18.542 1.00 10.41 N ANISOU 3618 NE ARG E 15 1318 1148 1490 -89 68 66 N ATOM 3619 CZ ARG E 15 13.356 -8.513 19.118 1.00 10.64 C ANISOU 3619 CZ ARG E 15 1401 1229 1412 -137 64 -47 C ATOM 3620 NH1 ARG E 15 12.451 -9.369 19.571 1.00 10.52 N ANISOU 3620 NH1 ARG E 15 1340 1191 1465 -109 55 64 N ATOM 3621 NH2 ARG E 15 14.636 -8.755 19.272 1.00 11.58 N ANISOU 3621 NH2 ARG E 15 1553 1333 1514 -60 95 -99 N ATOM 3622 H ARG E 15 9.859 -2.836 18.039 1.00 11.79 H ATOM 3623 HA ARG E 15 11.054 -3.855 15.877 1.00 11.87 H ATOM 3624 HB2 ARG E 15 9.560 -5.265 17.748 1.00 12.42 H ATOM 3625 HB3 ARG E 15 9.873 -5.871 16.310 1.00 12.42 H ATOM 3626 HG2 ARG E 15 12.105 -5.850 16.722 1.00 12.23 H ATOM 3627 HG3 ARG E 15 11.898 -5.042 18.066 1.00 12.23 H ATOM 3628 HD2 ARG E 15 11.093 -6.899 19.115 1.00 12.65 H ATOM 3629 HD3 ARG E 15 11.139 -7.724 17.749 1.00 12.65 H ATOM 3630 HE ARG E 15 13.653 -6.759 18.277 1.00 12.51 H ATOM 3631 HH11 ARG E 15 11.614 -9.208 19.459 1.00 12.64 H ATOM 3632 HH12 ARG E 15 12.702 -10.095 19.956 1.00 12.64 H ATOM 3633 HH21 ARG E 15 15.218 -8.187 18.991 1.00 13.91 H ATOM 3634 HH22 ARG E 15 14.894 -9.472 19.671 1.00 13.91 H ATOM 3635 N ALA E 16 8.851 -2.247 15.278 1.00 12.02 N ANISOU 3635 N ALA E 16 1493 1261 1813 -133 -129 5 N ATOM 3636 CA ALA E 16 8.041 -1.774 14.048 1.00 12.57 C ANISOU 3636 CA ALA E 16 1585 1385 1804 -184 177 -4 C ATOM 3637 C ALA E 16 8.939 -1.658 12.831 1.00 12.65 C ANISOU 3637 C ALA E 16 1660 1398 1748 -43 -33 82 C ATOM 3638 O ALA E 16 10.154 -1.816 12.861 1.00 13.45 O ANISOU 3638 O ALA E 16 1762 1484 1864 -153 59 22 O ATOM 3639 CB ALA E 16 7.384 -0.395 14.413 1.00 13.81 C ANISOU 3639 CB ALA E 16 1718 1676 1854 -23 21 -69 C ATOM 3640 H ALA E 16 9.072 -1.621 15.825 1.00 14.44 H ATOM 3641 HA ALA E 16 7.329 -2.419 13.853 1.00 15.09 H ATOM 3642 HB1 ALA E 16 6.875 -0.084 13.661 1.00 16.59 H ATOM 3643 HB2 ALA E 16 6.808 -0.515 15.171 1.00 16.59 H ATOM 3644 HB3 ALA E 16 8.077 0.235 14.623 1.00 16.59 H ATOM 3645 N ASP E 17 8.271 -1.326 11.710 1.00 13.78 N ANISOU 3645 N ASP E 17 1875 1650 1712 -240 52 156 N ATOM 3646 CA ASP E 17 9.024 -0.943 10.497 1.00 15.89 C ANISOU 3646 CA ASP E 17 2071 1875 2092 -229 106 121 C ATOM 3647 C ASP E 17 8.476 0.337 9.990 1.00 16.57 C ANISOU 3647 C ASP E 17 2130 1998 2169 -318 -183 434 C ATOM 3648 O ASP E 17 7.477 0.375 9.315 1.00 17.25 O ANISOU 3648 O ASP E 17 2373 1973 2210 -444 -183 475 O ATOM 3649 CB ASP E 17 8.871 -2.029 9.413 1.00 19.98 C ANISOU 3649 CB ASP E 17 2700 2432 2459 -192 121 -68 C ATOM 3650 CG ASP E 17 9.603 -1.729 8.083 1.00 24.02 C ANISOU 3650 CG ASP E 17 3425 3176 2525 -80 339 -162 C ATOM 3651 OD1 ASP E 17 10.184 -0.615 7.983 1.00 23.95 O ANISOU 3651 OD1 ASP E 17 3336 3393 2371 -213 418 -7 O ATOM 3652 OD2 ASP E 17 9.493 -2.570 7.165 1.00 27.25 O ANISOU 3652 OD2 ASP E 17 4001 3542 2810 -83 340 -137 O ATOM 3653 H ASP E 17 7.415 -1.313 11.626 1.00 16.55 H ATOM 3654 HA ASP E 17 9.974 -0.828 10.708 1.00 19.08 H ATOM 3655 HB2 ASP E 17 9.224 -2.864 9.759 1.00 23.99 H ATOM 3656 HB3 ASP E 17 7.928 -2.133 9.211 1.00 23.99 H ATOM 3657 N ILE E 18 9.089 1.420 10.488 1.00 16.95 N ANISOU 3657 N ILE E 18 2212 1890 2337 -378 -416 720 N ATOM 3658 CA ILE E 18 8.685 2.788 10.137 1.00 18.57 C ANISOU 3658 CA ILE E 18 2463 2046 2548 -375 -364 654 C ATOM 3659 C ILE E 18 9.672 3.260 9.101 1.00 18.89 C ANISOU 3659 C ILE E 18 2595 2017 2563 -246 -573 402 C ATOM 3660 O ILE E 18 10.882 3.275 9.329 1.00 18.19 O ANISOU 3660 O ILE E 18 2441 1955 2516 -152 -468 316 O ATOM 3661 CB ILE E 18 8.748 3.680 11.415 1.00 20.66 C ANISOU 3661 CB ILE E 18 2720 2357 2772 -212 -187 845 C ATOM 3662 CG1 ILE E 18 7.964 3.130 12.642 1.00 24.64 C ANISOU 3662 CG1 ILE E 18 3131 2954 3275 -265 -173 646 C ATOM 3663 CG2 ILE E 18 8.353 5.140 11.066 1.00 21.28 C ANISOU 3663 CG2 ILE E 18 2771 2472 2844 -12 -330 1002 C ATOM 3664 CD1 ILE E 18 6.589 2.865 12.295 1.00 28.74 C ANISOU 3664 CD1 ILE E 18 3631 3535 3752 -356 -287 593 C ATOM 3665 H ILE E 18 9.749 1.387 11.038 1.00 20.35 H ATOM 3666 HA ILE E 18 7.778 2.800 9.765 1.00 22.30 H ATOM 3667 HB ILE E 18 9.680 3.707 11.680 1.00 24.80 H ATOM 3668 HG12 ILE E 18 8.370 2.301 12.939 1.00 29.58 H ATOM 3669 HG13 ILE E 18 7.978 3.788 13.355 1.00 29.58 H ATOM 3670 HG21 ILE E 18 8.397 5.674 11.863 1.00 25.55 H ATOM 3671 HG22 ILE E 18 8.965 5.480 10.410 1.00 25.55 H ATOM 3672 HG23 ILE E 18 7.459 5.147 10.716 1.00 25.55 H ATOM 3673 HD11 ILE E 18 6.132 2.527 13.069 1.00 34.50 H ATOM 3674 HD12 ILE E 18 6.178 3.681 12.001 1.00 34.50 H ATOM 3675 HD13 ILE E 18 6.565 2.213 11.591 1.00 34.50 H ATOM 3676 N ILE E 19 9.158 3.793 7.995 1.00 21.10 N ANISOU 3676 N ILE E 19 2878 2346 2791 -290 -640 308 N ATOM 3677 CA ILE E 19 10.058 4.243 6.940 1.00 24.48 C ANISOU 3677 CA ILE E 19 3286 2825 3191 -404 -602 302 C ATOM 3678 C ILE E 19 10.597 5.642 7.319 1.00 18.31 C ANISOU 3678 C ILE E 19 2654 1881 2420 -336 -371 374 C ATOM 3679 O ILE E 19 9.833 6.550 7.576 1.00 18.73 O ANISOU 3679 O ILE E 19 2582 2101 2431 -303 -417 376 O ATOM 3680 CB ILE E 19 9.264 4.323 5.620 1.00 35.00 C ANISOU 3680 CB ILE E 19 4458 4309 4532 -444 -702 214 C ATOM 3681 CG1 ILE E 19 10.157 4.856 4.517 1.00 38.05 C ANISOU 3681 CG1 ILE E 19 4777 4741 4939 -528 -759 144 C ATOM 3682 CG2 ILE E 19 8.036 5.202 5.743 1.00 44.27 C ANISOU 3682 CG2 ILE E 19 5602 5517 5702 -482 -655 192 C ATOM 3683 CD1 ILE E 19 11.362 4.013 4.343 1.00 43.11 C ANISOU 3683 CD1 ILE E 19 5430 5395 5555 -566 -797 84 C ATOM 3684 H ILE E 19 8.320 3.901 7.834 1.00 25.33 H ATOM 3685 HA ILE E 19 10.807 3.619 6.837 1.00 29.40 H ATOM 3686 HB ILE E 19 8.979 3.429 5.378 1.00 42.01 H ATOM 3687 HG12 ILE E 19 9.665 4.860 3.681 1.00 45.67 H ATOM 3688 HG13 ILE E 19 10.444 5.754 4.743 1.00 45.67 H ATOM 3689 HG21 ILE E 19 7.579 5.220 4.899 1.00 53.14 H ATOM 3690 HG22 ILE E 19 7.460 4.840 6.420 1.00 53.14 H ATOM 3691 HG23 ILE E 19 8.310 6.090 5.986 1.00 53.14 H ATOM 3692 HD11 ILE E 19 11.900 4.380 3.639 1.00 51.75 H ATOM 3693 HD12 ILE E 19 11.858 4.004 5.165 1.00 51.75 H ATOM 3694 HD13 ILE E 19 11.088 3.121 4.116 1.00 51.75 H ATOM 3695 N ARG E 20 11.905 5.742 7.389 1.00 14.94 N ANISOU 3695 N ARG E 20 2294 1478 1904 -327 -158 282 N ATOM 3696 CA ARG E 20 12.558 7.007 7.722 1.00 13.74 C ANISOU 3696 CA ARG E 20 2033 1433 1755 -143 -87 196 C ATOM 3697 C ARG E 20 13.757 7.172 6.746 1.00 13.68 C ANISOU 3697 C ARG E 20 2239 1201 1758 -255 100 -73 C ATOM 3698 O ARG E 20 14.148 6.249 6.048 1.00 14.34 O ANISOU 3698 O ARG E 20 2513 1262 1673 -146 77 -90 O ATOM 3699 CB ARG E 20 13.054 7.016 9.177 1.00 13.67 C ANISOU 3699 CB ARG E 20 1910 1538 1746 -164 -96 106 C ATOM 3700 CG ARG E 20 11.934 7.035 10.205 1.00 13.57 C ANISOU 3700 CG ARG E 20 1766 1566 1823 -73 -96 101 C ATOM 3701 CD ARG E 20 11.139 8.332 10.175 1.00 14.23 C ANISOU 3701 CD ARG E 20 1890 1637 1879 -102 90 300 C ATOM 3702 NE ARG E 20 10.061 8.341 11.188 1.00 14.11 N ANISOU 3702 NE ARG E 20 1892 1523 1948 -133 141 194 N ATOM 3703 CZ ARG E 20 10.191 8.679 12.455 1.00 14.53 C ANISOU 3703 CZ ARG E 20 1948 1535 2039 34 264 139 C ATOM 3704 NH1 ARG E 20 11.383 9.036 12.936 1.00 14.53 N ANISOU 3704 NH1 ARG E 20 1915 1616 1990 -91 192 34 N ATOM 3705 NH2 ARG E 20 9.122 8.689 13.266 1.00 16.44 N ANISOU 3705 NH2 ARG E 20 2194 1815 2237 234 419 26 N ATOM 3706 H ARG E 20 12.450 5.092 7.249 1.00 17.94 H ATOM 3707 HA ARG E 20 11.935 7.752 7.592 1.00 16.51 H ATOM 3708 HB2 ARG E 20 13.585 6.219 9.332 1.00 16.42 H ATOM 3709 HB3 ARG E 20 13.598 7.806 9.317 1.00 16.42 H ATOM 3710 HG2 ARG E 20 11.323 6.304 10.022 1.00 16.29 H ATOM 3711 HG3 ARG E 20 12.315 6.936 11.091 1.00 16.29 H ATOM 3712 HD2 ARG E 20 11.735 9.075 10.359 1.00 17.09 H ATOM 3713 HD3 ARG E 20 10.734 8.437 9.300 1.00 17.09 H ATOM 3714 HE ARG E 20 9.177 8.074 10.892 1.00 16.95 H ATOM 3715 HH11 ARG E 20 12.070 9.044 12.419 1.00 17.45 H ATOM 3716 HH12 ARG E 20 11.466 9.253 13.764 1.00 17.45 H ATOM 3717 HH21 ARG E 20 8.351 8.454 12.964 1.00 19.74 H ATOM 3718 HH22 ARG E 20 9.213 8.896 14.096 1.00 19.74 H ATOM 3719 N TYR E 21 14.286 8.377 6.714 1.00 14.14 N ANISOU 3719 N TYR E 21 2230 1257 1886 -390 249 -86 N ATOM 3720 CA TYR E 21 15.435 8.761 5.903 1.00 14.35 C ANISOU 3720 CA TYR E 21 2156 1430 1865 -153 190 201 C ATOM 3721 C TYR E 21 16.662 9.052 6.722 1.00 13.55 C ANISOU 3721 C TYR E 21 2100 1300 1747 124 419 147 C ATOM 3722 O TYR E 21 16.506 9.597 7.832 1.00 13.45 O ANISOU 3722 O TYR E 21 2205 1258 1647 163 368 85 O ATOM 3723 CB TYR E 21 15.125 10.017 5.044 1.00 16.69 C ANISOU 3723 CB TYR E 21 2267 1881 2192 -416 -353 257 C ATOM 3724 CG TYR E 21 14.180 9.662 3.901 1.00 19.76 C ANISOU 3724 CG TYR E 21 2800 2146 2562 -478 -704 395 C ATOM 3725 CD1 TYR E 21 12.856 9.600 4.088 1.00 22.62 C ANISOU 3725 CD1 TYR E 21 3101 2529 2966 -400 -1012 288 C ATOM 3726 CD2 TYR E 21 14.706 9.406 2.613 1.00 23.09 C ANISOU 3726 CD2 TYR E 21 3190 2661 2922 -568 -820 408 C ATOM 3727 CE1 TYR E 21 12.015 9.219 3.007 1.00 24.46 C ANISOU 3727 CE1 TYR E 21 3281 2833 3178 -453 -1269 254 C ATOM 3728 CE2 TYR E 21 13.908 9.062 1.579 1.00 25.21 C ANISOU 3728 CE2 TYR E 21 3391 2997 3192 -597 -1045 384 C ATOM 3729 CZ TYR E 21 12.590 9.014 1.768 1.00 25.42 C ANISOU 3729 CZ TYR E 21 3439 2990 3229 -645 -1337 147 C ATOM 3730 OH TYR E 21 11.842 8.644 0.643 1.00 29.30 O ANISOU 3730 OH TYR E 21 3955 3504 3674 -669 -1360 -70 O ATOM 3731 H TYR E 21 13.981 9.031 7.181 1.00 16.98 H ATOM 3732 HA TYR E 21 15.650 8.025 5.292 1.00 17.23 H ATOM 3733 HB2 TYR E 21 14.699 10.690 5.597 1.00 20.04 H ATOM 3734 HB3 TYR E 21 15.949 10.361 4.665 1.00 20.04 H ATOM 3735 HD1 TYR E 21 12.495 9.752 4.931 1.00 27.16 H ATOM 3736 HD2 TYR E 21 15.625 9.453 2.481 1.00 27.72 H ATOM 3737 HE1 TYR E 21 11.092 9.180 3.115 1.00 29.36 H ATOM 3738 HE2 TYR E 21 14.270 8.902 0.738 1.00 30.27 H ATOM 3739 HH TYR E 21 12.106 7.923 0.354 1.00 35.17 H ATOM 3740 N PHE E 22 17.856 8.751 6.202 1.00 14.30 N ANISOU 3740 N PHE E 22 2080 1516 1838 -208 551 90 N ATOM 3741 CA PHE E 22 19.119 9.162 6.818 1.00 14.96 C ANISOU 3741 CA PHE E 22 2178 1552 1955 -92 718 101 C ATOM 3742 C PHE E 22 19.991 9.730 5.710 1.00 15.60 C ANISOU 3742 C PHE E 22 2488 1474 1965 -85 789 13 C ATOM 3743 O PHE E 22 19.868 9.313 4.552 1.00 17.01 O ANISOU 3743 O PHE E 22 3070 1443 1949 -105 916 86 O ATOM 3744 CB PHE E 22 19.811 7.988 7.557 1.00 15.80 C ANISOU 3744 CB PHE E 22 2194 1755 2055 130 762 164 C ATOM 3745 CG PHE E 22 20.499 7.036 6.660 1.00 16.18 C ANISOU 3745 CG PHE E 22 2232 1801 2113 134 822 278 C ATOM 3746 CD1 PHE E 22 21.866 7.006 6.526 1.00 17.33 C ANISOU 3746 CD1 PHE E 22 2353 2008 2222 404 858 161 C ATOM 3747 CD2 PHE E 22 19.731 6.121 5.927 1.00 17.75 C ANISOU 3747 CD2 PHE E 22 2436 2067 2242 30 810 161 C ATOM 3748 CE1 PHE E 22 22.487 6.087 5.668 1.00 18.13 C ANISOU 3748 CE1 PHE E 22 2489 2064 2335 397 846 51 C ATOM 3749 CE2 PHE E 22 20.344 5.171 5.089 1.00 18.42 C ANISOU 3749 CE2 PHE E 22 2557 2085 2356 187 760 200 C ATOM 3750 CZ PHE E 22 21.664 5.207 4.940 1.00 18.14 C ANISOU 3750 CZ PHE E 22 2505 2039 2348 245 830 40 C ATOM 3751 H PHE E 22 17.961 8.300 5.477 1.00 17.18 H ATOM 3752 HA PHE E 22 18.946 9.874 7.468 1.00 17.97 H ATOM 3753 HB2 PHE E 22 20.472 8.350 8.167 1.00 18.98 H ATOM 3754 HB3 PHE E 22 19.140 7.494 8.055 1.00 18.98 H ATOM 3755 HD1 PHE E 22 22.387 7.615 6.998 1.00 20.81 H ATOM 3756 HD2 PHE E 22 18.805 6.119 6.022 1.00 21.32 H ATOM 3757 HE1 PHE E 22 23.411 6.075 5.565 1.00 21.77 H ATOM 3758 HE2 PHE E 22 19.829 4.580 4.590 1.00 22.11 H ATOM 3759 HZ PHE E 22 22.067 4.579 4.385 1.00 21.78 H ATOM 3760 N TYR E 23 20.902 10.608 6.083 1.00 15.71 N ANISOU 3760 N TYR E 23 2373 1525 2073 15 896 7 N ATOM 3761 CA TYR E 23 21.876 11.044 5.122 1.00 16.59 C ANISOU 3761 CA TYR E 23 2317 1785 2202 -89 972 143 C ATOM 3762 C TYR E 23 23.035 10.059 5.072 1.00 17.89 C ANISOU 3762 C TYR E 23 2482 1930 2385 161 1250 195 C ATOM 3763 O TYR E 23 23.667 9.741 6.109 1.00 18.25 O ANISOU 3763 O TYR E 23 2550 1785 2599 203 1114 163 O ATOM 3764 CB TYR E 23 22.423 12.445 5.500 1.00 16.65 C ANISOU 3764 CB TYR E 23 2264 1816 2246 -116 926 138 C ATOM 3765 CG TYR E 23 23.394 12.942 4.519 1.00 18.64 C ANISOU 3765 CG TYR E 23 2676 1892 2512 -169 1061 57 C ATOM 3766 CD1 TYR E 23 24.754 12.977 4.834 1.00 20.81 C ANISOU 3766 CD1 TYR E 23 2790 2360 2757 -141 1130 62 C ATOM 3767 CD2 TYR E 23 22.975 13.383 3.250 1.00 19.87 C ANISOU 3767 CD2 TYR E 23 2796 2157 2597 -245 1089 19 C ATOM 3768 CE1 TYR E 23 25.684 13.467 3.899 1.00 21.94 C ANISOU 3768 CE1 TYR E 23 2886 2582 2867 -255 1309 107 C ATOM 3769 CE2 TYR E 23 23.860 13.810 2.301 1.00 21.34 C ANISOU 3769 CE2 TYR E 23 2957 2415 2737 -395 1256 152 C ATOM 3770 CZ TYR E 23 25.208 13.859 2.629 1.00 22.24 C ANISOU 3770 CZ TYR E 23 3026 2601 2824 -404 1502 217 C ATOM 3771 OH TYR E 23 26.033 14.321 1.625 1.00 25.13 O ANISOU 3771 OH TYR E 23 3438 2986 3126 -552 1640 215 O ATOM 3772 H TYR E 23 20.974 10.957 6.866 1.00 18.87 H ATOM 3773 HA TYR E 23 21.466 11.094 4.233 1.00 19.93 H ATOM 3774 HB2 TYR E 23 21.686 13.074 5.541 1.00 19.99 H ATOM 3775 HB3 TYR E 23 22.864 12.392 6.362 1.00 19.99 H ATOM 3776 HD1 TYR E 23 25.042 12.708 5.677 1.00 24.99 H ATOM 3777 HD2 TYR E 23 22.072 13.333 3.032 1.00 23.86 H ATOM 3778 HE1 TYR E 23 26.593 13.483 4.094 1.00 26.34 H ATOM 3779 HE2 TYR E 23 23.563 14.093 1.467 1.00 25.62 H ATOM 3780 HH TYR E 23 25.816 15.082 1.412 1.00 30.17 H ATOM 3781 N ASN E 24 23.269 9.541 3.861 1.00 19.81 N ANISOU 3781 N ASN E 24 2782 2158 2588 400 1485 304 N ATOM 3782 CA ASN E 24 24.361 8.632 3.624 1.00 22.98 C ANISOU 3782 CA ASN E 24 3177 2619 2933 545 1555 295 C ATOM 3783 C ASN E 24 25.483 9.405 3.038 1.00 24.83 C ANISOU 3783 C ASN E 24 3539 2766 3127 702 1842 311 C ATOM 3784 O ASN E 24 25.508 9.726 1.816 1.00 24.19 O ANISOU 3784 O ASN E 24 3833 2501 2857 828 1892 385 O ATOM 3785 CB ASN E 24 23.873 7.541 2.630 1.00 24.73 C ANISOU 3785 CB ASN E 24 3334 2881 3183 510 1443 305 C ATOM 3786 CG ASN E 24 24.930 6.558 2.305 1.00 25.75 C ANISOU 3786 CG ASN E 24 3487 2996 3302 490 1360 220 C ATOM 3787 OD1 ASN E 24 26.130 6.760 2.534 1.00 25.41 O ANISOU 3787 OD1 ASN E 24 3591 2768 3294 711 1251 240 O ATOM 3788 ND2 ASN E 24 24.506 5.480 1.689 1.00 28.22 N ANISOU 3788 ND2 ASN E 24 3679 3419 3624 394 1402 133 N ATOM 3789 H ASN E 24 22.798 9.710 3.162 1.00 23.79 H ATOM 3790 HA ASN E 24 24.650 8.212 4.461 1.00 27.58 H ATOM 3791 HB2 ASN E 24 23.128 7.062 3.026 1.00 29.70 H ATOM 3792 HB3 ASN E 24 23.594 7.966 1.804 1.00 29.70 H ATOM 3793 HD21 ASN E 24 25.141 4.777 1.437 1.00 33.88 H ATOM 3794 HD22 ASN E 24 23.553 5.377 1.481 1.00 33.88 H ATOM 3795 N ALA E 25 26.434 9.746 3.894 1.00 28.90 N ANISOU 3795 N ALA E 25 3806 3446 3728 570 1943 185 N ATOM 3796 CA ALA E 25 27.532 10.635 3.489 1.00 33.93 C ANISOU 3796 CA ALA E 25 4277 4239 4377 464 2049 74 C ATOM 3797 C ALA E 25 28.434 9.975 2.447 1.00 34.20 C ANISOU 3797 C ALA E 25 4206 4408 4381 447 2265 81 C ATOM 3798 O ALA E 25 28.995 10.692 1.647 1.00 34.27 O ANISOU 3798 O ALA E 25 4158 4470 4393 215 2156 185 O ATOM 3799 CB ALA E 25 28.365 11.038 4.708 1.00 39.82 C ANISOU 3799 CB ALA E 25 5013 4976 5141 361 1929 0 C ATOM 3800 H ALA E 25 26.475 9.482 4.711 1.00 34.69 H ATOM 3801 HA ALA E 25 27.155 11.449 3.094 1.00 40.73 H ATOM 3802 HB1 ALA E 25 29.075 11.618 4.423 1.00 47.80 H ATOM 3803 HB2 ALA E 25 27.800 11.496 5.335 1.00 47.80 H ATOM 3804 HB3 ALA E 25 28.730 10.248 5.112 1.00 47.80 H ATOM 3805 N LYS E 26 28.481 8.645 2.405 1.00 35.04 N ANISOU 3805 N LYS E 26 4303 4492 4519 701 2511 120 N ATOM 3806 CA LYS E 26 29.220 7.937 1.303 1.00 38.38 C ANISOU 3806 CA LYS E 26 4827 4867 4889 730 2330 50 C ATOM 3807 C LYS E 26 28.549 8.141 -0.053 1.00 34.38 C ANISOU 3807 C LYS E 26 4406 4368 4289 824 2515 188 C ATOM 3808 O LYS E 26 29.243 8.291 -1.068 1.00 33.43 O ANISOU 3808 O LYS E 26 4398 4265 4040 832 2626 181 O ATOM 3809 CB LYS E 26 29.204 6.425 1.642 1.00 45.96 C ANISOU 3809 CB LYS E 26 5773 5768 5922 497 1957 -11 C ATOM 3810 CG LYS E 26 29.048 5.481 0.466 0.00 53.02 C ANISOU 3810 CG LYS E 26 6665 6656 6826 208 1587 1 C ATOM 3811 CD LYS E 26 30.350 5.308 -0.280 0.00 58.56 C ANISOU 3811 CD LYS E 26 7360 7351 7538 6 1305 23 C ATOM 3812 CE LYS E 26 30.393 3.971 -0.996 0.00 62.44 C ANISOU 3812 CE LYS E 26 7849 7841 8033 -119 1111 44 C ATOM 3813 NZ LYS E 26 30.440 2.830 -0.038 0.00 65.87 N ANISOU 3813 NZ LYS E 26 8271 8245 8510 -178 988 56 N ATOM 3814 H LYS E 26 28.109 8.123 2.978 1.00 42.06 H ATOM 3815 HA LYS E 26 30.147 8.250 1.257 1.00 46.07 H ATOM 3816 HB2 LYS E 26 30.039 6.203 2.083 1.00 55.17 H ATOM 3817 HB3 LYS E 26 28.465 6.256 2.248 1.00 55.17 H ATOM 3818 HG2 LYS E 26 28.765 4.611 0.789 0.00 63.64 H ATOM 3819 HG3 LYS E 26 28.391 5.841 -0.149 0.00 63.64 H ATOM 3820 HD2 LYS E 26 30.437 6.012 -0.942 0.00 70.28 H ATOM 3821 HD3 LYS E 26 31.088 5.342 0.348 0.00 70.28 H ATOM 3822 HE2 LYS E 26 29.597 3.875 -1.542 0.00 74.94 H ATOM 3823 HE3 LYS E 26 31.187 3.932 -1.552 0.00 74.94 H ATOM 3824 HZ1 LYS E 26 30.466 2.000 -0.519 0.00 79.05 H ATOM 3825 HZ2 LYS E 26 31.223 2.897 0.513 0.00 79.05 H ATOM 3826 HZ3 LYS E 26 29.661 2.841 0.523 0.00 79.05 H ATOM 3827 N ALA E 27 27.231 8.038 -0.161 1.00 32.78 N ANISOU 3827 N ALA E 27 4237 4130 4087 729 2489 241 N ATOM 3828 CA ALA E 27 26.542 8.257 -1.432 1.00 31.40 C ANISOU 3828 CA ALA E 27 4149 3855 3926 741 2362 278 C ATOM 3829 C ALA E 27 26.265 9.730 -1.706 1.00 30.38 C ANISOU 3829 C ALA E 27 4327 3614 3601 461 2364 425 C ATOM 3830 O ALA E 27 25.963 10.089 -2.861 1.00 30.65 O ANISOU 3830 O ALA E 27 4652 3539 3456 205 2319 663 O ATOM 3831 CB ALA E 27 25.271 7.489 -1.450 1.00 32.80 C ANISOU 3831 CB ALA E 27 4198 4046 4218 886 2315 220 C ATOM 3832 H ALA E 27 26.706 7.840 0.491 1.00 39.35 H ATOM 3833 HA ALA E 27 27.107 7.919 -2.158 1.00 37.70 H ATOM 3834 HB1 ALA E 27 24.827 7.640 -2.288 1.00 39.37 H ATOM 3835 HB2 ALA E 27 25.469 6.555 -1.347 1.00 39.37 H ATOM 3836 HB3 ALA E 27 24.715 7.788 -0.726 1.00 39.37 H ATOM 3837 N GLY E 28 26.325 10.613 -0.689 1.00 29.54 N ANISOU 3837 N GLY E 28 4020 3574 3631 371 2293 396 N ATOM 3838 CA GLY E 28 25.980 11.997 -0.897 1.00 29.67 C ANISOU 3838 CA GLY E 28 3937 3610 3727 247 2149 379 C ATOM 3839 C GLY E 28 24.481 12.164 -1.075 1.00 28.50 C ANISOU 3839 C GLY E 28 3960 3303 3566 161 2120 469 C ATOM 3840 O GLY E 28 24.003 13.141 -1.689 1.00 29.79 O ANISOU 3840 O GLY E 28 4371 3338 3611 272 1892 441 O ATOM 3841 H GLY E 28 26.563 10.422 0.115 1.00 35.47 H ATOM 3842 HA2 GLY E 28 26.264 12.524 -0.134 1.00 35.62 H ATOM 3843 HA3 GLY E 28 26.427 12.331 -1.691 1.00 35.62 H ATOM 3844 N LEU E 29 23.709 11.278 -0.449 1.00 28.41 N ANISOU 3844 N LEU E 29 3767 3404 3625 65 2291 377 N ATOM 3845 CA LEU E 29 22.299 11.210 -0.738 1.00 30.91 C ANISOU 3845 CA LEU E 29 4067 3734 3944 6 2084 326 C ATOM 3846 C LEU E 29 21.539 10.839 0.568 1.00 25.14 C ANISOU 3846 C LEU E 29 3649 2765 3138 89 1875 332 C ATOM 3847 O LEU E 29 22.038 10.038 1.326 1.00 23.88 O ANISOU 3847 O LEU E 29 3752 2365 2957 421 1787 256 O ATOM 3848 CB LEU E 29 22.006 10.040 -1.724 1.00 40.17 C ANISOU 3848 CB LEU E 29 5098 5024 5140 -109 1985 319 C ATOM 3849 CG LEU E 29 22.327 10.163 -3.204 1.00 45.37 C ANISOU 3849 CG LEU E 29 5712 5717 5809 -253 1927 379 C ATOM 3850 CD1 LEU E 29 21.941 8.916 -3.930 1.00 47.90 C ANISOU 3850 CD1 LEU E 29 6000 5995 6206 -312 1890 391 C ATOM 3851 CD2 LEU E 29 21.543 11.363 -3.748 1.00 50.00 C ANISOU 3851 CD2 LEU E 29 6274 6262 6460 -301 1882 404 C ATOM 3852 H LEU E 29 23.982 10.714 0.140 1.00 34.11 H ATOM 3853 HA LEU E 29 21.964 12.057 -1.101 1.00 37.11 H ATOM 3854 HB2 LEU E 29 22.496 9.266 -1.404 1.00 48.22 H ATOM 3855 HB3 LEU E 29 21.057 9.848 -1.668 1.00 48.22 H ATOM 3856 HG LEU E 29 23.276 10.322 -3.327 1.00 54.46 H ATOM 3857 HD11 LEU E 29 22.154 9.019 -4.860 1.00 57.50 H ATOM 3858 HD12 LEU E 29 22.430 8.177 -3.561 1.00 57.50 H ATOM 3859 HD13 LEU E 29 20.998 8.772 -3.822 1.00 57.50 H ATOM 3860 HD21 LEU E 29 21.731 11.460 -4.684 1.00 60.01 H ATOM 3861 HD22 LEU E 29 20.605 11.208 -3.617 1.00 60.01 H ATOM 3862 HD23 LEU E 29 21.814 12.153 -3.275 1.00 60.01 H ATOM 3863 N CYS E 30 20.314 11.298 0.690 1.00 22.21 N ANISOU 3863 N CYS E 30 3206 2460 2772 -4 1578 438 N ATOM 3864 CA CYS E 30 19.382 10.821 1.708 1.00 21.05 C ANISOU 3864 CA CYS E 30 2964 2395 2641 -106 1212 80 C ATOM 3865 C CYS E 30 18.797 9.531 1.183 1.00 21.55 C ANISOU 3865 C CYS E 30 3363 2412 2414 -464 1038 51 C ATOM 3866 O CYS E 30 18.463 9.408 0.004 1.00 23.87 O ANISOU 3866 O CYS E 30 3952 2751 2366 -398 620 -6 O ATOM 3867 CB CYS E 30 18.305 11.890 1.988 1.00 22.18 C ANISOU 3867 CB CYS E 30 2962 2582 2886 -44 1017 -83 C ATOM 3868 SG CYS E 30 19.007 13.310 2.862 1.00 21.62 S ANISOU 3868 SG CYS E 30 3022 2145 3049 -92 865 -101 S ATOM 3869 H CYS E 30 19.981 11.906 0.182 1.00 26.66 H ATOM 3870 HA CYS E 30 19.865 10.634 2.540 1.00 25.28 H ATOM 3871 HB2 CYS E 30 17.935 12.202 1.147 1.00 26.63 H ATOM 3872 HB3 CYS E 30 17.607 11.506 2.542 1.00 26.63 H ATOM 3873 N GLN E 31 18.710 8.532 2.051 1.00 20.73 N ANISOU 3873 N GLN E 31 3204 2195 2479 -678 1041 37 N ATOM 3874 CA GLN E 31 18.256 7.187 1.686 1.00 22.92 C ANISOU 3874 CA GLN E 31 3276 2663 2771 -612 1092 -23 C ATOM 3875 C GLN E 31 17.373 6.659 2.795 1.00 20.14 C ANISOU 3875 C GLN E 31 3208 2252 2193 -373 882 -125 C ATOM 3876 O GLN E 31 17.356 7.149 3.921 1.00 19.57 O ANISOU 3876 O GLN E 31 3475 2103 1858 -386 844 -439 O ATOM 3877 CB GLN E 31 19.412 6.225 1.554 1.00 27.81 C ANISOU 3877 CB GLN E 31 3630 3416 3520 -542 1501 -15 C ATOM 3878 CG GLN E 31 20.283 6.568 0.371 1.00 32.42 C ANISOU 3878 CG GLN E 31 4124 4024 4170 -392 1721 -45 C ATOM 3879 CD GLN E 31 21.459 5.596 0.259 1.00 36.18 C ANISOU 3879 CD GLN E 31 4661 4508 4576 -134 1787 -243 C ATOM 3880 OE1 GLN E 31 21.886 4.961 1.241 1.00 35.67 O ANISOU 3880 OE1 GLN E 31 4690 4417 4448 164 1680 -434 O ATOM 3881 NE2 GLN E 31 21.961 5.440 -0.979 1.00 41.87 N ANISOU 3881 NE2 GLN E 31 5305 5252 5353 -102 1797 -311 N ATOM 3882 H GLN E 31 18.914 8.607 2.883 1.00 24.89 H ATOM 3883 HA GLN E 31 17.750 7.210 0.846 1.00 27.52 H ATOM 3884 HB2 GLN E 31 19.957 6.266 2.355 1.00 33.39 H ATOM 3885 HB3 GLN E 31 19.068 5.326 1.427 1.00 33.39 H ATOM 3886 HG2 GLN E 31 19.759 6.510 -0.443 1.00 38.92 H ATOM 3887 HG3 GLN E 31 20.636 7.465 0.481 1.00 38.92 H ATOM 3888 HE21 GLN E 31 22.623 4.907 -1.110 1.00 50.26 H ATOM 3889 HE22 GLN E 31 21.620 5.873 -1.639 1.00 50.26 H ATOM 3890 N THR E 32 16.502 5.718 2.494 1.00 19.64 N ANISOU 3890 N THR E 32 3005 2220 2238 -296 609 -195 N ATOM 3891 CA THR E 32 15.621 5.141 3.475 1.00 20.41 C ANISOU 3891 CA THR E 32 2935 2291 2530 -37 336 -190 C ATOM 3892 C THR E 32 16.316 4.060 4.293 1.00 18.21 C ANISOU 3892 C THR E 32 2903 1821 2194 186 530 -59 C ATOM 3893 O THR E 32 17.296 3.435 3.886 1.00 19.33 O ANISOU 3893 O THR E 32 3255 2020 2071 131 635 -74 O ATOM 3894 CB THR E 32 14.454 4.509 2.824 1.00 23.30 C ANISOU 3894 CB THR E 32 3122 2734 2999 -102 -87 -390 C ATOM 3895 OG1 THR E 32 14.937 3.508 1.898 1.00 22.81 O ANISOU 3895 OG1 THR E 32 3138 2596 2935 -73 -174 -548 O ATOM 3896 CG2 THR E 32 13.635 5.517 2.075 1.00 27.77 C ANISOU 3896 CG2 THR E 32 3564 3385 3602 11 -319 -546 C ATOM 3897 H THR E 32 16.402 5.391 1.705 1.00 23.58 H ATOM 3898 HA THR E 32 15.301 5.839 4.084 1.00 24.51 H ATOM 3899 HB THR E 32 13.893 4.089 3.494 1.00 27.98 H ATOM 3900 HG1 THR E 32 14.305 3.143 1.524 1.00 27.39 H ATOM 3901 HG21 THR E 32 12.884 5.086 1.660 1.00 33.34 H ATOM 3902 HG22 THR E 32 13.314 6.191 2.679 1.00 33.34 H ATOM 3903 HG23 THR E 32 14.170 5.935 1.396 1.00 33.34 H ATOM 3904 N PHE E 33 15.757 3.890 5.487 1.00 16.72 N ANISOU 3904 N PHE E 33 2566 1780 2007 -38 413 -118 N ATOM 3905 CA PHE E 33 16.138 2.778 6.387 1.00 15.50 C ANISOU 3905 CA PHE E 33 2327 1620 1941 79 303 -127 C ATOM 3906 C PHE E 33 14.913 2.395 7.177 1.00 15.55 C ANISOU 3906 C PHE E 33 2420 1618 1871 106 276 -187 C ATOM 3907 O PHE E 33 13.905 3.107 7.227 1.00 15.26 O ANISOU 3907 O PHE E 33 2442 1564 1792 33 321 67 O ATOM 3908 CB PHE E 33 17.378 3.089 7.242 1.00 15.19 C ANISOU 3908 CB PHE E 33 2168 1643 1959 14 429 -55 C ATOM 3909 CG PHE E 33 17.137 4.042 8.402 1.00 14.28 C ANISOU 3909 CG PHE E 33 2112 1469 1843 107 455 0 C ATOM 3910 CD1 PHE E 33 17.084 3.545 9.685 1.00 14.76 C ANISOU 3910 CD1 PHE E 33 2062 1627 1919 91 478 157 C ATOM 3911 CD2 PHE E 33 16.901 5.404 8.195 1.00 14.24 C ANISOU 3911 CD2 PHE E 33 2081 1511 1820 23 409 -29 C ATOM 3912 CE1 PHE E 33 16.836 4.390 10.759 1.00 14.57 C ANISOU 3912 CE1 PHE E 33 1983 1678 1876 113 272 178 C ATOM 3913 CE2 PHE E 33 16.669 6.267 9.250 1.00 14.08 C ANISOU 3913 CE2 PHE E 33 1988 1494 1867 -38 395 10 C ATOM 3914 CZ PHE E 33 16.605 5.741 10.544 1.00 14.11 C ANISOU 3914 CZ PHE E 33 1915 1565 1880 41 309 132 C ATOM 3915 H PHE E 33 15.148 4.404 5.810 1.00 20.08 H ATOM 3916 HA PHE E 33 16.367 2.006 5.829 1.00 18.61 H ATOM 3917 HB2 PHE E 33 17.714 2.257 7.612 1.00 18.24 H ATOM 3918 HB3 PHE E 33 18.053 3.487 6.672 1.00 18.24 H ATOM 3919 HD1 PHE E 33 17.221 2.637 9.834 1.00 17.72 H ATOM 3920 HD2 PHE E 33 16.931 5.744 7.330 1.00 17.10 H ATOM 3921 HE1 PHE E 33 16.809 4.047 11.623 1.00 17.50 H ATOM 3922 HE2 PHE E 33 16.518 7.172 9.099 1.00 16.91 H ATOM 3923 HZ PHE E 33 16.458 6.306 11.267 1.00 16.94 H ATOM 3924 N VAL E 34 15.007 1.256 7.819 1.00 14.82 N ANISOU 3924 N VAL E 34 2239 1496 1895 201 397 -109 N ATOM 3925 CA VAL E 34 13.928 0.766 8.700 1.00 14.53 C ANISOU 3925 CA VAL E 34 2119 1507 1893 55 381 -66 C ATOM 3926 C VAL E 34 14.181 1.277 10.108 1.00 13.34 C ANISOU 3926 C VAL E 34 1893 1438 1740 77 321 32 C ATOM 3927 O VAL E 34 15.197 0.951 10.747 1.00 15.00 O ANISOU 3927 O VAL E 34 2224 1643 1832 196 343 -38 O ATOM 3928 CB VAL E 34 13.934 -0.779 8.749 1.00 16.45 C ANISOU 3928 CB VAL E 34 2344 1790 2117 -49 456 -254 C ATOM 3929 CG1 VAL E 34 12.910 -1.243 9.760 1.00 18.47 C ANISOU 3929 CG1 VAL E 34 2455 2172 2390 -16 464 -281 C ATOM 3930 CG2 VAL E 34 13.623 -1.317 7.361 1.00 19.30 C ANISOU 3930 CG2 VAL E 34 2605 2236 2491 -39 487 -399 C ATOM 3931 H VAL E 34 15.685 0.729 7.773 1.00 17.80 H ATOM 3932 HA VAL E 34 13.055 1.083 8.386 1.00 17.44 H ATOM 3933 HB VAL E 34 14.818 -1.100 9.023 1.00 19.75 H ATOM 3934 HG11 VAL E 34 12.914 -2.203 9.790 1.00 22.18 H ATOM 3935 HG12 VAL E 34 13.139 -0.887 10.621 1.00 22.18 H ATOM 3936 HG13 VAL E 34 12.044 -0.927 9.494 1.00 22.18 H ATOM 3937 HG21 VAL E 34 13.626 -2.276 7.390 1.00 23.17 H ATOM 3938 HG22 VAL E 34 12.758 -1.000 7.090 1.00 23.17 H ATOM 3939 HG23 VAL E 34 14.293 -1.005 6.748 1.00 23.17 H ATOM 3940 N TYR E 35 13.301 2.136 10.564 1.00 12.02 N ANISOU 3940 N TYR E 35 1706 1271 1590 -37 264 71 N ATOM 3941 CA TYR E 35 13.352 2.633 11.963 1.00 11.08 C ANISOU 3941 CA TYR E 35 1451 1256 1503 -25 128 96 C ATOM 3942 C TYR E 35 12.360 1.822 12.773 1.00 10.66 C ANISOU 3942 C TYR E 35 1343 1229 1479 -115 -39 135 C ATOM 3943 O TYR E 35 11.218 1.589 12.371 1.00 11.58 O ANISOU 3943 O TYR E 35 1530 1303 1565 -138 -77 143 O ATOM 3944 CB TYR E 35 12.980 4.126 11.964 1.00 11.39 C ANISOU 3944 CB TYR E 35 1485 1313 1530 -91 81 204 C ATOM 3945 CG TYR E 35 12.828 4.714 13.349 1.00 10.70 C ANISOU 3945 CG TYR E 35 1435 1192 1439 -47 108 180 C ATOM 3946 CD1 TYR E 35 13.788 4.506 14.327 1.00 10.48 C ANISOU 3946 CD1 TYR E 35 1415 1131 1438 -117 221 220 C ATOM 3947 CD2 TYR E 35 11.683 5.408 13.672 1.00 11.20 C ANISOU 3947 CD2 TYR E 35 1534 1212 1509 60 34 280 C ATOM 3948 CE1 TYR E 35 13.658 5.025 15.608 1.00 10.91 C ANISOU 3948 CE1 TYR E 35 1438 1222 1486 -67 126 153 C ATOM 3949 CE2 TYR E 35 11.541 5.999 14.920 1.00 10.94 C ANISOU 3949 CE2 TYR E 35 1499 1202 1456 50 71 205 C ATOM 3950 CZ TYR E 35 12.519 5.787 15.892 1.00 10.86 C ANISOU 3950 CZ TYR E 35 1547 1124 1455 14 42 155 C ATOM 3951 OH TYR E 35 12.419 6.315 17.160 1.00 11.70 O ANISOU 3951 OH TYR E 35 1733 1211 1501 -238 65 -93 O ATOM 3952 H TYR E 35 12.654 2.461 10.100 1.00 14.44 H ATOM 3953 HA TYR E 35 14.251 2.519 12.336 1.00 13.31 H ATOM 3954 HB2 TYR E 35 13.677 4.622 11.506 1.00 13.68 H ATOM 3955 HB3 TYR E 35 12.136 4.238 11.499 1.00 13.68 H ATOM 3956 HD1 TYR E 35 14.546 4.010 14.117 1.00 12.60 H ATOM 3957 HD2 TYR E 35 11.046 5.571 13.014 1.00 13.45 H ATOM 3958 HE1 TYR E 35 14.325 4.903 16.244 1.00 13.11 H ATOM 3959 HE2 TYR E 35 10.775 6.485 15.125 1.00 13.14 H ATOM 3960 HH TYR E 35 11.743 6.033 17.529 1.00 14.05 H ATOM 3961 N GLY E 36 12.860 1.277 13.878 1.00 10.06 N ANISOU 3961 N GLY E 36 1312 1085 1425 -156 -21 165 N ATOM 3962 CA GLY E 36 12.013 0.397 14.688 1.00 10.67 C ANISOU 3962 CA GLY E 36 1373 1245 1436 -185 66 93 C ATOM 3963 C GLY E 36 10.929 1.060 15.461 1.00 10.93 C ANISOU 3963 C GLY E 36 1433 1260 1460 -241 98 -6 C ATOM 3964 O GLY E 36 10.065 0.363 16.010 1.00 11.55 O ANISOU 3964 O GLY E 36 1594 1336 1457 -320 126 64 O ATOM 3965 H GLY E 36 13.658 1.394 14.175 1.00 12.09 H ATOM 3966 HA2 GLY E 36 11.600 -0.259 14.105 1.00 12.82 H ATOM 3967 HA3 GLY E 36 12.575 -0.080 15.319 1.00 12.82 H ATOM 3968 N GLY E 37 10.945 2.408 15.578 1.00 10.68 N ANISOU 3968 N GLY E 37 1259 1233 1564 -154 157 -29 N ATOM 3969 CA GLY E 37 9.852 3.141 16.190 1.00 11.12 C ANISOU 3969 CA GLY E 37 1315 1377 1533 -82 76 59 C ATOM 3970 C GLY E 37 10.172 3.762 17.534 1.00 11.06 C ANISOU 3970 C GLY E 37 1316 1336 1549 90 63 24 C ATOM 3971 O GLY E 37 9.301 4.450 18.066 1.00 13.38 O ANISOU 3971 O GLY E 37 1607 1754 1724 259 24 -232 O ATOM 3972 H GLY E 37 11.589 2.909 15.305 1.00 12.83 H ATOM 3973 HA2 GLY E 37 9.575 3.851 15.591 1.00 13.36 H ATOM 3974 HA3 GLY E 37 9.100 2.540 16.310 1.00 13.36 H ATOM 3975 N CYS E 38 11.363 3.534 18.096 1.00 10.35 N ANISOU 3975 N CYS E 38 1340 1149 1442 17 56 43 N ATOM 3976 CA CYS E 38 11.755 4.248 19.335 1.00 10.33 C ANISOU 3976 CA CYS E 38 1336 1150 1440 -113 16 110 C ATOM 3977 C CYS E 38 13.235 4.494 19.363 1.00 10.39 C ANISOU 3977 C CYS E 38 1372 1149 1428 -235 133 47 C ATOM 3978 O CYS E 38 14.046 3.848 18.705 1.00 11.05 O ANISOU 3978 O CYS E 38 1441 1117 1640 3 89 -3 O ATOM 3979 CB CYS E 38 11.356 3.405 20.575 1.00 11.73 C ANISOU 3979 CB CYS E 38 1473 1413 1570 -206 92 61 C ATOM 3980 SG CYS E 38 12.234 1.862 20.772 1.00 11.81 S ANISOU 3980 SG CYS E 38 1462 1419 1605 -129 87 8 S ATOM 3981 H CYS E 38 11.955 2.987 17.795 1.00 12.43 H ATOM 3982 HA CYS E 38 11.292 5.111 19.380 1.00 12.42 H ATOM 3983 HB2 CYS E 38 11.517 3.935 21.371 1.00 14.09 H ATOM 3984 HB3 CYS E 38 10.411 3.196 20.512 1.00 14.09 H ATOM 3985 N ARG E 39 13.605 5.445 20.204 1.00 11.48 N ANISOU 3985 N ARG E 39 1551 1193 1619 -391 148 -117 N ATOM 3986 CA ARG E 39 14.991 5.694 20.584 1.00 13.13 C ANISOU 3986 CA ARG E 39 1589 1559 1839 -501 10 -191 C ATOM 3987 C ARG E 39 15.817 6.164 19.370 1.00 13.02 C ANISOU 3987 C ARG E 39 1598 1546 1804 -292 244 -221 C ATOM 3988 O ARG E 39 17.008 5.878 19.239 1.00 14.91 O ANISOU 3988 O ARG E 39 1653 2040 1973 -304 277 -88 O ATOM 3989 CB ARG E 39 15.617 4.490 21.255 1.00 17.00 C ANISOU 3989 CB ARG E 39 2045 2168 2247 -667 -153 30 C ATOM 3990 CG ARG E 39 14.816 4.056 22.522 1.00 21.57 C ANISOU 3990 CG ARG E 39 2700 2698 2799 -569 -259 264 C ATOM 3991 CD ARG E 39 15.212 4.687 23.723 1.00 27.73 C ANISOU 3991 CD ARG E 39 3469 3510 3558 -340 -248 123 C ATOM 3992 NE ARG E 39 16.567 4.285 24.131 1.00 31.49 N ANISOU 3992 NE ARG E 39 3954 4018 3992 -335 -476 63 N ATOM 3993 CZ ARG E 39 17.263 4.962 25.034 1.00 35.80 C ANISOU 3993 CZ ARG E 39 4533 4550 4520 -244 -547 32 C ATOM 3994 NH1 ARG E 39 16.745 6.025 25.594 1.00 38.03 N ANISOU 3994 NH1 ARG E 39 4826 4780 4844 -215 -548 -71 N ATOM 3995 NH2 ARG E 39 18.490 4.588 25.305 1.00 40.00 N ANISOU 3995 NH2 ARG E 39 5027 5061 5111 -194 -634 6 N ATOM 3996 H ARG E 39 13.051 5.981 20.584 1.00 13.79 H ATOM 3997 HA ARG E 39 15.000 6.424 21.237 1.00 15.77 H ATOM 3998 HB2 ARG E 39 15.627 3.746 20.633 1.00 20.42 H ATOM 3999 HB3 ARG E 39 16.521 4.711 21.529 1.00 20.42 H ATOM 4000 HG2 ARG E 39 13.879 4.261 22.379 1.00 25.90 H ATOM 4001 HG3 ARG E 39 14.925 3.100 22.644 1.00 25.90 H ATOM 4002 HD2 ARG E 39 15.207 5.649 23.595 1.00 33.29 H ATOM 4003 HD3 ARG E 39 14.596 4.440 24.431 1.00 33.29 H ATOM 4004 HE ARG E 39 17.045 3.661 23.563 1.00 37.80 H ATOM 4005 HH11 ARG E 39 15.948 6.274 25.390 1.00 45.65 H ATOM 4006 HH12 ARG E 39 17.197 6.466 26.178 1.00 45.65 H ATOM 4007 HH21 ARG E 39 18.817 3.885 24.933 1.00 48.02 H ATOM 4008 HH22 ARG E 39 18.946 5.011 25.900 1.00 48.02 H ATOM 4009 N ALA E 40 15.186 6.899 18.492 1.00 12.83 N ANISOU 4009 N ALA E 40 1574 1510 1792 -360 315 -74 N ATOM 4010 CA ALA E 40 15.883 7.467 17.321 1.00 13.45 C ANISOU 4010 CA ALA E 40 1642 1670 1799 -453 227 -3 C ATOM 4011 C ALA E 40 17.135 8.224 17.672 1.00 14.49 C ANISOU 4011 C ALA E 40 1830 1801 1875 -593 242 -49 C ATOM 4012 O ALA E 40 17.180 8.946 18.659 1.00 16.26 O ANISOU 4012 O ALA E 40 1963 2184 2033 -800 417 -200 O ATOM 4013 CB ALA E 40 14.973 8.442 16.621 1.00 14.60 C ANISOU 4013 CB ALA E 40 1795 1796 1954 -400 61 238 C ATOM 4014 H ALA E 40 14.350 7.096 18.533 1.00 15.41 H ATOM 4015 HA ALA E 40 16.115 6.750 16.695 1.00 16.16 H ATOM 4016 HB1 ALA E 40 15.432 8.807 15.862 1.00 17.53 H ATOM 4017 HB2 ALA E 40 14.182 7.980 16.335 1.00 17.53 H ATOM 4018 HB3 ALA E 40 14.740 9.145 17.233 1.00 17.53 H ATOM 4019 N LYS E 41 18.143 8.116 16.809 1.00 13.89 N ANISOU 4019 N LYS E 41 1715 1717 1847 -598 132 77 N ATOM 4020 CA LYS E 41 19.269 9.020 16.803 1.00 14.65 C ANISOU 4020 CA LYS E 41 1771 1815 1980 -480 63 17 C ATOM 4021 C LYS E 41 18.961 10.165 15.846 1.00 14.03 C ANISOU 4021 C LYS E 41 1646 1797 1886 -514 110 -8 C ATOM 4022 O LYS E 41 17.874 10.215 15.251 1.00 14.57 O ANISOU 4022 O LYS E 41 1817 1746 1974 -470 78 66 O ATOM 4023 CB LYS E 41 20.515 8.261 16.394 1.00 18.52 C ANISOU 4023 CB LYS E 41 2232 2317 2490 -588 111 -15 C ATOM 4024 CG LYS E 41 20.995 7.306 17.561 1.00 23.52 C ANISOU 4024 CG LYS E 41 2902 2872 3165 -818 -31 -60 C ATOM 4025 CD LYS E 41 22.336 6.600 17.295 1.00 31.74 C ANISOU 4025 CD LYS E 41 3932 3961 4167 -885 -146 -126 C ATOM 4026 CE LYS E 41 22.691 5.713 18.479 1.00 40.30 C ANISOU 4026 CE LYS E 41 5040 5036 5236 -866 -180 -150 C ATOM 4027 NZ LYS E 41 23.884 4.808 18.226 1.00 47.76 N ANISOU 4027 NZ LYS E 41 6001 5972 6175 -870 -236 -157 N ATOM 4028 H LYS E 41 18.191 7.507 16.204 1.00 16.69 H ATOM 4029 HA LYS E 41 19.404 9.387 17.701 1.00 17.59 H ATOM 4030 HB2 LYS E 41 20.322 7.719 15.613 1.00 22.24 H ATOM 4031 HB3 LYS E 41 21.227 8.891 16.200 1.00 22.24 H ATOM 4032 HG2 LYS E 41 21.095 7.831 18.371 1.00 28.24 H ATOM 4033 HG3 LYS E 41 20.323 6.620 17.697 1.00 28.24 H ATOM 4034 HD2 LYS E 41 22.261 6.045 16.504 1.00 38.10 H ATOM 4035 HD3 LYS E 41 23.036 7.262 17.183 1.00 38.10 H ATOM 4036 HE2 LYS E 41 22.902 6.276 19.241 1.00 48.38 H ATOM 4037 HE3 LYS E 41 21.930 5.149 18.688 1.00 48.38 H ATOM 4038 HZ1 LYS E 41 24.061 4.274 19.004 1.00 57.33 H ATOM 4039 HZ2 LYS E 41 23.703 4.228 17.483 1.00 57.33 H ATOM 4040 HZ3 LYS E 41 24.660 5.337 18.028 1.00 57.33 H ATOM 4041 N ARG E 42 19.885 11.102 15.720 1.00 14.60 N ANISOU 4041 N ARG E 42 1815 1815 1917 -568 186 -85 N ATOM 4042 CA ARG E 42 19.545 12.343 15.037 1.00 15.18 C ANISOU 4042 CA ARG E 42 1957 1779 2032 -635 185 -117 C ATOM 4043 C ARG E 42 19.496 12.214 13.526 1.00 12.98 C ANISOU 4043 C ARG E 42 1677 1399 1854 -431 195 23 C ATOM 4044 O ARG E 42 18.804 13.035 12.885 1.00 13.76 O ANISOU 4044 O ARG E 42 1921 1346 1960 -141 276 87 O ATOM 4045 CB ARG E 42 20.512 13.451 15.442 1.00 18.90 C ANISOU 4045 CB ARG E 42 2404 2327 2451 -821 27 -373 C ATOM 4046 CG ARG E 42 20.334 13.914 16.956 1.00 23.60 C ANISOU 4046 CG ARG E 42 3036 2907 3023 -1063 -52 -486 C ATOM 4047 CD ARG E 42 21.493 14.893 17.372 1.00 28.72 C ANISOU 4047 CD ARG E 42 3676 3565 3671 -1110 -46 -390 C ATOM 4048 NE ARG E 42 22.801 14.245 17.310 0.00 32.12 N ANISOU 4048 NE ARG E 42 4075 4036 4092 -923 -53 -255 N ATOM 4049 CZ ARG E 42 23.934 14.817 17.701 0.00 34.90 C ANISOU 4049 CZ ARG E 42 4428 4419 4412 -767 -82 -145 C ATOM 4050 NH1 ARG E 42 23.917 16.050 18.184 0.00 37.16 N ANISOU 4050 NH1 ARG E 42 4695 4672 4751 -714 -128 -108 N ATOM 4051 NH2 ARG E 42 25.079 14.156 17.610 0.00 37.15 N ANISOU 4051 NH2 ARG E 42 4694 4671 4750 -715 -128 -107 N ATOM 4052 H ARG E 42 20.693 11.051 16.009 1.00 17.53 H ATOM 4053 HA ARG E 42 18.651 12.617 15.332 1.00 18.23 H ATOM 4054 HB2 ARG E 42 21.421 13.131 15.332 1.00 22.70 H ATOM 4055 HB3 ARG E 42 20.361 14.223 14.874 1.00 22.70 H ATOM 4056 HG2 ARG E 42 19.489 14.379 17.055 1.00 28.33 H ATOM 4057 HG3 ARG E 42 20.364 13.138 17.537 1.00 28.33 H ATOM 4058 HD2 ARG E 42 21.501 15.652 16.768 1.00 34.48 H ATOM 4059 HD3 ARG E 42 21.346 15.191 18.283 1.00 34.48 H ATOM 4060 HE ARG E 42 22.853 13.364 16.906 0.00 38.56 H ATOM 4061 HH11 ARG E 42 23.173 16.478 18.243 0.00 44.60 H ATOM 4062 HH12 ARG E 42 24.649 16.423 18.438 0.00 44.60 H ATOM 4063 HH21 ARG E 42 25.090 13.356 17.296 0.00 44.60 H ATOM 4064 HH22 ARG E 42 25.812 14.529 17.863 0.00 44.60 H ATOM 4065 N ASN E 43 20.245 11.280 12.927 1.00 13.46 N ANISOU 4065 N ASN E 43 1730 1581 1804 -230 303 92 N ATOM 4066 CA ASN E 43 20.238 11.095 11.455 1.00 12.52 C ANISOU 4066 CA ASN E 43 1500 1462 1796 -65 381 214 C ATOM 4067 C ASN E 43 19.041 10.231 11.070 1.00 11.88 C ANISOU 4067 C ASN E 43 1644 1123 1748 -94 299 204 C ATOM 4068 O ASN E 43 19.166 9.061 10.725 1.00 12.46 O ANISOU 4068 O ASN E 43 1771 1074 1890 -32 493 219 O ATOM 4069 CB ASN E 43 21.576 10.525 10.977 1.00 13.92 C ANISOU 4069 CB ASN E 43 1644 1724 1920 -142 488 181 C ATOM 4070 CG ASN E 43 21.751 10.578 9.496 1.00 13.84 C ANISOU 4070 CG ASN E 43 1644 1681 1933 -22 505 191 C ATOM 4071 OD1 ASN E 43 20.965 11.217 8.800 1.00 13.67 O ANISOU 4071 OD1 ASN E 43 1723 1628 1841 11 513 264 O ATOM 4072 ND2 ASN E 43 22.847 9.971 8.990 1.00 14.69 N ANISOU 4072 ND2 ASN E 43 1850 1697 2032 80 547 215 N ATOM 4073 H ASN E 43 20.768 10.739 13.343 1.00 16.17 H ATOM 4074 HA ASN E 43 20.120 11.970 11.030 1.00 15.04 H ATOM 4075 HB2 ASN E 43 22.296 11.036 11.380 1.00 16.72 H ATOM 4076 HB3 ASN E 43 21.637 9.597 11.251 1.00 16.72 H ATOM 4077 HD21 ASN E 43 23.009 9.977 8.023 1.00 17.64 H ATOM 4078 HD22 ASN E 43 23.481 9.524 9.590 1.00 17.64 H ATOM 4079 N ASN E 44 17.857 10.831 11.233 1.00 11.54 N ANISOU 4079 N ASN E 44 1505 1175 1705 -81 136 177 N ATOM 4080 CA ASN E 44 16.595 10.119 11.145 1.00 11.08 C ANISOU 4080 CA ASN E 44 1468 1181 1559 -55 38 81 C ATOM 4081 C ASN E 44 15.535 11.171 10.864 1.00 11.88 C ANISOU 4081 C ASN E 44 1533 1403 1578 28 92 61 C ATOM 4082 O ASN E 44 15.255 12.018 11.733 1.00 12.85 O ANISOU 4082 O ASN E 44 1829 1319 1733 47 150 -73 O ATOM 4083 CB ASN E 44 16.338 9.352 12.467 1.00 11.66 C ANISOU 4083 CB ASN E 44 1542 1307 1583 -118 129 166 C ATOM 4084 CG ASN E 44 14.992 8.647 12.471 1.00 11.94 C ANISOU 4084 CG ASN E 44 1578 1340 1618 15 133 185 C ATOM 4085 OD1 ASN E 44 14.016 9.066 11.838 1.00 12.91 O ANISOU 4085 OD1 ASN E 44 1678 1411 1819 -177 66 304 O ATOM 4086 ND2 ASN E 44 14.936 7.551 13.230 1.00 11.75 N ANISOU 4086 ND2 ASN E 44 1541 1340 1583 -75 166 110 N ATOM 4087 H ASN E 44 17.766 11.670 11.399 1.00 13.86 H ATOM 4088 HA ASN E 44 16.619 9.480 10.402 1.00 13.31 H ATOM 4089 HB2 ASN E 44 17.030 8.682 12.585 1.00 14.01 H ATOM 4090 HB3 ASN E 44 16.352 9.979 13.206 1.00 14.01 H ATOM 4091 HD21 ASN E 44 14.104 7.037 13.288 1.00 14.11 H ATOM 4092 HD22 ASN E 44 15.727 7.260 13.730 1.00 14.11 H ATOM 4093 N PHE E 45 14.995 11.151 9.667 1.00 11.68 N ANISOU 4093 N PHE E 45 1635 1230 1573 -27 84 20 N ATOM 4094 CA PHE E 45 14.080 12.179 9.197 1.00 11.87 C ANISOU 4094 CA PHE E 45 1577 1378 1553 -88 -32 77 C ATOM 4095 C PHE E 45 12.807 11.522 8.657 1.00 12.43 C ANISOU 4095 C PHE E 45 1758 1346 1620 -186 -73 -4 C ATOM 4096 O PHE E 45 12.812 10.417 8.093 1.00 12.88 O ANISOU 4096 O PHE E 45 1867 1273 1755 -205 84 47 O ATOM 4097 CB PHE E 45 14.742 12.971 8.038 1.00 12.56 C ANISOU 4097 CB PHE E 45 1631 1469 1673 -119 106 146 C ATOM 4098 CG PHE E 45 16.003 13.643 8.409 1.00 11.85 C ANISOU 4098 CG PHE E 45 1529 1152 1822 -52 174 232 C ATOM 4099 CD1 PHE E 45 17.226 12.993 8.316 1.00 13.22 C ANISOU 4099 CD1 PHE E 45 1731 1456 1836 58 178 207 C ATOM 4100 CD2 PHE E 45 15.962 14.944 8.935 1.00 13.23 C ANISOU 4100 CD2 PHE E 45 1627 1463 1938 -216 198 -9 C ATOM 4101 CE1 PHE E 45 18.395 13.617 8.700 1.00 13.70 C ANISOU 4101 CE1 PHE E 45 1815 1492 1899 55 195 219 C ATOM 4102 CE2 PHE E 45 17.152 15.568 9.360 1.00 13.92 C ANISOU 4102 CE2 PHE E 45 1796 1445 2049 -180 142 18 C ATOM 4103 CZ PHE E 45 18.375 14.899 9.205 1.00 14.60 C ANISOU 4103 CZ PHE E 45 1872 1666 2009 -186 96 98 C ATOM 4104 H PHE E 45 15.144 10.535 9.086 1.00 14.03 H ATOM 4105 HA PHE E 45 13.849 12.793 9.924 1.00 14.25 H ATOM 4106 HB2 PHE E 45 14.936 12.357 7.312 1.00 15.09 H ATOM 4107 HB3 PHE E 45 14.123 13.653 7.733 1.00 15.09 H ATOM 4108 HD1 PHE E 45 17.260 12.130 7.970 1.00 15.88 H ATOM 4109 HD2 PHE E 45 15.147 15.381 9.033 1.00 15.89 H ATOM 4110 HE1 PHE E 45 19.206 13.170 8.611 1.00 16.46 H ATOM 4111 HE2 PHE E 45 17.133 16.439 9.686 1.00 16.72 H ATOM 4112 HZ PHE E 45 19.168 15.310 9.466 1.00 17.54 H ATOM 4113 N LYS E 46 11.699 12.271 8.728 1.00 13.00 N ANISOU 4113 N LYS E 46 1684 1476 1781 -222 -8 -132 N ATOM 4114 CA LYS E 46 10.402 11.767 8.266 1.00 14.60 C ANISOU 4114 CA LYS E 46 1881 1704 1964 -327 -119 -141 C ATOM 4115 C LYS E 46 10.194 11.898 6.791 1.00 15.46 C ANISOU 4115 C LYS E 46 2187 1706 1979 -617 -297 59 C ATOM 4116 O LYS E 46 9.304 11.282 6.261 1.00 18.45 O ANISOU 4116 O LYS E 46 2592 2264 2155 -949 -458 128 O ATOM 4117 CB LYS E 46 9.265 12.436 9.064 1.00 16.63 C ANISOU 4117 CB LYS E 46 2098 1966 2253 -111 -48 -1 C ATOM 4118 CG LYS E 46 9.210 11.983 10.522 1.00 19.50 C ANISOU 4118 CG LYS E 46 2415 2382 2612 72 116 82 C ATOM 4119 CD LYS E 46 8.030 12.512 11.253 1.00 22.12 C ANISOU 4119 CD LYS E 46 2753 2667 2985 244 460 133 C ATOM 4120 CE LYS E 46 8.174 12.285 12.736 1.00 25.92 C ANISOU 4120 CE LYS E 46 3270 3146 3434 586 625 206 C ATOM 4121 NZ LYS E 46 6.931 12.759 13.482 1.00 30.60 N ANISOU 4121 NZ LYS E 46 3852 3794 3981 561 642 256 N ATOM 4122 H LYS E 46 11.673 13.073 9.038 1.00 15.62 H ATOM 4123 HA LYS E 46 10.365 10.809 8.470 1.00 17.54 H ATOM 4124 HB2 LYS E 46 9.397 13.397 9.055 1.00 19.97 H ATOM 4125 HB3 LYS E 46 8.417 12.214 8.650 1.00 19.97 H ATOM 4126 HG2 LYS E 46 9.169 11.015 10.549 1.00 23.41 H ATOM 4127 HG3 LYS E 46 10.008 12.294 10.978 1.00 23.41 H ATOM 4128 HD2 LYS E 46 7.954 13.466 11.095 1.00 26.56 H ATOM 4129 HD3 LYS E 46 7.231 12.054 10.949 1.00 26.56 H ATOM 4130 HE2 LYS E 46 8.290 11.337 12.907 1.00 31.12 H ATOM 4131 HE3 LYS E 46 8.938 12.784 13.066 1.00 31.12 H ATOM 4132 HZ1 LYS E 46 7.037 12.609 14.424 1.00 36.74 H ATOM 4133 HZ2 LYS E 46 6.796 13.697 13.330 1.00 36.74 H ATOM 4134 HZ3 LYS E 46 6.160 12.278 13.174 1.00 36.74 H ATOM 4135 N SER E 47 11.032 12.668 6.104 1.00 14.99 N ANISOU 4135 N SER E 47 2115 1732 1850 -480 -371 161 N ATOM 4136 CA SER E 47 10.908 12.757 4.656 1.00 16.52 C ANISOU 4136 CA SER E 47 2241 2070 1965 -277 -395 149 C ATOM 4137 C SER E 47 12.281 12.988 4.080 1.00 15.94 C ANISOU 4137 C SER E 47 2342 1869 1847 -477 -386 27 C ATOM 4138 O SER E 47 13.215 13.473 4.746 1.00 14.84 O ANISOU 4138 O SER E 47 2277 1641 1722 -288 -242 71 O ATOM 4139 CB SER E 47 9.974 13.911 4.253 1.00 17.60 C ANISOU 4139 CB SER E 47 2299 2152 2236 -301 -437 201 C ATOM 4140 OG SER E 47 10.612 15.144 4.564 1.00 17.92 O ANISOU 4140 OG SER E 47 2409 2104 2295 -177 -493 320 O ATOM 4141 H SER E 47 11.667 13.139 6.444 1.00 18.00 H ATOM 4142 HA SER E 47 10.549 11.917 4.299 1.00 19.84 H ATOM 4143 HB2 SER E 47 9.802 13.869 3.299 1.00 21.14 H ATOM 4144 HB3 SER E 47 9.144 13.843 4.749 1.00 21.14 H ATOM 4145 HG SER E 47 10.127 15.771 4.356 1.00 21.52 H ATOM 4146 N ALA E 48 12.391 12.744 2.755 1.00 17.13 N ANISOU 4146 N ALA E 48 2483 2008 2019 -494 -359 -86 N ATOM 4147 CA ALA E 48 13.632 13.096 2.101 1.00 17.99 C ANISOU 4147 CA ALA E 48 2507 2172 2156 -296 -215 -151 C ATOM 4148 C ALA E 48 13.884 14.612 2.099 1.00 17.66 C ANISOU 4148 C ALA E 48 2603 2131 1974 -250 -64 221 C ATOM 4149 O ALA E 48 15.010 15.037 2.197 1.00 17.22 O ANISOU 4149 O ALA E 48 2718 1977 1846 -141 -44 300 O ATOM 4150 CB ALA E 48 13.689 12.568 0.627 1.00 20.99 C ANISOU 4150 CB ALA E 48 2763 2601 2610 -136 -57 -236 C ATOM 4151 H ALA E 48 11.787 12.395 2.251 1.00 20.58 H ATOM 4152 HA ALA E 48 14.369 12.676 2.592 1.00 21.60 H ATOM 4153 HB1 ALA E 48 14.527 12.824 0.236 1.00 25.20 H ATOM 4154 HB2 ALA E 48 13.610 11.611 0.635 1.00 25.20 H ATOM 4155 HB3 ALA E 48 12.964 12.953 0.130 1.00 25.20 H ATOM 4156 N GLU E 49 12.832 15.403 1.981 1.00 18.56 N ANISOU 4156 N GLU E 49 2628 2172 2252 -294 -137 472 N ATOM 4157 CA GLU E 49 12.990 16.859 2.009 1.00 21.53 C ANISOU 4157 CA GLU E 49 2899 2539 2742 -180 -163 471 C ATOM 4158 C GLU E 49 13.589 17.339 3.337 1.00 17.96 C ANISOU 4158 C GLU E 49 2547 1949 2328 -114 -160 222 C ATOM 4159 O GLU E 49 14.455 18.183 3.349 1.00 17.18 O ANISOU 4159 O GLU E 49 2638 1703 2188 -117 -136 392 O ATOM 4160 CB GLU E 49 11.615 17.510 1.807 1.00 28.54 C ANISOU 4160 CB GLU E 49 3662 3482 3699 -68 -274 682 C ATOM 4161 CG GLU E 49 11.733 18.986 1.845 1.00 34.82 C ANISOU 4161 CG GLU E 49 4390 4325 4516 -86 -133 729 C ATOM 4162 CD GLU E 49 10.394 19.736 1.773 1.00 36.63 C ANISOU 4162 CD GLU E 49 4590 4615 4714 -103 77 807 C ATOM 4163 OE1 GLU E 49 10.508 20.959 1.382 1.00 37.22 O ANISOU 4163 OE1 GLU E 49 4697 4715 4731 -156 152 876 O ATOM 4164 OE2 GLU E 49 9.326 19.165 2.268 1.00 37.73 O ANISOU 4164 OE2 GLU E 49 4655 4820 4863 -29 83 691 O ATOM 4165 H GLU E 49 12.021 15.133 1.884 1.00 22.29 H ATOM 4166 HA GLU E 49 13.580 17.141 1.279 1.00 25.85 H ATOM 4167 HB2 GLU E 49 11.259 17.252 0.943 1.00 34.26 H ATOM 4168 HB3 GLU E 49 11.018 17.231 2.518 1.00 34.26 H ATOM 4169 HG2 GLU E 49 12.168 19.241 2.674 1.00 41.80 H ATOM 4170 HG3 GLU E 49 12.272 19.274 1.092 1.00 41.80 H ATOM 4171 N ASP E 50 13.159 16.766 4.446 1.00 15.71 N ANISOU 4171 N ASP E 50 2129 1731 2110 -244 -157 64 N ATOM 4172 CA ASP E 50 13.698 17.164 5.744 1.00 14.97 C ANISOU 4172 CA ASP E 50 1994 1699 1996 -234 -129 -45 C ATOM 4173 C ASP E 50 15.163 16.785 5.856 1.00 13.68 C ANISOU 4173 C ASP E 50 1965 1325 1909 -280 5 -164 C ATOM 4174 O ASP E 50 15.999 17.564 6.315 1.00 13.45 O ANISOU 4174 O ASP E 50 1982 1188 1940 -179 -11 -34 O ATOM 4175 CB ASP E 50 12.922 16.474 6.864 1.00 16.10 C ANISOU 4175 CB ASP E 50 2026 1966 2127 -205 -33 -81 C ATOM 4176 CG ASP E 50 11.496 16.951 7.074 1.00 17.95 C ANISOU 4176 CG ASP E 50 2184 2287 2349 -42 -142 -100 C ATOM 4177 OD1 ASP E 50 11.109 17.980 6.565 1.00 19.59 O ANISOU 4177 OD1 ASP E 50 2250 2403 2791 248 -213 69 O ATOM 4178 OD2 ASP E 50 10.753 16.220 7.730 1.00 18.61 O ANISOU 4178 OD2 ASP E 50 2055 2685 2330 204 89 -250 O ATOM 4179 H ASP E 50 12.561 16.149 4.482 1.00 18.87 H ATOM 4180 HA ASP E 50 13.614 18.134 5.854 1.00 17.98 H ATOM 4181 HB2 ASP E 50 12.884 15.524 6.670 1.00 19.34 H ATOM 4182 HB3 ASP E 50 13.399 16.613 7.697 1.00 19.34 H ATOM 4183 N CYS E 51 15.500 15.577 5.380 1.00 13.62 N ANISOU 4183 N CYS E 51 1879 1413 1884 -335 -100 -55 N ATOM 4184 CA CYS E 51 16.869 15.098 5.365 1.00 14.42 C ANISOU 4184 CA CYS E 51 1968 1506 2005 -96 21 -130 C ATOM 4185 C CYS E 51 17.755 15.965 4.483 1.00 15.49 C ANISOU 4185 C CYS E 51 2131 1579 2174 -91 91 13 C ATOM 4186 O CYS E 51 18.848 16.352 4.871 1.00 15.96 O ANISOU 4186 O CYS E 51 2255 1546 2264 -238 165 276 O ATOM 4187 CB CYS E 51 16.895 13.654 4.889 1.00 15.76 C ANISOU 4187 CB CYS E 51 2129 1657 2201 -108 129 -13 C ATOM 4188 SG CYS E 51 18.499 12.924 4.852 1.00 17.74 S ANISOU 4188 SG CYS E 51 2493 1611 2637 46 341 81 S ATOM 4189 H CYS E 51 14.935 15.015 5.056 1.00 16.36 H ATOM 4190 HA CYS E 51 17.228 15.125 6.277 1.00 17.32 H ATOM 4191 HB2 CYS E 51 16.343 13.121 5.483 1.00 18.92 H ATOM 4192 HB3 CYS E 51 16.534 13.618 3.989 1.00 18.92 H ATOM 4193 N MET E 52 17.270 16.348 3.305 1.00 16.41 N ANISOU 4193 N MET E 52 2115 1818 2301 -421 128 91 N ATOM 4194 CA MET E 52 18.066 17.160 2.388 1.00 18.91 C ANISOU 4194 CA MET E 52 2490 2085 2611 -502 249 177 C ATOM 4195 C MET E 52 18.225 18.547 2.904 1.00 17.68 C ANISOU 4195 C MET E 52 2466 1744 2506 -288 470 236 C ATOM 4196 O MET E 52 19.291 19.126 2.749 1.00 18.17 O ANISOU 4196 O MET E 52 2612 1584 2706 -177 540 143 O ATOM 4197 CB MET E 52 17.345 17.210 1.015 1.00 24.53 C ANISOU 4197 CB MET E 52 3204 2922 3196 -603 90 197 C ATOM 4198 CG MET E 52 17.166 15.870 0.289 1.00 31.61 C ANISOU 4198 CG MET E 52 4050 4032 3928 -567 -129 69 C ATOM 4199 SD MET E 52 16.336 16.157 -1.348 1.00 36.49 S ANISOU 4199 SD MET E 52 4802 4887 4177 -446 -240 -44 S ATOM 4200 CE MET E 52 14.611 16.421 -0.971 1.00 39.39 C ANISOU 4200 CE MET E 52 4999 5009 4958 -458 -351 -56 C ATOM 4201 H MET E 52 16.485 16.151 3.013 1.00 19.70 H ATOM 4202 HA MET E 52 18.947 16.750 2.265 1.00 22.71 H ATOM 4203 HB2 MET E 52 16.461 17.584 1.150 1.00 29.46 H ATOM 4204 HB3 MET E 52 17.853 17.790 0.427 1.00 29.46 H ATOM 4205 HG2 MET E 52 18.034 15.467 0.131 1.00 37.95 H ATOM 4206 HG3 MET E 52 16.607 15.283 0.822 1.00 37.95 H ATOM 4207 HE1 MET E 52 14.133 16.575 -1.789 1.00 47.28 H ATOM 4208 HE2 MET E 52 14.266 15.641 -0.531 1.00 47.28 H ATOM 4209 HE3 MET E 52 14.531 17.185 -0.395 1.00 47.28 H ATOM 4210 N ARG E 53 17.207 19.068 3.552 1.00 17.05 N ANISOU 4210 N ARG E 53 2411 1686 2381 -273 336 136 N ATOM 4211 CA ARG E 53 17.316 20.420 4.150 1.00 18.15 C ANISOU 4211 CA ARG E 53 2475 1885 2536 -237 196 106 C ATOM 4212 C ARG E 53 18.420 20.435 5.186 1.00 17.13 C ANISOU 4212 C ARG E 53 2312 1611 2585 -360 187 -48 C ATOM 4213 O ARG E 53 19.228 21.360 5.219 1.00 19.05 O ANISOU 4213 O ARG E 53 2441 1853 2945 -441 169 -88 O ATOM 4214 CB ARG E 53 16.009 20.776 4.751 1.00 20.87 C ANISOU 4214 CB ARG E 53 2754 2354 2820 -65 174 195 C ATOM 4215 CG ARG E 53 16.093 22.120 5.430 1.00 25.39 C ANISOU 4215 CG ARG E 53 3262 3033 3352 142 231 83 C ATOM 4216 CD ARG E 53 14.760 22.550 6.023 1.00 31.21 C ANISOU 4216 CD ARG E 53 3973 3818 4069 276 410 -46 C ATOM 4217 NE ARG E 53 13.747 22.761 4.987 1.00 38.26 N ANISOU 4217 NE ARG E 53 4863 4727 4945 253 486 -206 N ATOM 4218 CZ ARG E 53 12.653 22.020 4.822 1.00 46.06 C ANISOU 4218 CZ ARG E 53 5840 5778 5882 151 437 -263 C ATOM 4219 NH1 ARG E 53 12.422 20.957 5.589 1.00 50.66 N ANISOU 4219 NH1 ARG E 53 6385 6340 6523 27 422 -335 N ATOM 4220 NH2 ARG E 53 11.803 22.350 3.874 1.00 51.82 N ANISOU 4220 NH2 ARG E 53 6534 6501 6655 131 379 -262 N ATOM 4221 H ARG E 53 16.447 18.683 3.668 1.00 20.47 H ATOM 4222 HA ARG E 53 17.530 21.075 3.453 1.00 21.79 H ATOM 4223 HB2 ARG E 53 15.335 20.825 4.055 1.00 25.06 H ATOM 4224 HB3 ARG E 53 15.765 20.111 5.414 1.00 25.06 H ATOM 4225 HG2 ARG E 53 16.742 22.072 6.149 1.00 30.48 H ATOM 4226 HG3 ARG E 53 16.363 22.787 4.780 1.00 30.48 H ATOM 4227 HD2 ARG E 53 14.440 21.859 6.624 1.00 37.47 H ATOM 4228 HD3 ARG E 53 14.879 23.383 6.505 1.00 37.47 H ATOM 4229 HE ARG E 53 13.883 23.499 4.372 1.00 45.92 H ATOM 4230 HH11 ARG E 53 12.974 20.750 6.215 1.00 60.81 H ATOM 4231 HH12 ARG E 53 11.714 20.484 5.465 1.00 60.81 H ATOM 4232 HH21 ARG E 53 11.961 23.030 3.372 1.00 62.20 H ATOM 4233 HH22 ARG E 53 11.102 21.870 3.739 1.00 62.20 H ATOM 4234 N THR E 54 18.456 19.430 6.061 1.00 16.11 N ANISOU 4234 N THR E 54 2126 1642 2354 -278 189 -138 N ATOM 4235 CA THR E 54 19.398 19.454 7.148 1.00 16.89 C ANISOU 4235 CA THR E 54 2097 1877 2445 -152 245 -234 C ATOM 4236 C THR E 54 20.790 19.004 6.742 1.00 17.52 C ANISOU 4236 C THR E 54 2108 1866 2683 -244 119 -308 C ATOM 4237 O THR E 54 21.776 19.609 7.163 1.00 18.36 O ANISOU 4237 O THR E 54 2101 1966 2909 -93 -17 -439 O ATOM 4238 CB THR E 54 18.850 18.576 8.307 1.00 18.19 C ANISOU 4238 CB THR E 54 2242 2184 2484 -18 306 -273 C ATOM 4239 OG1 THR E 54 17.593 19.096 8.754 1.00 18.40 O ANISOU 4239 OG1 THR E 54 2278 2195 2518 141 403 -192 O ATOM 4240 CG2 THR E 54 19.823 18.503 9.465 1.00 19.96 C ANISOU 4240 CG2 THR E 54 2509 2454 2621 25 156 -425 C ATOM 4241 H THR E 54 17.948 18.737 6.039 1.00 19.35 H ATOM 4242 HA THR E 54 19.469 20.374 7.480 1.00 20.29 H ATOM 4243 HB THR E 54 18.715 17.674 7.977 1.00 21.84 H ATOM 4244 HG1 THR E 54 17.687 19.865 9.021 1.00 22.09 H ATOM 4245 HG21 THR E 54 19.459 17.956 10.164 1.00 23.97 H ATOM 4246 HG22 THR E 54 20.654 18.123 9.171 1.00 23.97 H ATOM 4247 HG23 THR E 54 19.987 19.384 9.811 1.00 23.97 H ATOM 4248 N CYS E 55 20.821 17.946 5.931 1.00 17.59 N ANISOU 4248 N CYS E 55 2168 1919 2597 -187 230 -398 N ATOM 4249 CA CYS E 55 22.081 17.289 5.608 1.00 19.81 C ANISOU 4249 CA CYS E 55 2429 2231 2867 -362 570 -320 C ATOM 4250 C CYS E 55 22.583 17.409 4.174 1.00 24.38 C ANISOU 4250 C CYS E 55 2900 2778 3586 -413 1049 -333 C ATOM 4251 O CYS E 55 23.713 17.007 3.917 1.00 23.45 O ANISOU 4251 O CYS E 55 2827 2460 3624 -438 1091 -267 O ATOM 4252 CB CYS E 55 21.980 15.772 6.007 1.00 19.22 C ANISOU 4252 CB CYS E 55 2351 2165 2787 -413 491 -174 C ATOM 4253 SG CYS E 55 21.731 15.409 7.705 1.00 17.71 S ANISOU 4253 SG CYS E 55 2047 1726 2955 -128 517 -174 S ATOM 4254 H CYS E 55 20.130 17.594 5.559 1.00 21.13 H ATOM 4255 HA CYS E 55 22.774 17.685 6.178 1.00 23.79 H ATOM 4256 HB2 CYS E 55 21.237 15.382 5.520 1.00 23.08 H ATOM 4257 HB3 CYS E 55 22.803 15.334 5.739 1.00 23.08 H ATOM 4258 N GLY E 56 21.753 17.921 3.299 1.00 33.27 N ANISOU 4258 N GLY E 56 4111 4067 4463 -370 1250 -167 N ATOM 4259 CA GLY E 56 22.186 18.194 1.930 1.00 45.39 C ANISOU 4259 CA GLY E 56 5696 5657 5894 -322 1097 61 C ATOM 4260 C GLY E 56 22.201 16.977 1.034 1.00 55.74 C ANISOU 4260 C GLY E 56 7017 6999 7162 -264 954 249 C ATOM 4261 O GLY E 56 21.279 16.120 1.100 1.00 55.14 O ANISOU 4261 O GLY E 56 6969 6917 7064 -217 919 279 O ATOM 4262 H GLY E 56 20.933 18.123 3.460 1.00 39.94 H ATOM 4263 HA2 GLY E 56 21.593 18.852 1.536 1.00 54.48 H ATOM 4264 HA3 GLY E 56 23.082 18.567 1.949 1.00 54.48 H ATOM 4265 N GLY E 57 23.259 16.888 0.202 1.00 68.01 N ANISOU 4265 N GLY E 57 8554 8526 8760 -316 782 357 N ATOM 4266 CA GLY E 57 24.347 17.882 0.178 1.00 79.36 C ANISOU 4266 CA GLY E 57 9994 9953 10206 -326 578 394 C ATOM 4267 C GLY E 57 25.698 17.409 0.734 1.00 82.46 C ANISOU 4267 C GLY E 57 10432 10410 10489 -347 460 416 C ATOM 4268 O GLY E 57 26.538 16.873 -0.032 1.00 82.61 O ANISOU 4268 O GLY E 57 10496 10455 10437 -343 456 438 O ATOM 4269 H GLY E 57 23.367 16.250 -0.365 1.00 81.62 H ATOM 4270 HA2 GLY E 57 24.488 18.166 -0.739 1.00 95.24 H ATOM 4271 HA3 GLY E 57 24.072 18.657 0.691 1.00 95.24 H ATOM 4272 N ALA E 58 25.910 17.642 2.038 1.00 87.86 N ANISOU 4272 N ALA E 58 11081 11028 11272 -372 325 402 N ATOM 4273 CA ALA E 58 27.065 17.134 2.783 1.00 91.85 C ANISOU 4273 CA ALA E 58 11601 11478 11818 -383 113 397 C ATOM 4274 C ALA E 58 26.631 16.675 4.199 1.00 89.37 C ANISOU 4274 C ALA E 58 11322 11020 11616 -374 23 416 C ATOM 4275 O ALA E 58 27.023 17.203 5.243 1.00 88.20 O ANISOU 4275 O ALA E 58 11183 10754 11576 -371 -110 451 O ATOM 4276 CB ALA E 58 28.147 18.163 2.842 1.00 99.70 C ANISOU 4276 CB ALA E 58 12542 12457 12883 -384 -15 388 C ATOM 4277 H ALA E 58 25.376 18.109 2.525 1.00105.44 H ATOM 4278 HA ALA E 58 27.423 16.352 2.314 1.00110.23 H ATOM 4279 HB1 ALA E 58 28.890 17.806 3.334 1.00119.66 H ATOM 4280 HB2 ALA E 58 28.420 18.380 1.948 1.00119.66 H ATOM 4281 HB3 ALA E 58 27.809 18.947 3.281 1.00119.66 H TER 4282 ALA E 58 HETATM 4283 CA CA A 1 -3.570 -11.831 1.412 1.00 15.57 CA ANISOU 4283 CA CA A 1 2308 1967 1640 217 -350 -14 CA HETATM 4284 O HOH A 2 14.995 -5.350 17.859 1.00 11.08 O ANISOU 4284 O HOH A 2 1242 1170 1797 -34 163 58 O HETATM 4285 O HOH A 4 11.482 -13.858 21.141 1.00 10.42 O ANISOU 4285 O HOH A 4 1246 1131 1581 149 123 89 O HETATM 4286 O HOH A 5 8.215 -13.080 10.051 1.00 11.15 O ANISOU 4286 O HOH A 5 1555 1285 1399 138 133 -81 O HETATM 4287 O HOH A 6 6.036 -2.680 27.851 1.00 10.64 O ANISOU 4287 O HOH A 6 1273 1510 1259 157 83 31 O HETATM 4288 O HOH A 7 14.974 -15.017 21.604 1.00 14.63 O ANISOU 4288 O HOH A 7 2446 1459 1654 -298 32 51 O HETATM 4289 O HOH A 8 10.741 -12.690 31.660 1.00 11.48 O ANISOU 4289 O HOH A 8 1417 1359 1587 241 -96 234 O HETATM 4290 O HOH A 9 2.972 -17.203 36.182 1.00 11.34 O ANISOU 4290 O HOH A 9 1165 1420 1724 -55 241 224 O HETATM 4291 O HOH A 10 3.307 -9.649 14.627 1.00 10.33 O ANISOU 4291 O HOH A 10 1395 1109 1421 -50 107 -177 O HETATM 4292 O HOH A 11 -0.794 -8.255 20.359 1.00 12.91 O ANISOU 4292 O HOH A 11 1498 1472 1935 -493 499 -451 O HETATM 4293 O HOH A 12 18.389 -10.133 19.722 1.00 11.59 O ANISOU 4293 O HOH A 12 1389 1401 1612 0 18 -45 O HETATM 4294 O HOH A 13 3.709 -8.694 12.000 1.00 11.00 O ANISOU 4294 O HOH A 13 1367 1195 1617 64 0 -104 O HETATM 4295 O HOH A 14 -11.972 0.618 37.238 1.00 14.58 O ANISOU 4295 O HOH A 14 1908 1482 2150 -77 312 125 O HETATM 4296 O AHOH A 15 8.368 -2.522 26.380 0.84 9.58 O ANISOU 4296 O AHOH A 15 1106 1142 1393 -55 78 5 O HETATM 4297 O BHOH A 15 7.361 -4.025 26.229 0.16 6.32 O ANISOU 4297 O BHOH A 15 735 523 1145 -350 -215 -2 O HETATM 4298 O HOH A 35 15.619 -5.821 11.006 1.00 20.23 O ANISOU 4298 O HOH A 35 2785 2314 2589 -428 1039 -746 O HETATM 4299 O HOH A 68 -6.575 -2.499 37.906 1.00 19.63 O ANISOU 4299 O HOH A 68 2796 2263 2399 -38 335 -94 O HETATM 4300 O HOH A 131 -3.197 7.685 22.230 1.00 29.73 O ANISOU 4300 O HOH A 131 4321 1610 5365 -13 -444 852 O HETATM 4301 O HOH A 208 -1.453 2.007 37.318 1.00 41.30 O ANISOU 4301 O HOH A 208 5116 5221 5353 398 -11 -701 O HETATM 4302 O HOH A 247 0.570 -11.519 30.313 1.00 9.40 O ANISOU 4302 O HOH A 247 1160 1092 1321 316 49 117 O HETATM 4303 O HOH A 248 -5.080 -19.004 33.296 1.00 13.49 O ANISOU 4303 O HOH A 248 1781 1385 1959 141 262 401 O HETATM 4304 O HOH A 249 -7.586 7.623 12.400 1.00 43.59 O ANISOU 4304 O HOH A 249 5254 4831 6476 -1 -582 -99 O HETATM 4305 O HOH A 250 0.507 -3.205 1.397 1.00 38.12 O ANISOU 4305 O HOH A 250 5608 5514 3361 -599 1070 30 O HETATM 4306 O HOH A 251 0.584 -16.121 18.075 1.00 10.22 O ANISOU 4306 O HOH A 251 1132 1062 1691 -77 83 25 O HETATM 4307 O HOH A 252 -13.015 -8.065 34.570 1.00 50.97 O ANISOU 4307 O HOH A 252 6334 6256 6775 343 166 -148 O HETATM 4308 O HOH A 253 -3.142 0.384 33.397 1.00 14.19 O ANISOU 4308 O HOH A 253 1590 1611 2189 357 412 20 O HETATM 4309 O HOH A 254 24.525 -6.417 29.173 1.00 38.88 O ANISOU 4309 O HOH A 254 3531 5058 6185 -94 759 -292 O HETATM 4310 O HOH A 255 -2.477 -1.810 -0.228 1.00 40.45 O ANISOU 4310 O HOH A 255 6195 5412 3761 632 1549 1264 O HETATM 4311 O HOH A 256 -7.127 -12.059 11.431 1.00 14.26 O ANISOU 4311 O HOH A 256 1694 1952 1770 -366 -408 373 O HETATM 4312 O HOH A 257 -2.531 -4.544 -0.715 1.00 40.21 O ANISOU 4312 O HOH A 257 6542 5978 2758 170 980 189 O HETATM 4313 O HOH A 258 -4.461 -10.820 9.277 1.00 12.73 O ANISOU 4313 O HOH A 258 1655 1522 1658 -62 -133 -153 O HETATM 4314 O HOH A 259 -9.307 7.409 19.463 1.00 52.82 O ANISOU 4314 O HOH A 259 6736 6152 7179 1171 -656 186 O HETATM 4315 O HOH A 260 9.862 -8.542 21.179 1.00 13.34 O ANISOU 4315 O HOH A 260 1735 1576 1759 -235 -79 -32 O HETATM 4316 O HOH A 261 -7.721 -11.612 34.095 1.00 18.38 O ANISOU 4316 O HOH A 261 2968 1541 2473 713 1074 382 O HETATM 4317 O HOH A 262 -1.831 -7.020 3.202 1.00 14.77 O ANISOU 4317 O HOH A 262 2283 1804 1523 265 -98 188 O HETATM 4318 O HOH A 263 6.451 7.987 20.200 1.00 53.45 O ANISOU 4318 O HOH A 263 6582 6823 6902 796 144 356 O HETATM 4319 O HOH A 264 3.742 8.118 14.492 1.00 45.27 O ANISOU 4319 O HOH A 264 5509 5364 6329 -4 -392 7 O HETATM 4320 O HOH A 265 -3.340 -17.135 10.671 1.00 15.32 O ANISOU 4320 O HOH A 265 2139 1507 2173 -122 -4 103 O HETATM 4321 O HOH A 266 -15.671 -0.074 8.041 1.00 34.77 O ANISOU 4321 O HOH A 266 4381 4821 4009 -196 -702 1883 O HETATM 4322 O HOH A 267 9.604 -22.860 16.467 1.00 15.67 O ANISOU 4322 O HOH A 267 1961 1676 2315 373 145 -296 O HETATM 4323 O HOH A 268 11.438 -17.463 10.443 1.00 16.15 O ANISOU 4323 O HOH A 268 2777 1260 2100 150 -308 -32 O HETATM 4324 O HOH A 269 -9.466 1.241 34.792 1.00 14.08 O ANISOU 4324 O HOH A 269 1577 2079 1693 -110 140 -299 O HETATM 4325 O HOH A 270 12.788 -14.694 38.406 1.00 17.12 O ANISOU 4325 O HOH A 270 2278 2220 2008 -86 -108 221 O HETATM 4326 O HOH A 271 2.694 -3.197 33.881 1.00 17.88 O ANISOU 4326 O HOH A 271 2282 1976 2535 445 417 248 O HETATM 4327 O HOH A 272 21.862 -2.499 30.181 1.00 20.42 O ANISOU 4327 O HOH A 272 2631 2976 2153 -389 85 162 O HETATM 4328 O HOH A 273 -6.401 -15.809 9.378 1.00 21.01 O ANISOU 4328 O HOH A 273 2133 2677 3172 556 383 395 O HETATM 4329 O HOH A 274 -5.573 -5.554 35.094 1.00 18.26 O ANISOU 4329 O HOH A 274 2427 2406 2105 620 -309 -116 O HETATM 4330 O HOH A 275 -4.904 -8.204 35.593 1.00 18.98 O ANISOU 4330 O HOH A 275 2323 2486 2402 379 776 507 O HETATM 4331 O HOH A 276 13.784 -21.594 10.468 1.00 24.43 O ANISOU 4331 O HOH A 276 2100 4232 2952 635 161 -1665 O HETATM 4332 O HOH A 277 16.474 -5.275 33.782 1.00 15.31 O ANISOU 4332 O HOH A 277 1960 1734 2126 -5 -119 155 O HETATM 4333 O HOH A 278 13.924 0.256 29.718 1.00 20.65 O ANISOU 4333 O HOH A 278 2370 1524 3951 -703 -1277 790 O HETATM 4334 O HOH A 279 11.359 -22.762 14.388 1.00 20.72 O ANISOU 4334 O HOH A 279 2724 2244 2903 -17 838 -136 O HETATM 4335 O HOH A 280 12.675 -23.198 29.178 1.00 36.67 O ANISOU 4335 O HOH A 280 5079 4702 4153 1124 66 1821 O HETATM 4336 O HOH A 281 -0.852 -24.016 14.089 1.00 49.05 O ANISOU 4336 O HOH A 281 6541 5729 6365 46 -133 812 O HETATM 4337 O AHOH A 282 -3.913 1.430 36.832 0.64 34.30 O ANISOU 4337 O AHOH A 282 3781 3957 5296 -32 276 -102 O HETATM 4338 O BHOH A 282 -3.559 2.966 37.799 0.36 16.14 O ANISOU 4338 O BHOH A 282 2727 1202 2204 530 876 -61 O HETATM 4339 O AHOH A 283 -2.385 -17.006 8.140 0.74 13.47 O ANISOU 4339 O AHOH A 283 2087 1391 1640 -47 -275 -137 O HETATM 4340 O BHOH A 283 -1.520 -18.266 8.782 0.26 12.72 O ANISOU 4340 O BHOH A 283 1455 1443 1933 218 -9 -291 O HETATM 4341 O HOH A 284 -4.256 -14.258 10.141 1.00 16.93 O ANISOU 4341 O HOH A 284 2324 2145 1965 506 -176 225 O HETATM 4342 O HOH A 285 7.440 -18.020 36.632 1.00 20.70 O ANISOU 4342 O HOH A 285 1630 3821 2412 -91 38 -976 O HETATM 4343 O HOH A 286 11.374 -23.309 18.631 1.00 18.52 O ANISOU 4343 O HOH A 286 2151 2226 2660 539 136 -407 O HETATM 4344 O HOH A 287 0.325 -23.101 19.777 1.00 46.35 O ANISOU 4344 O HOH A 287 6121 5396 6092 163 466 1130 O HETATM 4345 O HOH A 288 9.388 4.142 32.872 1.00 22.25 O ANISOU 4345 O HOH A 288 2537 3732 2183 -1168 457 -1018 O HETATM 4346 O HOH A 289 -10.637 5.984 26.866 1.00 29.84 O ANISOU 4346 O HOH A 289 3285 2936 5115 -94 -1963 702 O HETATM 4347 O AHOH A 290 -11.810 -5.385 34.435 0.58 14.07 O ANISOU 4347 O AHOH A 290 1819 1240 2288 -239 83 2 O HETATM 4348 O BHOH A 290 -12.121 -4.033 34.857 0.42 16.29 O ANISOU 4348 O BHOH A 290 1872 1100 3217 60 502 -654 O HETATM 4349 O HOH A 291 -10.318 -11.476 33.235 1.00 29.05 O ANISOU 4349 O HOH A 291 2359 2878 5802 -665 1424 840 O HETATM 4350 O HOH A 292 -13.004 0.737 7.055 1.00 23.59 O ANISOU 4350 O HOH A 292 2602 2756 3607 302 -1384 487 O HETATM 4351 O HOH A 293 -5.106 6.967 27.005 1.00 33.45 O ANISOU 4351 O HOH A 293 4937 3984 3790 -869 -274 -408 O HETATM 4352 O HOH A 294 17.420 -5.178 14.623 1.00 23.08 O ANISOU 4352 O HOH A 294 2148 2947 3675 255 -534 -1018 O HETATM 4353 O HOH A 295 17.239 1.213 35.503 1.00 14.23 O ANISOU 4353 O HOH A 295 1465 1851 2092 -469 -31 -544 O HETATM 4354 O HOH A 296 15.098 -17.217 9.830 1.00 18.87 O ANISOU 4354 O HOH A 296 3890 1698 1583 336 527 -220 O HETATM 4355 O HOH A 297 -16.287 -0.432 22.473 1.00 29.35 O ANISOU 4355 O HOH A 297 2608 4145 4398 653 788 -112 O HETATM 4356 O AHOH A 298 3.590 -23.379 33.757 0.33 11.02 O ANISOU 4356 O AHOH A 298 1501 957 1730 -575 165 198 O HETATM 4357 O BHOH A 298 2.215 -23.435 33.894 0.67 21.53 O ANISOU 4357 O BHOH A 298 2055 2069 4056 -905 133 1031 O HETATM 4358 O AHOH A 299 2.441 -24.495 31.431 0.44 16.59 O ANISOU 4358 O AHOH A 299 2203 1698 2402 209 -614 -488 O HETATM 4359 O BHOH A 299 1.872 -24.409 30.239 0.56 14.20 O ANISOU 4359 O BHOH A 299 2054 1366 1975 60 -112 41 O HETATM 4360 O HOH A 300 -5.316 8.741 18.197 1.00 33.81 O ANISOU 4360 O HOH A 300 4075 3453 5318 116 951 936 O HETATM 4361 O HOH A 301 -17.749 -3.408 27.184 1.00 37.51 O ANISOU 4361 O HOH A 301 3921 4914 5417 -517 -892 -202 O HETATM 4362 O HOH A 302 -0.475 -5.568 5.214 1.00 16.23 O ANISOU 4362 O HOH A 302 2150 2160 1857 38 -87 392 O HETATM 4363 O HOH A 303 17.100 -13.481 20.695 1.00 16.72 O ANISOU 4363 O HOH A 303 2835 1816 1702 -541 190 -5 O HETATM 4364 O HOH A 304 -10.629 -11.607 23.904 1.00 19.50 O ANISOU 4364 O HOH A 304 2094 2541 2776 936 847 986 O HETATM 4365 O HOH A 305 -6.229 -11.277 38.024 1.00 32.21 O ANISOU 4365 O HOH A 305 2701 4331 5207 -548 -336 258 O HETATM 4366 O HOH A 306 -16.187 -5.290 20.310 1.00 21.81 O ANISOU 4366 O HOH A 306 2304 2421 3564 362 -343 444 O HETATM 4367 O HOH A 307 18.376 -10.499 37.369 1.00 20.26 O ANISOU 4367 O HOH A 307 2916 2274 2509 -313 -873 -22 O HETATM 4368 O HOH A 308 -3.612 -9.505 1.009 1.00 17.55 O ANISOU 4368 O HOH A 308 2601 2180 1888 93 -447 280 O HETATM 4369 O HOH A 309 -6.520 5.426 28.790 1.00 15.41 O ANISOU 4369 O HOH A 309 1684 1848 2322 246 -139 47 O HETATM 4370 O HOH A 310 15.151 -20.589 26.156 1.00 25.10 O ANISOU 4370 O HOH A 310 2235 2640 4661 92 -287 1697 O HETATM 4371 O HOH A 311 3.776 -11.450 36.555 1.00 31.50 O ANISOU 4371 O HOH A 311 2755 4900 4315 -841 -203 705 O HETATM 4372 O HOH A 312 11.726 6.984 21.640 1.00 22.07 O ANISOU 4372 O HOH A 312 3549 2139 2699 430 1629 197 O HETATM 4373 O HOH A 313 1.995 10.590 14.168 1.00 53.24 O ANISOU 4373 O HOH A 313 6603 6630 6993 -249 -130 84 O HETATM 4374 O HOH A 314 -11.030 -12.184 26.509 1.00 19.62 O ANISOU 4374 O HOH A 314 1439 2909 3106 189 154 -233 O HETATM 4375 O AHOH A 315 15.821 0.129 27.349 0.52 24.93 O ANISOU 4375 O AHOH A 315 2025 2833 4614 847 770 237 O HETATM 4376 O BHOH A 315 15.346 2.268 27.376 0.48 24.16 O ANISOU 4376 O BHOH A 315 1469 3104 4605 1285 62 674 O HETATM 4377 O HOH A 316 -9.679 -12.186 31.094 1.00 32.26 O ANISOU 4377 O HOH A 316 3902 3994 4359 276 1127 967 O HETATM 4378 O HOH A 317 24.684 -12.920 18.342 1.00 20.35 O ANISOU 4378 O HOH A 317 1738 2912 3081 66 526 137 O HETATM 4379 O HOH A 318 15.255 -23.319 25.356 1.00 34.63 O ANISOU 4379 O HOH A 318 4502 4007 4649 792 467 850 O HETATM 4380 O HOH A 319 9.943 -15.383 36.761 1.00 27.03 O ANISOU 4380 O HOH A 319 2451 4241 3580 882 1556 1123 O HETATM 4381 O HOH A 320 5.141 -23.814 36.435 1.00 44.84 O ANISOU 4381 O HOH A 320 6507 5153 5378 169 428 1068 O HETATM 4382 O HOH A 321 -5.597 -1.029 35.787 1.00 16.97 O ANISOU 4382 O HOH A 321 2487 1583 2380 235 580 -354 O HETATM 4383 O HOH A 322 8.190 -23.052 6.992 1.00 18.46 O ANISOU 4383 O HOH A 322 2161 2426 2425 518 -101 -881 O HETATM 4384 O HOH A 323 -1.952 -21.755 22.995 1.00 23.45 O ANISOU 4384 O HOH A 323 4326 1907 2677 150 623 -291 O HETATM 4385 O HOH A 324 14.346 -21.495 28.584 1.00 33.91 O ANISOU 4385 O HOH A 324 4719 4156 4009 1953 475 1124 O HETATM 4386 O HOH A 325 -7.393 5.130 10.814 1.00 18.50 O ANISOU 4386 O HOH A 325 1979 1973 3076 307 89 685 O HETATM 4387 O HOH A 326 -7.011 -9.839 35.965 1.00 19.94 O ANISOU 4387 O HOH A 326 2314 2479 2785 -100 765 269 O HETATM 4388 O HOH A 327 15.327 -3.794 35.340 1.00 37.48 O ANISOU 4388 O HOH A 327 4549 4972 4721 -646 -1649 1350 O HETATM 4389 O HOH A 328 3.750 -13.955 -2.736 1.00 34.62 O ANISOU 4389 O HOH A 328 4605 4655 3894 686 1293 -112 O HETATM 4390 O HOH A 329 19.150 -21.548 17.314 1.00 47.20 O ANISOU 4390 O HOH A 329 6077 5060 6798 -193 -211 537 O HETATM 4391 O HOH A 330 -19.025 4.399 26.007 1.00 40.73 O ANISOU 4391 O HOH A 330 4871 4866 5738 134 -368 138 O HETATM 4392 O HOH A 331 -1.730 5.591 7.586 1.00 40.30 O ANISOU 4392 O HOH A 331 5155 4931 5224 825 1268 1072 O HETATM 4393 O HOH A 332 21.454 -3.735 27.879 1.00 24.07 O ANISOU 4393 O HOH A 332 2903 3661 2581 892 -276 -224 O HETATM 4394 O HOH A 333 22.359 -6.092 27.399 1.00 27.57 O ANISOU 4394 O HOH A 333 2524 2767 5184 -260 905 462 O HETATM 4395 O HOH A 334 -8.459 -17.771 23.130 1.00 19.97 O ANISOU 4395 O HOH A 334 2816 1745 3026 -254 409 79 O HETATM 4396 O HOH A 335 6.626 -8.049 34.171 1.00 19.84 O ANISOU 4396 O HOH A 335 2399 2099 3040 121 696 501 O HETATM 4397 O HOH A 336 -7.736 5.328 8.011 1.00 36.29 O ANISOU 4397 O HOH A 336 4867 5117 3804 -1146 -893 626 O HETATM 4398 O HOH A 337 8.412 -14.440 1.136 1.00 38.00 O ANISOU 4398 O HOH A 337 5058 5717 3664 557 676 -900 O HETATM 4399 O HOH A 338 10.626 3.262 35.169 1.00 36.84 O ANISOU 4399 O HOH A 338 4213 5166 4617 -98 38 493 O HETATM 4400 O AHOH A 339 15.592 2.167 30.578 0.59 13.67 O ANISOU 4400 O AHOH A 339 1981 1020 2192 -470 -903 -251 O HETATM 4401 O BHOH A 339 14.971 1.693 31.858 0.41 21.99 O ANISOU 4401 O BHOH A 339 1980 3175 3202 169 -462 -977 O HETATM 4402 O HOH A 340 -4.059 -20.888 20.865 1.00 37.08 O ANISOU 4402 O HOH A 340 4893 4657 4539 -1826 -582 -506 O HETATM 4403 O HOH A 341 0.629 -21.666 22.281 1.00 38.75 O ANISOU 4403 O HOH A 341 5424 4695 4606 -1103 485 -406 O HETATM 4404 O HOH A 342 -15.444 -4.056 28.488 1.00 22.18 O ANISOU 4404 O HOH A 342 2186 2212 4029 -757 -253 -76 O HETATM 4405 O HOH A 343 -1.147 -23.792 5.189 1.00 38.08 O ANISOU 4405 O HOH A 343 5576 4412 4479 204 -3 -2227 O HETATM 4406 O HOH A 344 19.533 -20.126 31.347 1.00 38.04 O ANISOU 4406 O HOH A 344 5725 4281 4447 949 -1606 1023 O HETATM 4407 O HOH A 345 1.067 -23.241 12.344 1.00 28.36 O ANISOU 4407 O HOH A 345 3899 3506 3369 -1474 -649 403 O HETATM 4408 O HOH A 346 -9.169 4.555 28.575 1.00 17.62 O ANISOU 4408 O HOH A 346 2225 1742 2726 94 -415 219 O HETATM 4409 O HOH A 347 -12.264 -5.898 3.171 1.00 25.20 O ANISOU 4409 O HOH A 347 3833 2585 3155 -86 -2039 425 O HETATM 4410 O HOH A 348 -15.543 -5.044 31.378 1.00 45.65 O ANISOU 4410 O HOH A 348 5772 5749 5824 -39 1385 -479 O HETATM 4411 O HOH A 349 22.523 -5.622 24.833 1.00 32.93 O ANISOU 4411 O HOH A 349 4159 4203 4152 529 544 -1072 O HETATM 4412 O HOH A 350 20.795 -17.981 13.135 1.00 39.42 O ANISOU 4412 O HOH A 350 4258 5088 5630 -92 1595 -584 O HETATM 4413 O HOH A 351 2.484 -25.814 12.037 1.00 39.43 O ANISOU 4413 O HOH A 351 5410 3720 5851 -527 54 -876 O HETATM 4414 O AHOH A 352 -4.435 -2.169 33.769 0.52 13.97 O ANISOU 4414 O AHOH A 352 1966 1516 1825 526 120 77 O HETATM 4415 O BHOH A 352 -5.032 -3.158 33.926 0.48 12.69 O ANISOU 4415 O BHOH A 352 1271 1960 1590 519 -40 -453 O HETATM 4416 O HOH A 353 -14.403 -18.941 15.316 1.00 39.62 O ANISOU 4416 O HOH A 353 4577 4419 6059 -1202 -423 -600 O HETATM 4417 O HOH A 354 3.935 6.167 20.169 1.00 24.81 O ANISOU 4417 O HOH A 354 3433 1778 4216 -516 -1607 662 O HETATM 4418 O HOH A 355 -17.464 3.271 30.418 1.00 21.55 O ANISOU 4418 O HOH A 355 2153 3407 2629 826 582 629 O HETATM 4419 O HOH A 356 6.727 -8.541 5.655 1.00 23.29 O ANISOU 4419 O HOH A 356 2488 4210 2151 279 607 722 O HETATM 4420 O HOH A 357 19.056 -20.996 24.031 1.00 26.98 O ANISOU 4420 O HOH A 357 2892 1829 5530 -93 413 70 O HETATM 4421 O HOH A 358 -16.274 4.532 16.666 1.00 35.78 O ANISOU 4421 O HOH A 358 4161 4432 5000 715 1 208 O HETATM 4422 O HOH A 359 -12.811 -13.197 6.475 1.00 20.69 O ANISOU 4422 O HOH A 359 2580 2642 2641 -352 -10 -54 O HETATM 4423 O HOH A 360 7.502 -12.285 34.112 1.00 17.09 O ANISOU 4423 O HOH A 360 2218 2144 2133 367 108 -254 O HETATM 4424 O HOH A 361 7.563 -22.079 36.058 1.00 22.90 O ANISOU 4424 O HOH A 361 2285 4047 2370 1156 215 817 O HETATM 4425 O HOH A 362 -7.839 8.072 17.745 1.00 31.45 O ANISOU 4425 O HOH A 362 3858 2221 5870 910 -2045 -495 O HETATM 4426 O HOH A 363 4.970 -13.971 33.584 1.00 24.00 O ANISOU 4426 O HOH A 363 3547 1255 4317 -250 -369 125 O HETATM 4427 O HOH A 364 19.179 -0.991 37.308 1.00 22.80 O ANISOU 4427 O HOH A 364 2296 3633 2732 -1474 58 -821 O HETATM 4428 O HOH A 365 18.294 -18.852 12.799 1.00 20.80 O ANISOU 4428 O HOH A 365 2129 3260 2513 686 335 -789 O HETATM 4429 O HOH A 366 4.111 -24.970 28.250 1.00 24.56 O ANISOU 4429 O HOH A 366 4170 1945 3214 -1204 -378 598 O HETATM 4430 O HOH A 367 17.625 2.424 28.645 1.00 21.22 O ANISOU 4430 O HOH A 367 2763 2172 3126 278 -250 -160 O HETATM 4431 O HOH A 368 -6.746 -14.396 3.093 1.00 26.18 O ANISOU 4431 O HOH A 368 3768 3225 2953 -480 105 -818 O HETATM 4432 O HOH A 369 20.881 -9.592 37.261 1.00 21.38 O ANISOU 4432 O HOH A 369 2207 2020 3898 189 -500 254 O HETATM 4433 O HOH A 370 6.471 -23.885 33.024 1.00 24.57 O ANISOU 4433 O HOH A 370 2455 2946 3936 -488 -26 676 O HETATM 4434 O HOH A 371 4.371 -7.618 36.577 1.00 26.58 O ANISOU 4434 O HOH A 371 3103 3720 3277 720 -381 1016 O HETATM 4435 O HOH A 372 17.663 -19.927 26.461 1.00 28.70 O ANISOU 4435 O HOH A 372 2697 2583 5625 -476 -1256 1878 O HETATM 4436 O HOH A 373 -16.601 -4.778 8.853 1.00 26.19 O ANISOU 4436 O HOH A 373 3253 3876 2821 172 -913 178 O HETATM 4437 O HOH A 374 -15.336 -6.734 7.296 1.00 28.79 O ANISOU 4437 O HOH A 374 3648 3282 4009 152 -1347 404 O HETATM 4438 O HOH A 375 7.550 5.412 20.380 1.00 23.24 O ANISOU 4438 O HOH A 375 4277 2386 2166 -956 527 -78 O HETATM 4439 O HOH A 376 1.022 -22.522 24.832 1.00 24.90 O ANISOU 4439 O HOH A 376 1796 2584 5082 406 88 -1421 O HETATM 4440 O HOH A 377 8.870 -0.878 36.561 1.00 28.00 O ANISOU 4440 O HOH A 377 5346 2838 2454 -1129 549 -801 O HETATM 4441 O HOH A 378 -14.145 -14.966 18.471 1.00 23.19 O ANISOU 4441 O HOH A 378 2049 3630 3132 -770 -111 -90 O HETATM 4442 O HOH A 379 17.533 -16.558 19.804 1.00 22.05 O ANISOU 4442 O HOH A 379 2456 3346 2578 772 -138 -821 O HETATM 4443 O HOH A 380 19.309 -7.396 14.088 1.00 25.58 O ANISOU 4443 O HOH A 380 2881 4229 2607 32 298 -662 O HETATM 4444 O HOH A 381 0.515 7.581 25.697 1.00 22.36 O ANISOU 4444 O HOH A 381 3148 2146 3202 -483 -313 751 O HETATM 4445 O HOH A 382 18.126 -5.116 36.126 1.00 23.84 O ANISOU 4445 O HOH A 382 4111 2548 2397 -1208 -665 184 O HETATM 4446 O AHOH A 383 17.232 -0.441 24.878 0.64 17.40 O ANISOU 4446 O AHOH A 383 1990 1991 2629 635 416 -324 O HETATM 4447 O BHOH A 383 15.837 -0.476 25.139 0.36 15.85 O ANISOU 4447 O BHOH A 383 1937 2018 2069 349 11 -522 O HETATM 4448 O AHOH A 384 6.103 -0.628 34.865 0.48 16.20 O ANISOU 4448 O AHOH A 384 2263 2222 1671 -390 -127 221 O HETATM 4449 O BHOH A 384 4.868 -0.717 34.491 0.52 20.42 O ANISOU 4449 O BHOH A 384 2607 2536 2614 -751 304 -456 O HETATM 4450 O AHOH A 385 19.297 -15.411 21.563 0.55 18.07 O ANISOU 4450 O AHOH A 385 2354 1824 2686 407 13 40 O HETATM 4451 O BHOH A 385 18.823 -14.293 22.666 0.45 17.63 O ANISOU 4451 O BHOH A 385 1856 2526 2314 770 270 317 O HETATM 4452 O HOH A 386 23.901 -9.492 33.705 1.00 26.56 O ANISOU 4452 O HOH A 386 2575 3625 3890 -377 -1389 993 O HETATM 4453 O HOH A 387 -9.234 -8.195 36.529 1.00 26.64 O ANISOU 4453 O HOH A 387 3583 2545 3993 423 974 1018 O HETATM 4454 O HOH A 388 -2.505 -7.693 -0.704 1.00 32.03 O ANISOU 4454 O HOH A 388 4337 4469 3364 -62 288 806 O HETATM 4455 O HOH A 389 -2.668 -19.975 18.868 1.00 27.25 O ANISOU 4455 O HOH A 389 3667 2710 3977 211 167 328 O HETATM 4456 O HOH A 390 -3.560 -10.312 -5.392 1.00 31.10 O ANISOU 4456 O HOH A 390 4517 5054 2246 205 -368 1008 O HETATM 4457 O HOH A 391 1.012 9.275 12.117 1.00 31.23 O ANISOU 4457 O HOH A 391 4215 2491 5158 -875 137 1338 O HETATM 4458 O HOH A 392 6.170 4.238 7.942 1.00 27.69 O ANISOU 4458 O HOH A 392 3664 3854 3005 -410 -621 442 O HETATM 4459 O HOH A 393 -7.187 -0.396 0.878 1.00 40.62 O ANISOU 4459 O HOH A 393 6020 5647 3767 -795 -1585 819 O HETATM 4460 O HOH A 394 -11.707 -3.987 1.394 1.00 30.58 O ANISOU 4460 O HOH A 394 4672 3844 3103 0 -1232 864 O HETATM 4461 O HOH A 395 -8.913 -5.722 39.336 1.00 29.88 O ANISOU 4461 O HOH A 395 3971 4035 3346 214 733 1216 O HETATM 4462 O HOH A 396 19.442 -15.010 10.519 1.00 31.20 O ANISOU 4462 O HOH A 396 3955 4157 3742 1081 -252 -756 O HETATM 4463 O HOH A 397 17.266 -19.965 29.486 1.00 33.80 O ANISOU 4463 O HOH A 397 4828 3839 4177 -585 -548 -645 O HETATM 4464 O HOH A 398 8.552 -22.151 4.280 1.00 32.21 O ANISOU 4464 O HOH A 398 3453 5002 3782 1583 488 494 O HETATM 4465 O HOH A 399 15.933 -24.302 20.222 1.00 40.00 O ANISOU 4465 O HOH A 399 4540 4698 5961 854 597 117 O HETATM 4466 O HOH A 400 -6.301 -17.150 3.356 1.00 30.63 O ANISOU 4466 O HOH A 400 5456 2948 3234 -182 -112 -359 O HETATM 4467 O HOH A 401 6.878 -15.867 2.712 1.00 31.93 O ANISOU 4467 O HOH A 401 3204 4782 4148 981 295 -1582 O HETATM 4468 O HOH A 402 1.443 1.595 -0.640 1.00 38.19 O ANISOU 4468 O HOH A 402 6696 4484 3331 637 964 1447 O HETATM 4469 O HOH A 403 10.185 -19.684 4.255 1.00 39.24 O ANISOU 4469 O HOH A 403 5571 4803 4536 -186 751 -1777 O HETATM 4470 O HOH A 404 4.383 2.401 34.774 1.00 31.70 O ANISOU 4470 O HOH A 404 4414 5282 2350 1350 -682 -684 O HETATM 4471 O HOH A 405 4.448 2.087 6.925 1.00 36.47 O ANISOU 4471 O HOH A 405 4483 4532 4842 -300 -480 1539 O HETATM 4472 O HOH A 406 -9.338 -17.449 17.712 1.00 31.47 O ANISOU 4472 O HOH A 406 5795 2951 3210 1219 -907 -136 O HETATM 4473 O HOH A 407 17.596 -8.042 11.702 1.00 29.84 O ANISOU 4473 O HOH A 407 2725 3435 5177 -185 -127 -1106 O HETATM 4474 O HOH A 408 -7.309 -19.120 17.884 1.00 35.45 O ANISOU 4474 O HOH A 408 4494 4043 4931 -495 -8 397 O HETATM 4475 O HOH A 409 1.811 -9.088 37.071 1.00 33.03 O ANISOU 4475 O HOH A 409 3587 4928 4034 260 -800 1607 O HETATM 4476 O HOH A 410 10.171 9.907 27.419 1.00 33.96 O ANISOU 4476 O HOH A 410 5067 2752 5084 788 -774 -2 O HETATM 4477 O HOH A 411 8.558 1.538 35.622 1.00 33.33 O ANISOU 4477 O HOH A 411 4797 4427 3442 258 -1211 -27 O HETATM 4478 O HOH A 412 5.213 6.270 32.420 1.00 31.07 O ANISOU 4478 O HOH A 412 3141 5129 3535 -768 -466 -1784 O HETATM 4479 O HOH A 413 1.701 -22.834 5.511 1.00 31.27 O ANISOU 4479 O HOH A 413 4377 3947 3556 -994 188 -1053 O HETATM 4480 O HOH A 414 -12.392 -11.113 1.618 1.00 37.34 O ANISOU 4480 O HOH A 414 5398 4892 3897 -1368 -2330 272 O HETATM 4481 O HOH A 415 -15.569 -10.993 21.141 1.00 34.22 O ANISOU 4481 O HOH A 415 3466 3813 5722 -313 1150 481 O HETATM 4482 O HOH A 416 17.329 8.640 27.614 1.00 41.88 O ANISOU 4482 O HOH A 416 5126 5868 4920 -626 84 93 O HETATM 4483 O AHOH A 417 3.239 -4.612 2.995 0.59 22.34 O ANISOU 4483 O AHOH A 417 3813 2930 1743 622 386 52 O HETATM 4484 O BHOH A 417 1.619 -5.271 2.451 0.41 28.39 O ANISOU 4484 O BHOH A 417 4174 2928 3684 99 394 117 O HETATM 4485 O AHOH A 418 8.569 -15.002 34.115 0.86 29.60 O ANISOU 4485 O AHOH A 418 4269 3998 2980 59 -128 -416 O HETATM 4486 O BHOH A 418 8.946 -15.990 34.389 0.14 20.57 O ANISOU 4486 O BHOH A 418 2256 2200 3362 -21 196 480 O HETATM 4487 O AHOH A 419 21.182 -13.719 30.552 0.56 24.70 O ANISOU 4487 O AHOH A 419 4117 2038 3230 603 -736 -618 O HETATM 4488 O BHOH A 419 21.660 -13.284 29.055 0.44 18.88 O ANISOU 4488 O BHOH A 419 2021 2283 2870 12 832 -734 O HETATM 4489 O HOH A 420 2.382 8.555 27.064 1.00 39.29 O ANISOU 4489 O HOH A 420 4307 3841 6779 115 -808 50 O HETATM 4490 O AHOH A 421 11.139 -4.711 36.813 0.29 18.62 O ANISOU 4490 O AHOH A 421 2256 2565 2255 925 155 737 O HETATM 4491 O BHOH A 421 10.815 -6.432 36.185 0.71 34.00 O ANISOU 4491 O BHOH A 421 4534 4494 3890 853 -1297 -719 O HETATM 4492 O HOH A 422 1.755 -23.551 14.925 1.00 37.55 O ANISOU 4492 O HOH A 422 4376 5577 4313 -2062 198 -835 O HETATM 4493 O HOH A 423 8.090 -25.225 16.575 1.00 36.06 O ANISOU 4493 O HOH A 423 4819 3513 5370 -261 -1620 705 O HETATM 4494 O HOH A 424 4.779 4.298 14.898 1.00 39.25 O ANISOU 4494 O HOH A 424 4875 4449 5590 643 1668 938 O HETATM 4495 O HOH A 425 6.821 9.113 26.260 1.00 32.38 O ANISOU 4495 O HOH A 425 5291 2626 4386 1528 2126 1269 O HETATM 4496 O HOH A 426 -5.583 8.975 15.736 1.00 45.15 O ANISOU 4496 O HOH A 426 5922 5114 6120 -29 248 -164 O HETATM 4497 O HOH A 427 -11.359 -9.651 35.060 1.00 32.89 O ANISOU 4497 O HOH A 427 3944 3728 4826 -239 1078 115 O HETATM 4498 O HOH A 428 26.482 -11.364 24.162 1.00 40.78 O ANISOU 4498 O HOH A 428 3715 5696 6082 -110 15 -5 O HETATM 4499 O HOH A 429 -3.593 3.671 6.946 1.00 42.72 O ANISOU 4499 O HOH A 429 5521 4466 6244 28 933 1242 O HETATM 4500 O HOH A 430 -1.115 1.830 0.122 1.00 32.81 O ANISOU 4500 O HOH A 430 5037 3106 4322 -553 -1227 1496 O HETATM 4501 O HOH A 431 5.927 9.469 29.121 1.00 45.00 O ANISOU 4501 O HOH A 431 5848 5088 6160 325 -386 -1497 O HETATM 4502 O AHOH A 432 22.239 -12.927 6.930 0.46 25.30 O ANISOU 4502 O AHOH A 432 2596 3765 3253 73 414 254 O HETATM 4503 O BHOH A 432 21.861 -12.738 8.643 0.54 32.43 O ANISOU 4503 O BHOH A 432 3182 4809 4329 -431 -446 -288 O HETATM 4504 O HOH A 433 7.050 4.758 33.607 1.00 35.80 O ANISOU 4504 O HOH A 433 3956 4314 5331 818 782 -790 O HETATM 4505 O HOH A 434 2.813 5.871 7.453 1.00 28.27 O ANISOU 4505 O HOH A 434 3533 3868 3339 -326 -486 928 O HETATM 4506 O HOH A 435 3.863 8.749 30.342 1.00 43.48 O ANISOU 4506 O HOH A 435 5616 4719 6184 -139 782 -484 O HETATM 4507 O HOH A 436 4.535 3.123 4.030 1.00 45.26 O ANISOU 4507 O HOH A 436 6236 5039 5923 -214 270 1144 O HETATM 4508 O HOH A 437 -0.644 -1.489 34.725 1.00 43.69 O ANISOU 4508 O HOH A 437 6047 5732 4821 -2 145 -19 O HETATM 4509 O HOH A 438 11.551 -11.425 1.242 1.00 35.75 O ANISOU 4509 O HOH A 438 5242 5669 2674 888 374 -247 O HETATM 4510 O HOH A 439 -16.275 -13.184 19.177 1.00 34.83 O ANISOU 4510 O HOH A 439 3393 5089 4751 218 274 228 O HETATM 4511 O HOH A 440 7.117 7.812 32.495 1.00 36.20 O ANISOU 4511 O HOH A 440 4008 5347 4399 -2079 1552 -2029 O HETATM 4512 O HOH A 441 -6.152 -22.728 14.463 1.00 37.12 O ANISOU 4512 O HOH A 441 5061 3712 5332 -1551 116 136 O HETATM 4513 O HOH A 442 2.423 -23.973 18.047 1.00 34.83 O ANISOU 4513 O HOH A 442 4889 3210 5134 -1450 -455 186 O HETATM 4514 O HOH A 443 -0.983 0.901 34.962 1.00 33.84 O ANISOU 4514 O HOH A 443 3347 5388 4124 5 -1104 -405 O HETATM 4515 O HOH A 444 -8.593 -20.901 11.772 1.00 34.33 O ANISOU 4515 O HOH A 444 2862 4029 6153 -489 1091 729 O HETATM 4516 O HOH A 445 10.211 -24.698 28.175 1.00 31.14 O ANISOU 4516 O HOH A 445 3974 2870 4988 1171 1435 26 O HETATM 4517 O HOH A 446 4.164 -22.946 21.575 1.00 41.59 O ANISOU 4517 O HOH A 446 6225 3999 5579 -848 301 127 O HETATM 4518 O HOH A 447 8.226 -0.678 4.864 1.00 35.22 O ANISOU 4518 O HOH A 447 5217 4259 3907 -145 709 -253 O HETATM 4519 O HOH A 448 -20.024 0.422 26.949 1.00 31.76 O ANISOU 4519 O HOH A 448 3038 4851 4178 -472 -317 454 O HETATM 4520 O HOH A 449 5.882 -24.636 8.250 1.00 34.41 O ANISOU 4520 O HOH A 449 4524 3148 5403 379 -325 -1266 O HETATM 4521 O HOH A 450 7.684 -7.981 36.840 1.00 35.96 O ANISOU 4521 O HOH A 450 4949 4592 4121 -74 -43 130 O HETATM 4522 O HOH A 451 -11.906 -14.498 22.744 1.00 34.87 O ANISOU 4522 O HOH A 451 3596 5483 4169 -1517 -210 1040 O HETATM 4523 O HOH A 452 12.279 -8.399 1.911 1.00 37.73 O ANISOU 4523 O HOH A 452 6018 5493 2826 -171 1520 1367 O HETATM 4524 O HOH A 453 -5.126 -13.562 -6.062 1.00 33.33 O ANISOU 4524 O HOH A 453 4543 4804 3317 -677 123 -760 O HETATM 4525 O HOH A 454 -11.641 -19.048 14.088 1.00 33.33 O ANISOU 4525 O HOH A 454 3652 4062 4949 -1034 -194 -2066 O HETATM 4526 O AHOH A 455 -2.980 1.783 3.877 0.60 32.93 O ANISOU 4526 O AHOH A 455 4608 3961 3944 97 -466 178 O HETATM 4527 O BHOH A 455 -2.553 0.688 2.140 0.40 33.70 O ANISOU 4527 O BHOH A 455 4823 4113 3870 35 -156 501 O HETATM 4528 O HOH E 59 13.645 1.393 17.492 1.00 10.75 O ANISOU 4528 O HOH E 59 1224 1187 1673 78 211 211 O HETATM 4529 O HOH E 60 17.459 6.529 14.369 1.00 12.65 O ANISOU 4529 O HOH E 60 1689 1240 1879 -128 209 207 O HETATM 4530 O HOH E 61 19.483 7.085 12.582 1.00 15.35 O ANISOU 4530 O HOH E 61 1874 1462 2496 258 661 495 O HETATM 4531 O AHOH E 62 10.273 11.813 1.176 0.60 15.72 O ANISOU 4531 O AHOH E 62 2473 1787 1712 -291 -644 80 O HETATM 4532 O BHOH E 62 9.761 12.329 -0.918 0.40 31.78 O ANISOU 4532 O BHOH E 62 4085 3636 4354 302 188 333 O HETATM 4533 O HOH E 63 11.871 14.872 9.816 1.00 18.34 O ANISOU 4533 O HOH E 63 2163 1807 3000 -85 86 -554 O HETATM 4534 O HOH E 75 20.651 0.052 12.907 1.00 28.41 O ANISOU 4534 O HOH E 75 2617 2574 5603 718 1445 -96 O HETATM 4535 O HOH E 87 17.362 -0.440 7.458 1.00 28.42 O ANISOU 4535 O HOH E 87 3298 1795 5706 714 1805 56 O HETATM 4536 O HOH E 93 17.842 21.481 10.289 1.00 22.56 O ANISOU 4536 O HOH E 93 2696 2998 2879 476 703 -507 O HETATM 4537 O HOH E 100 10.503 8.096 17.609 1.00 23.38 O ANISOU 4537 O HOH E 100 3559 2850 2474 1059 563 -307 O HETATM 4538 O HOH E 107 22.305 11.180 17.358 1.00 27.68 O ANISOU 4538 O HOH E 107 3199 3351 3968 -442 -1120 -207 O HETATM 4539 O HOH E 110 26.381 9.476 6.725 1.00 29.55 O ANISOU 4539 O HOH E 110 3755 4764 2711 624 1066 -614 O HETATM 4540 O HOH E 116 19.253 6.065 20.996 1.00 36.94 O ANISOU 4540 O HOH E 116 4124 5065 4846 -751 -385 -324 O HETATM 4541 O HOH E 120 19.802 -0.679 15.483 1.00 26.81 O ANISOU 4541 O HOH E 120 2463 3083 4641 658 518 311 O HETATM 4542 O HOH E 121 14.757 19.454 8.484 1.00 24.63 O ANISOU 4542 O HOH E 121 2767 3027 3566 -384 399 -791 O HETATM 4543 O HOH E 122 10.343 14.539 0.583 1.00 29.88 O ANISOU 4543 O HOH E 122 3710 4548 3093 -1217 -1186 356 O HETATM 4544 O AHOH E 124 17.716 -3.640 16.975 0.52 17.87 O ANISOU 4544 O AHOH E 124 2444 2040 2306 -302 181 -234 O HETATM 4545 O BHOH E 124 17.995 -2.823 15.776 0.48 15.66 O ANISOU 4545 O BHOH E 124 1374 2028 2548 210 11 -68 O HETATM 4546 O HOH E 126 7.170 8.265 10.554 1.00 28.86 O ANISOU 4546 O HOH E 126 2905 3594 4465 -586 -297 577 O HETATM 4547 O HOH E 134 24.586 4.007 -3.492 1.00 29.51 O ANISOU 4547 O HOH E 134 4246 3008 3959 -210 1242 63 O HETATM 4548 O HOH E 135 24.352 1.411 10.961 1.00 26.83 O ANISOU 4548 O HOH E 135 2322 3578 4293 327 -41 140 O HETATM 4549 O HOH E 139 26.930 4.688 -2.369 1.00 32.75 O ANISOU 4549 O HOH E 139 4371 3715 4358 -242 809 -852 O HETATM 4550 O HOH E 143 9.457 7.417 20.074 1.00 25.22 O ANISOU 4550 O HOH E 143 3814 3070 2697 -401 488 -59 O HETATM 4551 O HOH E 145 6.458 -0.347 6.753 1.00 29.82 O ANISOU 4551 O HOH E 145 3875 4071 3383 -853 503 945 O HETATM 4552 O HOH E 147 11.296 14.394 12.493 1.00 30.12 O ANISOU 4552 O HOH E 147 3762 3053 4630 -73 281 -757 O HETATM 4553 O HOH E 149 19.250 7.049 27.494 1.00 31.78 O ANISOU 4553 O HOH E 149 4393 4221 3463 -852 -340 -291 O HETATM 4554 O HOH E 153 27.515 20.136 13.715 1.00 30.60 O ANISOU 4554 O HOH E 153 4297 2984 4347 -1077 -325 -263 O HETATM 4555 O HOH E 159 17.299 15.122 13.846 1.00 31.42 O ANISOU 4555 O HOH E 159 3878 3599 4461 647 355 -1146 O HETATM 4556 O AHOH E 174 12.174 10.739 15.442 0.48 29.20 O ANISOU 4556 O AHOH E 174 3986 3299 3809 178 -30 -355 O HETATM 4557 O BHOH E 174 11.239 9.681 15.710 0.52 23.94 O ANISOU 4557 O BHOH E 174 3829 2541 2724 122 -728 -678 O HETATM 4558 O HOH E 177 11.007 -2.457 4.705 1.00 49.45 O ANISOU 4558 O HOH E 177 6297 6174 6319 -10 -513 34 O HETATM 4559 O AHOH E 179 18.583 2.271 22.150 0.69 31.38 O ANISOU 4559 O AHOH E 179 2492 4410 5023 -302 91 -90 O HETATM 4560 O BHOH E 179 17.851 1.612 23.495 0.31 15.73 O ANISOU 4560 O BHOH E 179 2066 1852 2060 -864 -818 324 O HETATM 4561 O HOH E 180 26.150 3.306 -0.236 1.00 72.13 O ANISOU 4561 O HOH E 180 9176 8801 9430 -424 1046 150 O HETATM 4562 O HOH E 185 15.451 9.319 20.622 1.00 37.73 O ANISOU 4562 O HOH E 185 4249 5151 4936 -1479 2191 -1333 O HETATM 4563 O HOH E 187 20.770 2.639 2.187 1.00 54.51 O ANISOU 4563 O HOH E 187 7467 6365 6881 204 975 -267 O HETATM 4564 O AHOH E 193 7.848 6.076 15.999 0.50 23.98 O ANISOU 4564 O AHOH E 193 2847 3600 2664 935 -564 -89 O HETATM 4565 O BHOH E 193 6.935 4.957 17.167 0.50 21.50 O ANISOU 4565 O BHOH E 193 2251 1997 3920 -281 392 501 O HETATM 4566 O HOH E 198 19.814 14.583 0.000 1.00 38.87 O ANISOU 4566 O HOH E 198 5736 5463 3569 -309 1347 1933 O HETATM 4567 O HOH E 203 12.643 8.894 19.598 1.00 39.87 O ANISOU 4567 O HOH E 203 5034 5114 5002 -194 560 -57 O HETATM 4568 O HOH E 204 16.441 5.338 -0.572 1.00 32.58 O ANISOU 4568 O HOH E 204 5152 4139 3089 -190 -107 -736 O HETATM 4569 O HOH E 211 6.064 8.630 12.768 1.00 45.34 O ANISOU 4569 O HOH E 211 5585 5669 5973 -605 -1071 -77 O HETATM 4570 O AHOH E 215 12.234 20.517 7.968 0.61 29.82 O ANISOU 4570 O AHOH E 215 4633 3150 3548 -591 -1190 -203 O HETATM 4571 O BHOH E 215 10.631 19.918 8.251 0.39 21.05 O ANISOU 4571 O BHOH E 215 3332 1354 3311 278 2095 -340 O HETATM 4572 O HOH E 216 26.003 7.318 18.479 1.00 53.03 O ANISOU 4572 O HOH E 216 6292 6291 7565 -245 130 173 O HETATM 4573 O HOH E 218 15.021 20.030 1.127 1.00 34.87 O ANISOU 4573 O HOH E 218 5123 4396 3729 -553 -532 881 O HETATM 4574 O HOH E 221 24.537 2.070 18.242 1.00 41.78 O ANISOU 4574 O HOH E 221 4041 5642 6192 279 310 116 O HETATM 4575 O HOH E 227 14.976 0.745 3.599 1.00 42.07 O ANISOU 4575 O HOH E 227 5673 5166 5145 -964 -63 -790 O HETATM 4576 O HOH E 238 18.219 2.716 1.322 1.00 37.73 O ANISOU 4576 O HOH E 238 5895 4474 3965 -731 1332 105 O HETATM 4577 O HOH E 247 13.956 3.793 -0.651 1.00 40.59 O ANISOU 4577 O HOH E 247 5661 5134 4628 492 -846 -126 O HETATM 4578 O HOH E 248 15.449 12.082 14.798 1.00 42.88 O ANISOU 4578 O HOH E 248 5674 4621 5997 -777 623 35 O HETATM 4579 O HOH E 253 8.657 8.567 16.082 1.00 38.58 O ANISOU 4579 O HOH E 253 4799 5300 4560 1177 -62 -761 O HETATM 4580 O HOH E 262 11.664 1.507 6.211 1.00 44.07 O ANISOU 4580 O HOH E 262 5966 5069 5707 780 -646 406 O HETATM 4581 O HOH E 310 24.279 4.876 14.617 1.00 35.01 O ANISOU 4581 O HOH E 310 3497 4956 4850 1441 931 955 O HETATM 4582 O AHOH E 325 19.248 -1.874 19.062 0.51 26.09 O ANISOU 4582 O AHOH E 325 2667 2689 4559 339 -1063 399 O HETATM 4583 O BHOH E 325 18.660 -3.176 18.281 0.49 18.05 O ANISOU 4583 O BHOH E 325 1927 1766 3165 -445 238 292 O HETATM 4584 O HOH E 339 16.592 -2.709 5.805 1.00 37.81 O ANISOU 4584 O HOH E 339 5257 3575 5535 847 1625 -437 O HETATM 4585 O HOH E 347 21.903 7.888 13.447 1.00 19.19 O ANISOU 4585 O HOH E 347 2013 2778 2499 364 291 515 O HETATM 4586 O AHOH E 352 15.325 16.763 12.576 0.48 34.27 O ANISOU 4586 O AHOH E 352 4524 3607 4889 156 566 189 O HETATM 4587 O BHOH E 352 14.923 14.783 12.502 0.52 35.58 O ANISOU 4587 O BHOH E 352 4699 4011 4811 106 506 -139 O HETATM 4588 O HOH E 354 29.622 20.666 6.717 1.00 35.42 O ANISOU 4588 O HOH E 354 4548 3736 5175 -725 534 -1194 O HETATM 4589 O HOH E 359 7.848 15.984 1.685 1.00 44.85 O ANISOU 4589 O HOH E 359 6066 5304 5672 61 289 165 O CONECT 89 2108 CONECT 355 583 CONECT 583 355 CONECT 782 4283 CONECT 809 4283 CONECT 864 4283 CONECT 903 4283 CONECT 940 4283 CONECT 1796 2755 CONECT 2108 89 CONECT 2264 2476 CONECT 2476 2264 CONECT 2622 2943 CONECT 2755 1796 CONECT 2943 2622 CONECT 3478 4253 CONECT 3606 3980 CONECT 3868 4188 CONECT 3980 3606 CONECT 4188 3868 CONECT 4253 3478 CONECT 4283 782 809 864 903 CONECT 4283 940 4368 CONECT 4368 4283 MASTER 331 0 1 5 16 0 2 6 2434 2 24 23 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3p95
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Human mesotrypsin
Ligand Name
bovine pancreatic trypsin inhibitor variant (BPTI-K15R/R17D)
EC.Number
E.C.3.4.21.4
Resolution
1.3(Å)
Affinity (Kd/Ki/IC50)
Ki=1.5uM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) Biochem.J. Vol. 440: pp. 95-105
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):
P00974
P35030
Entrez Gene ID
NCBI Entrez Gene ID:
5646
ASD
Information of known allosteric effects of PDB entries
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