Browse entries in the PDBbind-CN Database
HEADER APOPTOSIS 02-NOV-09 3KJ2 TITLE MCL-1 IN COMPLEX WITH BIM BH3 MUTANT F4AE COMPND MOL_ID: 1; COMPND 2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- COMPND 3 1; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: (UNP 172-322); COMPND 6 SYNONYM: BCL-2-RELATED PROTEIN EAT/MCL1, MCL1/EAT, BCL-2-LIKE PROTEIN COMPND 7 3, BCL2-L-3; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: BCL-2-LIKE PROTEIN 11; COMPND 11 CHAIN: B; COMPND 12 FRAGMENT: BH3 REGION OF BIM (UNP 1-21); COMPND 13 SYNONYM: BCL2-L-11, BCL2-INTERACTING MEDIATOR OF CELL DEATH; COMPND 14 ENGINEERED: YES; COMPND 15 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: BCL2L3, MCL-1, MCL1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSV282; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: BCL2L11, BIM; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PSV282 KEYWDS BCL-2, BH3, APOPTOSIS, PROTEIN-PEPTIDE COMPLEX, ALTERNATIVE SPLICING, KEYWDS 2 CYTOPLASM, DEVELOPMENTAL PROTEIN, DIFFERENTIATION, ISOPEPTIDE BOND, KEYWDS 3 MEMBRANE, MITOCHONDRION, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, KEYWDS 4 TRANSMEMBRANE, UBL CONJUGATION EXPDTA X-RAY DIFFRACTION AUTHOR E.FIRE,R.A.GRANT,A.E.KEATING REVDAT 3 01-NOV-17 3KJ2 1 REMARK REVDAT 2 23-MAR-10 3KJ2 1 JRNL REVDAT 1 16-FEB-10 3KJ2 0 JRNL AUTH E.FIRE,S.V.GULLA,R.A.GRANT,A.E.KEATING JRNL TITL MCL-1-BIM COMPLEXES ACCOMMODATE SURPRISING POINT MUTATIONS JRNL TITL 2 VIA MINOR STRUCTURAL CHANGES. JRNL REF PROTEIN SCI. V. 19 507 2010 JRNL REFN ISSN 0961-8368 JRNL PMID 20066663 JRNL DOI 10.1002/PRO.329 REMARK 2 REMARK 2 RESOLUTION. 2.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.29 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 9515 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.710 REMARK 3 FREE R VALUE TEST SET COUNT : 448 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 24.2910 - 3.3880 1.00 3110 147 0.1980 0.2340 REMARK 3 2 3.3880 - 2.6900 1.00 3003 153 0.2020 0.2380 REMARK 3 3 2.6900 - 2.3510 1.00 2954 148 0.2290 0.2760 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 : 0.30 REMARK 3 B_SOL : 50.00 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.31 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 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 : 0.002 1437 REMARK 3 ANGLE : 0.549 1931 REMARK 3 CHIRALITY : 0.041 210 REMARK 3 PLANARITY : 0.001 250 REMARK 3 DIHEDRAL : 13.794 537 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 3.5994 20.3008 42.3212 REMARK 3 T TENSOR REMARK 3 T11: 0.0998 T22: 0.0522 REMARK 3 T33: 0.1440 T12: 0.0065 REMARK 3 T13: 0.0124 T23: -0.0133 REMARK 3 L TENSOR REMARK 3 L11: 1.6991 L22: 0.2390 REMARK 3 L33: 0.7566 L12: -0.5589 REMARK 3 L13: 0.2710 L23: 0.0492 REMARK 3 S TENSOR REMARK 3 S11: -0.0164 S12: -0.0662 S13: -0.0307 REMARK 3 S21: 0.0739 S22: 0.0128 S23: 0.0189 REMARK 3 S31: 0.0414 S32: -0.0348 S33: 0.0110 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 3KJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-09. REMARK 100 THE DEPOSITION ID IS D_1000056053. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-OCT-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : VARIMAXHR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9519 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 9.400 REMARK 200 R MERGE (I) : 0.08300 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : 0.44900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.97 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, 0.2 M ZINC ACETATE, REMARK 280 2% PEG 3350, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.72800 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.74350 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 59.71750 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 25.72800 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.74350 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.71750 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.72800 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 35.74350 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.71750 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 25.72800 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 35.74350 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 59.71750 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 14720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30990 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -606.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 71.48700 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 119.43500 REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 71.48700 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 119.43500 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 5 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 31 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 33 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 170 REMARK 465 SER A 171 REMARK 465 ASP A 323 REMARK 465 LEU A 324 REMARK 465 GLU A 325 REMARK 465 GLY A 326 REMARK 465 GLY A 327 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 194 CG CD CE NZ 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 ZN B 23 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 224 NE2 REMARK 620 2 GLU B 16 OE1 105.4 REMARK 620 3 GLU B 17 OE2 106.2 106.3 REMARK 620 4 HOH B 28 O 111.5 125.8 99.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 2 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 241 OD1 REMARK 620 2 GLU A 240 OE2 92.7 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 3 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 304 OD1 REMARK 620 2 ACT A1428 OXT 97.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 4 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 320 NE2 REMARK 620 2 GLU A 322 OE2 93.2 REMARK 620 3 GLU A 322 OE1 119.6 53.9 REMARK 620 4 HOH A 8 O 96.9 165.7 112.0 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 23 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1428 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3KJ0 RELATED DB: PDB REMARK 900 MCL-1 IN COMPLEX WITH BIM BH3 MUTANT I2DY REMARK 900 RELATED ID: 3KJ2 RELATED DB: PDB REMARK 900 MCL-1 IN COMPLEX WITH BIM BH3 MUTANT I2DA REMARK 900 RELATED ID: 2PQK RELATED DB: PDB REMARK 900 HUMAN MCL-1 IN COMPLEX WITH WILD-TYPE BIM BH3 DBREF 3KJ2 A 172 327 UNP Q07820 MCL1_HUMAN 172 327 DBREF 3KJ2 B 1 21 UNP O43521 B2L11_HUMAN 143 163 SEQADV 3KJ2 GLY A 170 UNP Q07820 EXPRESSION TAG SEQADV 3KJ2 SER A 171 UNP Q07820 EXPRESSION TAG SEQADV 3KJ2 GLU B 17 UNP O43521 PHE 159 ENGINEERED SEQADV 3KJ2 ARG B 22 UNP O43521 EXPRESSION TAG SEQRES 1 A 158 GLY SER ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SEQRES 2 A 158 SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP SEQRES 3 A 158 THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS SEQRES 4 A 158 ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN SEQRES 5 A 158 ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS SEQRES 6 A 158 LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER SEQRES 7 A 158 ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN SEQRES 8 A 158 TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE SEQRES 9 A 158 VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS SEQRES 10 A 158 ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL SEQRES 11 A 158 ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP SEQRES 12 A 158 ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU SEQRES 13 A 158 GLY GLY SEQRES 1 B 22 ARG PRO GLU ILE TRP ILE ALA GLN GLU LEU ARG ARG ILE SEQRES 2 B 22 GLY ASP GLU GLU ASN ALA TYR TYR ARG HET ZN A 2 1 HET ZN A 3 1 HET ZN A 4 1 HET ACT A1428 4 HET ZN B 23 1 HETNAM ZN ZINC ION HETNAM ACT ACETATE ION FORMUL 3 ZN 4(ZN 2+) FORMUL 6 ACT C2 H3 O2 1- FORMUL 8 HOH *64(H2 O) HELIX 1 1 ASP A 172 GLY A 192 1 21 HELIX 2 2 SER A 202 HIS A 224 1 23 HELIX 3 3 HIS A 224 ASP A 236 1 13 HELIX 4 4 VAL A 243 PHE A 254 1 12 HELIX 5 5 ASN A 260 ASN A 282 1 23 HELIX 6 6 ILE A 287 LYS A 302 1 16 HELIX 7 7 LYS A 302 GLN A 309 1 8 HELIX 8 8 GLY A 311 PHE A 319 1 9 HELIX 9 9 ARG B 1 ARG B 22 1 22 SSBOND 1 CYS A 286 CYS A 286 1555 3556 2.01 LINK NE2 HIS A 224 ZN ZN B 23 1555 1555 2.24 LINK OD1 ASP A 241 ZN ZN A 2 1555 1555 2.37 LINK OD1 ASP A 304 ZN ZN A 3 1555 1555 2.20 LINK NE2 HIS A 320 ZN ZN A 4 1555 1555 2.26 LINK OE2 GLU A 322 ZN ZN A 4 1555 1555 2.40 LINK OE1 GLU B 16 ZN ZN B 23 1555 1555 2.32 LINK OE2 GLU B 17 ZN ZN B 23 1555 1555 2.26 LINK ZN ZN A 3 OXT ACT A1428 1555 1555 2.19 LINK OE1 GLU A 322 ZN ZN A 4 1555 1555 2.46 LINK ZN ZN A 4 O HOH A 8 1555 1555 2.59 LINK ZN ZN B 23 O HOH B 28 1555 1555 2.65 LINK OE2 GLU A 240 ZN ZN A 2 1555 1555 2.70 SITE 1 AC1 4 HIS A 224 GLU B 16 GLU B 17 HOH B 28 SITE 1 AC2 3 GLU A 240 ASP A 241 GLU A 292 SITE 1 AC3 4 HOH A 29 HIS A 252 ASP A 304 ACT A1428 SITE 1 AC4 4 HOH A 8 HIS A 320 GLU A 322 GLU B 9 SITE 1 AC5 7 ZN A 3 HOH A 39 HIS A 252 ASP A 304 SITE 2 AC5 7 ALA B 7 GLN B 8 ARG B 11 CRYST1 51.456 71.487 119.435 90.00 90.00 90.00 I 2 2 2 8 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 0.019434 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013989 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008373 0.00000 ATOM 1 N ASP A 172 -15.728 25.184 48.452 1.00 60.83 N ANISOU 1 N ASP A 172 7231 8221 7661 275 378 -212 N ATOM 2 CA ASP A 172 -14.568 25.316 47.578 1.00 55.35 C ANISOU 2 CA ASP A 172 6601 7394 7035 256 349 -232 C ATOM 3 C ASP A 172 -14.065 23.944 47.138 1.00 46.82 C ANISOU 3 C ASP A 172 5531 6247 6013 174 367 -166 C ATOM 4 O ASP A 172 -13.114 23.408 47.706 1.00 41.97 O ANISOU 4 O ASP A 172 4942 5603 5404 160 368 -131 O ATOM 5 CB ASP A 172 -13.454 26.089 48.286 1.00 52.66 C ANISOU 5 CB ASP A 172 6301 7029 6679 309 316 -271 C ATOM 6 CG ASP A 172 -12.363 26.542 47.335 1.00 55.47 C ANISOU 6 CG ASP A 172 6714 7259 7104 299 283 -298 C ATOM 7 OD1 ASP A 172 -12.447 26.217 46.132 1.00 52.88 O ANISOU 7 OD1 ASP A 172 6394 6873 6826 257 286 -284 O ATOM 8 OD2 ASP A 172 -11.422 27.224 47.793 1.00 58.26 O ANISOU 8 OD2 ASP A 172 7098 7579 7460 336 252 -335 O ATOM 9 N GLU A 173 -14.711 23.382 46.121 1.00 41.28 N ANISOU 9 N GLU A 173 4808 5521 5355 125 376 -157 N ATOM 10 CA GLU A 173 -14.380 22.045 45.639 1.00 41.59 C ANISOU 10 CA GLU A 173 4848 5494 5460 50 387 -109 C ATOM 11 C GLU A 173 -13.050 22.001 44.890 1.00 46.28 C ANISOU 11 C GLU A 173 5502 5979 6104 42 358 -126 C ATOM 12 O GLU A 173 -12.302 21.029 44.996 1.00 41.79 O ANISOU 12 O GLU A 173 4951 5355 5572 2 361 -86 O ATOM 13 CB GLU A 173 -15.501 21.505 44.749 1.00 41.57 C ANISOU 13 CB GLU A 173 4797 5504 5494 5 398 -113 C ATOM 14 CG GLU A 173 -15.162 20.200 44.042 1.00 55.26 C ANISOU 14 CG GLU A 173 6530 7153 7311 -67 396 -87 C ATOM 15 CD GLU A 173 -14.867 19.066 45.008 1.00 64.76 C ANISOU 15 CD GLU A 173 7725 8344 8539 -113 419 -5 C ATOM 16 OE1 GLU A 173 -15.223 19.185 46.199 1.00 64.82 O ANISOU 16 OE1 GLU A 173 7707 8432 8489 -95 446 42 O ATOM 17 OE2 GLU A 173 -14.280 18.053 44.572 1.00 61.09 O ANISOU 17 OE2 GLU A 173 7274 7789 8146 -161 410 14 O ATOM 18 N LEU A 174 -12.762 23.051 44.127 1.00 33.27 N ANISOU 18 N LEU A 174 3882 4303 4457 82 332 -181 N ATOM 19 CA LEU A 174 -11.513 23.114 43.378 1.00 33.50 C ANISOU 19 CA LEU A 174 3958 4244 4527 78 306 -193 C ATOM 20 C LEU A 174 -10.322 22.952 44.314 1.00 36.39 C ANISOU 20 C LEU A 174 4360 4581 4886 83 301 -170 C ATOM 21 O LEU A 174 -9.392 22.200 44.025 1.00 42.55 O ANISOU 21 O LEU A 174 5165 5300 5703 53 295 -149 O ATOM 22 CB LEU A 174 -11.406 24.430 42.604 1.00 29.80 C ANISOU 22 CB LEU A 174 3507 3759 4057 126 282 -238 C ATOM 23 CG LEU A 174 -10.114 24.629 41.808 1.00 38.45 C ANISOU 23 CG LEU A 174 4642 4775 5191 126 259 -241 C ATOM 24 CD1 LEU A 174 -9.863 23.451 40.874 1.00 27.52 C ANISOU 24 CD1 LEU A 174 3252 3359 3845 80 261 -227 C ATOM 25 CD2 LEU A 174 -10.148 25.939 41.032 1.00 33.18 C ANISOU 25 CD2 LEU A 174 3982 4096 4530 172 239 -267 C ATOM 26 N TYR A 175 -10.362 23.657 45.441 1.00 35.92 N ANISOU 26 N TYR A 175 4299 4574 4775 127 300 -180 N ATOM 27 CA TYR A 175 -9.293 23.585 46.429 1.00 34.62 C ANISOU 27 CA TYR A 175 4160 4402 4593 142 293 -167 C ATOM 28 C TYR A 175 -9.234 22.203 47.067 1.00 40.94 C ANISOU 28 C TYR A 175 4947 5216 5391 101 321 -96 C ATOM 29 O TYR A 175 -8.159 21.617 47.202 1.00 39.51 O ANISOU 29 O TYR A 175 4796 4986 5232 86 314 -72 O ATOM 30 CB TYR A 175 -9.489 24.649 47.511 1.00 36.33 C ANISOU 30 CB TYR A 175 4366 4687 4749 209 282 -208 C ATOM 31 CG TYR A 175 -8.384 24.675 48.543 1.00 37.19 C ANISOU 31 CG TYR A 175 4495 4801 4833 235 268 -209 C ATOM 32 CD1 TYR A 175 -7.290 25.517 48.394 1.00 42.54 C ANISOU 32 CD1 TYR A 175 5209 5417 5539 259 230 -259 C ATOM 33 CD2 TYR A 175 -8.432 23.855 49.662 1.00 38.99 C ANISOU 33 CD2 TYR A 175 4702 5101 5011 236 294 -157 C ATOM 34 CE1 TYR A 175 -6.275 25.543 49.332 1.00 47.65 C ANISOU 34 CE1 TYR A 175 5868 6074 6162 284 214 -269 C ATOM 35 CE2 TYR A 175 -7.421 23.873 50.606 1.00 47.90 C ANISOU 35 CE2 TYR A 175 5844 6246 6108 268 281 -160 C ATOM 36 CZ TYR A 175 -6.346 24.719 50.435 1.00 50.58 C ANISOU 36 CZ TYR A 175 6219 6525 6475 292 239 -223 C ATOM 37 OH TYR A 175 -5.337 24.743 51.371 1.00 63.98 O ANISOU 37 OH TYR A 175 7925 8245 8141 326 222 -236 O ATOM 38 N ARG A 176 -10.394 21.690 47.464 1.00 37.84 N ANISOU 38 N ARG A 176 4507 4893 4978 84 352 -58 N ATOM 39 CA ARG A 176 -10.480 20.374 48.083 1.00 37.95 C ANISOU 39 CA ARG A 176 4499 4918 5002 40 383 26 C ATOM 40 C ARG A 176 -9.866 19.310 47.180 1.00 31.21 C ANISOU 40 C ARG A 176 3669 3956 4232 -18 374 47 C ATOM 41 O ARG A 176 -9.011 18.534 47.608 1.00 33.49 O ANISOU 41 O ARG A 176 3980 4208 4539 -31 376 93 O ATOM 42 CB ARG A 176 -11.936 20.015 48.386 1.00 40.65 C ANISOU 42 CB ARG A 176 4777 5343 5327 19 418 65 C ATOM 43 CG ARG A 176 -12.092 18.730 49.186 1.00 44.81 C ANISOU 43 CG ARG A 176 5271 5890 5866 -25 453 170 C ATOM 44 CD ARG A 176 -13.415 18.042 48.893 1.00 42.71 C ANISOU 44 CD ARG A 176 4942 5649 5638 -82 481 212 C ATOM 45 NE ARG A 176 -13.473 17.543 47.522 1.00 52.49 N ANISOU 45 NE ARG A 176 6190 6784 6970 -136 461 175 N ATOM 46 CZ ARG A 176 -12.926 16.401 47.118 1.00 49.98 C ANISOU 46 CZ ARG A 176 5887 6364 6739 -190 453 209 C ATOM 47 NH1 ARG A 176 -13.027 16.026 45.851 1.00 41.92 N ANISOU 47 NH1 ARG A 176 4868 5265 5794 -227 429 158 N ATOM 48 NH2 ARG A 176 -12.276 15.633 47.982 1.00 50.59 N ANISOU 48 NH2 ARG A 176 5975 6422 6825 -201 467 290 N ATOM 49 N GLN A 177 -10.310 19.281 45.929 1.00 29.76 N ANISOU 49 N GLN A 177 3480 3731 4098 -44 363 8 N ATOM 50 CA GLN A 177 -9.821 18.306 44.962 1.00 35.85 C ANISOU 50 CA GLN A 177 4265 4409 4946 -90 348 9 C ATOM 51 C GLN A 177 -8.319 18.454 44.733 1.00 38.44 C ANISOU 51 C GLN A 177 4648 4675 5282 -69 321 -10 C ATOM 52 O GLN A 177 -7.593 17.461 44.664 1.00 40.22 O ANISOU 52 O GLN A 177 4891 4839 5552 -94 315 17 O ATOM 53 CB GLN A 177 -10.569 18.444 43.635 1.00 33.62 C ANISOU 53 CB GLN A 177 3959 4117 4697 -104 336 -45 C ATOM 54 CG GLN A 177 -10.073 17.497 42.552 1.00 42.39 C ANISOU 54 CG GLN A 177 5079 5145 5883 -139 314 -65 C ATOM 55 CD GLN A 177 -10.810 17.669 41.241 1.00 44.30 C ANISOU 55 CD GLN A 177 5290 5397 6145 -141 299 -126 C ATOM 56 OE1 GLN A 177 -11.256 18.766 40.903 1.00 45.42 O ANISOU 56 OE1 GLN A 177 5426 5590 6241 -103 299 -160 O ATOM 57 NE2 GLN A 177 -10.936 16.581 40.488 1.00 34.65 N ANISOU 57 NE2 GLN A 177 4047 4126 4995 -181 284 -144 N ATOM 58 N SER A 178 -7.861 19.698 44.620 1.00 34.07 N ANISOU 58 N SER A 178 4119 4135 4690 -22 304 -57 N ATOM 59 CA SER A 178 -6.452 19.978 44.367 1.00 27.70 C ANISOU 59 CA SER A 178 3356 3277 3892 -3 278 -76 C ATOM 60 C SER A 178 -5.574 19.528 45.528 1.00 28.31 C ANISOU 60 C SER A 178 3453 3354 3949 5 282 -36 C ATOM 61 O SER A 178 -4.531 18.905 45.322 1.00 24.33 O ANISOU 61 O SER A 178 2976 2797 3473 -5 269 -25 O ATOM 62 CB SER A 178 -6.240 21.469 44.099 1.00 27.02 C ANISOU 62 CB SER A 178 3283 3202 3782 41 259 -126 C ATOM 63 OG SER A 178 -6.906 21.881 42.919 1.00 27.36 O ANISOU 63 OG SER A 178 3310 3243 3842 40 255 -155 O ATOM 64 N LEU A 179 -5.996 19.854 46.746 1.00 26.49 N ANISOU 64 N LEU A 179 3206 3196 3663 31 299 -16 N ATOM 65 CA LEU A 179 -5.255 19.476 47.944 1.00 39.45 C ANISOU 65 CA LEU A 179 4858 4863 5270 50 304 24 C ATOM 66 C LEU A 179 -5.126 17.963 48.035 1.00 38.61 C ANISOU 66 C LEU A 179 4749 4716 5205 7 321 99 C ATOM 67 O LEU A 179 -4.096 17.442 48.468 1.00 38.84 O ANISOU 67 O LEU A 179 4803 4720 5235 15 314 127 O ATOM 68 CB LEU A 179 -5.953 20.003 49.200 1.00 37.87 C ANISOU 68 CB LEU A 179 4625 4771 4993 92 323 34 C ATOM 69 CG LEU A 179 -5.274 19.610 50.517 1.00 35.66 C ANISOU 69 CG LEU A 179 4346 4543 4661 123 331 80 C ATOM 70 CD1 LEU A 179 -3.859 20.152 50.563 1.00 26.73 C ANISOU 70 CD1 LEU A 179 3254 3375 3526 155 295 29 C ATOM 71 CD2 LEU A 179 -6.060 20.082 51.730 1.00 34.87 C ANISOU 71 CD2 LEU A 179 4203 4573 4475 172 350 89 C ATOM 72 N GLU A 180 -6.177 17.262 47.626 1.00 32.10 N ANISOU 72 N GLU A 180 3893 3882 4423 -39 340 129 N ATOM 73 CA GLU A 180 -6.208 15.809 47.729 1.00 37.21 C ANISOU 73 CA GLU A 180 4530 4479 5129 -85 354 202 C ATOM 74 C GLU A 180 -5.244 15.139 46.751 1.00 37.88 C ANISOU 74 C GLU A 180 4650 4458 5284 -104 323 176 C ATOM 75 O GLU A 180 -4.450 14.280 47.137 1.00 39.00 O ANISOU 75 O GLU A 180 4811 4556 5449 -107 320 222 O ATOM 76 CB GLU A 180 -7.630 15.316 47.479 1.00 35.57 C ANISOU 76 CB GLU A 180 4271 4284 4961 -134 377 230 C ATOM 77 CG GLU A 180 -7.789 13.811 47.348 1.00 49.00 C ANISOU 77 CG GLU A 180 5954 5908 6756 -194 384 296 C ATOM 78 CD GLU A 180 -9.227 13.405 47.074 1.00 65.87 C ANISOU 78 CD GLU A 180 8030 8058 8939 -247 403 315 C ATOM 79 OE1 GLU A 180 -10.064 14.296 46.829 1.00 73.39 O ANISOU 79 OE1 GLU A 180 8958 9080 9847 -233 410 268 O ATOM 80 OE2 GLU A 180 -9.526 12.194 47.104 1.00 74.65 O ANISOU 80 OE2 GLU A 180 9116 9109 10139 -302 411 377 O ATOM 81 N ILE A 181 -5.332 15.531 45.483 1.00 31.83 N ANISOU 81 N ILE A 181 3888 3661 4546 -110 300 103 N ATOM 82 CA ILE A 181 -4.447 15.015 44.445 1.00 33.07 C ANISOU 82 CA ILE A 181 4070 3739 4755 -117 268 65 C ATOM 83 C ILE A 181 -2.987 15.281 44.806 1.00 32.93 C ANISOU 83 C ILE A 181 4094 3711 4705 -79 252 63 C ATOM 84 O ILE A 181 -2.144 14.387 44.722 1.00 39.80 O ANISOU 84 O ILE A 181 4984 4525 5612 -82 237 78 O ATOM 85 CB ILE A 181 -4.773 15.647 43.076 1.00 29.73 C ANISOU 85 CB ILE A 181 3637 3317 4342 -113 249 -11 C ATOM 86 CG1 ILE A 181 -6.202 15.283 42.650 1.00 33.31 C ANISOU 86 CG1 ILE A 181 4044 3781 4832 -150 261 -17 C ATOM 87 CG2 ILE A 181 -3.760 15.201 42.025 1.00 25.48 C ANISOU 87 CG2 ILE A 181 3119 2721 3840 -105 216 -52 C ATOM 88 CD1 ILE A 181 -6.795 16.218 41.609 1.00 28.58 C ANISOU 88 CD1 ILE A 181 3426 3220 4211 -132 252 -81 C ATOM 89 N ILE A 182 -2.695 16.514 45.209 1.00 27.98 N ANISOU 89 N ILE A 182 3478 3138 4014 -41 252 38 N ATOM 90 CA ILE A 182 -1.331 16.911 45.535 1.00 32.29 C ANISOU 90 CA ILE A 182 4056 3680 4531 -7 233 25 C ATOM 91 C ILE A 182 -0.840 16.267 46.835 1.00 38.80 C ANISOU 91 C ILE A 182 4889 4522 5330 7 245 86 C ATOM 92 O ILE A 182 0.319 15.862 46.935 1.00 37.10 O ANISOU 92 O ILE A 182 4699 4278 5119 21 229 91 O ATOM 93 CB ILE A 182 -1.199 18.446 45.597 1.00 31.13 C ANISOU 93 CB ILE A 182 3912 3575 4341 26 224 -24 C ATOM 94 CG1 ILE A 182 -1.506 19.050 44.223 1.00 24.13 C ANISOU 94 CG1 ILE A 182 3018 2668 3481 18 211 -70 C ATOM 95 CG2 ILE A 182 0.190 18.851 46.067 1.00 23.36 C ANISOU 95 CG2 ILE A 182 2952 2590 3334 57 203 -38 C ATOM 96 CD1 ILE A 182 -1.474 20.561 44.189 1.00 26.43 C ANISOU 96 CD1 ILE A 182 3309 2984 3749 47 201 -109 C ATOM 97 N SER A 183 -1.725 16.165 47.823 1.00 43.44 N ANISOU 97 N SER A 183 5452 5167 5887 7 275 135 N ATOM 98 CA SER A 183 -1.381 15.518 49.088 1.00 42.88 C ANISOU 98 CA SER A 183 5379 5130 5783 26 292 208 C ATOM 99 C SER A 183 -1.099 14.030 48.903 1.00 35.02 C ANISOU 99 C SER A 183 4392 4056 4857 -6 293 270 C ATOM 100 O SER A 183 -0.113 13.508 49.422 1.00 33.86 O ANISOU 100 O SER A 183 4266 3897 4702 17 286 303 O ATOM 101 CB SER A 183 -2.495 15.706 50.121 1.00 36.88 C ANISOU 101 CB SER A 183 4579 4465 4971 35 327 256 C ATOM 102 OG SER A 183 -2.595 17.057 50.530 1.00 43.14 O ANISOU 102 OG SER A 183 5365 5334 5693 81 319 194 O ATOM 103 N ARG A 184 -1.973 13.349 48.169 1.00 31.85 N ANISOU 103 N ARG A 184 3972 3601 4530 -57 298 281 N ATOM 104 CA ARG A 184 -1.825 11.916 47.952 1.00 38.86 C ANISOU 104 CA ARG A 184 4863 4399 5505 -91 293 333 C ATOM 105 C ARG A 184 -0.539 11.583 47.204 1.00 38.65 C ANISOU 105 C ARG A 184 4875 4300 5509 -74 254 283 C ATOM 106 O ARG A 184 0.140 10.611 47.530 1.00 44.02 O ANISOU 106 O ARG A 184 5573 4931 6224 -68 246 331 O ATOM 107 CB ARG A 184 -3.033 11.349 47.205 1.00 37.10 C ANISOU 107 CB ARG A 184 4604 4128 5364 -150 298 332 C ATOM 108 CG ARG A 184 -4.299 11.294 48.037 1.00 44.52 C ANISOU 108 CG ARG A 184 5495 5131 6290 -175 340 408 C ATOM 109 CD ARG A 184 -5.285 10.295 47.465 1.00 46.99 C ANISOU 109 CD ARG A 184 5769 5371 6712 -243 342 431 C ATOM 110 NE ARG A 184 -6.469 10.160 48.307 1.00 55.09 N ANISOU 110 NE ARG A 184 6741 6462 7729 -272 387 519 N ATOM 111 CZ ARG A 184 -7.334 9.156 48.221 1.00 55.48 C ANISOU 111 CZ ARG A 184 6745 6456 7879 -337 398 578 C ATOM 112 NH1 ARG A 184 -7.144 8.189 47.334 1.00 55.18 N ANISOU 112 NH1 ARG A 184 6713 6289 7963 -376 362 548 N ATOM 113 NH2 ARG A 184 -8.385 9.116 49.027 1.00 60.72 N ANISOU 113 NH2 ARG A 184 7352 7195 8523 -362 443 666 N ATOM 114 N TYR A 185 -0.208 12.391 46.201 1.00 32.68 N ANISOU 114 N TYR A 185 4130 3547 4740 -62 229 192 N ATOM 115 CA TYR A 185 1.010 12.177 45.430 1.00 32.57 C ANISOU 115 CA TYR A 185 4145 3486 4745 -41 194 143 C ATOM 116 C TYR A 185 2.247 12.349 46.307 1.00 37.12 C ANISOU 116 C TYR A 185 4748 4090 5264 2 190 165 C ATOM 117 O TYR A 185 3.136 11.497 46.315 1.00 38.09 O ANISOU 117 O TYR A 185 4890 4167 5414 17 172 180 O ATOM 118 CB TYR A 185 1.074 13.128 44.234 1.00 34.73 C ANISOU 118 CB TYR A 185 4414 3776 5004 -35 175 58 C ATOM 119 CG TYR A 185 2.330 12.968 43.410 1.00 33.21 C ANISOU 119 CG TYR A 185 4242 3557 4821 -9 141 11 C ATOM 120 CD1 TYR A 185 2.590 11.783 42.735 1.00 23.99 C ANISOU 120 CD1 TYR A 185 3075 2322 3718 -14 116 -4 C ATOM 121 CD2 TYR A 185 3.257 13.998 43.307 1.00 30.76 C ANISOU 121 CD2 TYR A 185 3942 3288 4456 21 132 -19 C ATOM 122 CE1 TYR A 185 3.738 11.626 41.982 1.00 24.66 C ANISOU 122 CE1 TYR A 185 3171 2396 3801 17 84 -51 C ATOM 123 CE2 TYR A 185 4.407 13.850 42.554 1.00 27.12 C ANISOU 123 CE2 TYR A 185 3491 2816 3999 44 104 -55 C ATOM 124 CZ TYR A 185 4.642 12.661 41.894 1.00 25.03 C ANISOU 124 CZ TYR A 185 3226 2498 3785 45 81 -71 C ATOM 125 OH TYR A 185 5.782 12.502 41.141 1.00 29.15 O ANISOU 125 OH TYR A 185 3751 3023 4302 76 53 -110 O ATOM 126 N LEU A 186 2.300 13.455 47.043 1.00 30.89 N ANISOU 126 N LEU A 186 3956 3379 4399 28 202 159 N ATOM 127 CA LEU A 186 3.407 13.715 47.959 1.00 34.68 C ANISOU 127 CA LEU A 186 4454 3902 4822 73 197 169 C ATOM 128 C LEU A 186 3.560 12.615 49.007 1.00 33.74 C ANISOU 128 C LEU A 186 4338 3781 4701 85 212 259 C ATOM 129 O LEU A 186 4.669 12.151 49.271 1.00 32.16 O ANISOU 129 O LEU A 186 4158 3567 4493 115 197 270 O ATOM 130 CB LEU A 186 3.235 15.072 48.649 1.00 35.44 C ANISOU 130 CB LEU A 186 4538 4083 4846 99 204 139 C ATOM 131 CG LEU A 186 3.929 16.279 48.010 1.00 36.65 C ANISOU 131 CG LEU A 186 4697 4240 4987 111 177 58 C ATOM 132 CD1 LEU A 186 3.585 16.393 46.537 1.00 31.96 C ANISOU 132 CD1 LEU A 186 4101 3596 4445 79 167 21 C ATOM 133 CD2 LEU A 186 3.573 17.564 48.743 1.00 30.57 C ANISOU 133 CD2 LEU A 186 3912 3540 4164 136 179 25 C ATOM 134 N ARG A 187 2.445 12.207 49.608 1.00 37.77 N ANISOU 134 N ARG A 187 4823 4308 5219 63 245 329 N ATOM 135 CA ARG A 187 2.465 11.169 50.636 1.00 38.70 C ANISOU 135 CA ARG A 187 4935 4430 5339 73 267 437 C ATOM 136 C ARG A 187 2.935 9.846 50.038 1.00 40.10 C ANISOU 136 C ARG A 187 5133 4491 5611 54 246 463 C ATOM 137 O ARG A 187 3.716 9.113 50.645 1.00 46.67 O ANISOU 137 O ARG A 187 5981 5309 6442 84 243 520 O ATOM 138 CB ARG A 187 1.078 11.009 51.273 1.00 32.89 C ANISOU 138 CB ARG A 187 4158 3738 4600 46 309 514 C ATOM 139 CG ARG A 187 1.051 10.069 52.475 1.00 47.44 C ANISOU 139 CG ARG A 187 5985 5608 6431 62 339 647 C ATOM 140 CD ARG A 187 -0.307 10.039 53.174 1.00 55.34 C ANISOU 140 CD ARG A 187 6933 6680 7414 40 386 730 C ATOM 141 NE ARG A 187 -0.558 11.237 53.974 1.00 63.47 N ANISOU 141 NE ARG A 187 7940 7854 8321 89 401 699 N ATOM 142 CZ ARG A 187 -1.499 12.135 53.698 1.00 64.27 C ANISOU 142 CZ ARG A 187 8017 8004 8398 76 407 641 C ATOM 143 NH1 ARG A 187 -2.285 11.972 52.644 1.00 63.99 N ANISOU 143 NH1 ARG A 187 7975 7891 8447 13 404 612 N ATOM 144 NH2 ARG A 187 -1.658 13.194 54.480 1.00 68.84 N ANISOU 144 NH2 ARG A 187 8574 8711 8869 130 414 606 N ATOM 145 N GLU A 188 2.455 9.560 48.835 1.00 36.30 N ANISOU 145 N GLU A 188 4649 3931 5213 10 229 413 N ATOM 146 CA GLU A 188 2.823 8.358 48.107 1.00 37.54 C ANISOU 146 CA GLU A 188 4820 3973 5470 -6 199 411 C ATOM 147 C GLU A 188 4.326 8.348 47.868 1.00 41.83 C ANISOU 147 C GLU A 188 5398 4508 5987 44 165 363 C ATOM 148 O GLU A 188 4.996 7.330 48.047 1.00 38.85 O ANISOU 148 O GLU A 188 5038 4069 5652 63 149 401 O ATOM 149 CB GLU A 188 2.109 8.366 46.761 1.00 33.42 C ANISOU 149 CB GLU A 188 4282 3399 5016 -48 180 331 C ATOM 150 CG GLU A 188 1.499 7.052 46.341 1.00 43.42 C ANISOU 150 CG GLU A 188 5533 4556 6410 -92 167 358 C ATOM 151 CD GLU A 188 0.822 7.158 44.993 1.00 56.57 C ANISOU 151 CD GLU A 188 7177 6190 8129 -123 143 261 C ATOM 152 OE1 GLU A 188 -0.399 6.911 44.923 1.00 58.85 O ANISOU 152 OE1 GLU A 188 7428 6460 8472 -174 158 282 O ATOM 153 OE2 GLU A 188 1.506 7.507 44.008 1.00 58.39 O ANISOU 153 OE2 GLU A 188 7421 6425 8341 -95 109 167 O ATOM 154 N GLN A 189 4.844 9.498 47.449 1.00 39.48 N ANISOU 154 N GLN A 189 5107 4270 5623 65 154 282 N ATOM 155 CA GLN A 189 6.257 9.652 47.132 1.00 37.71 C ANISOU 155 CA GLN A 189 4907 4053 5370 108 123 231 C ATOM 156 C GLN A 189 7.133 9.505 48.370 1.00 36.68 C ANISOU 156 C GLN A 189 4790 3966 5180 155 130 287 C ATOM 157 O GLN A 189 8.175 8.854 48.330 1.00 46.03 O ANISOU 157 O GLN A 189 5994 5121 6374 189 106 287 O ATOM 158 CB GLN A 189 6.499 11.016 46.482 1.00 36.29 C ANISOU 158 CB GLN A 189 4721 3930 5139 112 115 148 C ATOM 159 CG GLN A 189 5.911 11.150 45.087 1.00 30.20 C ANISOU 159 CG GLN A 189 3934 3125 4414 82 101 86 C ATOM 160 CD GLN A 189 6.791 10.527 44.026 1.00 40.04 C ANISOU 160 CD GLN A 189 5188 4329 5697 101 64 34 C ATOM 161 OE1 GLN A 189 6.367 9.634 43.293 1.00 46.68 O ANISOU 161 OE1 GLN A 189 6021 5106 6608 87 46 15 O ATOM 162 NE2 GLN A 189 8.030 10.992 43.942 1.00 30.06 N ANISOU 162 NE2 GLN A 189 3933 3104 4385 137 48 5 N ATOM 163 N ALA A 190 6.697 10.112 49.469 1.00 30.72 N ANISOU 163 N ALA A 190 4021 3293 4359 165 161 330 N ATOM 164 CA ALA A 190 7.462 10.107 50.710 1.00 40.44 C ANISOU 164 CA ALA A 190 5256 4592 5516 218 168 377 C ATOM 165 C ALA A 190 7.471 8.738 51.393 1.00 56.43 C ANISOU 165 C ALA A 190 7287 6575 7577 231 180 487 C ATOM 166 O ALA A 190 8.512 8.279 51.864 1.00 63.08 O ANISOU 166 O ALA A 190 8146 7427 8396 279 167 511 O ATOM 167 CB ALA A 190 6.928 11.170 51.659 1.00 31.47 C ANISOU 167 CB ALA A 190 4096 3566 4296 234 193 379 C ATOM 168 N THR A 191 6.310 8.093 51.448 1.00 52.70 N ANISOU 168 N THR A 191 6798 6057 7168 187 205 559 N ATOM 169 CA THR A 191 6.186 6.804 52.123 1.00 52.67 C ANISOU 169 CA THR A 191 6793 6005 7214 190 221 683 C ATOM 170 C THR A 191 6.455 5.632 51.183 1.00 51.31 C ANISOU 170 C THR A 191 6642 5686 7167 168 187 674 C ATOM 171 O THR A 191 6.807 4.540 51.627 1.00 58.07 O ANISOU 171 O THR A 191 7508 6483 8071 187 184 759 O ATOM 172 CB THR A 191 4.793 6.630 52.758 1.00 45.43 C ANISOU 172 CB THR A 191 5836 5114 6310 151 268 783 C ATOM 173 OG1 THR A 191 3.792 6.621 51.733 1.00 40.58 O ANISOU 173 OG1 THR A 191 5209 4428 5781 82 263 737 O ATOM 174 CG2 THR A 191 4.507 7.762 53.731 1.00 43.61 C ANISOU 174 CG2 THR A 191 5580 5039 5950 185 298 785 C ATOM 175 N GLY A 192 6.285 5.864 49.886 1.00 45.91 N ANISOU 175 N GLY A 192 5962 4948 6534 135 158 568 N ATOM 176 CA GLY A 192 6.492 4.825 48.895 1.00 45.20 C ANISOU 176 CA GLY A 192 5885 4730 6560 121 117 533 C ATOM 177 C GLY A 192 5.334 3.848 48.839 1.00 56.15 C ANISOU 177 C GLY A 192 7248 6017 8068 62 127 601 C ATOM 178 O GLY A 192 5.424 2.799 48.201 1.00 59.71 O ANISOU 178 O GLY A 192 7705 6345 8635 51 91 586 O ATOM 179 N ALA A 193 4.241 4.194 49.509 1.00 54.81 N ANISOU 179 N ALA A 193 7047 5901 7877 25 174 674 N ATOM 180 CA ALA A 193 3.074 3.322 49.560 1.00 64.19 C ANISOU 180 CA ALA A 193 8202 7006 9181 -39 189 753 C ATOM 181 C ALA A 193 1.843 3.997 48.967 1.00 69.58 C ANISOU 181 C ALA A 193 8850 7719 9869 -95 203 698 C ATOM 182 O ALA A 193 1.506 5.125 49.327 1.00 69.40 O ANISOU 182 O ALA A 193 8815 7816 9739 -86 233 685 O ATOM 183 CB ALA A 193 2.802 2.885 50.990 1.00 64.44 C ANISOU 183 CB ALA A 193 8215 7076 9192 -32 237 921 C ATOM 184 N LYS A 194 1.174 3.299 48.056 1.00 71.76 N ANISOU 184 N LYS A 194 9106 7885 10274 -148 177 660 N ATOM 185 CA LYS A 194 -0.048 3.815 47.456 1.00 75.43 C ANISOU 185 CA LYS A 194 9532 8375 10754 -202 188 609 C ATOM 186 C LYS A 194 -1.173 3.832 48.484 1.00 75.76 C ANISOU 186 C LYS A 194 9529 8470 10786 -243 245 735 C ATOM 187 O LYS A 194 -1.200 3.007 49.398 1.00 70.41 O ANISOU 187 O LYS A 194 8840 7759 10152 -251 268 869 O ATOM 188 CB LYS A 194 -0.453 2.968 46.249 1.00 78.71 C ANISOU 188 CB LYS A 194 9930 8661 11314 -244 140 530 C ATOM 189 N ASP A 195 -2.093 4.780 48.337 1.00 82.12 N ANISOU 189 N ASP A 195 10304 9366 11532 -264 270 698 N ATOM 190 CA ASP A 195 -3.231 4.883 49.243 1.00 87.89 C ANISOU 190 CA ASP A 195 10984 10168 12243 -299 324 807 C ATOM 191 C ASP A 195 -4.486 4.290 48.609 1.00 94.70 C ANISOU 191 C ASP A 195 11793 10956 13232 -380 321 804 C ATOM 192 O ASP A 195 -4.844 4.623 47.477 1.00 92.21 O ANISOU 192 O ASP A 195 11472 10622 12943 -398 291 681 O ATOM 193 CB ASP A 195 -3.466 6.341 49.656 1.00 83.18 C ANISOU 193 CB ASP A 195 10382 9730 11491 -262 354 772 C ATOM 194 CG ASP A 195 -4.701 6.516 50.528 1.00 87.86 C ANISOU 194 CG ASP A 195 10915 10418 12051 -290 409 870 C ATOM 195 OD1 ASP A 195 -5.222 5.508 51.050 1.00 94.45 O ANISOU 195 OD1 ASP A 195 11712 11208 12967 -333 433 995 O ATOM 196 OD2 ASP A 195 -5.151 7.670 50.694 1.00 89.63 O ANISOU 196 OD2 ASP A 195 11125 10760 12169 -266 427 824 O ATOM 197 N THR A 196 -5.139 3.399 49.349 1.00103.80 N ANISOU 197 N THR A 196 12903 12072 14465 -429 352 944 N ATOM 198 CA THR A 196 -6.378 2.780 48.898 1.00118.11 C ANISOU 198 CA THR A 196 14653 13815 16408 -514 352 959 C ATOM 199 C THR A 196 -7.581 3.371 49.629 1.00127.02 C ANISOU 199 C THR A 196 15720 15078 17466 -541 413 1037 C ATOM 200 O THR A 196 -8.052 2.826 50.628 1.00132.07 O ANISOU 200 O THR A 196 16314 15737 18129 -569 459 1197 O ATOM 201 CB THR A 196 -6.356 1.250 49.089 1.00124.42 C ANISOU 201 CB THR A 196 15435 14455 17385 -564 339 1064 C ATOM 202 OG1 THR A 196 -6.351 0.936 50.487 1.00126.62 O ANISOU 202 OG1 THR A 196 15695 14785 17628 -556 394 1252 O ATOM 203 CG2 THR A 196 -5.122 0.652 48.436 1.00124.42 C ANISOU 203 CG2 THR A 196 15496 14330 17449 -525 276 984 C ATOM 204 N LYS A 197 -8.054 4.505 49.125 1.00128.70 N ANISOU 204 N LYS A 197 15927 15388 17587 -527 414 928 N ATOM 205 CA LYS A 197 -9.287 5.119 49.595 1.00130.76 C ANISOU 205 CA LYS A 197 16124 15774 17784 -549 462 970 C ATOM 206 C LYS A 197 -10.011 5.722 48.401 1.00137.47 C ANISOU 206 C LYS A 197 16958 16631 18645 -571 436 826 C ATOM 207 O LYS A 197 -9.384 6.356 47.551 1.00136.96 O ANISOU 207 O LYS A 197 16941 16559 18537 -528 398 695 O ATOM 208 CB LYS A 197 -9.000 6.215 50.626 1.00126.43 C ANISOU 208 CB LYS A 197 15590 15394 17053 -473 501 1001 C ATOM 209 CG LYS A 197 -8.547 5.707 51.986 1.00123.51 C ANISOU 209 CG LYS A 197 15216 15066 16646 -446 540 1162 C ATOM 210 CD LYS A 197 -8.565 6.820 53.026 1.00119.50 C ANISOU 210 CD LYS A 197 14698 14750 15955 -372 578 1182 C ATOM 211 CE LYS A 197 -7.659 6.495 54.204 1.00117.06 C ANISOU 211 CE LYS A 197 14407 14489 15582 -313 599 1295 C ATOM 212 NZ LYS A 197 -6.219 6.575 53.829 1.00115.67 N ANISOU 212 NZ LYS A 197 14311 14241 15396 -263 552 1210 N ATOM 213 N PRO A 198 -11.332 5.512 48.319 1.00144.23 N ANISOU 213 N PRO A 198 17738 17504 19557 -636 457 855 N ATOM 214 CA PRO A 198 -12.107 6.212 47.294 1.00144.80 C ANISOU 214 CA PRO A 198 17787 17613 19615 -646 438 724 C ATOM 215 C PRO A 198 -11.806 7.706 47.327 1.00137.96 C ANISOU 215 C PRO A 198 16961 16877 18580 -565 445 647 C ATOM 216 O PRO A 198 -11.850 8.318 48.397 1.00136.41 O ANISOU 216 O PRO A 198 16760 16799 18270 -526 487 717 O ATOM 217 CB PRO A 198 -13.551 5.948 47.719 1.00148.81 C ANISOU 217 CB PRO A 198 18203 18175 20164 -714 479 808 C ATOM 218 CG PRO A 198 -13.489 4.617 48.390 1.00150.56 C ANISOU 218 CG PRO A 198 18397 18298 20512 -772 494 955 C ATOM 219 CD PRO A 198 -12.164 4.590 49.111 1.00148.16 C ANISOU 219 CD PRO A 198 18163 17987 20143 -706 497 1012 C ATOM 220 N MET A 199 -11.483 8.272 46.167 1.00132.49 N ANISOU 220 N MET A 199 16302 16163 17873 -537 402 505 N ATOM 221 CA MET A 199 -11.203 9.697 46.036 1.00128.41 C ANISOU 221 CA MET A 199 15821 15748 17220 -466 402 428 C ATOM 222 C MET A 199 -12.421 10.510 46.438 1.00128.62 C ANISOU 222 C MET A 199 15794 15903 17171 -465 439 440 C ATOM 223 O MET A 199 -12.319 11.686 46.795 1.00127.62 O ANISOU 223 O MET A 199 15688 15877 16926 -404 451 413 O ATOM 224 CB MET A 199 -10.852 10.025 44.583 1.00125.20 C ANISOU 224 CB MET A 199 15442 15294 16832 -448 352 289 C ATOM 225 CG MET A 199 -9.494 9.527 44.127 1.00124.81 C ANISOU 225 CG MET A 199 15451 15148 16822 -425 312 254 C ATOM 226 SD MET A 199 -8.159 10.560 44.760 1.00 74.03 S ANISOU 226 SD MET A 199 9090 8775 10261 -344 318 258 S ATOM 227 CE MET A 199 -6.795 10.033 43.722 1.00 84.23 C ANISOU 227 CE MET A 199 10432 9964 11607 -322 263 181 C ATOM 228 N GLY A 200 -13.580 9.867 46.370 1.00128.58 N ANISOU 228 N GLY A 200 15718 15893 17243 -532 455 478 N ATOM 229 CA GLY A 200 -14.838 10.553 46.564 1.00122.79 C ANISOU 229 CA GLY A 200 14924 15281 16448 -535 486 477 C ATOM 230 C GLY A 200 -15.186 11.385 45.346 1.00112.09 C ANISOU 230 C GLY A 200 13574 13945 15069 -511 454 339 C ATOM 231 O GLY A 200 -15.291 10.864 44.234 1.00109.36 O ANISOU 231 O GLY A 200 13219 13518 14815 -544 417 266 O ATOM 232 N ARG A 201 -15.328 12.690 45.552 1.00102.95 N ANISOU 232 N ARG A 201 12431 12898 13788 -445 465 300 N ATOM 233 CA ARG A 201 -15.913 13.569 44.542 1.00100.17 C ANISOU 233 CA ARG A 201 12068 12588 13403 -419 446 191 C ATOM 234 C ARG A 201 -15.102 13.773 43.266 1.00 98.52 C ANISOU 234 C ARG A 201 11911 12304 13218 -392 398 88 C ATOM 235 O ARG A 201 -13.909 14.086 43.312 1.00100.65 O ANISOU 235 O ARG A 201 12246 12539 13457 -351 382 78 O ATOM 236 CB ARG A 201 -16.252 14.926 45.146 1.00 98.07 C ANISOU 236 CB ARG A 201 11805 12450 13007 -350 467 180 C ATOM 237 CG ARG A 201 -17.440 15.563 44.464 1.00101.43 C ANISOU 237 CG ARG A 201 12182 12947 13409 -342 465 113 C ATOM 238 CD ARG A 201 -17.829 16.893 45.073 1.00106.62 C ANISOU 238 CD ARG A 201 12839 13726 13946 -268 482 97 C ATOM 239 NE ARG A 201 -18.921 17.495 44.314 1.00110.78 N ANISOU 239 NE ARG A 201 13323 14315 14454 -255 476 28 N ATOM 240 CZ ARG A 201 -18.761 18.139 43.161 1.00111.16 C ANISOU 240 CZ ARG A 201 13400 14337 14500 -220 443 -61 C ATOM 241 NH1 ARG A 201 -17.551 18.272 42.636 1.00104.42 N ANISOU 241 NH1 ARG A 201 12615 13398 13663 -199 414 -90 N ATOM 242 NH2 ARG A 201 -19.810 18.650 42.531 1.00114.71 N ANISOU 242 NH2 ARG A 201 13805 14853 14927 -203 440 -115 N ATOM 243 N SER A 202 -15.796 13.650 42.136 1.00 93.10 N ANISOU 243 N SER A 202 11187 11611 12577 -412 375 12 N ATOM 244 CA SER A 202 -15.175 13.657 40.818 1.00 83.07 C ANISOU 244 CA SER A 202 9945 10282 11334 -390 329 -83 C ATOM 245 C SER A 202 -13.964 12.734 40.843 1.00 70.48 C ANISOU 245 C SER A 202 8396 8577 9807 -405 307 -63 C ATOM 246 O SER A 202 -12.875 13.088 40.386 1.00 60.17 O ANISOU 246 O SER A 202 7145 7244 8472 -359 283 -102 O ATOM 247 CB SER A 202 -14.804 15.077 40.380 1.00 79.94 C ANISOU 247 CB SER A 202 9590 9946 10837 -311 322 -138 C ATOM 248 OG SER A 202 -14.440 15.877 41.491 1.00 81.39 O ANISOU 248 OG SER A 202 9810 10175 10940 -274 348 -84 O ATOM 249 N GLY A 203 -14.183 11.541 41.387 1.00 56.12 N ANISOU 249 N GLY A 203 6548 6695 8082 -470 315 3 N ATOM 250 CA GLY A 203 -13.127 10.571 41.605 1.00 54.19 C ANISOU 250 CA GLY A 203 6342 6341 7907 -485 297 39 C ATOM 251 C GLY A 203 -12.391 10.161 40.348 1.00 53.38 C ANISOU 251 C GLY A 203 6262 6162 7859 -468 241 -62 C ATOM 252 O GLY A 203 -11.184 9.927 40.382 1.00 48.58 O ANISOU 252 O GLY A 203 5708 5498 7252 -441 223 -58 O ATOM 253 N ALA A 204 -13.115 10.068 39.238 1.00 52.47 N ANISOU 253 N ALA A 204 6099 6056 7782 -478 213 -156 N ATOM 254 CA ALA A 204 -12.519 9.667 37.968 1.00 49.01 C ANISOU 254 CA ALA A 204 5669 5566 7387 -452 157 -264 C ATOM 255 C ALA A 204 -11.407 10.625 37.548 1.00 46.57 C ANISOU 255 C ALA A 204 5422 5301 6974 -374 149 -297 C ATOM 256 O ALA A 204 -10.299 10.200 37.220 1.00 46.62 O ANISOU 256 O ALA A 204 5464 5249 7000 -349 119 -321 O ATOM 257 CB ALA A 204 -13.583 9.579 36.886 1.00 45.27 C ANISOU 257 CB ALA A 204 5125 5128 6949 -464 131 -363 C ATOM 258 N THR A 205 -11.714 11.917 37.560 1.00 50.00 N ANISOU 258 N THR A 205 5862 5834 7302 -334 175 -296 N ATOM 259 CA THR A 205 -10.744 12.947 37.206 1.00 45.65 C ANISOU 259 CA THR A 205 5362 5323 6659 -266 172 -315 C ATOM 260 C THR A 205 -9.533 12.918 38.134 1.00 45.30 C ANISOU 260 C THR A 205 5379 5235 6597 -256 182 -248 C ATOM 261 O THR A 205 -8.390 12.994 37.681 1.00 45.64 O ANISOU 261 O THR A 205 5460 5258 6623 -219 160 -273 O ATOM 262 CB THR A 205 -11.377 14.351 37.255 1.00 39.92 C ANISOU 262 CB THR A 205 4631 4697 5839 -231 199 -312 C ATOM 263 OG1 THR A 205 -12.321 14.490 36.187 1.00 37.88 O ANISOU 263 OG1 THR A 205 4319 4492 5582 -222 184 -385 O ATOM 264 CG2 THR A 205 -10.307 15.426 37.125 1.00 36.49 C ANISOU 264 CG2 THR A 205 4251 4286 5327 -170 198 -309 C ATOM 265 N SER A 206 -9.791 12.806 39.433 1.00 39.81 N ANISOU 265 N SER A 206 4689 4538 5900 -285 217 -162 N ATOM 266 CA SER A 206 -8.725 12.814 40.429 1.00 36.04 C ANISOU 266 CA SER A 206 4263 4035 5394 -271 229 -96 C ATOM 267 C SER A 206 -7.753 11.655 40.239 1.00 41.72 C ANISOU 267 C SER A 206 5005 4658 6188 -281 199 -97 C ATOM 268 O SER A 206 -6.542 11.828 40.371 1.00 42.94 O ANISOU 268 O SER A 206 5207 4797 6310 -245 189 -92 O ATOM 269 CB SER A 206 -9.307 12.789 41.844 1.00 37.62 C ANISOU 269 CB SER A 206 4450 4268 5575 -295 272 -2 C ATOM 270 OG SER A 206 -10.002 13.990 42.130 1.00 41.49 O ANISOU 270 OG SER A 206 4927 4856 5982 -269 297 -6 O ATOM 271 N ARG A 207 -8.283 10.476 39.928 1.00 44.65 N ANISOU 271 N ARG A 207 5340 4961 6666 -328 181 -108 N ATOM 272 CA ARG A 207 -7.443 9.301 39.726 1.00 43.89 C ANISOU 272 CA ARG A 207 5261 4760 6655 -335 145 -116 C ATOM 273 C ARG A 207 -6.592 9.424 38.466 1.00 39.08 C ANISOU 273 C ARG A 207 4668 4149 6030 -284 100 -219 C ATOM 274 O ARG A 207 -5.406 9.103 38.478 1.00 40.50 O ANISOU 274 O ARG A 207 4888 4288 6211 -254 80 -220 O ATOM 275 CB ARG A 207 -8.284 8.023 39.691 1.00 47.03 C ANISOU 275 CB ARG A 207 5609 5073 7188 -402 131 -107 C ATOM 276 CG ARG A 207 -8.690 7.525 41.069 1.00 61.53 C ANISOU 276 CG ARG A 207 7435 6885 9060 -451 173 26 C ATOM 277 CD ARG A 207 -9.414 6.193 40.992 1.00 70.38 C ANISOU 277 CD ARG A 207 8503 7901 10337 -524 155 44 C ATOM 278 NE ARG A 207 -10.705 6.314 40.323 1.00 75.01 N ANISOU 278 NE ARG A 207 9023 8523 10956 -560 151 -17 N ATOM 279 CZ ARG A 207 -11.835 6.648 40.938 1.00 79.62 C ANISOU 279 CZ ARG A 207 9559 9175 11517 -600 196 47 C ATOM 280 NH1 ARG A 207 -11.833 6.898 42.241 1.00 74.04 N ANISOU 280 NH1 ARG A 207 8864 8515 10754 -604 249 174 N ATOM 281 NH2 ARG A 207 -12.966 6.735 40.252 1.00 83.03 N ANISOU 281 NH2 ARG A 207 9927 9641 11980 -630 187 -19 N ATOM 282 N LYS A 208 -7.200 9.890 37.380 1.00 32.40 N ANISOU 282 N LYS A 208 3787 3359 5165 -269 84 -303 N ATOM 283 CA LYS A 208 -6.460 10.137 36.149 1.00 24.32 C ANISOU 283 CA LYS A 208 2769 2365 4107 -211 47 -393 C ATOM 284 C LYS A 208 -5.403 11.209 36.380 1.00 31.26 C ANISOU 284 C LYS A 208 3698 3296 4884 -161 65 -360 C ATOM 285 O LYS A 208 -4.329 11.178 35.779 1.00 28.98 O ANISOU 285 O LYS A 208 3428 3009 4575 -118 39 -396 O ATOM 286 CB LYS A 208 -7.404 10.556 35.021 1.00 32.83 C ANISOU 286 CB LYS A 208 3793 3515 5168 -197 34 -476 C ATOM 287 CG LYS A 208 -7.985 9.394 34.229 1.00 40.18 C ANISOU 287 CG LYS A 208 4669 4395 6203 -219 -13 -564 C ATOM 288 CD LYS A 208 -9.026 9.874 33.229 1.00 56.47 C ANISOU 288 CD LYS A 208 6672 6546 8237 -203 -22 -642 C ATOM 289 CE LYS A 208 -9.209 8.878 32.092 1.00 69.40 C ANISOU 289 CE LYS A 208 8256 8159 9955 -192 -85 -766 C ATOM 290 NZ LYS A 208 -9.524 7.505 32.578 1.00 75.56 N ANISOU 290 NZ LYS A 208 9017 8809 10884 -261 -110 -766 N ATOM 291 N ALA A 209 -5.716 12.157 37.256 1.00 31.73 N ANISOU 291 N ALA A 209 3773 3402 4882 -168 108 -295 N ATOM 292 CA ALA A 209 -4.774 13.209 37.611 1.00 39.37 C ANISOU 292 CA ALA A 209 4784 4408 5767 -128 123 -264 C ATOM 293 C ALA A 209 -3.602 12.622 38.386 1.00 35.54 C ANISOU 293 C ALA A 209 4341 3867 5296 -126 118 -220 C ATOM 294 O ALA A 209 -2.446 12.946 38.121 1.00 28.70 O ANISOU 294 O ALA A 209 3502 3009 4394 -88 105 -232 O ATOM 295 CB ALA A 209 -5.464 14.290 38.428 1.00 39.33 C ANISOU 295 CB ALA A 209 4780 4459 5704 -132 162 -218 C ATOM 296 N LEU A 210 -3.910 11.752 39.341 1.00 34.59 N ANISOU 296 N LEU A 210 4222 3693 5229 -165 131 -163 N ATOM 297 CA LEU A 210 -2.880 11.102 40.141 1.00 34.61 C ANISOU 297 CA LEU A 210 4261 3642 5246 -159 127 -112 C ATOM 298 C LEU A 210 -2.018 10.196 39.269 1.00 39.04 C ANISOU 298 C LEU A 210 4829 4143 5861 -139 81 -170 C ATOM 299 O LEU A 210 -0.807 10.097 39.468 1.00 41.10 O ANISOU 299 O LEU A 210 5126 4392 6101 -107 69 -161 O ATOM 300 CB LEU A 210 -3.512 10.302 41.283 1.00 35.99 C ANISOU 300 CB LEU A 210 4425 3776 5472 -205 152 -26 C ATOM 301 CG LEU A 210 -2.557 9.782 42.358 1.00 44.42 C ANISOU 301 CG LEU A 210 5530 4809 6538 -193 159 49 C ATOM 302 CD1 LEU A 210 -1.742 10.923 42.948 1.00 39.49 C ANISOU 302 CD1 LEU A 210 4939 4259 5807 -148 175 61 C ATOM 303 CD2 LEU A 210 -3.322 9.048 43.449 1.00 49.73 C ANISOU 303 CD2 LEU A 210 6181 5456 7256 -237 191 151 C ATOM 304 N GLU A 211 -2.648 9.541 38.298 1.00 28.07 N ANISOU 304 N GLU A 211 3403 2724 4540 -154 51 -237 N ATOM 305 CA GLU A 211 -1.934 8.673 37.368 1.00 32.77 C ANISOU 305 CA GLU A 211 3994 3270 5186 -126 0 -312 C ATOM 306 C GLU A 211 -1.031 9.492 36.453 1.00 33.49 C ANISOU 306 C GLU A 211 4093 3439 5191 -64 -15 -368 C ATOM 307 O GLU A 211 0.145 9.173 36.276 1.00 36.69 O ANISOU 307 O GLU A 211 4521 3832 5589 -26 -39 -385 O ATOM 308 CB GLU A 211 -2.920 7.841 36.544 1.00 26.00 C ANISOU 308 CB GLU A 211 3085 2371 4422 -153 -33 -385 C ATOM 309 CG GLU A 211 -3.720 6.844 37.369 1.00 48.14 C ANISOU 309 CG GLU A 211 5874 5080 7338 -220 -26 -325 C ATOM 310 CD GLU A 211 -4.801 6.146 36.565 1.00 64.22 C ANISOU 310 CD GLU A 211 7849 7078 9474 -254 -59 -403 C ATOM 311 OE1 GLU A 211 -4.815 6.292 35.324 1.00 62.57 O ANISOU 311 OE1 GLU A 211 7612 6914 9247 -215 -96 -516 O ATOM 312 OE2 GLU A 211 -5.639 5.449 37.177 1.00 64.00 O ANISOU 312 OE2 GLU A 211 7795 6980 9541 -319 -48 -350 O ATOM 313 N THR A 212 -1.591 10.549 35.872 1.00 30.65 N ANISOU 313 N THR A 212 3711 3165 4770 -54 1 -391 N ATOM 314 CA THR A 212 -0.821 11.477 35.056 1.00 33.16 C ANISOU 314 CA THR A 212 4029 3564 5006 0 -3 -420 C ATOM 315 C THR A 212 0.326 12.048 35.880 1.00 30.68 C ANISOU 315 C THR A 212 3761 3255 4640 14 16 -357 C ATOM 316 O THR A 212 1.441 12.225 35.389 1.00 30.53 O ANISOU 316 O THR A 212 3749 3267 4586 55 0 -375 O ATOM 317 CB THR A 212 -1.699 12.643 34.568 1.00 33.44 C ANISOU 317 CB THR A 212 4037 3682 4986 5 20 -425 C ATOM 318 OG1 THR A 212 -2.737 12.142 33.717 1.00 37.88 O ANISOU 318 OG1 THR A 212 4550 4254 5588 -1 0 -494 O ATOM 319 CG2 THR A 212 -0.865 13.658 33.803 1.00 27.16 C ANISOU 319 CG2 THR A 212 3241 2966 4113 57 21 -430 C ATOM 320 N LEU A 213 0.032 12.322 37.145 1.00 25.04 N ANISOU 320 N LEU A 213 3071 2520 3922 -19 49 -286 N ATOM 321 CA LEU A 213 0.986 12.933 38.062 1.00 32.03 C ANISOU 321 CA LEU A 213 3994 3417 4758 -6 66 -233 C ATOM 322 C LEU A 213 2.133 11.984 38.408 1.00 37.86 C ANISOU 322 C LEU A 213 4759 4104 5521 10 44 -224 C ATOM 323 O LEU A 213 3.265 12.419 38.613 1.00 35.82 O ANISOU 323 O LEU A 213 4522 3870 5218 37 42 -212 O ATOM 324 CB LEU A 213 0.258 13.386 39.330 1.00 28.77 C ANISOU 324 CB LEU A 213 3592 3009 4331 -36 103 -170 C ATOM 325 CG LEU A 213 0.968 14.312 40.317 1.00 35.01 C ANISOU 325 CG LEU A 213 4411 3831 5061 -19 121 -129 C ATOM 326 CD1 LEU A 213 1.613 15.489 39.603 1.00 23.47 C ANISOU 326 CD1 LEU A 213 2946 2415 3554 10 114 -158 C ATOM 327 CD2 LEU A 213 -0.020 14.794 41.369 1.00 35.30 C ANISOU 327 CD2 LEU A 213 4442 3893 5077 -39 153 -87 C ATOM 328 N ARG A 214 1.837 10.689 38.474 1.00 37.62 N ANISOU 328 N ARG A 214 4725 4001 5567 -8 26 -229 N ATOM 329 CA ARG A 214 2.869 9.685 38.717 1.00 36.31 C ANISOU 329 CA ARG A 214 4583 3777 5435 13 0 -224 C ATOM 330 C ARG A 214 3.826 9.612 37.534 1.00 36.98 C ANISOU 330 C ARG A 214 4658 3892 5500 64 -38 -300 C ATOM 331 O ARG A 214 5.045 9.626 37.702 1.00 38.77 O ANISOU 331 O ARG A 214 4905 4132 5692 99 -48 -293 O ATOM 332 CB ARG A 214 2.245 8.307 38.949 1.00 38.38 C ANISOU 332 CB ARG A 214 4837 3941 5804 -19 -16 -214 C ATOM 333 CG ARG A 214 1.470 8.164 40.247 1.00 37.94 C ANISOU 333 CG ARG A 214 4788 3858 5770 -66 23 -117 C ATOM 334 CD ARG A 214 1.013 6.727 40.441 1.00 37.67 C ANISOU 334 CD ARG A 214 4743 3712 5858 -99 5 -94 C ATOM 335 NE ARG A 214 0.255 6.545 41.675 1.00 43.85 N ANISOU 335 NE ARG A 214 5521 4479 6661 -144 47 15 N ATOM 336 CZ ARG A 214 -1.063 6.383 41.726 1.00 45.92 C ANISOU 336 CZ ARG A 214 5745 4728 6976 -198 64 35 C ATOM 337 NH1 ARG A 214 -1.775 6.376 40.607 1.00 47.91 N ANISOU 337 NH1 ARG A 214 5960 4977 7267 -214 40 -54 N ATOM 338 NH2 ARG A 214 -1.670 6.223 42.893 1.00 40.59 N ANISOU 338 NH2 ARG A 214 5059 4053 6308 -233 106 146 N ATOM 339 N ARG A 215 3.258 9.533 36.336 1.00 32.71 N ANISOU 339 N ARG A 215 4078 3374 4975 73 -60 -374 N ATOM 340 CA ARG A 215 4.039 9.406 35.113 1.00 29.20 C ANISOU 340 CA ARG A 215 3611 2978 4506 129 -97 -451 C ATOM 341 C ARG A 215 4.953 10.609 34.879 1.00 33.78 C ANISOU 341 C ARG A 215 4193 3652 4989 161 -79 -430 C ATOM 342 O ARG A 215 6.175 10.470 34.848 1.00 41.19 O ANISOU 342 O ARG A 215 5142 4607 5901 197 -94 -433 O ATOM 343 CB ARG A 215 3.111 9.193 33.914 1.00 31.87 C ANISOU 343 CB ARG A 215 3898 3341 4868 137 -122 -534 C ATOM 344 CG ARG A 215 3.785 9.336 32.563 1.00 34.51 C ANISOU 344 CG ARG A 215 4196 3767 5149 205 -153 -611 C ATOM 345 CD ARG A 215 2.874 8.857 31.442 1.00 32.48 C ANISOU 345 CD ARG A 215 3886 3531 4926 221 -187 -709 C ATOM 346 NE ARG A 215 1.520 9.396 31.556 1.00 38.48 N ANISOU 346 NE ARG A 215 4629 4298 5694 174 -157 -689 N ATOM 347 CZ ARG A 215 1.122 10.547 31.022 1.00 36.64 C ANISOU 347 CZ ARG A 215 4372 4164 5385 187 -130 -676 C ATOM 348 NH1 ARG A 215 1.976 11.296 30.335 1.00 22.44 N ANISOU 348 NH1 ARG A 215 2560 2464 3501 240 -126 -670 N ATOM 349 NH2 ARG A 215 -0.131 10.952 31.177 1.00 29.86 N ANISOU 349 NH2 ARG A 215 3498 3307 4538 148 -106 -662 N ATOM 350 N VAL A 216 4.360 11.788 34.719 1.00 35.93 N ANISOU 350 N VAL A 216 4452 3984 5217 146 -48 -407 N ATOM 351 CA VAL A 216 5.137 12.987 34.420 1.00 41.42 C ANISOU 351 CA VAL A 216 5142 4759 5838 169 -32 -381 C ATOM 352 C VAL A 216 5.906 13.486 35.641 1.00 31.99 C ANISOU 352 C VAL A 216 3986 3544 4624 154 -11 -317 C ATOM 353 O VAL A 216 7.017 13.999 35.515 1.00 23.10 O ANISOU 353 O VAL A 216 2858 2460 3458 177 -12 -304 O ATOM 354 CB VAL A 216 4.252 14.122 33.861 1.00 41.32 C ANISOU 354 CB VAL A 216 5101 4806 5793 163 -8 -372 C ATOM 355 CG1 VAL A 216 3.265 13.571 32.842 1.00 32.08 C ANISOU 355 CG1 VAL A 216 3890 3655 4645 174 -27 -439 C ATOM 356 CG2 VAL A 216 3.516 14.828 34.982 1.00 46.71 C ANISOU 356 CG2 VAL A 216 5810 5456 6481 118 27 -317 C ATOM 357 N GLY A 217 5.311 13.326 36.820 1.00 29.96 N ANISOU 357 N GLY A 217 3757 3230 4394 116 8 -277 N ATOM 358 CA GLY A 217 5.935 13.760 38.057 1.00 29.25 C ANISOU 358 CA GLY A 217 3700 3131 4281 108 25 -224 C ATOM 359 C GLY A 217 7.237 13.034 38.340 1.00 32.72 C ANISOU 359 C GLY A 217 4158 3555 4720 136 3 -225 C ATOM 360 O GLY A 217 8.263 13.663 38.600 1.00 33.17 O ANISOU 360 O GLY A 217 4220 3646 4736 152 4 -210 O ATOM 361 N ASP A 218 7.197 11.706 38.294 1.00 29.12 N ANISOU 361 N ASP A 218 3710 3042 4314 143 -20 -243 N ATOM 362 CA ASP A 218 8.395 10.901 38.498 1.00 33.84 C ANISOU 362 CA ASP A 218 4325 3619 4915 179 -45 -248 C ATOM 363 C ASP A 218 9.425 11.201 37.413 1.00 32.91 C ANISOU 363 C ASP A 218 4180 3570 4754 223 -67 -294 C ATOM 364 O ASP A 218 10.630 11.174 37.660 1.00 37.37 O ANISOU 364 O ASP A 218 4754 4158 5289 252 -77 -288 O ATOM 365 CB ASP A 218 8.050 9.409 38.502 1.00 31.59 C ANISOU 365 CB ASP A 218 4047 3247 4709 180 -72 -264 C ATOM 366 CG ASP A 218 7.130 9.023 39.646 1.00 46.80 C ANISOU 366 CG ASP A 218 5993 5110 6681 136 -46 -197 C ATOM 367 OD1 ASP A 218 6.907 9.860 40.545 1.00 47.19 O ANISOU 367 OD1 ASP A 218 6052 5193 6686 116 -10 -143 O ATOM 368 OD2 ASP A 218 6.629 7.879 39.647 1.00 58.44 O ANISOU 368 OD2 ASP A 218 7466 6501 8237 123 -64 -199 O ATOM 369 N GLY A 219 8.939 11.491 36.210 1.00 32.49 N ANISOU 369 N GLY A 219 4090 3561 4694 230 -73 -338 N ATOM 370 CA GLY A 219 9.806 11.813 35.091 1.00 33.19 C ANISOU 370 CA GLY A 219 4143 3735 4734 276 -89 -374 C ATOM 371 C GLY A 219 10.616 13.076 35.323 1.00 38.28 C ANISOU 371 C GLY A 219 4782 4441 5323 271 -65 -325 C ATOM 372 O GLY A 219 11.821 13.105 35.064 1.00 37.11 O ANISOU 372 O GLY A 219 4618 4341 5139 304 -78 -329 O ATOM 373 N VAL A 220 9.953 14.122 35.809 1.00 35.45 N ANISOU 373 N VAL A 220 4430 4078 4961 230 -33 -283 N ATOM 374 CA VAL A 220 10.617 15.387 36.111 1.00 31.44 C ANISOU 374 CA VAL A 220 3916 3610 4422 218 -15 -240 C ATOM 375 C VAL A 220 11.727 15.194 37.142 1.00 30.16 C ANISOU 375 C VAL A 220 3778 3432 4251 223 -22 -224 C ATOM 376 O VAL A 220 12.828 15.727 36.988 1.00 33.02 O ANISOU 376 O VAL A 220 4119 3842 4586 235 -26 -213 O ATOM 377 CB VAL A 220 9.619 16.441 36.632 1.00 31.08 C ANISOU 377 CB VAL A 220 3879 3545 4387 178 13 -208 C ATOM 378 CG1 VAL A 220 10.357 17.665 37.150 1.00 29.42 C ANISOU 378 CG1 VAL A 220 3665 3352 4163 164 23 -173 C ATOM 379 CG2 VAL A 220 8.651 16.842 35.538 1.00 37.86 C ANISOU 379 CG2 VAL A 220 4705 4435 5243 179 21 -219 C ATOM 380 N GLN A 221 11.431 14.429 38.189 1.00 31.53 N ANISOU 380 N GLN A 221 3990 3542 4446 215 -23 -217 N ATOM 381 CA GLN A 221 12.395 14.167 39.254 1.00 30.22 C ANISOU 381 CA GLN A 221 3848 3368 4268 227 -30 -200 C ATOM 382 C GLN A 221 13.604 13.386 38.743 1.00 35.81 C ANISOU 382 C GLN A 221 4545 4100 4960 273 -58 -227 C ATOM 383 O GLN A 221 14.742 13.676 39.114 1.00 48.28 O ANISOU 383 O GLN A 221 6118 5715 6509 289 -64 -220 O ATOM 384 CB GLN A 221 11.725 13.426 40.417 1.00 29.82 C ANISOU 384 CB GLN A 221 3835 3254 4242 216 -21 -174 C ATOM 385 CG GLN A 221 10.685 14.259 41.162 1.00 34.63 C ANISOU 385 CG GLN A 221 4451 3857 4850 179 8 -146 C ATOM 386 CD GLN A 221 9.965 13.480 42.249 1.00 40.42 C ANISOU 386 CD GLN A 221 5210 4545 5602 170 20 -108 C ATOM 387 OE1 GLN A 221 9.833 12.261 42.175 1.00 61.50 O ANISOU 387 OE1 GLN A 221 7892 7166 8310 177 9 -102 O ATOM 388 NE2 GLN A 221 9.485 14.188 43.260 1.00 57.11 N ANISOU 388 NE2 GLN A 221 7330 6677 7693 156 42 -81 N ATOM 389 N ARG A 222 13.351 12.394 37.893 1.00 29.53 N ANISOU 389 N ARG A 222 3743 3290 4188 298 -80 -266 N ATOM 390 CA ARG A 222 14.422 11.622 37.271 1.00 37.58 C ANISOU 390 CA ARG A 222 4747 4340 5192 353 -113 -306 C ATOM 391 C ARG A 222 15.278 12.500 36.370 1.00 40.27 C ANISOU 391 C ARG A 222 5039 4783 5480 370 -111 -311 C ATOM 392 O ARG A 222 16.504 12.522 36.484 1.00 41.61 O ANISOU 392 O ARG A 222 5196 4999 5616 397 -122 -309 O ATOM 393 CB ARG A 222 13.847 10.477 36.434 1.00 46.12 C ANISOU 393 CB ARG A 222 5822 5385 6314 379 -142 -363 C ATOM 394 CG ARG A 222 13.501 9.226 37.221 1.00 56.40 C ANISOU 394 CG ARG A 222 7166 6582 7681 379 -159 -360 C ATOM 395 CD ARG A 222 13.307 8.034 36.294 1.00 57.98 C ANISOU 395 CD ARG A 222 7352 6747 7930 418 -203 -434 C ATOM 396 NE ARG A 222 12.269 8.283 35.297 1.00 59.98 N ANISOU 396 NE ARG A 222 7572 7020 8197 403 -203 -476 N ATOM 397 CZ ARG A 222 10.972 8.092 35.511 1.00 63.16 C ANISOU 397 CZ ARG A 222 7984 7355 8659 357 -192 -467 C ATOM 398 NH1 ARG A 222 10.551 7.649 36.688 1.00 65.76 N ANISOU 398 NH1 ARG A 222 8353 7593 9040 319 -178 -410 N ATOM 399 NH2 ARG A 222 10.095 8.343 34.549 1.00 53.06 N ANISOU 399 NH2 ARG A 222 6668 6108 7383 351 -195 -512 N ATOM 400 N ASN A 223 14.613 13.219 35.472 1.00 33.71 N ANISOU 400 N ASN A 223 4174 3992 4641 355 -96 -310 N ATOM 401 CA ASN A 223 15.287 13.980 34.426 1.00 29.20 C ANISOU 401 CA ASN A 223 3547 3525 4024 375 -92 -303 C ATOM 402 C ASN A 223 15.962 15.257 34.917 1.00 29.68 C ANISOU 402 C ASN A 223 3594 3614 4070 340 -69 -246 C ATOM 403 O ASN A 223 16.803 15.827 34.224 1.00 34.47 O ANISOU 403 O ASN A 223 4150 4305 4643 354 -66 -226 O ATOM 404 CB ASN A 223 14.304 14.289 33.295 1.00 40.43 C ANISOU 404 CB ASN A 223 4935 4984 5441 377 -84 -315 C ATOM 405 CG ASN A 223 13.767 13.032 32.636 1.00 41.93 C ANISOU 405 CG ASN A 223 5122 5160 5648 418 -116 -390 C ATOM 406 OD1 ASN A 223 12.610 12.974 32.226 1.00 52.97 O ANISOU 406 OD1 ASN A 223 6517 6541 7069 407 -114 -411 O ATOM 407 ND2 ASN A 223 14.609 12.011 32.542 1.00 40.54 N ANISOU 407 ND2 ASN A 223 4947 4991 5466 468 -151 -437 N ATOM 408 N HIS A 224 15.600 15.697 36.117 1.00 25.81 N ANISOU 408 N HIS A 224 3143 3056 3607 297 -55 -220 N ATOM 409 CA HIS A 224 16.193 16.898 36.694 1.00 30.98 C ANISOU 409 CA HIS A 224 3785 3724 4262 264 -42 -181 C ATOM 410 C HIS A 224 16.675 16.654 38.114 1.00 28.47 C ANISOU 410 C HIS A 224 3505 3365 3947 260 -50 -185 C ATOM 411 O HIS A 224 16.562 17.525 38.976 1.00 30.79 O ANISOU 411 O HIS A 224 3807 3635 4256 228 -40 -168 O ATOM 412 CB HIS A 224 15.193 18.052 36.666 1.00 28.99 C ANISOU 412 CB HIS A 224 3530 3448 4037 221 -18 -152 C ATOM 413 CG HIS A 224 14.708 18.386 35.292 1.00 28.65 C ANISOU 413 CG HIS A 224 3447 3455 3985 230 -8 -139 C ATOM 414 ND1 HIS A 224 15.416 19.193 34.430 1.00 31.96 N ANISOU 414 ND1 HIS A 224 3809 3946 4390 233 0 -99 N ATOM 415 CD2 HIS A 224 13.589 18.011 34.627 1.00 26.35 C ANISOU 415 CD2 HIS A 224 3158 3160 3695 241 -4 -158 C ATOM 416 CE1 HIS A 224 14.752 19.307 33.292 1.00 25.70 C ANISOU 416 CE1 HIS A 224 2985 3199 3581 250 10 -90 C ATOM 417 NE2 HIS A 224 13.643 18.600 33.387 1.00 23.28 N ANISOU 417 NE2 HIS A 224 2713 2847 3283 256 6 -132 N ATOM 418 N GLU A 225 17.219 15.464 38.345 1.00 27.87 N ANISOU 418 N GLU A 225 3448 3285 3856 300 -70 -209 N ATOM 419 CA GLU A 225 17.722 15.086 39.659 1.00 38.57 C ANISOU 419 CA GLU A 225 4835 4613 5205 309 -78 -208 C ATOM 420 C GLU A 225 18.842 16.012 40.128 1.00 34.91 C ANISOU 420 C GLU A 225 4344 4198 4724 299 -81 -200 C ATOM 421 O GLU A 225 18.882 16.408 41.292 1.00 37.54 O ANISOU 421 O GLU A 225 4694 4513 5058 286 -79 -196 O ATOM 422 CB GLU A 225 18.206 13.635 39.645 1.00 48.78 C ANISOU 422 CB GLU A 225 6149 5897 6490 362 -103 -232 C ATOM 423 CG GLU A 225 18.818 13.170 40.955 1.00 59.95 C ANISOU 423 CG GLU A 225 7593 7294 7890 383 -111 -221 C ATOM 424 CD GLU A 225 19.273 11.726 40.904 1.00 72.84 C ANISOU 424 CD GLU A 225 9246 8905 9524 439 -138 -239 C ATOM 425 OE1 GLU A 225 18.623 10.920 40.205 1.00 71.72 O ANISOU 425 OE1 GLU A 225 9113 8720 9415 450 -148 -259 O ATOM 426 OE2 GLU A 225 20.279 11.395 41.566 1.00 85.10 O ANISOU 426 OE2 GLU A 225 10804 10482 11048 474 -152 -238 O ATOM 427 N THR A 226 19.749 16.356 39.218 1.00 27.39 N ANISOU 427 N THR A 226 3339 3312 3754 308 -87 -199 N ATOM 428 CA THR A 226 20.886 17.206 39.560 1.00 33.02 C ANISOU 428 CA THR A 226 4014 4072 4462 293 -93 -191 C ATOM 429 C THR A 226 20.445 18.604 39.989 1.00 35.57 C ANISOU 429 C THR A 226 4326 4363 4825 237 -80 -172 C ATOM 430 O THR A 226 20.894 19.118 41.014 1.00 34.04 O ANISOU 430 O THR A 226 4132 4163 4640 224 -89 -185 O ATOM 431 CB THR A 226 21.889 17.316 38.393 1.00 37.80 C ANISOU 431 CB THR A 226 4555 4765 5042 310 -97 -182 C ATOM 432 OG1 THR A 226 22.457 16.028 38.127 1.00 35.41 O ANISOU 432 OG1 THR A 226 4260 4495 4699 372 -118 -214 O ATOM 433 CG2 THR A 226 23.005 18.290 38.738 1.00 34.67 C ANISOU 433 CG2 THR A 226 4109 4409 4653 282 -102 -167 C ATOM 434 N ALA A 227 19.563 19.215 39.204 1.00 29.45 N ANISOU 434 N ALA A 227 3540 3573 4077 210 -61 -148 N ATOM 435 CA ALA A 227 19.053 20.544 39.524 1.00 30.68 C ANISOU 435 CA ALA A 227 3687 3690 4281 161 -52 -131 C ATOM 436 C ALA A 227 18.224 20.523 40.806 1.00 30.14 C ANISOU 436 C ALA A 227 3669 3562 4220 157 -53 -157 C ATOM 437 O ALA A 227 18.339 21.416 41.646 1.00 29.15 O ANISOU 437 O ALA A 227 3538 3416 4121 136 -62 -171 O ATOM 438 CB ALA A 227 18.235 21.095 38.364 1.00 31.18 C ANISOU 438 CB ALA A 227 3729 3753 4365 144 -32 -94 C ATOM 439 N PHE A 228 17.391 19.495 40.949 1.00 29.05 N ANISOU 439 N PHE A 228 3577 3401 4061 180 -46 -164 N ATOM 440 CA PHE A 228 16.546 19.342 42.131 1.00 29.49 C ANISOU 440 CA PHE A 228 3674 3415 4114 180 -41 -176 C ATOM 441 C PHE A 228 17.365 19.217 43.413 1.00 33.03 C ANISOU 441 C PHE A 228 4130 3882 4539 201 -58 -197 C ATOM 442 O PHE A 228 17.040 19.838 44.425 1.00 32.05 O ANISOU 442 O PHE A 228 4012 3749 4417 195 -61 -213 O ATOM 443 CB PHE A 228 15.622 18.131 41.975 1.00 29.58 C ANISOU 443 CB PHE A 228 3723 3400 4117 197 -30 -169 C ATOM 444 CG PHE A 228 14.315 18.449 41.308 1.00 33.60 C ANISOU 444 CG PHE A 228 4234 3883 4650 173 -12 -159 C ATOM 445 CD1 PHE A 228 14.258 19.340 40.251 1.00 32.88 C ANISOU 445 CD1 PHE A 228 4107 3809 4576 155 -6 -148 C ATOM 446 CD2 PHE A 228 13.142 17.844 41.730 1.00 39.66 C ANISOU 446 CD2 PHE A 228 5033 4614 5422 171 1 -154 C ATOM 447 CE1 PHE A 228 13.056 19.634 39.635 1.00 34.04 C ANISOU 447 CE1 PHE A 228 4254 3940 4740 140 10 -139 C ATOM 448 CE2 PHE A 228 11.938 18.130 41.116 1.00 35.95 C ANISOU 448 CE2 PHE A 228 4560 4127 4972 151 17 -149 C ATOM 449 CZ PHE A 228 11.894 19.026 40.067 1.00 33.13 C ANISOU 449 CZ PHE A 228 4171 3790 4627 138 20 -145 C ATOM 450 N GLN A 229 18.423 18.412 43.367 1.00 32.96 N ANISOU 450 N GLN A 229 4116 3906 4500 233 -72 -201 N ATOM 451 CA GLN A 229 19.297 18.229 44.523 1.00 34.73 C ANISOU 451 CA GLN A 229 4342 4160 4692 262 -90 -221 C ATOM 452 C GLN A 229 19.913 19.553 44.962 1.00 30.03 C ANISOU 452 C GLN A 229 3706 3585 4118 237 -105 -249 C ATOM 453 O GLN A 229 20.043 19.821 46.155 1.00 44.57 O ANISOU 453 O GLN A 229 5552 5441 5944 251 -118 -278 O ATOM 454 CB GLN A 229 20.397 17.210 44.217 1.00 29.89 C ANISOU 454 CB GLN A 229 3725 3584 4047 303 -104 -223 C ATOM 455 CG GLN A 229 19.909 15.772 44.125 1.00 45.84 C ANISOU 455 CG GLN A 229 5788 5572 6055 338 -100 -205 C ATOM 456 CD GLN A 229 20.988 14.819 43.645 1.00 56.80 C ANISOU 456 CD GLN A 229 7169 6993 7420 384 -120 -216 C ATOM 457 OE1 GLN A 229 20.820 13.600 43.686 1.00 56.24 O ANISOU 457 OE1 GLN A 229 7131 6891 7347 421 -126 -208 O ATOM 458 NE2 GLN A 229 22.105 15.373 43.186 1.00 63.37 N ANISOU 458 NE2 GLN A 229 7952 7886 8238 383 -132 -233 N ATOM 459 N GLY A 230 20.292 20.376 43.989 1.00 40.67 N ANISOU 459 N GLY A 230 5011 4936 5505 201 -106 -240 N ATOM 460 CA GLY A 230 20.848 21.686 44.274 1.00 35.99 C ANISOU 460 CA GLY A 230 4373 4345 4957 167 -124 -262 C ATOM 461 C GLY A 230 19.814 22.615 44.881 1.00 38.56 C ANISOU 461 C GLY A 230 4711 4620 5320 145 -124 -281 C ATOM 462 O GLY A 230 20.103 23.343 45.831 1.00 35.75 O ANISOU 462 O GLY A 230 4338 4264 4981 143 -148 -329 O ATOM 463 N MET A 231 18.604 22.584 44.331 1.00 34.45 N ANISOU 463 N MET A 231 4217 4061 4810 134 -100 -253 N ATOM 464 CA MET A 231 17.508 23.411 44.829 1.00 34.33 C ANISOU 464 CA MET A 231 4215 4004 4826 120 -98 -271 C ATOM 465 C MET A 231 17.128 23.041 46.259 1.00 29.51 C ANISOU 465 C MET A 231 3634 3411 4168 157 -105 -308 C ATOM 466 O MET A 231 16.892 23.914 47.094 1.00 34.21 O ANISOU 466 O MET A 231 4219 3999 4782 159 -123 -354 O ATOM 467 CB MET A 231 16.287 23.291 43.914 1.00 36.29 C ANISOU 467 CB MET A 231 4484 4221 5083 107 -69 -231 C ATOM 468 CG MET A 231 16.380 24.115 42.640 1.00 39.87 C ANISOU 468 CG MET A 231 4900 4659 5590 72 -63 -193 C ATOM 469 SD MET A 231 14.954 23.883 41.560 1.00 46.26 S ANISOU 469 SD MET A 231 5728 5451 6396 69 -31 -153 S ATOM 470 CE MET A 231 15.377 22.339 40.771 1.00 27.57 C ANISOU 470 CE MET A 231 3369 3133 3972 98 -21 -137 C ATOM 471 N LEU A 232 17.066 21.742 46.533 1.00 35.44 N ANISOU 471 N LEU A 232 4417 4187 4860 191 -91 -288 N ATOM 472 CA LEU A 232 16.752 21.254 47.871 1.00 41.75 C ANISOU 472 CA LEU A 232 5240 5018 5606 233 -91 -302 C ATOM 473 C LEU A 232 17.813 21.717 48.859 1.00 46.71 C ANISOU 473 C LEU A 232 5839 5693 6217 257 -125 -357 C ATOM 474 O LEU A 232 17.532 21.946 50.036 1.00 45.07 O ANISOU 474 O LEU A 232 5630 5519 5974 290 -134 -392 O ATOM 475 CB LEU A 232 16.671 19.726 47.873 1.00 36.48 C ANISOU 475 CB LEU A 232 4608 4358 4894 262 -73 -256 C ATOM 476 CG LEU A 232 16.467 19.052 49.232 1.00 40.82 C ANISOU 476 CG LEU A 232 5177 4949 5384 310 -68 -247 C ATOM 477 CD1 LEU A 232 15.120 19.436 49.824 1.00 44.08 C ANISOU 477 CD1 LEU A 232 5599 5359 5790 308 -51 -243 C ATOM 478 CD2 LEU A 232 16.589 17.542 49.107 1.00 46.50 C ANISOU 478 CD2 LEU A 232 5927 5660 6081 335 -55 -193 C ATOM 479 N ARG A 233 19.036 21.857 48.362 1.00 49.60 N ANISOU 479 N ARG A 233 6173 6070 6602 245 -143 -366 N ATOM 480 CA ARG A 233 20.173 22.223 49.192 1.00 53.61 C ANISOU 480 CA ARG A 233 6646 6628 7097 266 -177 -422 C ATOM 481 C ARG A 233 20.113 23.697 49.578 1.00 45.58 C ANISOU 481 C ARG A 233 5590 5588 6140 241 -207 -486 C ATOM 482 O ARG A 233 20.359 24.056 50.729 1.00 48.15 O ANISOU 482 O ARG A 233 5897 5955 6443 274 -236 -551 O ATOM 483 CB ARG A 233 21.471 21.918 48.445 1.00 64.97 C ANISOU 483 CB ARG A 233 8056 8089 8542 257 -186 -409 C ATOM 484 CG ARG A 233 22.624 21.477 49.324 1.00 70.35 C ANISOU 484 CG ARG A 233 8719 8841 9169 304 -211 -444 C ATOM 485 CD ARG A 233 23.519 20.521 48.556 1.00 72.65 C ANISOU 485 CD ARG A 233 9009 9159 9436 318 -205 -408 C ATOM 486 NE ARG A 233 23.824 21.030 47.222 1.00 80.27 N ANISOU 486 NE ARG A 233 9940 10101 10458 265 -199 -384 N ATOM 487 CZ ARG A 233 24.041 20.261 46.160 1.00 84.13 C ANISOU 487 CZ ARG A 233 10434 10597 10933 270 -184 -341 C ATOM 488 NH1 ARG A 233 23.977 18.941 46.269 1.00 83.45 N ANISOU 488 NH1 ARG A 233 10391 10524 10792 322 -176 -323 N ATOM 489 NH2 ARG A 233 24.312 20.813 44.984 1.00 80.80 N ANISOU 489 NH2 ARG A 233 9973 10174 10556 228 -177 -314 N ATOM 490 N LYS A 234 19.781 24.547 48.612 1.00 44.84 N ANISOU 490 N LYS A 234 5481 5430 6125 186 -203 -468 N ATOM 491 CA LYS A 234 19.687 25.981 48.863 1.00 41.30 C ANISOU 491 CA LYS A 234 4997 4939 5757 158 -234 -524 C ATOM 492 C LYS A 234 18.437 26.329 49.663 1.00 41.76 C ANISOU 492 C LYS A 234 5080 4987 5800 185 -235 -560 C ATOM 493 O LYS A 234 18.401 27.339 50.365 1.00 45.74 O ANISOU 493 O LYS A 234 5556 5479 6345 190 -273 -637 O ATOM 494 CB LYS A 234 19.718 26.768 47.551 1.00 37.12 C ANISOU 494 CB LYS A 234 4441 4343 5320 94 -227 -477 C ATOM 495 CG LYS A 234 21.046 26.686 46.821 1.00 49.51 C ANISOU 495 CG LYS A 234 5966 5934 6912 66 -231 -446 C ATOM 496 CD LYS A 234 21.285 27.914 45.958 1.00 54.61 C ANISOU 496 CD LYS A 234 6561 6518 7672 2 -240 -418 C ATOM 497 CE LYS A 234 22.731 27.977 45.489 1.00 58.79 C ANISOU 497 CE LYS A 234 7029 7081 8227 -26 -251 -398 C ATOM 498 NZ LYS A 234 23.071 29.303 44.901 1.00 65.77 N ANISOU 498 NZ LYS A 234 7851 7901 9239 -92 -266 -372 N ATOM 499 N LEU A 235 17.414 25.487 49.554 1.00 40.80 N ANISOU 499 N LEU A 235 5006 4873 5622 203 -196 -510 N ATOM 500 CA LEU A 235 16.182 25.691 50.302 1.00 39.13 C ANISOU 500 CA LEU A 235 4814 4670 5383 232 -191 -534 C ATOM 501 C LEU A 235 16.443 25.504 51.792 1.00 46.07 C ANISOU 501 C LEU A 235 5683 5631 6190 295 -213 -594 C ATOM 502 O LEU A 235 15.867 26.203 52.625 1.00 47.98 O ANISOU 502 O LEU A 235 5912 5892 6426 325 -234 -658 O ATOM 503 CB LEU A 235 15.101 24.718 49.829 1.00 40.70 C ANISOU 503 CB LEU A 235 5059 4864 5542 232 -143 -458 C ATOM 504 CG LEU A 235 13.674 24.994 50.307 1.00 41.71 C ANISOU 504 CG LEU A 235 5202 4995 5652 250 -129 -467 C ATOM 505 CD1 LEU A 235 13.185 26.337 49.787 1.00 37.19 C ANISOU 505 CD1 LEU A 235 4612 4358 5162 218 -146 -499 C ATOM 506 CD2 LEU A 235 12.738 23.879 49.871 1.00 42.58 C ANISOU 506 CD2 LEU A 235 5350 5104 5725 246 -83 -391 C ATOM 507 N ASP A 236 17.321 24.557 52.115 1.00 56.89 N ANISOU 507 N ASP A 236 7056 7057 7501 323 -210 -576 N ATOM 508 CA ASP A 236 17.681 24.265 53.499 1.00 64.64 C ANISOU 508 CA ASP A 236 8024 8133 8401 392 -229 -622 C ATOM 509 C ASP A 236 16.455 24.269 54.413 1.00 65.82 C ANISOU 509 C ASP A 236 8186 8330 8492 438 -216 -630 C ATOM 510 O ASP A 236 16.420 24.976 55.421 1.00 63.98 O ANISOU 510 O ASP A 236 7920 8153 8237 482 -250 -715 O ATOM 511 CB ASP A 236 18.735 25.259 54.000 1.00 67.06 C ANISOU 511 CB ASP A 236 8276 8459 8746 397 -286 -725 C ATOM 512 CG ASP A 236 19.360 24.836 55.318 1.00 69.80 C ANISOU 512 CG ASP A 236 8601 8920 8998 475 -308 -773 C ATOM 513 OD1 ASP A 236 19.036 23.734 55.807 1.00 70.04 O ANISOU 513 OD1 ASP A 236 8663 9013 8937 523 -275 -711 O ATOM 514 OD2 ASP A 236 20.177 25.606 55.866 1.00 76.75 O ANISOU 514 OD2 ASP A 236 9431 9829 9902 489 -359 -871 O ATOM 515 N ILE A 237 15.452 23.474 54.048 1.00 63.29 N ANISOU 515 N ILE A 237 7905 7993 8148 429 -168 -545 N ATOM 516 CA ILE A 237 14.216 23.380 54.819 1.00 60.62 C ANISOU 516 CA ILE A 237 7575 7705 7754 466 -147 -533 C ATOM 517 C ILE A 237 14.447 22.643 56.137 1.00 64.57 C ANISOU 517 C ILE A 237 8065 8323 8146 544 -143 -522 C ATOM 518 O ILE A 237 14.959 21.523 56.156 1.00 67.37 O ANISOU 518 O ILE A 237 8438 8695 8464 556 -123 -454 O ATOM 519 CB ILE A 237 13.093 22.693 54.011 1.00 50.66 C ANISOU 519 CB ILE A 237 6352 6390 6506 428 -98 -441 C ATOM 520 CG1 ILE A 237 11.827 22.566 54.861 1.00 50.67 C ANISOU 520 CG1 ILE A 237 6351 6456 6445 466 -73 -422 C ATOM 521 CG2 ILE A 237 13.548 21.332 53.514 1.00 49.02 C ANISOU 521 CG2 ILE A 237 6173 6163 6287 416 -71 -356 C ATOM 522 CD1 ILE A 237 10.620 22.051 54.103 1.00 46.93 C ANISOU 522 CD1 ILE A 237 5905 5930 5995 424 -30 -346 C ATOM 523 N LYS A 238 14.064 23.282 57.238 1.00 65.54 N ANISOU 523 N LYS A 238 8155 8531 8217 602 -164 -590 N ATOM 524 CA LYS A 238 14.408 22.789 58.566 1.00 67.46 C ANISOU 524 CA LYS A 238 8374 8910 8349 688 -168 -595 C ATOM 525 C LYS A 238 13.398 21.796 59.143 1.00 64.75 C ANISOU 525 C LYS A 238 8045 8636 7921 724 -114 -489 C ATOM 526 O LYS A 238 13.777 20.863 59.854 1.00 62.83 O ANISOU 526 O LYS A 238 7799 8474 7599 776 -97 -427 O ATOM 527 CB LYS A 238 14.649 23.967 59.514 1.00 67.66 C ANISOU 527 CB LYS A 238 8345 9011 8353 745 -225 -735 C ATOM 528 CG LYS A 238 16.024 24.601 59.316 1.00 72.52 C ANISOU 528 CG LYS A 238 8933 9593 9029 728 -280 -828 C ATOM 529 CD LYS A 238 15.934 26.108 59.114 1.00 76.39 C ANISOU 529 CD LYS A 238 9392 10018 9616 701 -334 -951 C ATOM 530 CE LYS A 238 17.290 26.722 58.765 1.00 76.56 C ANISOU 530 CE LYS A 238 9381 9986 9721 665 -385 -1026 C ATOM 531 NZ LYS A 238 17.604 26.675 57.306 1.00 71.67 N ANISOU 531 NZ LYS A 238 8790 9235 9205 568 -365 -956 N ATOM 532 N ASN A 239 12.122 21.984 58.826 1.00 67.83 N ANISOU 532 N ASN A 239 8445 8994 8331 696 -87 -460 N ATOM 533 CA ASN A 239 11.085 21.069 59.296 1.00 67.64 C ANISOU 533 CA ASN A 239 8428 9030 8242 717 -33 -350 C ATOM 534 C ASN A 239 9.852 21.051 58.397 1.00 62.64 C ANISOU 534 C ASN A 239 7819 8310 7669 651 0 -301 C ATOM 535 O ASN A 239 9.797 21.753 57.386 1.00 60.07 O ANISOU 535 O ASN A 239 7508 7883 7432 593 -17 -349 O ATOM 536 CB ASN A 239 10.700 21.391 60.742 1.00 76.27 C ANISOU 536 CB ASN A 239 9471 10287 9220 813 -40 -386 C ATOM 537 CG ASN A 239 10.576 22.880 60.993 1.00 81.47 C ANISOU 537 CG ASN A 239 10094 10967 9894 837 -93 -537 C ATOM 538 OD1 ASN A 239 9.723 23.551 60.412 1.00 81.76 O ANISOU 538 OD1 ASN A 239 10138 10938 9990 798 -93 -565 O ATOM 539 ND2 ASN A 239 11.429 23.405 61.866 1.00 82.80 N ANISOU 539 ND2 ASN A 239 10222 11226 10014 907 -142 -640 N ATOM 540 N GLU A 240 8.867 20.243 58.775 1.00 59.36 N ANISOU 540 N GLU A 240 7404 7943 7208 660 49 -199 N ATOM 541 CA GLU A 240 7.665 20.066 57.971 1.00 55.28 C ANISOU 541 CA GLU A 240 6904 7354 6744 598 84 -145 C ATOM 542 C GLU A 240 6.857 21.355 57.862 1.00 54.46 C ANISOU 542 C GLU A 240 6781 7256 6656 598 65 -236 C ATOM 543 O GLU A 240 6.030 21.504 56.963 1.00 43.52 O ANISOU 543 O GLU A 240 5411 5794 5332 543 80 -222 O ATOM 544 CB GLU A 240 6.793 18.961 58.567 1.00 49.18 C ANISOU 544 CB GLU A 240 6123 6646 5919 612 138 -16 C ATOM 545 CG GLU A 240 6.189 19.325 59.912 1.00 54.01 C ANISOU 545 CG GLU A 240 6681 7421 6417 693 147 -23 C ATOM 546 CD GLU A 240 5.326 18.222 60.486 1.00 58.70 C ANISOU 546 CD GLU A 240 7258 8083 6962 701 206 125 C ATOM 547 OE1 GLU A 240 5.649 17.037 60.270 1.00 61.38 O ANISOU 547 OE1 GLU A 240 7622 8366 7334 672 231 232 O ATOM 548 OE2 GLU A 240 4.325 18.542 61.160 1.00 60.95 O ANISOU 548 OE2 GLU A 240 7500 8479 7181 737 227 135 O ATOM 549 N ASP A 241 7.102 22.284 58.781 1.00 57.26 N ANISOU 549 N ASP A 241 7098 7702 6956 667 27 -336 N ATOM 550 CA ASP A 241 6.335 23.524 58.842 1.00 58.07 C ANISOU 550 CA ASP A 241 7177 7818 7069 684 1 -432 C ATOM 551 C ASP A 241 7.048 24.675 58.141 1.00 50.02 C ANISOU 551 C ASP A 241 6164 6694 6145 654 -54 -544 C ATOM 552 O ASP A 241 6.445 25.712 57.866 1.00 46.99 O ANISOU 552 O ASP A 241 5772 6275 5805 650 -77 -615 O ATOM 553 CB ASP A 241 6.047 23.897 60.298 1.00 62.65 C ANISOU 553 CB ASP A 241 7702 8568 7533 786 -12 -485 C ATOM 554 CG ASP A 241 5.253 22.831 61.023 1.00 59.47 C ANISOU 554 CG ASP A 241 7281 8281 7033 817 48 -359 C ATOM 555 OD1 ASP A 241 4.472 22.123 60.355 1.00 60.80 O ANISOU 555 OD1 ASP A 241 7474 8389 7240 754 96 -254 O ATOM 556 OD2 ASP A 241 5.408 22.702 62.255 1.00 59.60 O ANISOU 556 OD2 ASP A 241 7254 8453 6937 906 46 -362 O ATOM 557 N ASP A 242 8.332 24.486 57.857 1.00 46.78 N ANISOU 557 N ASP A 242 5768 6236 5771 634 -76 -554 N ATOM 558 CA ASP A 242 9.137 25.523 57.224 1.00 44.96 C ANISOU 558 CA ASP A 242 5536 5910 5637 601 -127 -646 C ATOM 559 C ASP A 242 8.880 25.575 55.722 1.00 42.64 C ANISOU 559 C ASP A 242 5277 5480 5443 514 -109 -598 C ATOM 560 O ASP A 242 9.725 25.174 54.923 1.00 37.95 O ANISOU 560 O ASP A 242 4704 4818 4898 467 -106 -561 O ATOM 561 CB ASP A 242 10.624 25.285 57.498 1.00 53.01 C ANISOU 561 CB ASP A 242 6547 6944 6651 613 -155 -672 C ATOM 562 CG ASP A 242 11.492 26.443 57.050 1.00 56.13 C ANISOU 562 CG ASP A 242 6924 7257 7144 584 -213 -773 C ATOM 563 OD1 ASP A 242 10.942 27.534 56.788 1.00 57.59 O ANISOU 563 OD1 ASP A 242 7098 7388 7394 572 -239 -837 O ATOM 564 OD2 ASP A 242 12.724 26.262 56.962 1.00 55.43 O ANISOU 564 OD2 ASP A 242 6829 7158 7073 573 -233 -784 O ATOM 565 N VAL A 243 7.707 26.077 55.347 1.00 34.75 N ANISOU 565 N VAL A 243 4281 4454 4469 500 -97 -600 N ATOM 566 CA VAL A 243 7.309 26.138 53.946 1.00 36.69 C ANISOU 566 CA VAL A 243 4555 4590 4797 429 -77 -553 C ATOM 567 C VAL A 243 7.238 27.576 53.445 1.00 35.25 C ANISOU 567 C VAL A 243 4360 4331 4704 415 -118 -631 C ATOM 568 O VAL A 243 6.885 27.822 52.292 1.00 40.70 O ANISOU 568 O VAL A 243 5067 4937 5462 364 -106 -596 O ATOM 569 CB VAL A 243 5.938 25.470 53.725 1.00 42.76 C ANISOU 569 CB VAL A 243 5336 5378 5532 418 -26 -476 C ATOM 570 CG1 VAL A 243 6.000 23.993 54.086 1.00 32.82 C ANISOU 570 CG1 VAL A 243 4089 4169 4211 420 15 -382 C ATOM 571 CG2 VAL A 243 4.866 26.179 54.540 1.00 44.11 C ANISOU 571 CG2 VAL A 243 5479 5623 5657 471 -33 -529 C ATOM 572 N LYS A 244 7.575 28.522 54.316 1.00 35.96 N ANISOU 572 N LYS A 244 4417 4450 4796 463 -170 -737 N ATOM 573 CA LYS A 244 7.497 29.940 53.976 1.00 43.73 C ANISOU 573 CA LYS A 244 5385 5353 5877 455 -217 -818 C ATOM 574 C LYS A 244 8.402 30.314 52.806 1.00 36.36 C ANISOU 574 C LYS A 244 4459 4300 5056 384 -229 -793 C ATOM 575 O LYS A 244 7.998 31.061 51.916 1.00 40.51 O ANISOU 575 O LYS A 244 4989 4738 5666 350 -233 -783 O ATOM 576 CB LYS A 244 7.823 30.808 55.195 1.00 52.95 C ANISOU 576 CB LYS A 244 6511 6575 7033 525 -279 -950 C ATOM 577 CG LYS A 244 6.664 30.971 56.167 1.00 57.64 C ANISOU 577 CG LYS A 244 7086 7275 7539 602 -278 -998 C ATOM 578 CD LYS A 244 7.066 31.807 57.372 1.00 55.90 C ANISOU 578 CD LYS A 244 6817 7120 7302 681 -347 -1144 C ATOM 579 CE LYS A 244 5.850 32.237 58.176 1.00 59.12 C ANISOU 579 CE LYS A 244 7199 7624 7639 762 -356 -1208 C ATOM 580 NZ LYS A 244 4.960 33.139 57.391 1.00 62.17 N ANISOU 580 NZ LYS A 244 7597 7908 8115 739 -366 -1224 N ATOM 581 N SER A 245 9.625 29.794 52.811 1.00 36.20 N ANISOU 581 N SER A 245 4436 4286 5032 367 -233 -777 N ATOM 582 CA SER A 245 10.579 30.087 51.748 1.00 32.65 C ANISOU 582 CA SER A 245 3983 3744 4678 303 -243 -747 C ATOM 583 C SER A 245 10.122 29.495 50.418 1.00 33.05 C ANISOU 583 C SER A 245 4066 3751 4742 252 -191 -638 C ATOM 584 O SER A 245 10.155 30.166 49.387 1.00 35.60 O ANISOU 584 O SER A 245 4383 3992 5151 209 -194 -612 O ATOM 585 CB SER A 245 11.974 29.570 52.112 1.00 30.32 C ANISOU 585 CB SER A 245 3674 3485 4362 303 -257 -756 C ATOM 586 OG SER A 245 11.983 28.158 52.229 1.00 51.87 O ANISOU 586 OG SER A 245 6430 6281 6995 316 -213 -684 O ATOM 587 N LEU A 246 9.693 28.237 50.445 1.00 31.56 N ANISOU 587 N LEU A 246 3904 3618 4470 260 -146 -574 N ATOM 588 CA LEU A 246 9.203 27.576 49.241 1.00 34.22 C ANISOU 588 CA LEU A 246 4267 3923 4814 220 -102 -486 C ATOM 589 C LEU A 246 7.992 28.314 48.678 1.00 36.73 C ANISOU 589 C LEU A 246 4587 4201 5169 212 -94 -483 C ATOM 590 O LEU A 246 7.825 28.418 47.464 1.00 28.52 O ANISOU 590 O LEU A 246 3551 3110 4175 175 -78 -433 O ATOM 591 CB LEU A 246 8.845 26.116 49.531 1.00 26.31 C ANISOU 591 CB LEU A 246 3289 2980 3727 233 -62 -430 C ATOM 592 CG LEU A 246 8.325 25.313 48.336 1.00 27.56 C ANISOU 592 CG LEU A 246 3469 3107 3894 196 -24 -354 C ATOM 593 CD1 LEU A 246 9.357 25.283 47.220 1.00 27.17 C ANISOU 593 CD1 LEU A 246 3415 3014 3894 161 -30 -329 C ATOM 594 CD2 LEU A 246 7.940 23.901 48.751 1.00 26.73 C ANISOU 594 CD2 LEU A 246 3384 3047 3725 209 9 -304 C ATOM 595 N SER A 247 7.152 28.830 49.570 1.00 32.25 N ANISOU 595 N SER A 247 4011 3666 4575 254 -107 -539 N ATOM 596 CA SER A 247 5.981 29.593 49.157 1.00 30.86 C ANISOU 596 CA SER A 247 3835 3459 4431 257 -104 -546 C ATOM 597 C SER A 247 6.399 30.849 48.395 1.00 28.58 C ANISOU 597 C SER A 247 3531 3073 4255 230 -138 -564 C ATOM 598 O SER A 247 5.820 31.179 47.361 1.00 34.39 O ANISOU 598 O SER A 247 4272 3762 5033 207 -121 -519 O ATOM 599 CB SER A 247 5.123 29.963 50.368 1.00 30.08 C ANISOU 599 CB SER A 247 3723 3427 4279 318 -119 -615 C ATOM 600 OG SER A 247 3.929 30.611 49.965 1.00 42.92 O ANISOU 600 OG SER A 247 5349 5031 5927 326 -114 -621 O ATOM 601 N ARG A 248 7.411 31.541 48.910 1.00 25.03 N ANISOU 601 N ARG A 248 3058 2596 3856 234 -185 -626 N ATOM 602 CA ARG A 248 7.939 32.730 48.248 1.00 31.76 C ANISOU 602 CA ARG A 248 3888 3346 4832 202 -219 -635 C ATOM 603 C ARG A 248 8.582 32.372 46.913 1.00 37.48 C ANISOU 603 C ARG A 248 4615 4034 5592 144 -189 -535 C ATOM 604 O ARG A 248 8.531 33.150 45.959 1.00 36.13 O ANISOU 604 O ARG A 248 4431 3789 5506 115 -192 -493 O ATOM 605 CB ARG A 248 8.957 33.444 49.141 1.00 30.58 C ANISOU 605 CB ARG A 248 3706 3177 4735 215 -279 -729 C ATOM 606 CG ARG A 248 8.356 34.123 50.362 1.00 31.74 C ANISOU 606 CG ARG A 248 3838 3352 4868 280 -324 -846 C ATOM 607 CD ARG A 248 9.386 34.991 51.071 1.00 37.39 C ANISOU 607 CD ARG A 248 4513 4030 5662 289 -394 -951 C ATOM 608 NE ARG A 248 10.493 34.208 51.615 1.00 43.18 N ANISOU 608 NE ARG A 248 5237 4833 6337 289 -395 -961 N ATOM 609 CZ ARG A 248 10.550 33.764 52.867 1.00 45.78 C ANISOU 609 CZ ARG A 248 5556 5271 6566 353 -408 -1033 C ATOM 610 NH1 ARG A 248 9.560 34.026 53.711 1.00 48.73 N ANISOU 610 NH1 ARG A 248 5927 5705 6884 421 -422 -1102 N ATOM 611 NH2 ARG A 248 11.595 33.059 53.277 1.00 43.70 N ANISOU 611 NH2 ARG A 248 5283 5067 6252 354 -408 -1032 N ATOM 612 N VAL A 249 9.191 31.192 46.853 1.00 24.89 N ANISOU 612 N VAL A 249 3032 2495 3930 134 -162 -496 N ATOM 613 CA VAL A 249 9.816 30.715 45.628 1.00 18.71 C ANISOU 613 CA VAL A 249 2247 1700 3163 91 -135 -411 C ATOM 614 C VAL A 249 8.768 30.475 44.548 1.00 24.30 C ANISOU 614 C VAL A 249 2970 2405 3857 83 -95 -344 C ATOM 615 O VAL A 249 8.922 30.921 43.411 1.00 23.85 O ANISOU 615 O VAL A 249 2897 2310 3854 56 -86 -285 O ATOM 616 CB VAL A 249 10.606 29.412 45.863 1.00 25.53 C ANISOU 616 CB VAL A 249 3122 2628 3951 94 -118 -394 C ATOM 617 CG1 VAL A 249 10.958 28.760 44.538 1.00 24.88 C ANISOU 617 CG1 VAL A 249 3039 2550 3865 64 -86 -312 C ATOM 618 CG2 VAL A 249 11.858 29.686 46.682 1.00 21.58 C ANISOU 618 CG2 VAL A 249 2595 2134 3470 97 -158 -450 C ATOM 619 N MET A 250 7.702 29.770 44.915 1.00 19.32 N ANISOU 619 N MET A 250 2366 1821 3153 109 -71 -350 N ATOM 620 CA MET A 250 6.639 29.431 43.974 1.00 22.22 C ANISOU 620 CA MET A 250 2745 2196 3501 105 -35 -299 C ATOM 621 C MET A 250 5.913 30.673 43.462 1.00 23.69 C ANISOU 621 C MET A 250 2919 2331 3752 108 -45 -297 C ATOM 622 O MET A 250 5.644 30.793 42.266 1.00 27.99 O ANISOU 622 O MET A 250 3456 2862 4316 93 -25 -237 O ATOM 623 CB MET A 250 5.652 28.450 44.611 1.00 30.00 C ANISOU 623 CB MET A 250 3753 3240 4404 127 -11 -309 C ATOM 624 CG MET A 250 6.261 27.090 44.930 1.00 27.78 C ANISOU 624 CG MET A 250 3486 3002 4067 124 4 -291 C ATOM 625 SD MET A 250 5.071 25.924 45.620 1.00 31.72 S ANISOU 625 SD MET A 250 4003 3559 4489 142 37 -280 S ATOM 626 CE MET A 250 4.766 26.660 47.225 1.00 23.93 C ANISOU 626 CE MET A 250 3007 2612 3473 188 14 -347 C ATOM 627 N ILE A 251 5.594 31.592 44.368 1.00 23.26 N ANISOU 627 N ILE A 251 2859 2250 3726 133 -78 -364 N ATOM 628 CA ILE A 251 4.992 32.862 43.984 1.00 28.39 C ANISOU 628 CA ILE A 251 3498 2837 4453 142 -97 -369 C ATOM 629 C ILE A 251 5.899 33.568 42.984 1.00 33.25 C ANISOU 629 C ILE A 251 4088 3382 5162 104 -106 -310 C ATOM 630 O ILE A 251 5.440 34.101 41.972 1.00 35.03 O ANISOU 630 O ILE A 251 4305 3576 5429 98 -93 -250 O ATOM 631 CB ILE A 251 4.784 33.784 45.204 1.00 31.76 C ANISOU 631 CB ILE A 251 3918 3241 4910 180 -145 -469 C ATOM 632 CG1 ILE A 251 3.690 33.230 46.119 1.00 28.79 C ANISOU 632 CG1 ILE A 251 3556 2948 4436 226 -131 -516 C ATOM 633 CG2 ILE A 251 4.435 35.197 44.755 1.00 18.61 C ANISOU 633 CG2 ILE A 251 2236 1482 3351 186 -175 -474 C ATOM 634 CD1 ILE A 251 2.321 33.184 45.478 1.00 33.85 C ANISOU 634 CD1 ILE A 251 4206 3607 5049 238 -100 -480 C ATOM 635 N HIS A 252 7.195 33.554 43.276 1.00 28.33 N ANISOU 635 N HIS A 252 3450 2745 4571 79 -127 -320 N ATOM 636 CA HIS A 252 8.187 34.213 42.438 1.00 26.65 C ANISOU 636 CA HIS A 252 3202 2473 4451 38 -136 -260 C ATOM 637 C HIS A 252 8.255 33.584 41.047 1.00 26.48 C ANISOU 637 C HIS A 252 3175 2492 4395 18 -90 -155 C ATOM 638 O HIS A 252 8.466 34.278 40.053 1.00 21.81 O ANISOU 638 O HIS A 252 2554 1862 3870 -2 -84 -79 O ATOM 639 CB HIS A 252 9.557 34.156 43.115 1.00 22.93 C ANISOU 639 CB HIS A 252 2710 1997 4004 17 -167 -300 C ATOM 640 CG HIS A 252 10.594 35.012 42.459 1.00 32.93 C ANISOU 640 CG HIS A 252 3931 3194 5385 -30 -184 -248 C ATOM 641 ND1 HIS A 252 11.017 36.209 42.995 1.00 41.48 N ANISOU 641 ND1 HIS A 252 4985 4187 6591 -43 -238 -300 N ATOM 642 CD2 HIS A 252 11.293 34.845 41.314 1.00 42.85 C ANISOU 642 CD2 HIS A 252 5160 4464 6657 -66 -156 -146 C ATOM 643 CE1 HIS A 252 11.933 36.742 42.208 1.00 40.61 C ANISOU 643 CE1 HIS A 252 4830 4028 6573 -93 -240 -223 C ATOM 644 NE2 HIS A 252 12.120 35.932 41.179 1.00 40.57 N ANISOU 644 NE2 HIS A 252 4824 4093 6498 -105 -188 -125 N ATOM 645 N VAL A 253 8.074 32.269 40.981 1.00 24.60 N ANISOU 645 N VAL A 253 2960 2334 4053 29 -58 -151 N ATOM 646 CA VAL A 253 8.109 31.556 39.707 1.00 28.52 C ANISOU 646 CA VAL A 253 3447 2881 4506 21 -20 -73 C ATOM 647 C VAL A 253 7.083 32.115 38.723 1.00 31.20 C ANISOU 647 C VAL A 253 3780 3213 4862 34 -1 -21 C ATOM 648 O VAL A 253 7.346 32.211 37.524 1.00 28.28 O ANISOU 648 O VAL A 253 3380 2863 4501 27 19 59 O ATOM 649 CB VAL A 253 7.864 30.046 39.896 1.00 24.28 C ANISOU 649 CB VAL A 253 2940 2418 3868 36 3 -94 C ATOM 650 CG1 VAL A 253 7.585 29.377 38.557 1.00 19.48 C ANISOU 650 CG1 VAL A 253 2322 1862 3218 40 35 -34 C ATOM 651 CG2 VAL A 253 9.056 29.398 40.588 1.00 14.78 C ANISOU 651 CG2 VAL A 253 1738 1233 2644 27 -11 -122 C ATOM 652 N PHE A 254 5.918 32.490 39.237 1.00 24.57 N ANISOU 652 N PHE A 254 2961 2354 4021 59 -8 -65 N ATOM 653 CA PHE A 254 4.845 33.006 38.395 1.00 26.84 C ANISOU 653 CA PHE A 254 3242 2638 4316 79 9 -23 C ATOM 654 C PHE A 254 4.871 34.528 38.273 1.00 27.96 C ANISOU 654 C PHE A 254 3364 2690 4570 78 -18 1 C ATOM 655 O PHE A 254 4.043 35.111 37.575 1.00 34.54 O ANISOU 655 O PHE A 254 4190 3512 5421 99 -8 43 O ATOM 656 CB PHE A 254 3.486 32.553 38.930 1.00 24.05 C ANISOU 656 CB PHE A 254 2918 2321 3899 110 18 -79 C ATOM 657 CG PHE A 254 3.253 31.074 38.821 1.00 23.39 C ANISOU 657 CG PHE A 254 2849 2316 3724 109 47 -85 C ATOM 658 CD1 PHE A 254 3.215 30.456 37.582 1.00 16.20 C ANISOU 658 CD1 PHE A 254 1922 1455 2778 108 73 -32 C ATOM 659 CD2 PHE A 254 3.061 30.304 39.956 1.00 27.44 C ANISOU 659 CD2 PHE A 254 3386 2853 4187 112 44 -144 C ATOM 660 CE1 PHE A 254 2.995 29.095 37.477 1.00 21.12 C ANISOU 660 CE1 PHE A 254 2555 2135 3333 107 91 -48 C ATOM 661 CE2 PHE A 254 2.840 28.943 39.858 1.00 23.70 C ANISOU 661 CE2 PHE A 254 2923 2434 3647 108 68 -143 C ATOM 662 CZ PHE A 254 2.807 28.338 38.618 1.00 22.78 C ANISOU 662 CZ PHE A 254 2794 2352 3511 103 88 -100 C ATOM 663 N SER A 255 5.828 35.165 38.942 1.00 23.73 N ANISOU 663 N SER A 255 2816 2087 4113 55 -54 -27 N ATOM 664 CA SER A 255 5.880 36.624 39.007 1.00 26.80 C ANISOU 664 CA SER A 255 3185 2368 4629 51 -90 -20 C ATOM 665 C SER A 255 6.119 37.272 37.646 1.00 30.92 C ANISOU 665 C SER A 255 3669 2863 5215 34 -70 107 C ATOM 666 O SER A 255 6.026 38.492 37.511 1.00 31.18 O ANISOU 666 O SER A 255 3684 2800 5363 32 -95 136 O ATOM 667 CB SER A 255 6.954 37.086 39.995 1.00 23.52 C ANISOU 667 CB SER A 255 2756 1889 4291 25 -137 -84 C ATOM 668 OG SER A 255 8.248 36.977 39.428 1.00 40.89 O ANISOU 668 OG SER A 255 4920 4089 6525 -21 -129 -15 O ATOM 669 N ASP A 256 6.427 36.458 36.641 1.00 21.97 N ANISOU 669 N ASP A 256 2520 1817 4009 26 -28 184 N ATOM 670 CA ASP A 256 6.656 36.979 35.298 1.00 29.79 C ANISOU 670 CA ASP A 256 3467 2813 5039 19 -3 315 C ATOM 671 C ASP A 256 5.356 37.050 34.500 1.00 31.50 C ANISOU 671 C ASP A 256 3690 3071 5208 66 23 354 C ATOM 672 O ASP A 256 5.328 37.581 33.390 1.00 30.70 O ANISOU 672 O ASP A 256 3551 2980 5133 74 44 466 O ATOM 673 CB ASP A 256 7.704 36.143 34.556 1.00 29.85 C ANISOU 673 CB ASP A 256 3443 2910 4990 -2 26 378 C ATOM 674 CG ASP A 256 7.221 34.742 34.242 1.00 32.22 C ANISOU 674 CG ASP A 256 3766 3328 5149 28 56 346 C ATOM 675 OD1 ASP A 256 6.167 34.335 34.774 1.00 37.28 O ANISOU 675 OD1 ASP A 256 4448 3978 5739 54 55 270 O ATOM 676 OD2 ASP A 256 7.899 34.046 33.459 1.00 34.34 O ANISOU 676 OD2 ASP A 256 4005 3681 5361 26 80 395 O ATOM 677 N GLY A 257 4.284 36.514 35.073 1.00 27.59 N ANISOU 677 N GLY A 257 3236 2607 4640 98 23 266 N ATOM 678 CA GLY A 257 2.978 36.560 34.441 1.00 31.33 C ANISOU 678 CA GLY A 257 3716 3124 5066 143 44 285 C ATOM 679 C GLY A 257 2.691 35.384 33.527 1.00 36.96 C ANISOU 679 C GLY A 257 4419 3964 5661 160 85 309 C ATOM 680 O GLY A 257 1.632 35.320 32.904 1.00 43.24 O ANISOU 680 O GLY A 257 5211 4811 6407 199 103 322 O ATOM 681 N VAL A 258 3.632 34.450 33.443 1.00 29.52 N ANISOU 681 N VAL A 258 3470 3073 4674 135 94 307 N ATOM 682 CA VAL A 258 3.461 33.272 32.598 1.00 29.39 C ANISOU 682 CA VAL A 258 3442 3173 4554 155 123 314 C ATOM 683 C VAL A 258 2.866 32.106 33.383 1.00 30.44 C ANISOU 683 C VAL A 258 3615 3334 4617 156 122 212 C ATOM 684 O VAL A 258 3.347 31.762 34.463 1.00 26.16 O ANISOU 684 O VAL A 258 3100 2755 4084 131 105 153 O ATOM 685 CB VAL A 258 4.793 32.832 31.959 1.00 36.42 C ANISOU 685 CB VAL A 258 4295 4113 5429 136 134 370 C ATOM 686 CG1 VAL A 258 4.618 31.518 31.210 1.00 35.09 C ANISOU 686 CG1 VAL A 258 4117 4063 5154 163 154 350 C ATOM 687 CG2 VAL A 258 5.321 33.915 31.029 1.00 33.39 C ANISOU 687 CG2 VAL A 258 3859 3721 5107 136 144 494 C ATOM 688 N THR A 259 1.815 31.504 32.836 1.00 28.19 N ANISOU 688 N THR A 259 3328 3119 4265 186 139 194 N ATOM 689 CA THR A 259 1.164 30.370 33.480 1.00 30.47 C ANISOU 689 CA THR A 259 3646 3434 4497 183 140 110 C ATOM 690 C THR A 259 0.979 29.211 32.506 1.00 33.34 C ANISOU 690 C THR A 259 3988 3890 4790 200 156 104 C ATOM 691 O THR A 259 0.354 29.362 31.457 1.00 28.94 O ANISOU 691 O THR A 259 3399 3394 4204 234 168 133 O ATOM 692 CB THR A 259 -0.211 30.757 34.059 1.00 30.01 C ANISOU 692 CB THR A 259 3607 3357 4438 200 138 67 C ATOM 693 OG1 THR A 259 -0.090 31.962 34.824 1.00 31.60 O ANISOU 693 OG1 THR A 259 3822 3474 4711 198 116 66 O ATOM 694 CG2 THR A 259 -0.750 29.641 34.949 1.00 23.77 C ANISOU 694 CG2 THR A 259 2844 2585 3604 187 139 -8 C ATOM 695 N ASN A 260 1.530 28.055 32.860 1.00 33.90 N ANISOU 695 N ASN A 260 4072 3973 4834 181 151 63 N ATOM 696 CA ASN A 260 1.351 26.845 32.066 1.00 24.07 C ANISOU 696 CA ASN A 260 2809 2804 3534 197 157 35 C ATOM 697 C ASN A 260 1.454 25.589 32.928 1.00 23.44 C ANISOU 697 C ASN A 260 2760 2701 3443 172 148 -28 C ATOM 698 O ASN A 260 1.967 25.639 34.045 1.00 28.84 O ANISOU 698 O ASN A 260 3477 3329 4153 146 140 -38 O ATOM 699 CB ASN A 260 2.341 26.802 30.895 1.00 17.48 C ANISOU 699 CB ASN A 260 1931 2034 2676 219 160 86 C ATOM 700 CG ASN A 260 3.792 26.785 31.347 1.00 20.72 C ANISOU 700 CG ASN A 260 2348 2413 3111 193 151 106 C ATOM 701 OD1 ASN A 260 4.174 26.017 32.229 1.00 22.02 O ANISOU 701 OD1 ASN A 260 2546 2543 3279 170 140 57 O ATOM 702 ND2 ASN A 260 4.612 27.627 30.729 1.00 15.99 N ANISOU 702 ND2 ASN A 260 1714 1832 2532 198 157 184 N ATOM 703 N TRP A 261 0.953 24.470 32.413 1.00 25.10 N ANISOU 703 N TRP A 261 2959 2958 3622 183 146 -71 N ATOM 704 CA TRP A 261 0.946 23.217 33.165 1.00 27.51 C ANISOU 704 CA TRP A 261 3289 3233 3929 159 138 -122 C ATOM 705 C TRP A 261 2.355 22.699 33.435 1.00 24.10 C ANISOU 705 C TRP A 261 2870 2784 3501 151 126 -117 C ATOM 706 O TRP A 261 2.597 22.031 34.440 1.00 25.35 O ANISOU 706 O TRP A 261 3061 2897 3673 128 120 -138 O ATOM 707 CB TRP A 261 0.118 22.148 32.444 1.00 22.21 C ANISOU 707 CB TRP A 261 2595 2605 3241 172 132 -173 C ATOM 708 CG TRP A 261 -1.358 22.407 32.481 1.00 25.65 C ANISOU 708 CG TRP A 261 3020 3051 3674 171 143 -190 C ATOM 709 CD1 TRP A 261 -2.165 22.714 31.422 1.00 25.02 C ANISOU 709 CD1 TRP A 261 2901 3038 3569 205 146 -197 C ATOM 710 CD2 TRP A 261 -2.205 22.387 33.638 1.00 16.60 C ANISOU 710 CD2 TRP A 261 1900 1861 2547 140 152 -201 C ATOM 711 NE1 TRP A 261 -3.461 22.881 31.849 1.00 28.64 N ANISOU 711 NE1 TRP A 261 3359 3490 4032 194 156 -216 N ATOM 712 CE2 TRP A 261 -3.512 22.688 33.204 1.00 19.76 C ANISOU 712 CE2 TRP A 261 2273 2302 2934 154 160 -217 C ATOM 713 CE3 TRP A 261 -1.985 22.143 34.998 1.00 16.82 C ANISOU 713 CE3 TRP A 261 1965 1833 2593 109 154 -197 C ATOM 714 CZ2 TRP A 261 -4.594 22.750 34.081 1.00 22.11 C ANISOU 714 CZ2 TRP A 261 2579 2585 3239 134 171 -229 C ATOM 715 CZ3 TRP A 261 -3.059 22.205 35.866 1.00 23.05 C ANISOU 715 CZ3 TRP A 261 2760 2614 3385 92 167 -205 C ATOM 716 CH2 TRP A 261 -4.348 22.507 35.404 1.00 29.50 C ANISOU 716 CH2 TRP A 261 3549 3471 4190 103 175 -221 C ATOM 717 N GLY A 262 3.282 23.005 32.533 1.00 19.90 N ANISOU 717 N GLY A 262 2309 2298 2956 173 123 -85 N ATOM 718 CA GLY A 262 4.665 22.607 32.711 1.00 26.36 C ANISOU 718 CA GLY A 262 3131 3112 3773 170 112 -79 C ATOM 719 C GLY A 262 5.224 23.109 34.028 1.00 29.79 C ANISOU 719 C GLY A 262 3602 3477 4240 137 110 -65 C ATOM 720 O GLY A 262 5.836 22.355 34.785 1.00 26.74 O ANISOU 720 O GLY A 262 3241 3064 3855 126 99 -89 O ATOM 721 N ARG A 263 5.009 24.391 34.303 1.00 21.57 N ANISOU 721 N ARG A 263 2561 2408 3228 127 116 -32 N ATOM 722 CA ARG A 263 5.462 24.990 35.552 1.00 21.27 C ANISOU 722 CA ARG A 263 2549 2308 3223 102 108 -34 C ATOM 723 C ARG A 263 4.716 24.401 36.743 1.00 23.31 C ANISOU 723 C ARG A 263 2846 2536 3475 92 107 -79 C ATOM 724 O ARG A 263 5.315 24.077 37.767 1.00 29.44 O ANISOU 724 O ARG A 263 3645 3289 4252 82 98 -96 O ATOM 725 CB ARG A 263 5.260 26.504 35.520 1.00 21.40 C ANISOU 725 CB ARG A 263 2553 2293 3283 99 109 2 C ATOM 726 CG ARG A 263 6.098 27.222 34.484 1.00 26.48 C ANISOU 726 CG ARG A 263 3154 2961 3947 102 112 69 C ATOM 727 CD ARG A 263 5.882 28.720 34.564 1.00 28.30 C ANISOU 727 CD ARG A 263 3373 3137 4241 95 108 108 C ATOM 728 NE ARG A 263 6.748 29.443 33.640 1.00 23.80 N ANISOU 728 NE ARG A 263 2758 2585 3703 91 114 190 N ATOM 729 CZ ARG A 263 6.956 30.753 33.686 1.00 18.90 C ANISOU 729 CZ ARG A 263 2119 1903 3160 76 106 239 C ATOM 730 NH1 ARG A 263 6.358 31.487 34.615 1.00 24.42 N ANISOU 730 NH1 ARG A 263 2846 2520 3910 69 88 199 N ATOM 731 NH2 ARG A 263 7.763 31.328 32.805 1.00 22.46 N ANISOU 731 NH2 ARG A 263 2520 2373 3641 69 115 328 N ATOM 732 N ILE A 264 3.402 24.270 36.600 1.00 23.03 N ANISOU 732 N ILE A 264 2812 2511 3429 98 119 -94 N ATOM 733 CA ILE A 264 2.563 23.743 37.670 1.00 23.97 C ANISOU 733 CA ILE A 264 2955 2612 3539 87 124 -124 C ATOM 734 C ILE A 264 3.005 22.352 38.121 1.00 26.00 C ANISOU 734 C ILE A 264 3230 2864 3784 78 120 -139 C ATOM 735 O ILE A 264 3.172 22.104 39.316 1.00 25.61 O ANISOU 735 O ILE A 264 3204 2796 3732 70 119 -144 O ATOM 736 CB ILE A 264 1.078 23.712 37.257 1.00 20.07 C ANISOU 736 CB ILE A 264 2449 2142 3036 93 137 -136 C ATOM 737 CG1 ILE A 264 0.529 25.138 37.155 1.00 22.32 C ANISOU 737 CG1 ILE A 264 2724 2421 3334 107 139 -123 C ATOM 738 CG2 ILE A 264 0.263 22.898 38.251 1.00 16.91 C ANISOU 738 CG2 ILE A 264 2064 1735 2625 77 146 -156 C ATOM 739 CD1 ILE A 264 -0.946 25.207 36.822 1.00 25.19 C ANISOU 739 CD1 ILE A 264 3073 2815 3683 118 152 -136 C ATOM 740 N VAL A 265 3.201 21.447 37.168 1.00 26.79 N ANISOU 740 N VAL A 265 3316 2985 3878 85 116 -146 N ATOM 741 CA VAL A 265 3.586 20.080 37.504 1.00 28.55 C ANISOU 741 CA VAL A 265 3554 3190 4103 79 107 -162 C ATOM 742 C VAL A 265 5.023 20.016 38.016 1.00 29.33 C ANISOU 742 C VAL A 265 3667 3278 4197 84 95 -151 C ATOM 743 O VAL A 265 5.370 19.132 38.798 1.00 33.55 O ANISOU 743 O VAL A 265 4225 3790 4733 81 90 -154 O ATOM 744 CB VAL A 265 3.410 19.117 36.315 1.00 25.28 C ANISOU 744 CB VAL A 265 3117 2799 3691 93 97 -189 C ATOM 745 CG1 VAL A 265 4.553 19.275 35.322 1.00 18.38 C ANISOU 745 CG1 VAL A 265 2219 1965 2798 121 84 -187 C ATOM 746 CG2 VAL A 265 3.331 17.686 36.812 1.00 29.78 C ANISOU 746 CG2 VAL A 265 3704 3329 4284 81 87 -208 C ATOM 747 N THR A 266 5.853 20.958 37.578 1.00 21.17 N ANISOU 747 N THR A 266 2618 2264 3162 92 90 -135 N ATOM 748 CA THR A 266 7.232 21.029 38.049 1.00 19.60 C ANISOU 748 CA THR A 266 2425 2061 2961 94 77 -127 C ATOM 749 C THR A 266 7.284 21.411 39.527 1.00 26.04 C ANISOU 749 C THR A 266 3266 2848 3781 84 76 -131 C ATOM 750 O THR A 266 8.061 20.845 40.294 1.00 32.26 O ANISOU 750 O THR A 266 4070 3630 4556 89 67 -137 O ATOM 751 CB THR A 266 8.071 22.020 37.221 1.00 25.88 C ANISOU 751 CB THR A 266 3186 2884 3764 98 74 -100 C ATOM 752 OG1 THR A 266 8.222 21.521 35.886 1.00 24.44 O ANISOU 752 OG1 THR A 266 2973 2752 3562 120 74 -96 O ATOM 753 CG2 THR A 266 9.450 22.202 37.841 1.00 30.37 C ANISOU 753 CG2 THR A 266 3755 3447 4336 94 60 -95 C ATOM 754 N LEU A 267 6.450 22.369 39.922 1.00 29.84 N ANISOU 754 N LEU A 267 3748 3317 4273 77 83 -133 N ATOM 755 CA LEU A 267 6.359 22.772 41.322 1.00 24.44 C ANISOU 755 CA LEU A 267 3081 2621 3584 78 79 -149 C ATOM 756 C LEU A 267 5.869 21.615 42.190 1.00 29.79 C ANISOU 756 C LEU A 267 3780 3304 4234 82 89 -149 C ATOM 757 O LEU A 267 6.353 21.416 43.304 1.00 28.65 O ANISOU 757 O LEU A 267 3649 3167 4070 93 84 -154 O ATOM 758 CB LEU A 267 5.434 23.981 41.485 1.00 24.36 C ANISOU 758 CB LEU A 267 3063 2601 3591 79 81 -159 C ATOM 759 CG LEU A 267 5.902 25.298 40.860 1.00 27.99 C ANISOU 759 CG LEU A 267 3501 3040 4094 75 68 -150 C ATOM 760 CD1 LEU A 267 4.874 26.392 41.084 1.00 30.20 C ANISOU 760 CD1 LEU A 267 3777 3302 4396 83 67 -164 C ATOM 761 CD2 LEU A 267 7.251 25.712 41.420 1.00 28.47 C ANISOU 761 CD2 LEU A 267 3555 3085 4175 71 45 -161 C ATOM 762 N ILE A 268 4.909 20.855 41.672 1.00 28.02 N ANISOU 762 N ILE A 268 3555 3079 4011 73 104 -141 N ATOM 763 CA ILE A 268 4.380 19.699 42.388 1.00 24.31 C ANISOU 763 CA ILE A 268 3100 2605 3532 68 116 -127 C ATOM 764 C ILE A 268 5.428 18.592 42.488 1.00 20.43 C ANISOU 764 C ILE A 268 2622 2099 3041 76 104 -117 C ATOM 765 O ILE A 268 5.563 17.947 43.526 1.00 27.42 O ANISOU 765 O ILE A 268 3522 2983 3912 82 109 -96 O ATOM 766 CB ILE A 268 3.108 19.145 41.711 1.00 23.11 C ANISOU 766 CB ILE A 268 2935 2448 3397 51 130 -125 C ATOM 767 CG1 ILE A 268 2.041 20.236 41.605 1.00 25.33 C ANISOU 767 CG1 ILE A 268 3201 2750 3673 51 141 -136 C ATOM 768 CG2 ILE A 268 2.571 17.948 42.483 1.00 16.51 C ANISOU 768 CG2 ILE A 268 2107 1598 2567 38 143 -99 C ATOM 769 CD1 ILE A 268 0.787 19.800 40.878 1.00 19.14 C ANISOU 769 CD1 ILE A 268 2397 1972 2903 36 153 -141 C ATOM 770 N SER A 269 6.168 18.378 41.404 1.00 24.01 N ANISOU 770 N SER A 269 3068 2549 3507 81 90 -130 N ATOM 771 CA SER A 269 7.220 17.368 41.383 1.00 24.82 C ANISOU 771 CA SER A 269 3180 2640 3609 96 74 -129 C ATOM 772 C SER A 269 8.323 17.697 42.383 1.00 27.63 C ANISOU 772 C SER A 269 3547 3010 3940 112 65 -123 C ATOM 773 O SER A 269 8.804 16.818 43.099 1.00 26.29 O ANISOU 773 O SER A 269 3396 2833 3761 127 61 -108 O ATOM 774 CB SER A 269 7.810 17.226 39.979 1.00 27.56 C ANISOU 774 CB SER A 269 3506 3002 3963 108 58 -150 C ATOM 775 OG SER A 269 6.851 16.714 39.072 1.00 33.45 O ANISOU 775 OG SER A 269 4238 3741 4729 103 60 -167 O ATOM 776 N PHE A 270 8.726 18.963 42.424 1.00 20.16 N ANISOU 776 N PHE A 270 2587 2084 2989 110 60 -135 N ATOM 777 CA PHE A 270 9.737 19.402 43.377 1.00 25.24 C ANISOU 777 CA PHE A 270 3232 2744 3613 124 47 -143 C ATOM 778 C PHE A 270 9.207 19.281 44.799 1.00 31.93 C ANISOU 778 C PHE A 270 4096 3603 4434 136 56 -137 C ATOM 779 O PHE A 270 9.954 18.976 45.727 1.00 33.24 O ANISOU 779 O PHE A 270 4269 3790 4572 159 47 -136 O ATOM 780 CB PHE A 270 10.174 20.840 43.090 1.00 21.57 C ANISOU 780 CB PHE A 270 2743 2286 3168 114 36 -160 C ATOM 781 CG PHE A 270 11.275 21.329 43.989 1.00 24.62 C ANISOU 781 CG PHE A 270 3122 2688 3546 125 15 -181 C ATOM 782 CD1 PHE A 270 12.512 20.703 43.992 1.00 25.79 C ANISOU 782 CD1 PHE A 270 3267 2854 3677 140 2 -180 C ATOM 783 CD2 PHE A 270 11.076 22.416 44.826 1.00 22.76 C ANISOU 783 CD2 PHE A 270 2878 2451 3318 126 5 -210 C ATOM 784 CE1 PHE A 270 13.530 21.148 44.819 1.00 29.06 C ANISOU 784 CE1 PHE A 270 3669 3290 4083 151 -20 -206 C ATOM 785 CE2 PHE A 270 12.091 22.867 45.653 1.00 29.58 C ANISOU 785 CE2 PHE A 270 3729 3333 4178 139 -21 -243 C ATOM 786 CZ PHE A 270 13.319 22.233 45.649 1.00 28.16 C ANISOU 786 CZ PHE A 270 3544 3175 3980 150 -32 -240 C ATOM 787 N GLY A 271 7.910 19.521 44.961 1.00 31.65 N ANISOU 787 N GLY A 271 4060 3566 4400 124 74 -131 N ATOM 788 CA GLY A 271 7.262 19.358 46.248 1.00 32.94 C ANISOU 788 CA GLY A 271 4229 3757 4530 139 88 -117 C ATOM 789 C GLY A 271 7.424 17.940 46.758 1.00 31.98 C ANISOU 789 C GLY A 271 4124 3632 4395 149 97 -72 C ATOM 790 O GLY A 271 7.698 17.722 47.937 1.00 34.11 O ANISOU 790 O GLY A 271 4397 3939 4625 177 100 -55 O ATOM 791 N ALA A 272 7.255 16.972 45.862 1.00 25.06 N ANISOU 791 N ALA A 272 3254 2711 3555 131 100 -54 N ATOM 792 CA ALA A 272 7.437 15.567 46.204 1.00 32.85 C ANISOU 792 CA ALA A 272 4256 3673 4551 138 103 -11 C ATOM 793 C ALA A 272 8.896 15.282 46.549 1.00 38.77 C ANISOU 793 C ALA A 272 5018 4435 5279 172 82 -15 C ATOM 794 O ALA A 272 9.190 14.546 47.491 1.00 34.04 O ANISOU 794 O ALA A 272 4430 3846 4660 196 87 26 O ATOM 795 CB ALA A 272 6.974 14.678 45.059 1.00 24.45 C ANISOU 795 CB ALA A 272 3192 2552 3544 114 100 -12 C ATOM 796 N PHE A 273 9.805 15.869 45.778 1.00 22.58 N ANISOU 796 N PHE A 273 2959 2390 3231 175 61 -59 N ATOM 797 CA PHE A 273 11.234 15.728 46.028 1.00 23.73 C ANISOU 797 CA PHE A 273 3106 2556 3353 205 40 -70 C ATOM 798 C PHE A 273 11.586 16.225 47.429 1.00 37.35 C ANISOU 798 C PHE A 273 4828 4333 5028 232 39 -69 C ATOM 799 O PHE A 273 12.399 15.619 48.128 1.00 39.89 O ANISOU 799 O PHE A 273 5158 4677 5321 267 31 -53 O ATOM 800 CB PHE A 273 12.034 16.500 44.976 1.00 23.75 C ANISOU 800 CB PHE A 273 3088 2569 3367 197 22 -111 C ATOM 801 CG PHE A 273 13.507 16.202 44.990 1.00 36.59 C ANISOU 801 CG PHE A 273 4709 4218 4974 226 -1 -124 C ATOM 802 CD1 PHE A 273 14.020 15.144 44.258 1.00 35.76 C ANISOU 802 CD1 PHE A 273 4611 4097 4881 244 -14 -123 C ATOM 803 CD2 PHE A 273 14.379 16.984 45.730 1.00 33.41 C ANISOU 803 CD2 PHE A 273 4292 3857 4545 238 -14 -144 C ATOM 804 CE1 PHE A 273 15.376 14.869 44.266 1.00 36.38 C ANISOU 804 CE1 PHE A 273 4680 4204 4936 275 -35 -136 C ATOM 805 CE2 PHE A 273 15.735 16.715 45.742 1.00 33.07 C ANISOU 805 CE2 PHE A 273 4239 3843 4483 265 -35 -158 C ATOM 806 CZ PHE A 273 16.235 15.656 45.009 1.00 24.25 C ANISOU 806 CZ PHE A 273 3129 2715 3370 284 -44 -150 C ATOM 807 N VAL A 274 10.967 17.331 47.834 1.00 29.61 N ANISOU 807 N VAL A 274 3835 3379 4038 223 45 -91 N ATOM 808 CA VAL A 274 11.172 17.879 49.169 1.00 31.60 C ANISOU 808 CA VAL A 274 4076 3691 4239 256 40 -106 C ATOM 809 C VAL A 274 10.557 16.967 50.225 1.00 40.21 C ANISOU 809 C VAL A 274 5177 4811 5291 282 64 -47 C ATOM 810 O VAL A 274 11.152 16.724 51.276 1.00 40.28 O ANISOU 810 O VAL A 274 5181 4874 5247 326 59 -36 O ATOM 811 CB VAL A 274 10.558 19.284 49.307 1.00 26.27 C ANISOU 811 CB VAL A 274 3381 3031 3570 245 36 -154 C ATOM 812 CG1 VAL A 274 10.682 19.778 50.740 1.00 36.91 C ANISOU 812 CG1 VAL A 274 4713 4450 4861 290 26 -182 C ATOM 813 CG2 VAL A 274 11.224 20.256 48.343 1.00 27.01 C ANISOU 813 CG2 VAL A 274 3459 3093 3710 220 13 -198 C ATOM 814 N ALA A 275 9.361 16.462 49.936 1.00 32.95 N ANISOU 814 N ALA A 275 4263 3860 4396 254 91 -3 N ATOM 815 CA ALA A 275 8.655 15.583 50.860 1.00 29.96 C ANISOU 815 CA ALA A 275 3886 3505 3993 269 119 71 C ATOM 816 C ALA A 275 9.480 14.339 51.179 1.00 33.91 C ANISOU 816 C ALA A 275 4403 3990 4490 295 116 125 C ATOM 817 O ALA A 275 9.453 13.838 52.302 1.00 38.16 O ANISOU 817 O ALA A 275 4936 4579 4982 331 131 184 O ATOM 818 CB ALA A 275 7.297 15.196 50.292 1.00 20.52 C ANISOU 818 CB ALA A 275 2688 2264 2843 224 144 106 C ATOM 819 N LYS A 276 10.211 13.847 50.184 1.00 36.68 N ANISOU 819 N LYS A 276 4771 4278 4888 283 95 106 N ATOM 820 CA LYS A 276 11.074 12.687 50.371 1.00 37.05 C ANISOU 820 CA LYS A 276 4836 4302 4940 314 85 146 C ATOM 821 C LYS A 276 12.200 12.996 51.352 1.00 49.95 C ANISOU 821 C LYS A 276 6462 6014 6501 369 71 133 C ATOM 822 O LYS A 276 12.512 12.191 52.228 1.00 54.40 O ANISOU 822 O LYS A 276 7033 6603 7035 411 78 194 O ATOM 823 CB LYS A 276 11.663 12.236 49.034 1.00 34.93 C ANISOU 823 CB LYS A 276 4579 3965 4728 298 60 108 C ATOM 824 CG LYS A 276 10.657 11.608 48.085 1.00 40.36 C ANISOU 824 CG LYS A 276 5271 4574 5491 255 67 119 C ATOM 825 CD LYS A 276 11.312 11.252 46.760 1.00 38.19 C ANISOU 825 CD LYS A 276 5000 4254 5257 255 36 66 C ATOM 826 CE LYS A 276 10.340 10.543 45.838 1.00 48.24 C ANISOU 826 CE LYS A 276 6271 5453 6605 220 36 64 C ATOM 827 NZ LYS A 276 10.962 10.201 44.529 1.00 53.67 N ANISOU 827 NZ LYS A 276 6955 6115 7323 232 2 2 N ATOM 828 N HIS A 277 12.806 14.169 51.195 1.00 56.96 N ANISOU 828 N HIS A 277 7334 6941 7367 371 50 54 N ATOM 829 CA HIS A 277 13.911 14.585 52.050 1.00 56.67 C ANISOU 829 CA HIS A 277 7282 6980 7269 420 29 21 C ATOM 830 C HIS A 277 13.459 14.781 53.493 1.00 56.03 C ANISOU 830 C HIS A 277 7185 6987 7116 463 45 47 C ATOM 831 O HIS A 277 14.212 14.515 54.429 1.00 57.27 O ANISOU 831 O HIS A 277 7333 7213 7212 521 36 58 O ATOM 832 CB HIS A 277 14.541 15.874 51.518 1.00 62.65 C ANISOU 832 CB HIS A 277 8018 7749 8039 401 1 -68 C ATOM 833 CG HIS A 277 15.693 16.366 52.336 1.00 68.08 C ANISOU 833 CG HIS A 277 8682 8510 8675 445 -26 -116 C ATOM 834 ND1 HIS A 277 16.984 15.920 52.151 1.00 72.45 N ANISOU 834 ND1 HIS A 277 9234 9073 9220 469 -48 -127 N ATOM 835 CD2 HIS A 277 15.750 17.271 53.344 1.00 65.48 C ANISOU 835 CD2 HIS A 277 8324 8255 8300 475 -39 -166 C ATOM 836 CE1 HIS A 277 17.785 16.525 53.008 1.00 68.80 C ANISOU 836 CE1 HIS A 277 8743 8687 8711 506 -72 -178 C ATOM 837 NE2 HIS A 277 17.062 17.350 53.743 1.00 70.20 N ANISOU 837 NE2 HIS A 277 8902 8903 8866 511 -69 -206 N ATOM 838 N LEU A 278 12.227 15.249 53.666 1.00 49.44 N ANISOU 838 N LEU A 278 6340 6162 6282 441 67 56 N ATOM 839 CA LEU A 278 11.674 15.475 54.997 1.00 43.98 C ANISOU 839 CA LEU A 278 5625 5571 5515 487 83 79 C ATOM 840 C LEU A 278 11.548 14.173 55.773 1.00 55.37 C ANISOU 840 C LEU A 278 7074 7039 6925 522 112 193 C ATOM 841 O LEU A 278 11.780 14.135 56.981 1.00 59.73 O ANISOU 841 O LEU A 278 7604 7697 7394 587 116 216 O ATOM 842 CB LEU A 278 10.308 16.155 54.908 1.00 39.25 C ANISOU 842 CB LEU A 278 5012 4974 4926 456 103 69 C ATOM 843 CG LEU A 278 10.307 17.631 54.513 1.00 49.93 C ANISOU 843 CG LEU A 278 6350 6324 6297 439 74 -39 C ATOM 844 CD1 LEU A 278 8.891 18.184 54.533 1.00 53.33 C ANISOU 844 CD1 LEU A 278 6768 6767 6730 421 95 -41 C ATOM 845 CD2 LEU A 278 11.210 18.425 55.441 1.00 48.44 C ANISOU 845 CD2 LEU A 278 6134 6221 6051 496 40 -116 C ATOM 846 N LYS A 279 11.169 13.109 55.074 1.00 58.73 N ANISOU 846 N LYS A 279 7526 7369 7421 482 129 264 N ATOM 847 CA LYS A 279 11.015 11.807 55.705 1.00 67.55 C ANISOU 847 CA LYS A 279 8650 8484 8534 506 155 385 C ATOM 848 C LYS A 279 12.311 11.365 56.367 1.00 64.93 C ANISOU 848 C LYS A 279 8321 8201 8148 575 136 398 C ATOM 849 O LYS A 279 12.329 11.038 57.551 1.00 69.81 O ANISOU 849 O LYS A 279 8921 8911 8693 634 155 468 O ATOM 850 CB LYS A 279 10.547 10.763 54.689 1.00 69.23 C ANISOU 850 CB LYS A 279 8888 8561 8854 449 162 435 C ATOM 851 CG LYS A 279 9.061 10.830 54.396 1.00 69.12 C ANISOU 851 CG LYS A 279 8862 8517 8884 391 191 465 C ATOM 852 CD LYS A 279 8.264 10.843 55.691 1.00 65.65 C ANISOU 852 CD LYS A 279 8388 8181 8374 420 230 550 C ATOM 853 CE LYS A 279 6.769 10.778 55.433 1.00 66.33 C ANISOU 853 CE LYS A 279 8456 8241 8506 362 263 592 C ATOM 854 NZ LYS A 279 6.001 10.654 56.704 1.00 72.17 N ANISOU 854 NZ LYS A 279 9155 9092 9174 393 305 692 N ATOM 855 N THR A 280 13.397 11.371 55.603 1.00 75.65 N ANISOU 855 N THR A 280 9698 9509 9536 573 101 332 N ATOM 856 CA THR A 280 14.691 10.941 56.121 1.00 82.60 C ANISOU 856 CA THR A 280 10581 10435 10370 638 80 336 C ATOM 857 C THR A 280 15.016 11.560 57.483 1.00 87.53 C ANISOU 857 C THR A 280 11169 11208 10880 709 79 321 C ATOM 858 O THR A 280 15.451 10.861 58.398 1.00 91.23 O ANISOU 858 O THR A 280 11633 11741 11291 776 87 391 O ATOM 859 CB THR A 280 15.832 11.252 55.127 1.00 77.85 C ANISOU 859 CB THR A 280 9989 9791 9799 626 39 240 C ATOM 860 OG1 THR A 280 16.254 12.612 55.284 1.00 77.89 O ANISOU 860 OG1 THR A 280 9964 9867 9762 628 17 138 O ATOM 861 CG2 THR A 280 15.373 11.019 53.693 1.00 71.83 C ANISOU 861 CG2 THR A 280 9249 8908 9136 556 37 224 C ATOM 862 N ILE A 281 14.792 12.865 57.617 1.00 86.26 N ANISOU 862 N ILE A 281 10981 11105 10689 700 67 227 N ATOM 863 CA ILE A 281 15.206 13.597 58.819 1.00 91.19 C ANISOU 863 CA ILE A 281 11564 11874 11210 772 52 177 C ATOM 864 C ILE A 281 14.271 13.362 60.010 1.00 99.70 C ANISOU 864 C ILE A 281 12616 13057 12210 820 90 261 C ATOM 865 O ILE A 281 14.700 13.395 61.169 1.00105.96 O ANISOU 865 O ILE A 281 13376 13984 12900 905 86 266 O ATOM 866 CB ILE A 281 15.418 15.103 58.542 1.00 80.03 C ANISOU 866 CB ILE A 281 10127 10476 9806 750 16 34 C ATOM 867 CG1 ILE A 281 14.095 15.818 58.257 1.00 72.21 C ANISOU 867 CG1 ILE A 281 9131 9459 8847 702 33 17 C ATOM 868 CG2 ILE A 281 16.379 15.286 57.376 1.00 76.09 C ANISOU 868 CG2 ILE A 281 9644 9886 9380 704 -15 -29 C ATOM 869 CD1 ILE A 281 14.282 17.216 57.699 1.00 66.57 C ANISOU 869 CD1 ILE A 281 8401 8717 8176 666 -4 -110 C ATOM 870 N ASN A 282 12.997 13.132 59.709 1.00 98.65 N ANISOU 870 N ASN A 282 12490 12872 12120 769 126 326 N ATOM 871 CA ASN A 282 12.068 12.535 60.663 1.00100.04 C ANISOU 871 CA ASN A 282 12644 13126 12241 802 172 450 C ATOM 872 C ASN A 282 10.891 11.870 59.946 1.00 98.12 C ANISOU 872 C ASN A 282 12420 12770 12091 723 209 539 C ATOM 873 O ASN A 282 10.404 12.379 58.924 1.00 98.86 O ANISOU 873 O ASN A 282 12529 12773 12259 652 201 474 O ATOM 874 CB ASN A 282 11.571 13.548 61.689 1.00102.90 C ANISOU 874 CB ASN A 282 12952 13645 12499 858 173 397 C ATOM 875 CG ASN A 282 10.751 12.902 62.788 1.00107.66 C ANISOU 875 CG ASN A 282 13520 14362 13023 908 223 534 C ATOM 876 OD1 ASN A 282 11.043 11.789 63.232 1.00112.33 O ANISOU 876 OD1 ASN A 282 14116 14965 13599 940 247 662 O ATOM 877 ND2 ASN A 282 9.719 13.600 63.237 1.00105.45 N ANISOU 877 ND2 ASN A 282 13201 14172 12694 918 240 515 N ATOM 878 N GLN A 283 10.438 10.738 60.482 1.00 97.48 N ANISOU 878 N GLN A 283 12334 12694 12008 736 249 691 N ATOM 879 CA GLN A 283 9.436 9.925 59.806 1.00 96.95 C ANISOU 879 CA GLN A 283 12283 12506 12048 659 279 782 C ATOM 880 C GLN A 283 8.009 10.278 60.220 1.00 95.03 C ANISOU 880 C GLN A 283 11999 12330 11777 638 320 827 C ATOM 881 O GLN A 283 7.047 9.719 59.691 1.00 88.49 O ANISOU 881 O GLN A 283 11173 11413 11036 569 345 895 O ATOM 882 CB GLN A 283 9.712 8.444 60.059 1.00102.26 C ANISOU 882 CB GLN A 283 12970 13120 12762 673 297 928 C ATOM 883 CG GLN A 283 10.950 7.906 59.350 1.00106.20 C ANISOU 883 CG GLN A 283 13516 13516 13320 678 256 886 C ATOM 884 CD GLN A 283 10.938 8.196 57.862 1.00111.49 C ANISOU 884 CD GLN A 283 14218 14051 14090 601 226 777 C ATOM 885 OE1 GLN A 283 9.890 8.150 57.217 1.00109.96 O ANISOU 885 OE1 GLN A 283 14023 13784 13971 531 241 786 O ATOM 886 NE2 GLN A 283 12.107 8.496 57.308 1.00118.65 N ANISOU 886 NE2 GLN A 283 15147 14937 14996 618 183 675 N ATOM 887 N GLU A 284 7.881 11.205 61.165 1.00103.30 N ANISOU 887 N GLU A 284 13003 13539 12706 702 322 782 N ATOM 888 CA GLU A 284 6.573 11.658 61.631 1.00106.99 C ANISOU 888 CA GLU A 284 13424 14097 13128 697 356 810 C ATOM 889 C GLU A 284 6.136 12.937 60.938 1.00 94.71 C ANISOU 889 C GLU A 284 11872 12521 11593 660 330 661 C ATOM 890 O GLU A 284 5.241 13.629 61.413 1.00 90.57 O ANISOU 890 O GLU A 284 11307 12098 11009 679 345 641 O ATOM 891 CB GLU A 284 6.593 11.879 63.141 1.00117.78 C ANISOU 891 CB GLU A 284 14734 15674 14344 802 374 851 C ATOM 892 CG GLU A 284 6.331 10.624 63.938 1.00125.03 C ANISOU 892 CG GLU A 284 15627 16640 15239 829 426 1050 C ATOM 893 CD GLU A 284 6.963 10.671 65.305 1.00131.75 C ANISOU 893 CD GLU A 284 16435 17685 15940 951 429 1082 C ATOM 894 OE1 GLU A 284 8.009 11.338 65.453 1.00132.56 O ANISOU 894 OE1 GLU A 284 16546 17834 15988 1006 381 952 O ATOM 895 OE2 GLU A 284 6.417 10.034 66.228 1.00134.73 O ANISOU 895 OE2 GLU A 284 16764 18174 16253 992 480 1240 O ATOM 896 N SER A 285 6.771 13.249 59.815 1.00 84.89 N ANISOU 896 N SER A 285 10673 11151 10431 613 291 562 N ATOM 897 CA SER A 285 6.436 14.456 59.075 1.00 74.29 C ANISOU 897 CA SER A 285 9335 9775 9118 578 265 431 C ATOM 898 C SER A 285 5.170 14.278 58.256 1.00 64.30 C ANISOU 898 C SER A 285 8073 8429 7931 499 291 466 C ATOM 899 O SER A 285 5.117 13.434 57.356 1.00 58.25 O ANISOU 899 O SER A 285 7336 7535 7260 438 297 512 O ATOM 900 CB SER A 285 7.581 14.853 58.141 1.00 70.76 C ANISOU 900 CB SER A 285 8926 9232 8729 556 217 327 C ATOM 901 OG SER A 285 8.808 14.949 58.839 1.00 67.31 O ANISOU 901 OG SER A 285 8484 8864 8228 623 190 293 O ATOM 902 N CYS A 286 4.148 15.065 58.574 1.00 67.03 N ANISOU 902 N CYS A 286 8383 8853 8234 507 304 437 N ATOM 903 CA CYS A 286 3.021 15.203 57.677 1.00 69.51 C ANISOU 903 CA CYS A 286 8698 9095 8618 437 319 432 C ATOM 904 C CYS A 286 3.571 15.910 56.452 1.00 66.73 C ANISOU 904 C CYS A 286 8385 8633 8338 398 276 316 C ATOM 905 O CYS A 286 4.385 16.829 56.567 1.00 66.74 O ANISOU 905 O CYS A 286 8390 8659 8310 435 239 217 O ATOM 906 CB CYS A 286 1.902 16.041 58.310 1.00 69.80 C ANISOU 906 CB CYS A 286 8686 9252 8583 467 335 409 C ATOM 907 SG CYS A 286 0.402 15.096 58.797 0.50 48.76 S ANISOU 907 SG CYS A 286 5972 6645 5909 439 402 567 S ATOM 908 N ILE A 287 3.165 15.451 55.278 1.00 60.84 N ANISOU 908 N ILE A 287 7661 7769 7688 327 281 330 N ATOM 909 CA ILE A 287 3.503 16.136 54.047 1.00 48.82 C ANISOU 909 CA ILE A 287 6166 6158 6227 291 248 234 C ATOM 910 C ILE A 287 2.444 17.209 53.846 1.00 44.30 C ANISOU 910 C ILE A 287 5572 5617 5645 283 251 177 C ATOM 911 O ILE A 287 2.511 18.012 52.921 1.00 38.98 O ANISOU 911 O ILE A 287 4911 4888 5013 261 227 100 O ATOM 912 CB ILE A 287 3.548 15.152 52.863 1.00 40.91 C ANISOU 912 CB ILE A 287 5191 5030 5322 231 248 266 C ATOM 913 CG1 ILE A 287 2.274 14.302 52.815 1.00 41.52 C ANISOU 913 CG1 ILE A 287 5249 5089 5439 188 286 351 C ATOM 914 CG2 ILE A 287 4.763 14.247 52.986 1.00 35.02 C ANISOU 914 CG2 ILE A 287 4471 4249 4587 249 235 300 C ATOM 915 CD1 ILE A 287 1.096 14.984 52.146 1.00 32.78 C ANISOU 915 CD1 ILE A 287 4124 3978 4354 151 293 308 C ATOM 916 N GLU A 288 1.479 17.225 54.758 1.00 48.83 N ANISOU 916 N GLU A 288 6107 6287 6159 307 281 221 N ATOM 917 CA GLU A 288 0.317 18.103 54.667 1.00 45.71 C ANISOU 917 CA GLU A 288 5685 5934 5749 305 288 178 C ATOM 918 C GLU A 288 0.651 19.595 54.545 1.00 40.97 C ANISOU 918 C GLU A 288 5088 5345 5135 339 246 52 C ATOM 919 O GLU A 288 0.149 20.270 53.648 1.00 43.64 O ANISOU 919 O GLU A 288 5432 5629 5519 310 235 1 O ATOM 920 CB GLU A 288 -0.603 17.851 55.858 1.00 56.62 C ANISOU 920 CB GLU A 288 7017 7446 7050 341 326 249 C ATOM 921 CG GLU A 288 -2.027 17.561 55.467 1.00 66.72 C ANISOU 921 CG GLU A 288 8269 8722 8359 293 361 299 C ATOM 922 CD GLU A 288 -2.573 16.356 56.193 1.00 71.96 C ANISOU 922 CD GLU A 288 8899 9436 9007 281 409 441 C ATOM 923 OE1 GLU A 288 -1.934 15.283 56.128 1.00 69.80 O ANISOU 923 OE1 GLU A 288 8647 9094 8780 257 415 515 O ATOM 924 OE2 GLU A 288 -3.639 16.484 56.825 1.00 68.02 O ANISOU 924 OE2 GLU A 288 8348 9045 8453 296 441 481 O ATOM 925 N PRO A 289 1.489 20.119 55.452 1.00 41.73 N ANISOU 925 N PRO A 289 5176 5510 5171 402 220 3 N ATOM 926 CA PRO A 289 1.876 21.531 55.366 1.00 38.62 C ANISOU 926 CA PRO A 289 4781 5110 4782 431 173 -121 C ATOM 927 C PRO A 289 2.501 21.866 54.011 1.00 42.17 C ANISOU 927 C PRO A 289 5267 5427 5328 376 147 -161 C ATOM 928 O PRO A 289 2.281 22.956 53.481 1.00 38.64 O ANISOU 928 O PRO A 289 4820 4942 4920 371 123 -233 O ATOM 929 CB PRO A 289 2.920 21.672 56.475 1.00 42.07 C ANISOU 929 CB PRO A 289 5205 5628 5153 498 147 -156 C ATOM 930 CG PRO A 289 2.573 20.598 57.452 1.00 46.28 C ANISOU 930 CG PRO A 289 5715 6262 5609 528 190 -50 C ATOM 931 CD PRO A 289 2.085 19.452 56.623 1.00 45.49 C ANISOU 931 CD PRO A 289 5637 6074 5573 454 230 57 C ATOM 932 N LEU A 290 3.271 20.933 53.462 1.00 37.11 N ANISOU 932 N LEU A 290 4654 4721 4725 340 153 -110 N ATOM 933 CA LEU A 290 3.914 21.131 52.168 1.00 31.96 C ANISOU 933 CA LEU A 290 4029 3961 4152 294 133 -137 C ATOM 934 C LEU A 290 2.875 21.150 51.050 1.00 38.19 C ANISOU 934 C LEU A 290 4822 4694 4994 246 151 -123 C ATOM 935 O LEU A 290 2.889 22.029 50.187 1.00 32.48 O ANISOU 935 O LEU A 290 4103 3922 4317 229 132 -171 O ATOM 936 CB LEU A 290 4.935 20.021 51.916 1.00 38.17 C ANISOU 936 CB LEU A 290 4840 4708 4956 279 135 -89 C ATOM 937 CG LEU A 290 5.998 20.251 50.843 1.00 40.79 C ANISOU 937 CG LEU A 290 5190 4963 5346 252 107 -124 C ATOM 938 CD1 LEU A 290 6.862 21.450 51.198 1.00 46.95 C ANISOU 938 CD1 LEU A 290 5956 5760 6122 279 68 -204 C ATOM 939 CD2 LEU A 290 6.853 19.006 50.681 1.00 43.69 C ANISOU 939 CD2 LEU A 290 5577 5303 5721 247 111 -73 C ATOM 940 N ALA A 291 1.976 20.172 51.076 1.00 31.82 N ANISOU 940 N ALA A 291 4010 3897 4182 224 187 -52 N ATOM 941 CA ALA A 291 0.927 20.060 50.070 1.00 27.79 C ANISOU 941 CA ALA A 291 3496 3345 3718 180 203 -40 C ATOM 942 C ALA A 291 -0.005 21.265 50.102 1.00 32.66 C ANISOU 942 C ALA A 291 4093 3998 4319 198 199 -92 C ATOM 943 O ALA A 291 -0.478 21.723 49.063 1.00 34.80 O ANISOU 943 O ALA A 291 4365 4225 4633 173 195 -116 O ATOM 944 CB ALA A 291 0.140 18.776 50.273 1.00 29.12 C ANISOU 944 CB ALA A 291 3653 3521 3891 153 240 45 C ATOM 945 N GLU A 292 -0.266 21.774 51.301 1.00 36.39 N ANISOU 945 N GLU A 292 4542 4559 4726 248 199 -112 N ATOM 946 CA GLU A 292 -1.150 22.920 51.468 1.00 42.69 C ANISOU 946 CA GLU A 292 5317 5399 5504 278 190 -170 C ATOM 947 C GLU A 292 -0.510 24.197 50.936 1.00 36.96 C ANISOU 947 C GLU A 292 4605 4614 4823 289 146 -254 C ATOM 948 O GLU A 292 -1.188 25.053 50.371 1.00 35.05 O ANISOU 948 O GLU A 292 4357 4350 4609 289 137 -291 O ATOM 949 CB GLU A 292 -1.542 23.083 52.938 1.00 36.65 C ANISOU 949 CB GLU A 292 4517 4758 4649 340 197 -175 C ATOM 950 CG GLU A 292 -2.418 21.956 53.456 1.00 48.57 C ANISOU 950 CG GLU A 292 6001 6337 6117 328 246 -77 C ATOM 951 CD GLU A 292 -2.778 22.112 54.919 1.00 59.30 C ANISOU 951 CD GLU A 292 7317 7842 7373 398 257 -73 C ATOM 952 OE1 GLU A 292 -2.122 22.915 55.616 1.00 59.50 O ANISOU 952 OE1 GLU A 292 7337 7914 7357 460 221 -150 O ATOM 953 OE2 GLU A 292 -3.718 21.426 55.371 1.00 62.81 O ANISOU 953 OE2 GLU A 292 7726 8360 7779 392 300 8 O ATOM 954 N SER A 293 0.801 24.316 51.115 1.00 36.54 N ANISOU 954 N SER A 293 4567 4535 4783 297 118 -279 N ATOM 955 CA SER A 293 1.536 25.474 50.621 1.00 35.60 C ANISOU 955 CA SER A 293 4455 4351 4721 299 76 -347 C ATOM 956 C SER A 293 1.501 25.527 49.097 1.00 34.32 C ANISOU 956 C SER A 293 4309 4101 4631 247 81 -322 C ATOM 957 O SER A 293 1.355 26.598 48.507 1.00 39.90 O ANISOU 957 O SER A 293 5012 4762 5386 246 61 -359 O ATOM 958 CB SER A 293 2.983 25.439 51.114 1.00 38.08 C ANISOU 958 CB SER A 293 4774 4662 5034 312 48 -371 C ATOM 959 OG SER A 293 3.721 26.538 50.609 1.00 57.50 O ANISOU 959 OG SER A 293 7232 7052 7562 304 7 -429 O ATOM 960 N ILE A 294 1.635 24.365 48.467 1.00 30.67 N ANISOU 960 N ILE A 294 3862 3617 4176 208 107 -259 N ATOM 961 CA ILE A 294 1.619 24.271 47.012 1.00 23.94 C ANISOU 961 CA ILE A 294 3017 2701 3376 168 112 -238 C ATOM 962 C ILE A 294 0.215 24.500 46.467 1.00 27.32 C ANISOU 962 C ILE A 294 3433 3138 3809 161 131 -233 C ATOM 963 O ILE A 294 0.025 25.245 45.506 1.00 26.15 O ANISOU 963 O ILE A 294 3282 2953 3700 155 122 -246 O ATOM 964 CB ILE A 294 2.122 22.898 46.531 1.00 33.42 C ANISOU 964 CB ILE A 294 4233 3882 4583 139 128 -187 C ATOM 965 CG1 ILE A 294 3.528 22.624 47.068 1.00 35.93 C ANISOU 965 CG1 ILE A 294 4562 4198 4892 151 110 -191 C ATOM 966 CG2 ILE A 294 2.105 22.825 45.011 1.00 33.99 C ANISOU 966 CG2 ILE A 294 4306 3908 4701 109 129 -177 C ATOM 967 CD1 ILE A 294 4.040 21.233 46.754 1.00 28.67 C ANISOU 967 CD1 ILE A 294 3657 3261 3976 133 121 -145 C ATOM 968 N THR A 295 -0.764 23.851 47.088 1.00 26.57 N ANISOU 968 N THR A 295 3327 3097 3673 165 157 -209 N ATOM 969 CA THR A 295 -2.156 23.974 46.674 1.00 23.69 C ANISOU 969 CA THR A 295 2943 2754 3306 158 177 -205 C ATOM 970 C THR A 295 -2.637 25.412 46.819 1.00 28.49 C ANISOU 970 C THR A 295 3539 3373 3912 197 157 -261 C ATOM 971 O THR A 295 -3.340 25.934 45.954 1.00 25.50 O ANISOU 971 O THR A 295 3153 2977 3557 193 157 -270 O ATOM 972 CB THR A 295 -3.069 23.050 47.504 1.00 24.57 C ANISOU 972 CB THR A 295 3033 2929 3371 155 210 -163 C ATOM 973 OG1 THR A 295 -2.679 21.687 47.304 1.00 35.09 O ANISOU 973 OG1 THR A 295 4376 4233 4725 117 225 -107 O ATOM 974 CG2 THR A 295 -4.524 23.222 47.092 1.00 23.82 C ANISOU 974 CG2 THR A 295 2912 2865 3274 148 228 -163 C ATOM 975 N ASP A 296 -2.245 26.045 47.919 1.00 30.82 N ANISOU 975 N ASP A 296 3831 3699 4180 239 135 -303 N ATOM 976 CA ASP A 296 -2.634 27.420 48.203 1.00 34.66 C ANISOU 976 CA ASP A 296 4306 4192 4673 283 106 -370 C ATOM 977 C ASP A 296 -2.178 28.375 47.104 1.00 34.84 C ANISOU 977 C ASP A 296 4341 4124 4774 271 80 -387 C ATOM 978 O ASP A 296 -2.941 29.228 46.657 1.00 31.67 O ANISOU 978 O ASP A 296 3931 3708 4396 288 72 -409 O ATOM 979 CB ASP A 296 -2.075 27.859 49.560 1.00 37.10 C ANISOU 979 CB ASP A 296 4605 4546 4945 334 78 -425 C ATOM 980 CG ASP A 296 -2.265 29.338 49.819 1.00 54.62 C ANISOU 980 CG ASP A 296 6812 6751 7190 383 34 -512 C ATOM 981 OD1 ASP A 296 -1.571 30.151 49.173 1.00 58.39 O ANISOU 981 OD1 ASP A 296 7302 7137 7748 370 2 -536 O ATOM 982 OD2 ASP A 296 -3.099 29.689 50.680 1.00 71.75 O ANISOU 982 OD2 ASP A 296 8955 9000 9305 437 30 -555 O ATOM 983 N VAL A 297 -0.931 28.229 46.672 1.00 38.18 N ANISOU 983 N VAL A 297 4779 4490 5237 243 68 -371 N ATOM 984 CA VAL A 297 -0.392 29.076 45.616 1.00 34.04 C ANISOU 984 CA VAL A 297 4258 3886 4788 227 47 -369 C ATOM 985 C VAL A 297 -1.147 28.872 44.308 1.00 38.78 C ANISOU 985 C VAL A 297 4856 4477 5401 206 73 -322 C ATOM 986 O VAL A 297 -1.634 29.828 43.706 1.00 45.09 O ANISOU 986 O VAL A 297 5648 5247 6237 220 63 -328 O ATOM 987 CB VAL A 297 1.103 28.802 45.379 1.00 33.55 C ANISOU 987 CB VAL A 297 4206 3784 4757 199 35 -350 C ATOM 988 CG1 VAL A 297 1.593 29.560 44.153 1.00 36.22 C ANISOU 988 CG1 VAL A 297 4539 4053 5169 178 24 -324 C ATOM 989 CG2 VAL A 297 1.913 29.181 46.610 1.00 30.76 C ANISOU 989 CG2 VAL A 297 3849 3440 4400 225 2 -407 C ATOM 990 N LEU A 298 -1.247 27.619 43.878 1.00 38.14 N ANISOU 990 N LEU A 298 4779 4421 5292 177 103 -280 N ATOM 991 CA LEU A 298 -1.882 27.288 42.608 1.00 32.02 C ANISOU 991 CA LEU A 298 3996 3646 4524 159 123 -247 C ATOM 992 C LEU A 298 -3.345 27.728 42.539 1.00 31.94 C ANISOU 992 C LEU A 298 3969 3671 4497 181 134 -262 C ATOM 993 O LEU A 298 -3.750 28.418 41.606 1.00 34.22 O ANISOU 993 O LEU A 298 4247 3944 4809 192 131 -255 O ATOM 994 CB LEU A 298 -1.779 25.784 42.339 1.00 33.73 C ANISOU 994 CB LEU A 298 4216 3881 4720 128 145 -216 C ATOM 995 CG LEU A 298 -0.366 25.206 42.208 1.00 49.69 C ANISOU 995 CG LEU A 298 6251 5874 6754 110 136 -200 C ATOM 996 CD1 LEU A 298 -0.415 23.695 42.038 1.00 47.49 C ANISOU 996 CD1 LEU A 298 5976 5607 6462 86 152 -178 C ATOM 997 CD2 LEU A 298 0.380 25.854 41.049 1.00 48.25 C ANISOU 997 CD2 LEU A 298 6062 5659 6610 108 123 -185 C ATOM 998 N VAL A 299 -4.131 27.324 43.531 1.00 28.02 N ANISOU 998 N VAL A 299 3464 3228 3953 191 147 -277 N ATOM 999 CA VAL A 299 -5.576 27.529 43.495 1.00 33.77 C ANISOU 999 CA VAL A 299 4170 4006 4656 209 162 -288 C ATOM 1000 C VAL A 299 -5.990 28.964 43.818 1.00 42.09 C ANISOU 1000 C VAL A 299 5218 5056 5719 260 137 -334 C ATOM 1001 O VAL A 299 -6.997 29.455 43.308 1.00 40.86 O ANISOU 1001 O VAL A 299 5047 4918 5561 280 141 -342 O ATOM 1002 CB VAL A 299 -6.300 26.555 44.448 1.00 38.82 C ANISOU 1002 CB VAL A 299 4792 4715 5241 201 188 -276 C ATOM 1003 CG1 VAL A 299 -7.800 26.814 44.444 1.00 39.04 C ANISOU 1003 CG1 VAL A 299 4789 4805 5240 220 203 -289 C ATOM 1004 CG2 VAL A 299 -6.001 25.116 44.057 1.00 29.16 C ANISOU 1004 CG2 VAL A 299 3573 3481 4028 150 209 -230 C ATOM 1005 N ARG A 300 -5.212 29.634 44.661 1.00 41.89 N ANISOU 1005 N ARG A 300 5203 5005 5706 284 107 -371 N ATOM 1006 CA ARG A 300 -5.553 30.988 45.086 1.00 36.20 C ANISOU 1006 CA ARG A 300 4476 4272 5006 337 73 -430 C ATOM 1007 C ARG A 300 -5.040 32.060 44.122 1.00 30.42 C ANISOU 1007 C ARG A 300 3753 3446 4358 338 46 -423 C ATOM 1008 O ARG A 300 -5.731 33.042 43.857 1.00 37.10 O ANISOU 1008 O ARG A 300 4592 4275 5231 375 31 -445 O ATOM 1009 CB ARG A 300 -5.043 31.253 46.507 1.00 41.17 C ANISOU 1009 CB ARG A 300 5104 4926 5613 371 46 -488 C ATOM 1010 CG ARG A 300 -5.391 32.629 47.051 1.00 53.13 C ANISOU 1010 CG ARG A 300 6607 6428 7151 434 2 -568 C ATOM 1011 CD ARG A 300 -4.967 32.774 48.507 1.00 56.19 C ANISOU 1011 CD ARG A 300 6984 6867 7501 478 -26 -638 C ATOM 1012 NE ARG A 300 -3.551 32.472 48.700 1.00 53.91 N ANISOU 1012 NE ARG A 300 6710 6535 7239 447 -39 -631 N ATOM 1013 CZ ARG A 300 -2.568 33.350 48.527 1.00 54.24 C ANISOU 1013 CZ ARG A 300 6759 6483 7368 444 -84 -666 C ATOM 1014 NH1 ARG A 300 -2.843 34.592 48.154 1.00 53.93 N ANISOU 1014 NH1 ARG A 300 6715 6371 7405 468 -120 -706 N ATOM 1015 NH2 ARG A 300 -1.308 32.985 48.725 1.00 54.63 N ANISOU 1015 NH2 ARG A 300 6815 6507 7433 415 -93 -659 N ATOM 1016 N THR A 301 -3.834 31.869 43.594 1.00 25.60 N ANISOU 1016 N THR A 301 3156 2779 3791 300 42 -387 N ATOM 1017 CA THR A 301 -3.237 32.865 42.705 1.00 32.34 C ANISOU 1017 CA THR A 301 4011 3548 4730 296 20 -363 C ATOM 1018 C THR A 301 -3.529 32.595 41.229 1.00 30.35 C ANISOU 1018 C THR A 301 3751 3299 4481 277 49 -293 C ATOM 1019 O THR A 301 -3.358 33.476 40.386 1.00 37.04 O ANISOU 1019 O THR A 301 4591 4093 5389 284 38 -258 O ATOM 1020 CB THR A 301 -1.709 32.991 42.918 1.00 28.39 C ANISOU 1020 CB THR A 301 3517 2989 4280 268 -3 -361 C ATOM 1021 OG1 THR A 301 -1.038 31.880 42.312 1.00 25.64 O ANISOU 1021 OG1 THR A 301 3174 2661 3907 226 25 -306 O ATOM 1022 CG2 THR A 301 -1.376 33.039 44.401 1.00 23.66 C ANISOU 1022 CG2 THR A 301 2919 2409 3660 291 -30 -436 C ATOM 1023 N LYS A 302 -3.972 31.380 40.919 1.00 23.07 N ANISOU 1023 N LYS A 302 2826 2441 3497 256 83 -272 N ATOM 1024 CA LYS A 302 -4.311 31.023 39.543 1.00 26.53 C ANISOU 1024 CA LYS A 302 3251 2901 3929 246 107 -221 C ATOM 1025 C LYS A 302 -5.738 30.490 39.435 1.00 27.29 C ANISOU 1025 C LYS A 302 3331 3068 3969 258 130 -236 C ATOM 1026 O LYS A 302 -6.070 29.761 38.500 1.00 31.21 O ANISOU 1026 O LYS A 302 3812 3602 4443 245 150 -212 O ATOM 1027 CB LYS A 302 -3.319 29.995 38.991 1.00 27.57 C ANISOU 1027 CB LYS A 302 3386 3038 4053 207 119 -186 C ATOM 1028 CG LYS A 302 -1.868 30.449 39.027 1.00 26.49 C ANISOU 1028 CG LYS A 302 3256 2841 3967 192 99 -167 C ATOM 1029 CD LYS A 302 -1.653 31.698 38.187 1.00 30.47 C ANISOU 1029 CD LYS A 302 3746 3299 4533 207 87 -125 C ATOM 1030 CE LYS A 302 -0.197 32.138 38.219 1.00 44.19 C ANISOU 1030 CE LYS A 302 5482 4978 6331 183 67 -100 C ATOM 1031 NZ LYS A 302 0.056 33.307 37.333 1.00 51.74 N ANISOU 1031 NZ LYS A 302 6416 5885 7358 191 59 -38 N ATOM 1032 N ARG A 303 -6.574 30.869 40.396 1.00 32.94 N ANISOU 1032 N ARG A 303 4045 3809 4663 286 124 -281 N ATOM 1033 CA ARG A 303 -7.964 30.421 40.454 1.00 33.10 C ANISOU 1033 CA ARG A 303 4042 3903 4630 297 146 -297 C ATOM 1034 C ARG A 303 -8.650 30.384 39.089 1.00 29.54 C ANISOU 1034 C ARG A 303 3569 3478 4175 303 161 -270 C ATOM 1035 O ARG A 303 -9.046 29.320 38.613 1.00 29.07 O ANISOU 1035 O ARG A 303 3493 3465 4089 275 182 -261 O ATOM 1036 CB ARG A 303 -8.763 31.312 41.411 1.00 36.01 C ANISOU 1036 CB ARG A 303 4404 4294 4983 347 131 -347 C ATOM 1037 CG ARG A 303 -10.271 31.131 41.326 1.00 41.93 C ANISOU 1037 CG ARG A 303 5123 5125 5683 367 151 -361 C ATOM 1038 CD ARG A 303 -10.716 29.811 41.932 1.00 46.13 C ANISOU 1038 CD ARG A 303 5637 5727 6162 329 182 -355 C ATOM 1039 NE ARG A 303 -10.522 29.780 43.379 1.00 49.61 N ANISOU 1039 NE ARG A 303 6081 6195 6573 342 176 -381 N ATOM 1040 CZ ARG A 303 -10.997 28.828 44.176 1.00 44.20 C ANISOU 1040 CZ ARG A 303 5374 5582 5838 323 203 -368 C ATOM 1041 NH1 ARG A 303 -11.700 27.824 43.669 1.00 40.12 N ANISOU 1041 NH1 ARG A 303 4833 5102 5311 281 233 -335 N ATOM 1042 NH2 ARG A 303 -10.771 28.881 45.481 1.00 41.53 N ANISOU 1042 NH2 ARG A 303 5034 5281 5463 346 198 -387 N ATOM 1043 N ASP A 304 -8.788 31.550 38.466 1.00 28.55 N ANISOU 1043 N ASP A 304 3441 3324 4082 342 146 -258 N ATOM 1044 CA ASP A 304 -9.538 31.673 37.219 1.00 26.85 C ANISOU 1044 CA ASP A 304 3200 3149 3854 364 158 -233 C ATOM 1045 C ASP A 304 -8.866 30.982 36.039 1.00 29.86 C ANISOU 1045 C ASP A 304 3572 3539 4236 338 170 -189 C ATOM 1046 O ASP A 304 -9.541 30.500 35.131 1.00 33.09 O ANISOU 1046 O ASP A 304 3951 4011 4611 346 185 -186 O ATOM 1047 CB ASP A 304 -9.803 33.145 36.895 1.00 26.68 C ANISOU 1047 CB ASP A 304 3178 3088 3872 419 138 -221 C ATOM 1048 CG ASP A 304 -10.774 33.778 37.864 1.00 39.67 C ANISOU 1048 CG ASP A 304 4822 4749 5503 461 125 -278 C ATOM 1049 OD1 ASP A 304 -11.342 33.032 38.686 1.00 36.37 O ANISOU 1049 OD1 ASP A 304 4396 4391 5034 447 137 -319 O ATOM 1050 OD2 ASP A 304 -10.970 35.010 37.807 1.00 46.31 O ANISOU 1050 OD2 ASP A 304 5666 5544 6386 510 100 -280 O ATOM 1051 N TRP A 305 -7.538 30.940 36.050 1.00 33.31 N ANISOU 1051 N TRP A 305 4028 3922 4707 313 162 -161 N ATOM 1052 CA TRP A 305 -6.800 30.252 35.000 1.00 31.04 C ANISOU 1052 CA TRP A 305 3727 3652 4413 294 171 -124 C ATOM 1053 C TRP A 305 -7.123 28.762 35.029 1.00 28.39 C ANISOU 1053 C TRP A 305 3383 3367 4038 262 184 -158 C ATOM 1054 O TRP A 305 -7.347 28.144 33.989 1.00 30.46 O ANISOU 1054 O TRP A 305 3617 3682 4276 267 192 -156 O ATOM 1055 CB TRP A 305 -5.296 30.473 35.164 1.00 31.53 C ANISOU 1055 CB TRP A 305 3809 3651 4519 271 159 -92 C ATOM 1056 CG TRP A 305 -4.485 29.917 34.035 1.00 25.75 C ANISOU 1056 CG TRP A 305 3058 2949 3777 263 167 -51 C ATOM 1057 CD1 TRP A 305 -4.097 30.573 32.903 1.00 25.55 C ANISOU 1057 CD1 TRP A 305 3008 2937 3764 288 170 14 C ATOM 1058 CD2 TRP A 305 -3.966 28.586 33.925 1.00 20.99 C ANISOU 1058 CD2 TRP A 305 2455 2373 3146 235 171 -70 C ATOM 1059 NE1 TRP A 305 -3.366 29.734 32.096 1.00 36.14 N ANISOU 1059 NE1 TRP A 305 4329 4326 5077 280 177 31 N ATOM 1060 CE2 TRP A 305 -3.270 28.509 32.701 1.00 30.61 C ANISOU 1060 CE2 TRP A 305 3646 3630 4356 249 175 -26 C ATOM 1061 CE3 TRP A 305 -4.017 27.454 34.744 1.00 27.68 C ANISOU 1061 CE3 TRP A 305 3320 3219 3979 202 172 -115 C ATOM 1062 CZ2 TRP A 305 -2.634 27.344 32.276 1.00 27.20 C ANISOU 1062 CZ2 TRP A 305 3204 3231 3899 236 174 -40 C ATOM 1063 CZ3 TRP A 305 -3.383 26.298 34.320 1.00 21.63 C ANISOU 1063 CZ3 TRP A 305 2548 2472 3200 185 172 -122 C ATOM 1064 CH2 TRP A 305 -2.702 26.252 33.097 1.00 25.52 C ANISOU 1064 CH2 TRP A 305 3014 3000 3681 203 171 -93 C ATOM 1065 N LEU A 306 -7.150 28.193 36.229 1.00 26.25 N ANISOU 1065 N LEU A 306 3131 3080 3762 233 185 -189 N ATOM 1066 CA LEU A 306 -7.464 26.780 36.403 1.00 25.01 C ANISOU 1066 CA LEU A 306 2965 2954 3585 197 197 -212 C ATOM 1067 C LEU A 306 -8.885 26.467 35.947 1.00 25.03 C ANISOU 1067 C LEU A 306 2930 3020 3560 206 209 -237 C ATOM 1068 O LEU A 306 -9.107 25.523 35.189 1.00 26.46 O ANISOU 1068 O LEU A 306 3085 3232 3736 191 211 -251 O ATOM 1069 CB LEU A 306 -7.285 26.367 37.865 1.00 22.28 C ANISOU 1069 CB LEU A 306 2643 2586 3238 172 199 -224 C ATOM 1070 CG LEU A 306 -5.866 26.442 38.428 1.00 37.15 C ANISOU 1070 CG LEU A 306 4557 4414 5142 160 186 -210 C ATOM 1071 CD1 LEU A 306 -5.868 26.135 39.918 1.00 44.05 C ANISOU 1071 CD1 LEU A 306 5447 5288 6001 149 189 -223 C ATOM 1072 CD2 LEU A 306 -4.941 25.494 37.681 1.00 35.86 C ANISOU 1072 CD2 LEU A 306 4396 4240 4990 136 184 -194 C ATOM 1073 N VAL A 307 -9.843 27.263 36.414 1.00 23.41 N ANISOU 1073 N VAL A 307 2718 2838 3341 233 212 -250 N ATOM 1074 CA VAL A 307 -11.244 27.068 36.058 1.00 27.66 C ANISOU 1074 CA VAL A 307 3215 3444 3850 244 223 -275 C ATOM 1075 C VAL A 307 -11.440 27.085 34.545 1.00 32.93 C ANISOU 1075 C VAL A 307 3851 4152 4507 270 220 -273 C ATOM 1076 O VAL A 307 -12.168 26.260 33.994 1.00 36.14 O ANISOU 1076 O VAL A 307 4220 4611 4900 258 225 -302 O ATOM 1077 CB VAL A 307 -12.147 28.140 36.699 1.00 36.17 C ANISOU 1077 CB VAL A 307 4290 4544 4910 285 223 -290 C ATOM 1078 CG1 VAL A 307 -13.588 27.959 36.244 1.00 27.92 C ANISOU 1078 CG1 VAL A 307 3197 3580 3831 300 234 -316 C ATOM 1079 CG2 VAL A 307 -12.049 28.079 38.217 1.00 31.33 C ANISOU 1079 CG2 VAL A 307 3696 3917 4291 271 225 -301 C ATOM 1080 N LYS A 308 -10.783 28.028 33.878 1.00 26.59 N ANISOU 1080 N LYS A 308 3060 3329 3715 307 212 -236 N ATOM 1081 CA LYS A 308 -10.874 28.136 32.427 1.00 41.42 C ANISOU 1081 CA LYS A 308 4904 5260 5574 343 211 -221 C ATOM 1082 C LYS A 308 -10.279 26.906 31.743 1.00 46.14 C ANISOU 1082 C LYS A 308 5485 5879 6167 317 208 -236 C ATOM 1083 O LYS A 308 -10.683 26.540 30.638 1.00 45.93 O ANISOU 1083 O LYS A 308 5416 5924 6112 343 205 -255 O ATOM 1084 CB LYS A 308 -10.172 29.406 31.941 1.00 44.23 C ANISOU 1084 CB LYS A 308 5273 5584 5949 384 205 -157 C ATOM 1085 CG LYS A 308 -10.341 29.680 30.457 1.00 58.28 C ANISOU 1085 CG LYS A 308 7010 7435 7697 435 209 -125 C ATOM 1086 CD LYS A 308 -9.774 31.036 30.078 1.00 73.35 C ANISOU 1086 CD LYS A 308 8928 9305 9637 473 207 -45 C ATOM 1087 CE LYS A 308 -9.999 31.336 28.605 1.00 85.19 C ANISOU 1087 CE LYS A 308 10380 10893 11096 533 215 2 C ATOM 1088 NZ LYS A 308 -9.497 32.687 28.232 1.00 93.72 N ANISOU 1088 NZ LYS A 308 11464 11930 12217 569 215 99 N ATOM 1089 N GLN A 309 -9.321 26.271 32.410 1.00 38.98 N ANISOU 1089 N GLN A 309 4610 4914 5287 273 204 -234 N ATOM 1090 CA GLN A 309 -8.664 25.083 31.876 1.00 38.18 C ANISOU 1090 CA GLN A 309 4498 4820 5188 251 195 -255 C ATOM 1091 C GLN A 309 -9.414 23.807 32.245 1.00 37.49 C ANISOU 1091 C GLN A 309 4394 4739 5113 210 194 -310 C ATOM 1092 O GLN A 309 -8.916 22.703 32.024 1.00 36.63 O ANISOU 1092 O GLN A 309 4279 4616 5021 185 182 -335 O ATOM 1093 CB GLN A 309 -7.223 24.998 32.385 1.00 32.59 C ANISOU 1093 CB GLN A 309 3830 4046 4506 228 190 -224 C ATOM 1094 CG GLN A 309 -6.295 26.039 31.791 1.00 44.80 C ANISOU 1094 CG GLN A 309 5381 5588 6054 260 188 -166 C ATOM 1095 CD GLN A 309 -5.971 25.761 30.339 1.00 56.78 C ANISOU 1095 CD GLN A 309 6856 7179 7540 296 185 -158 C ATOM 1096 OE1 GLN A 309 -5.765 24.612 29.947 1.00 64.13 O ANISOU 1096 OE1 GLN A 309 7770 8136 8461 288 174 -201 O ATOM 1097 NE2 GLN A 309 -5.918 26.813 29.531 1.00 56.93 N ANISOU 1097 NE2 GLN A 309 6854 7234 7545 342 191 -102 N ATOM 1098 N ARG A 310 -10.608 23.963 32.807 1.00 33.42 N ANISOU 1098 N ARG A 310 3865 4242 4591 202 205 -326 N ATOM 1099 CA ARG A 310 -11.401 22.825 33.262 1.00 39.39 C ANISOU 1099 CA ARG A 310 4597 5001 5367 154 208 -364 C ATOM 1100 C ARG A 310 -10.701 22.083 34.398 1.00 33.63 C ANISOU 1100 C ARG A 310 3904 4200 4672 103 211 -344 C ATOM 1101 O ARG A 310 -10.840 20.869 34.541 1.00 32.38 O ANISOU 1101 O ARG A 310 3732 4022 4551 60 207 -364 O ATOM 1102 CB ARG A 310 -11.700 21.868 32.105 1.00 57.35 C ANISOU 1102 CB ARG A 310 6823 7318 7650 155 190 -419 C ATOM 1103 CG ARG A 310 -12.755 22.371 31.132 1.00 60.36 C ANISOU 1103 CG ARG A 310 7152 7789 7992 202 189 -450 C ATOM 1104 CD ARG A 310 -14.125 22.432 31.789 1.00 68.43 C ANISOU 1104 CD ARG A 310 8149 8839 9013 182 203 -465 C ATOM 1105 NE ARG A 310 -15.192 22.642 30.814 1.00 72.70 N ANISOU 1105 NE ARG A 310 8631 9472 9520 222 198 -509 N ATOM 1106 CZ ARG A 310 -15.839 21.661 30.193 1.00 72.74 C ANISOU 1106 CZ ARG A 310 8578 9517 9544 204 181 -577 C ATOM 1107 NH1 ARG A 310 -15.530 20.395 30.441 1.00 61.21 N ANISOU 1107 NH1 ARG A 310 7114 7998 8145 145 167 -604 N ATOM 1108 NH2 ARG A 310 -16.796 21.946 29.321 1.00 78.99 N ANISOU 1108 NH2 ARG A 310 9313 10402 10297 249 175 -619 N ATOM 1109 N GLY A 311 -9.944 22.824 35.200 1.00 33.14 N ANISOU 1109 N GLY A 311 3888 4100 4605 111 217 -305 N ATOM 1110 CA GLY A 311 -9.280 22.264 36.363 1.00 30.03 C ANISOU 1110 CA GLY A 311 3527 3652 4230 74 221 -282 C ATOM 1111 C GLY A 311 -8.341 21.115 36.049 1.00 32.26 C ANISOU 1111 C GLY A 311 3818 3892 4546 48 207 -287 C ATOM 1112 O GLY A 311 -7.427 21.247 35.236 1.00 26.02 O ANISOU 1112 O GLY A 311 3036 3096 3753 71 192 -289 O ATOM 1113 N TRP A 312 -8.575 19.977 36.695 1.00 28.05 N ANISOU 1113 N TRP A 312 3280 3331 4045 3 211 -284 N ATOM 1114 CA TRP A 312 -7.675 18.833 36.580 1.00 23.94 C ANISOU 1114 CA TRP A 312 2774 2758 3566 -20 195 -287 C ATOM 1115 C TRP A 312 -7.889 17.999 35.317 1.00 28.51 C ANISOU 1115 C TRP A 312 3314 3345 4174 -20 171 -343 C ATOM 1116 O TRP A 312 -7.069 17.143 34.987 1.00 29.06 O ANISOU 1116 O TRP A 312 3392 3375 4275 -24 149 -361 O ATOM 1117 CB TRP A 312 -7.751 17.964 37.838 1.00 19.15 C ANISOU 1117 CB TRP A 312 2177 2110 2989 -65 208 -250 C ATOM 1118 CG TRP A 312 -7.127 18.633 39.022 1.00 31.34 C ANISOU 1118 CG TRP A 312 3760 3649 4498 -52 223 -205 C ATOM 1119 CD1 TRP A 312 -7.769 19.297 40.024 1.00 34.57 C ANISOU 1119 CD1 TRP A 312 4167 4097 4872 -46 245 -181 C ATOM 1120 CD2 TRP A 312 -5.727 18.724 39.309 1.00 33.16 C ANISOU 1120 CD2 TRP A 312 4033 3845 4723 -38 212 -189 C ATOM 1121 NE1 TRP A 312 -6.856 19.788 40.927 1.00 38.79 N ANISOU 1121 NE1 TRP A 312 4738 4621 5380 -27 245 -158 N ATOM 1122 CE2 TRP A 312 -5.597 19.451 40.511 1.00 31.65 C ANISOU 1122 CE2 TRP A 312 3861 3670 4495 -24 226 -160 C ATOM 1123 CE3 TRP A 312 -4.573 18.259 38.673 1.00 22.54 C ANISOU 1123 CE3 TRP A 312 2705 2464 3397 -30 189 -201 C ATOM 1124 CZ2 TRP A 312 -4.356 19.721 41.087 1.00 31.21 C ANISOU 1124 CZ2 TRP A 312 3841 3592 4427 -8 217 -146 C ATOM 1125 CZ3 TRP A 312 -3.344 18.528 39.246 1.00 32.60 C ANISOU 1125 CZ3 TRP A 312 4014 3717 4655 -16 184 -179 C ATOM 1126 CH2 TRP A 312 -3.245 19.253 40.442 1.00 36.53 C ANISOU 1126 CH2 TRP A 312 4530 4227 5121 -7 197 -153 C ATOM 1127 N ASP A 313 -8.984 18.253 34.609 1.00 23.73 N ANISOU 1127 N ASP A 313 2664 2796 3557 -8 171 -379 N ATOM 1128 CA ASP A 313 -9.204 17.620 33.315 1.00 29.57 C ANISOU 1128 CA ASP A 313 3359 3562 4313 7 143 -447 C ATOM 1129 C ASP A 313 -8.296 18.259 32.272 1.00 30.46 C ANISOU 1129 C ASP A 313 3477 3716 4379 66 130 -455 C ATOM 1130 O ASP A 313 -7.839 17.595 31.342 1.00 32.53 O ANISOU 1130 O ASP A 313 3718 3992 4650 87 101 -503 O ATOM 1131 CB ASP A 313 -10.668 17.741 32.891 1.00 31.95 C ANISOU 1131 CB ASP A 313 3606 3925 4609 6 147 -485 C ATOM 1132 CG ASP A 313 -11.585 16.859 33.712 1.00 41.12 C ANISOU 1132 CG ASP A 313 4743 5051 5829 -60 156 -482 C ATOM 1133 OD1 ASP A 313 -11.112 15.819 34.216 1.00 50.74 O ANISOU 1133 OD1 ASP A 313 5976 6194 7110 -102 147 -470 O ATOM 1134 OD2 ASP A 313 -12.777 17.202 33.848 1.00 43.94 O ANISOU 1134 OD2 ASP A 313 5065 5459 6173 -68 172 -486 O ATOM 1135 N GLY A 314 -8.041 19.555 32.431 1.00 28.83 N ANISOU 1135 N GLY A 314 3295 3534 4127 96 149 -406 N ATOM 1136 CA GLY A 314 -7.105 20.257 31.573 1.00 22.84 C ANISOU 1136 CA GLY A 314 2539 2809 3329 146 142 -388 C ATOM 1137 C GLY A 314 -5.698 19.758 31.828 1.00 21.70 C ANISOU 1137 C GLY A 314 2429 2614 3203 136 131 -372 C ATOM 1138 O GLY A 314 -4.901 19.603 30.903 1.00 31.83 O ANISOU 1138 O GLY A 314 3696 3930 4467 171 115 -385 O ATOM 1139 N PHE A 315 -5.399 19.506 33.098 1.00 30.98 N ANISOU 1139 N PHE A 315 3645 3719 4406 95 140 -344 N ATOM 1140 CA PHE A 315 -4.126 18.924 33.500 1.00 31.63 C ANISOU 1140 CA PHE A 315 3760 3751 4507 84 129 -331 C ATOM 1141 C PHE A 315 -3.933 17.573 32.819 1.00 26.84 C ANISOU 1141 C PHE A 315 3130 3136 3931 84 100 -388 C ATOM 1142 O PHE A 315 -2.947 17.356 32.115 1.00 25.79 O ANISOU 1142 O PHE A 315 2993 3021 3784 116 81 -403 O ATOM 1143 CB PHE A 315 -4.085 18.768 35.022 1.00 31.49 C ANISOU 1143 CB PHE A 315 3782 3674 4511 44 144 -294 C ATOM 1144 CG PHE A 315 -2.875 18.037 35.534 1.00 28.06 C ANISOU 1144 CG PHE A 315 3379 3188 4096 34 133 -281 C ATOM 1145 CD1 PHE A 315 -1.667 18.696 35.697 1.00 19.28 C ANISOU 1145 CD1 PHE A 315 2292 2072 2961 53 131 -253 C ATOM 1146 CD2 PHE A 315 -2.952 16.695 35.872 1.00 24.77 C ANISOU 1146 CD2 PHE A 315 2963 2722 3726 5 122 -294 C ATOM 1147 CE1 PHE A 315 -0.555 18.027 36.176 1.00 18.67 C ANISOU 1147 CE1 PHE A 315 2241 1956 2896 48 120 -243 C ATOM 1148 CE2 PHE A 315 -1.844 16.021 36.351 1.00 24.91 C ANISOU 1148 CE2 PHE A 315 3011 2693 3762 2 111 -279 C ATOM 1149 CZ PHE A 315 -0.642 16.687 36.503 1.00 21.27 C ANISOU 1149 CZ PHE A 315 2576 2241 3266 26 110 -256 C ATOM 1150 N VAL A 316 -4.888 16.672 33.028 1.00 27.98 N ANISOU 1150 N VAL A 316 3255 3254 4121 50 95 -421 N ATOM 1151 CA VAL A 316 -4.865 15.354 32.405 1.00 24.40 C ANISOU 1151 CA VAL A 316 2775 2778 3718 47 59 -488 C ATOM 1152 C VAL A 316 -4.736 15.453 30.887 1.00 25.65 C ANISOU 1152 C VAL A 316 2888 3020 3839 107 34 -551 C ATOM 1153 O VAL A 316 -3.930 14.753 30.275 1.00 24.80 O ANISOU 1153 O VAL A 316 2771 2913 3738 135 2 -595 O ATOM 1154 CB VAL A 316 -6.142 14.554 32.742 1.00 25.14 C ANISOU 1154 CB VAL A 316 2840 2837 3876 -2 58 -514 C ATOM 1155 CG1 VAL A 316 -6.187 13.259 31.946 1.00 18.26 C ANISOU 1155 CG1 VAL A 316 1930 1938 3068 -1 12 -600 C ATOM 1156 CG2 VAL A 316 -6.218 14.273 34.236 1.00 23.92 C ANISOU 1156 CG2 VAL A 316 2721 2611 3756 -57 83 -443 C ATOM 1157 N GLU A 317 -5.532 16.329 30.286 1.00 24.44 N ANISOU 1157 N GLU A 317 2703 2945 3639 133 47 -554 N ATOM 1158 CA GLU A 317 -5.548 16.482 28.835 1.00 23.28 C ANISOU 1158 CA GLU A 317 2504 2899 3444 197 27 -606 C ATOM 1159 C GLU A 317 -4.203 16.948 28.285 1.00 29.59 C ANISOU 1159 C GLU A 317 3311 3742 4189 247 25 -574 C ATOM 1160 O GLU A 317 -3.709 16.408 27.295 1.00 32.30 O ANISOU 1160 O GLU A 317 3617 4142 4512 296 -5 -631 O ATOM 1161 CB GLU A 317 -6.651 17.454 28.412 1.00 21.24 C ANISOU 1161 CB GLU A 317 2213 2717 3140 219 47 -597 C ATOM 1162 CG GLU A 317 -7.026 17.358 26.946 1.00 27.98 C ANISOU 1162 CG GLU A 317 2997 3683 3949 284 22 -667 C ATOM 1163 CD GLU A 317 -7.602 16.003 26.581 1.00 30.59 C ANISOU 1163 CD GLU A 317 3284 4001 4337 271 -20 -779 C ATOM 1164 OE1 GLU A 317 -7.630 15.673 25.378 1.00 34.79 O ANISOU 1164 OE1 GLU A 317 3757 4623 4837 332 -53 -858 O ATOM 1165 OE2 GLU A 317 -8.026 15.267 27.498 1.00 34.74 O ANISOU 1165 OE2 GLU A 317 3828 4428 4943 202 -22 -787 O ATOM 1166 N PHE A 318 -3.614 17.951 28.929 1.00 19.22 N ANISOU 1166 N PHE A 318 2040 2407 2856 237 55 -487 N ATOM 1167 CA PHE A 318 -2.353 18.517 28.462 1.00 20.37 C ANISOU 1167 CA PHE A 318 2188 2594 2958 276 58 -442 C ATOM 1168 C PHE A 318 -1.221 17.493 28.465 1.00 16.38 C ANISOU 1168 C PHE A 318 1692 2061 2470 280 31 -474 C ATOM 1169 O PHE A 318 -0.418 17.443 27.534 1.00 18.91 O ANISOU 1169 O PHE A 318 1981 2457 2748 333 17 -485 O ATOM 1170 CB PHE A 318 -1.959 19.735 29.304 1.00 22.43 C ANISOU 1170 CB PHE A 318 2491 2816 3216 253 90 -350 C ATOM 1171 CG PHE A 318 -0.699 20.408 28.837 1.00 29.63 C ANISOU 1171 CG PHE A 318 3397 3766 4095 284 95 -294 C ATOM 1172 CD1 PHE A 318 -0.735 21.342 27.814 1.00 27.10 C ANISOU 1172 CD1 PHE A 318 3035 3534 3727 332 107 -251 C ATOM 1173 CD2 PHE A 318 0.521 20.104 29.416 1.00 25.44 C ANISOU 1173 CD2 PHE A 318 2897 3187 3580 266 89 -276 C ATOM 1174 CE1 PHE A 318 0.423 21.962 27.380 1.00 31.71 C ANISOU 1174 CE1 PHE A 318 3606 4155 4287 355 115 -185 C ATOM 1175 CE2 PHE A 318 1.682 20.721 28.987 1.00 28.24 C ANISOU 1175 CE2 PHE A 318 3239 3582 3908 290 94 -222 C ATOM 1176 CZ PHE A 318 1.632 21.651 27.968 1.00 26.86 C ANISOU 1176 CZ PHE A 318 3020 3493 3693 331 108 -173 C ATOM 1177 N PHE A 319 -1.161 16.680 29.515 1.00 20.82 N ANISOU 1177 N PHE A 319 2295 2523 3093 230 24 -485 N ATOM 1178 CA PHE A 319 -0.087 15.700 29.658 1.00 20.59 C ANISOU 1178 CA PHE A 319 2282 2453 3086 235 -2 -511 C ATOM 1179 C PHE A 319 -0.458 14.342 29.070 1.00 28.85 C ANISOU 1179 C PHE A 319 3295 3489 4175 248 -46 -611 C ATOM 1180 O PHE A 319 0.236 13.350 29.287 1.00 29.35 O ANISOU 1180 O PHE A 319 3374 3498 4278 249 -74 -643 O ATOM 1181 CB PHE A 319 0.308 15.550 31.127 1.00 20.22 C ANISOU 1181 CB PHE A 319 2296 2306 3081 182 13 -459 C ATOM 1182 CG PHE A 319 0.939 16.780 31.710 1.00 30.49 C ANISOU 1182 CG PHE A 319 3625 3612 4347 176 43 -379 C ATOM 1183 CD1 PHE A 319 2.258 17.096 31.427 1.00 21.61 C ANISOU 1183 CD1 PHE A 319 2501 2518 3190 203 39 -354 C ATOM 1184 CD2 PHE A 319 0.214 17.623 32.536 1.00 23.44 C ANISOU 1184 CD2 PHE A 319 2754 2695 3458 143 72 -335 C ATOM 1185 CE1 PHE A 319 2.842 18.231 31.959 1.00 25.16 C ANISOU 1185 CE1 PHE A 319 2972 2965 3625 192 61 -286 C ATOM 1186 CE2 PHE A 319 0.793 18.757 33.072 1.00 21.61 C ANISOU 1186 CE2 PHE A 319 2545 2460 3208 140 91 -276 C ATOM 1187 CZ PHE A 319 2.108 19.062 32.782 1.00 21.25 C ANISOU 1187 CZ PHE A 319 2499 2434 3141 161 85 -251 C ATOM 1188 N HIS A 320 -1.554 14.305 28.320 1.00 33.27 N ANISOU 1188 N HIS A 320 3808 4101 4733 263 -55 -666 N ATOM 1189 CA HIS A 320 -2.002 13.072 27.690 1.00 34.01 C ANISOU 1189 CA HIS A 320 3860 4186 4875 277 -103 -777 C ATOM 1190 C HIS A 320 -1.132 12.729 26.485 1.00 35.12 C ANISOU 1190 C HIS A 320 3958 4419 4967 359 -141 -844 C ATOM 1191 O HIS A 320 -1.096 13.471 25.503 1.00 40.42 O ANISOU 1191 O HIS A 320 4586 5218 5555 418 -134 -842 O ATOM 1192 CB HIS A 320 -3.465 13.192 27.268 1.00 31.62 C ANISOU 1192 CB HIS A 320 3512 3921 4581 268 -103 -821 C ATOM 1193 CG HIS A 320 -4.017 11.942 26.659 1.00 37.43 C ANISOU 1193 CG HIS A 320 4197 4640 5382 276 -158 -945 C ATOM 1194 ND1 HIS A 320 -4.424 10.866 27.414 1.00 37.46 N ANISOU 1194 ND1 HIS A 320 4216 4516 5500 212 -177 -969 N ATOM 1195 CD2 HIS A 320 -4.223 11.600 25.366 1.00 26.37 C ANISOU 1195 CD2 HIS A 320 2728 3336 3955 343 -201 -1053 C ATOM 1196 CE1 HIS A 320 -4.860 9.910 26.612 1.00 28.23 C ANISOU 1196 CE1 HIS A 320 2990 3351 4384 233 -233 -1092 C ATOM 1197 NE2 HIS A 320 -4.750 10.329 25.367 1.00 28.31 N ANISOU 1197 NE2 HIS A 320 2948 3501 4306 316 -250 -1153 N ATOM 1198 N VAL A 321 -0.433 11.600 26.561 1.00 35.48 N ANISOU 1198 N VAL A 321 4012 4404 5063 367 -182 -901 N ATOM 1199 CA VAL A 321 0.499 11.212 25.507 1.00 44.45 C ANISOU 1199 CA VAL A 321 5108 5631 6150 452 -222 -971 C ATOM 1200 C VAL A 321 -0.012 10.043 24.668 1.00 46.38 C ANISOU 1200 C VAL A 321 5295 5884 6443 491 -288 -1120 C ATOM 1201 O VAL A 321 -0.692 9.149 25.172 1.00 39.94 O ANISOU 1201 O VAL A 321 4489 4949 5737 438 -313 -1167 O ATOM 1202 CB VAL A 321 1.887 10.859 26.081 1.00 46.27 C ANISOU 1202 CB VAL A 321 5384 5809 6387 455 -227 -936 C ATOM 1203 CG1 VAL A 321 2.564 12.102 26.635 1.00 44.04 C ANISOU 1203 CG1 VAL A 321 5138 5551 6043 436 -171 -807 C ATOM 1204 CG2 VAL A 321 1.761 9.787 27.154 1.00 50.18 C ANISOU 1204 CG2 VAL A 321 5928 6140 6999 394 -246 -947 C ATOM 1205 N GLU A 322 0.325 10.062 23.382 1.00 46.38 N ANISOU 1205 N GLU A 322 5230 6030 6363 585 -317 -1194 N ATOM 1206 CA GLU A 322 -0.067 8.999 22.465 1.00 48.64 C ANISOU 1206 CA GLU A 322 5451 6346 6685 641 -389 -1356 C ATOM 1207 C GLU A 322 1.107 8.072 22.170 1.00 57.10 C ANISOU 1207 C GLU A 322 6516 7414 7764 702 -443 -1432 C ATOM 1208 O GLU A 322 2.117 8.495 21.605 1.00 61.43 O ANISOU 1208 O GLU A 322 7046 8087 8210 774 -435 -1409 O ATOM 1209 CB GLU A 322 -0.603 9.590 21.160 1.00 46.59 C ANISOU 1209 CB GLU A 322 5108 6273 6320 721 -393 -1406 C ATOM 1210 CG GLU A 322 -1.729 10.594 21.344 1.00 50.12 C ANISOU 1210 CG GLU A 322 5557 6742 6746 675 -341 -1330 C ATOM 1211 CD GLU A 322 -3.003 9.957 21.860 1.00 53.94 C ANISOU 1211 CD GLU A 322 6042 7107 7346 601 -359 -1388 C ATOM 1212 OE1 GLU A 322 -3.026 8.720 22.037 1.00 46.82 O ANISOU 1212 OE1 GLU A 322 5138 6100 6553 581 -414 -1485 O ATOM 1213 OE2 GLU A 322 -3.985 10.697 22.087 1.00 58.04 O ANISOU 1213 OE2 GLU A 322 6561 7638 7854 561 -319 -1334 O TER 1214 GLU A 322 ATOM 1215 N ARG B 1 18.366 35.635 47.225 1.00 69.21 N ANISOU 1215 N ARG B 1 8296 7819 10181 -118 -444 -666 N ATOM 1216 CA ARG B 1 19.404 35.230 46.279 1.00 67.35 C ANISOU 1216 CA ARG B 1 8029 7611 9951 -169 -413 -564 C ATOM 1217 C ARG B 1 19.386 33.724 46.005 1.00 60.88 C ANISOU 1217 C ARG B 1 7253 6907 8971 -136 -357 -511 C ATOM 1218 O ARG B 1 19.379 33.301 44.852 1.00 57.05 O ANISOU 1218 O ARG B 1 6772 6441 8463 -158 -310 -401 O ATOM 1219 CB ARG B 1 20.782 35.699 46.756 1.00 74.43 C ANISOU 1219 CB ARG B 1 8854 8495 10928 -203 -464 -623 C ATOM 1220 CG ARG B 1 21.918 35.309 45.827 1.00 83.16 C ANISOU 1220 CG ARG B 1 9917 9644 12037 -253 -434 -522 C ATOM 1221 CD ARG B 1 23.227 35.959 46.220 1.00 99.72 C ANISOU 1221 CD ARG B 1 11933 11715 14241 -299 -487 -575 C ATOM 1222 NE ARG B 1 23.969 36.442 45.060 1.00111.29 N ANISOU 1222 NE ARG B 1 13333 13145 15807 -376 -467 -452 N ATOM 1223 CZ ARG B 1 25.017 37.259 45.133 1.00119.56 C ANISOU 1223 CZ ARG B 1 14295 14140 16991 -438 -510 -466 C ATOM 1224 NH1 ARG B 1 25.440 37.679 46.314 1.00121.07 N ANISOU 1224 NH1 ARG B 1 14459 14308 17234 -429 -579 -613 N ATOM 1225 NH2 ARG B 1 25.642 37.664 44.032 1.00124.97 N ANISOU 1225 NH2 ARG B 1 14917 14803 17763 -508 -484 -334 N ATOM 1226 N PRO B 2 19.371 32.909 47.063 1.00 60.93 N ANISOU 1226 N PRO B 2 7290 6992 8868 -80 -365 -588 N ATOM 1227 CA PRO B 2 19.182 31.471 46.857 1.00 56.92 C ANISOU 1227 CA PRO B 2 6831 6576 8222 -45 -315 -538 C ATOM 1228 C PRO B 2 17.773 31.200 46.347 1.00 51.74 C ANISOU 1228 C PRO B 2 6227 5905 7527 -30 -274 -487 C ATOM 1229 O PRO B 2 17.579 30.348 45.480 1.00 56.74 O ANISOU 1229 O PRO B 2 6883 6572 8101 -31 -229 -407 O ATOM 1230 CB PRO B 2 19.333 30.894 48.266 1.00 62.60 C ANISOU 1230 CB PRO B 2 7565 7368 8852 15 -339 -633 C ATOM 1231 CG PRO B 2 20.033 31.960 49.056 1.00 66.23 C ANISOU 1231 CG PRO B 2 7969 7794 9402 6 -404 -735 C ATOM 1232 CD PRO B 2 19.566 33.248 48.480 1.00 62.44 C ANISOU 1232 CD PRO B 2 7466 7197 9059 -41 -421 -723 C ATOM 1233 N GLU B 3 16.799 31.926 46.887 1.00 49.39 N ANISOU 1233 N GLU B 3 5944 5562 7262 -11 -294 -541 N ATOM 1234 CA GLU B 3 15.405 31.754 46.492 1.00 51.89 C ANISOU 1234 CA GLU B 3 6304 5868 7543 6 -259 -502 C ATOM 1235 C GLU B 3 15.157 32.207 45.051 1.00 48.92 C ANISOU 1235 C GLU B 3 5917 5437 7234 -38 -232 -403 C ATOM 1236 O GLU B 3 14.316 31.640 44.352 1.00 42.80 O ANISOU 1236 O GLU B 3 5174 4684 6406 -29 -190 -343 O ATOM 1237 CB GLU B 3 14.475 32.492 47.463 1.00 49.83 C ANISOU 1237 CB GLU B 3 6053 5581 7300 43 -292 -591 C ATOM 1238 CG GLU B 3 14.647 32.067 48.920 1.00 55.03 C ANISOU 1238 CG GLU B 3 6715 6315 7878 99 -318 -688 C ATOM 1239 CD GLU B 3 13.548 32.593 49.826 1.00 67.62 C ANISOU 1239 CD GLU B 3 8321 7915 9458 151 -340 -769 C ATOM 1240 OE1 GLU B 3 12.844 33.544 49.425 1.00 65.26 O ANISOU 1240 OE1 GLU B 3 8019 7539 9239 140 -352 -773 O ATOM 1241 OE2 GLU B 3 13.389 32.055 50.942 1.00 78.12 O ANISOU 1241 OE2 GLU B 3 9658 9333 10691 209 -345 -825 O ATOM 1242 N ILE B 4 15.893 33.227 44.614 1.00 41.57 N ANISOU 1242 N ILE B 4 4935 4438 6420 -85 -257 -382 N ATOM 1243 CA ILE B 4 15.794 33.710 43.239 1.00 36.57 C ANISOU 1243 CA ILE B 4 4280 3764 5852 -124 -230 -272 C ATOM 1244 C ILE B 4 16.347 32.658 42.281 1.00 37.97 C ANISOU 1244 C ILE B 4 4453 4024 5951 -132 -185 -187 C ATOM 1245 O ILE B 4 15.764 32.394 41.229 1.00 34.74 O ANISOU 1245 O ILE B 4 4053 3634 5512 -129 -145 -108 O ATOM 1246 CB ILE B 4 16.548 35.045 43.032 1.00 43.61 C ANISOU 1246 CB ILE B 4 5109 4561 6901 -177 -267 -258 C ATOM 1247 CG1 ILE B 4 15.965 36.147 43.921 1.00 55.64 C ANISOU 1247 CG1 ILE B 4 6634 5991 8516 -165 -321 -353 C ATOM 1248 CG2 ILE B 4 16.472 35.486 41.576 1.00 36.87 C ANISOU 1248 CG2 ILE B 4 4227 3680 6104 -214 -232 -121 C ATOM 1249 CD1 ILE B 4 16.208 35.970 45.398 1.00 66.38 C ANISOU 1249 CD1 ILE B 4 8000 7382 9839 -127 -366 -494 C ATOM 1250 N TRP B 5 17.473 32.059 42.658 1.00 31.72 N ANISOU 1250 N TRP B 5 3644 3287 5123 -133 -194 -212 N ATOM 1251 CA TRP B 5 18.085 31.003 41.864 1.00 26.43 C ANISOU 1251 CA TRP B 5 2968 2702 4374 -130 -160 -149 C ATOM 1252 C TRP B 5 17.160 29.793 41.752 1.00 25.20 C ANISOU 1252 C TRP B 5 2873 2599 4104 -84 -126 -147 C ATOM 1253 O TRP B 5 17.013 29.211 40.677 1.00 35.09 O ANISOU 1253 O TRP B 5 4125 3894 5313 -79 -92 -81 O ATOM 1254 CB TRP B 5 19.428 30.587 42.467 1.00 33.52 C ANISOU 1254 CB TRP B 5 3838 3647 5251 -131 -182 -191 C ATOM 1255 CG TRP B 5 20.104 29.496 41.697 1.00 37.80 C ANISOU 1255 CG TRP B 5 4372 4279 5711 -118 -152 -137 C ATOM 1256 CD1 TRP B 5 20.936 29.643 40.626 1.00 37.57 C ANISOU 1256 CD1 TRP B 5 4285 4286 5705 -147 -137 -57 C ATOM 1257 CD2 TRP B 5 19.997 28.086 41.932 1.00 38.59 C ANISOU 1257 CD2 TRP B 5 4520 4447 5696 -69 -137 -159 C ATOM 1258 NE1 TRP B 5 21.357 28.413 40.182 1.00 43.46 N ANISOU 1258 NE1 TRP B 5 5040 5123 6350 -113 -116 -40 N ATOM 1259 CE2 TRP B 5 20.795 27.441 40.966 1.00 41.58 C ANISOU 1259 CE2 TRP B 5 4869 4897 6034 -66 -117 -103 C ATOM 1260 CE3 TRP B 5 19.307 27.308 42.866 1.00 37.92 C ANISOU 1260 CE3 TRP B 5 4496 4371 5542 -25 -138 -216 C ATOM 1261 CZ2 TRP B 5 20.921 26.054 40.908 1.00 35.47 C ANISOU 1261 CZ2 TRP B 5 4127 4188 5161 -19 -105 -114 C ATOM 1262 CZ3 TRP B 5 19.434 25.932 42.806 1.00 33.11 C ANISOU 1262 CZ3 TRP B 5 3918 3823 4841 14 -121 -212 C ATOM 1263 CH2 TRP B 5 20.235 25.319 41.834 1.00 34.83 C ANISOU 1263 CH2 TRP B 5 4109 4097 5029 18 -108 -166 C ATOM 1264 N ILE B 6 16.541 29.422 42.869 1.00 21.18 N ANISOU 1264 N ILE B 6 2408 2090 3548 -50 -137 -222 N ATOM 1265 CA ILE B 6 15.595 28.313 42.890 1.00 27.58 C ANISOU 1265 CA ILE B 6 3272 2939 4267 -13 -108 -219 C ATOM 1266 C ILE B 6 14.417 28.589 41.959 1.00 31.73 C ANISOU 1266 C ILE B 6 3810 3440 4807 -18 -81 -169 C ATOM 1267 O ILE B 6 13.984 27.710 41.215 1.00 33.30 O ANISOU 1267 O ILE B 6 4026 3677 4950 -4 -51 -132 O ATOM 1268 CB ILE B 6 15.072 28.042 44.315 1.00 27.14 C ANISOU 1268 CB ILE B 6 3253 2893 4168 23 -123 -295 C ATOM 1269 CG1 ILE B 6 16.238 27.757 45.265 1.00 27.41 C ANISOU 1269 CG1 ILE B 6 3271 2964 4178 38 -151 -346 C ATOM 1270 CG2 ILE B 6 14.090 26.878 44.313 1.00 26.13 C ANISOU 1270 CG2 ILE B 6 3172 2799 3958 53 -90 -278 C ATOM 1271 CD1 ILE B 6 15.818 27.533 46.703 1.00 30.22 C ANISOU 1271 CD1 ILE B 6 3651 3349 4481 83 -167 -417 C ATOM 1272 N ALA B 7 13.906 29.816 42.003 1.00 29.40 N ANISOU 1272 N ALA B 7 3502 3079 4589 -33 -95 -175 N ATOM 1273 CA ALA B 7 12.813 30.222 41.129 1.00 28.73 C ANISOU 1273 CA ALA B 7 3422 2970 4522 -34 -73 -126 C ATOM 1274 C ALA B 7 13.224 30.120 39.665 1.00 24.03 C ANISOU 1274 C ALA B 7 2793 2406 3930 -50 -45 -33 C ATOM 1275 O ALA B 7 12.436 29.700 38.818 1.00 25.67 O ANISOU 1275 O ALA B 7 3013 2646 4096 -34 -16 6 O ATOM 1276 CB ALA B 7 12.365 31.639 41.460 1.00 31.74 C ANISOU 1276 CB ALA B 7 3791 3268 4999 -44 -100 -149 C ATOM 1277 N GLN B 8 14.463 30.505 39.375 1.00 27.20 N ANISOU 1277 N GLN B 8 3148 2809 4379 -80 -56 0 N ATOM 1278 CA GLN B 8 14.993 30.442 38.017 1.00 29.28 C ANISOU 1278 CA GLN B 8 3366 3122 4638 -91 -30 94 C ATOM 1279 C GLN B 8 15.015 29.010 37.487 1.00 26.07 C ANISOU 1279 C GLN B 8 2976 2807 4121 -57 -5 97 C ATOM 1280 O GLN B 8 14.663 28.764 36.335 1.00 26.46 O ANISOU 1280 O GLN B 8 3010 2908 4137 -41 22 154 O ATOM 1281 CB GLN B 8 16.398 31.050 37.956 1.00 34.03 C ANISOU 1281 CB GLN B 8 3906 3715 5307 -131 -47 126 C ATOM 1282 CG GLN B 8 16.441 32.547 38.226 1.00 53.60 C ANISOU 1282 CG GLN B 8 6355 6091 7922 -172 -74 137 C ATOM 1283 CD GLN B 8 17.852 33.107 38.236 1.00 65.90 C ANISOU 1283 CD GLN B 8 7845 7635 9558 -219 -94 165 C ATOM 1284 OE1 GLN B 8 18.818 32.387 38.487 1.00 68.19 O ANISOU 1284 OE1 GLN B 8 8123 7991 9798 -217 -98 139 O ATOM 1285 NE2 GLN B 8 17.975 34.402 37.967 1.00 76.05 N ANISOU 1285 NE2 GLN B 8 9085 8836 10976 -263 -108 219 N ATOM 1286 N GLU B 9 15.431 28.071 38.332 1.00 28.75 N ANISOU 1286 N GLU B 9 3345 3170 4407 -40 -17 33 N ATOM 1287 CA GLU B 9 15.498 26.665 37.939 1.00 30.95 C ANISOU 1287 CA GLU B 9 3642 3520 4597 -5 -2 26 C ATOM 1288 C GLU B 9 14.116 26.100 37.648 1.00 26.16 C ANISOU 1288 C GLU B 9 3075 2914 3950 19 16 16 C ATOM 1289 O GLU B 9 13.886 25.514 36.591 1.00 28.60 O ANISOU 1289 O GLU B 9 3372 3276 4217 41 34 43 O ATOM 1290 CB GLU B 9 16.174 25.826 39.024 1.00 33.04 C ANISOU 1290 CB GLU B 9 3933 3797 4823 10 -22 -36 C ATOM 1291 CG GLU B 9 17.648 26.111 39.199 1.00 34.10 C ANISOU 1291 CG GLU B 9 4023 3955 4980 -7 -40 -33 C ATOM 1292 CD GLU B 9 18.414 26.020 37.897 1.00 41.47 C ANISOU 1292 CD GLU B 9 4900 4956 5900 -8 -25 33 C ATOM 1293 OE1 GLU B 9 18.179 25.071 37.120 1.00 36.15 O ANISOU 1293 OE1 GLU B 9 4235 4339 5162 27 -8 44 O ATOM 1294 OE2 GLU B 9 19.256 26.904 37.653 1.00 42.78 O ANISOU 1294 OE2 GLU B 9 5009 5122 6122 -43 -31 73 O ATOM 1295 N LEU B 10 13.204 26.274 38.599 1.00 34.24 N ANISOU 1295 N LEU B 10 4139 3886 4984 19 10 -28 N ATOM 1296 CA LEU B 10 11.844 25.767 38.463 1.00 29.55 C ANISOU 1296 CA LEU B 10 3579 3291 4358 37 27 -39 C ATOM 1297 C LEU B 10 11.167 26.326 37.218 1.00 24.17 C ANISOU 1297 C LEU B 10 2871 2622 3690 38 46 12 C ATOM 1298 O LEU B 10 10.444 25.615 36.521 1.00 27.20 O ANISOU 1298 O LEU B 10 3261 3042 4032 59 62 14 O ATOM 1299 CB LEU B 10 11.021 26.105 39.708 1.00 28.15 C ANISOU 1299 CB LEU B 10 3437 3068 4192 37 18 -87 C ATOM 1300 CG LEU B 10 11.439 25.415 41.008 1.00 23.72 C ANISOU 1300 CG LEU B 10 2902 2512 3598 49 4 -135 C ATOM 1301 CD1 LEU B 10 10.699 26.016 42.196 1.00 27.75 C ANISOU 1301 CD1 LEU B 10 3431 2993 4119 56 -7 -180 C ATOM 1302 CD2 LEU B 10 11.196 23.916 40.922 1.00 17.33 C ANISOU 1302 CD2 LEU B 10 2120 1734 2731 69 19 -136 C ATOM 1303 N ARG B 11 11.404 27.604 36.941 1.00 26.27 N ANISOU 1303 N ARG B 11 3105 2857 4019 18 42 54 N ATOM 1304 CA ARG B 11 10.824 28.247 35.770 1.00 29.92 C ANISOU 1304 CA ARG B 11 3537 3333 4497 23 61 118 C ATOM 1305 C ARG B 11 11.428 27.687 34.486 1.00 30.33 C ANISOU 1305 C ARG B 11 3546 3474 4502 41 79 170 C ATOM 1306 O ARG B 11 10.712 27.403 33.526 1.00 33.46 O ANISOU 1306 O ARG B 11 3932 3924 4858 69 97 191 O ATOM 1307 CB ARG B 11 11.023 29.762 35.832 1.00 27.87 C ANISOU 1307 CB ARG B 11 3250 3007 4333 -5 50 161 C ATOM 1308 CG ARG B 11 10.503 30.504 34.610 1.00 44.57 C ANISOU 1308 CG ARG B 11 5329 5135 6469 4 72 246 C ATOM 1309 CD ARG B 11 10.753 31.999 34.727 1.00 43.63 C ANISOU 1309 CD ARG B 11 5183 4931 6463 -27 57 294 C ATOM 1310 NE ARG B 11 9.989 32.593 35.819 1.00 33.50 N ANISOU 1310 NE ARG B 11 3940 3559 5229 -28 31 223 N ATOM 1311 CZ ARG B 11 10.167 33.831 36.268 1.00 32.67 C ANISOU 1311 CZ ARG B 11 3821 3358 5234 -52 3 226 C ATOM 1312 NH1 ARG B 11 11.091 34.610 35.721 1.00 27.42 N ANISOU 1312 NH1 ARG B 11 3103 2664 4652 -86 0 308 N ATOM 1313 NH2 ARG B 11 9.423 34.287 37.266 1.00 26.18 N ANISOU 1313 NH2 ARG B 11 3033 2470 4443 -41 -24 147 N ATOM 1314 N ARG B 12 12.749 27.530 34.479 1.00 24.83 N ANISOU 1314 N ARG B 12 2821 2806 3806 30 71 185 N ATOM 1315 CA ARG B 12 13.455 26.984 33.325 1.00 20.36 C ANISOU 1315 CA ARG B 12 2208 2341 3188 54 84 228 C ATOM 1316 C ARG B 12 12.986 25.565 33.026 1.00 22.24 C ANISOU 1316 C ARG B 12 2472 2635 3345 97 86 171 C ATOM 1317 O ARG B 12 12.721 25.216 31.876 1.00 26.99 O ANISOU 1317 O ARG B 12 3041 3315 3897 133 99 192 O ATOM 1318 CB ARG B 12 14.968 26.990 33.569 1.00 19.98 C ANISOU 1318 CB ARG B 12 2126 2314 3152 35 72 241 C ATOM 1319 CG ARG B 12 15.782 26.358 32.444 1.00 18.16 C ANISOU 1319 CG ARG B 12 1841 2202 2855 68 84 278 C ATOM 1320 CD ARG B 12 17.261 26.263 32.801 1.00 22.57 C ANISOU 1320 CD ARG B 12 2369 2787 3421 52 70 280 C ATOM 1321 NE ARG B 12 17.500 25.369 33.932 1.00 27.50 N ANISOU 1321 NE ARG B 12 3048 3377 4023 58 46 189 N ATOM 1322 CZ ARG B 12 17.641 24.051 33.827 1.00 33.09 C ANISOU 1322 CZ ARG B 12 3777 4136 4660 103 39 138 C ATOM 1323 NH1 ARG B 12 17.563 23.465 32.640 1.00 33.49 N ANISOU 1323 NH1 ARG B 12 3796 4278 4651 148 50 152 N ATOM 1324 NH2 ARG B 12 17.856 23.316 34.909 1.00 29.08 N ANISOU 1324 NH2 ARG B 12 3317 3590 4141 109 19 70 N ATOM 1325 N ILE B 13 12.891 24.752 34.073 1.00 25.18 N ANISOU 1325 N ILE B 13 2897 2965 3707 96 70 98 N ATOM 1326 CA ILE B 13 12.459 23.368 33.939 1.00 24.37 C ANISOU 1326 CA ILE B 13 2820 2889 3549 130 66 43 C ATOM 1327 C ILE B 13 10.978 23.289 33.578 1.00 23.90 C ANISOU 1327 C ILE B 13 2777 2821 3484 140 77 29 C ATOM 1328 O ILE B 13 10.574 22.478 32.744 1.00 29.87 O ANISOU 1328 O ILE B 13 3521 3630 4199 174 78 6 O ATOM 1329 CB ILE B 13 12.724 22.574 35.233 1.00 24.26 C ANISOU 1329 CB ILE B 13 2857 2827 3534 123 49 -13 C ATOM 1330 CG1 ILE B 13 14.222 22.563 35.548 1.00 27.39 C ANISOU 1330 CG1 ILE B 13 3233 3245 3929 120 35 -8 C ATOM 1331 CG2 ILE B 13 12.190 21.153 35.111 1.00 24.33 C ANISOU 1331 CG2 ILE B 13 2893 2843 3508 153 43 -63 C ATOM 1332 CD1 ILE B 13 14.563 21.963 36.895 1.00 31.16 C ANISOU 1332 CD1 ILE B 13 3755 3681 4404 118 18 -54 C ATOM 1333 N GLY B 14 10.174 24.141 34.207 1.00 22.91 N ANISOU 1333 N GLY B 14 2674 2631 3398 115 83 35 N ATOM 1334 CA GLY B 14 8.745 24.174 33.954 1.00 25.25 C ANISOU 1334 CA GLY B 14 2983 2921 3690 123 94 23 C ATOM 1335 C GLY B 14 8.412 24.451 32.501 1.00 29.46 C ANISOU 1335 C GLY B 14 3468 3527 4198 152 108 63 C ATOM 1336 O GLY B 14 7.629 23.726 31.883 1.00 24.94 O ANISOU 1336 O GLY B 14 2891 2996 3590 180 110 31 O ATOM 1337 N ASP B 15 9.011 25.503 31.953 1.00 27.64 N ANISOU 1337 N ASP B 15 3197 3317 3990 148 117 136 N ATOM 1338 CA ASP B 15 8.781 25.881 30.564 1.00 29.00 C ANISOU 1338 CA ASP B 15 3313 3572 4132 182 134 195 C ATOM 1339 C ASP B 15 9.310 24.825 29.603 1.00 22.13 C ANISOU 1339 C ASP B 15 2407 2810 3191 226 131 175 C ATOM 1340 O ASP B 15 8.722 24.581 28.551 1.00 20.66 O ANISOU 1340 O ASP B 15 2186 2706 2956 271 138 175 O ATOM 1341 CB ASP B 15 9.421 27.238 30.264 1.00 24.66 C ANISOU 1341 CB ASP B 15 2724 3013 3633 163 145 294 C ATOM 1342 CG ASP B 15 8.667 28.385 30.896 1.00 27.76 C ANISOU 1342 CG ASP B 15 3141 3307 4097 135 145 311 C ATOM 1343 OD1 ASP B 15 7.529 28.154 31.357 1.00 25.85 O ANISOU 1343 OD1 ASP B 15 2941 3033 3848 141 142 254 O ATOM 1344 OD2 ASP B 15 9.205 29.512 30.931 1.00 35.17 O ANISOU 1344 OD2 ASP B 15 4056 4202 5105 109 145 380 O ATOM 1345 N GLU B 16 10.424 24.202 29.973 1.00 24.44 N ANISOU 1345 N GLU B 16 2703 3108 3476 221 117 153 N ATOM 1346 CA GLU B 16 11.019 23.148 29.159 1.00 23.73 C ANISOU 1346 CA GLU B 16 2579 3117 3320 270 107 121 C ATOM 1347 C GLU B 16 10.101 21.929 29.102 1.00 23.99 C ANISOU 1347 C GLU B 16 2641 3148 3327 297 90 27 C ATOM 1348 O GLU B 16 9.931 21.317 28.048 1.00 26.44 O ANISOU 1348 O GLU B 16 2911 3551 3585 351 83 -3 O ATOM 1349 CB GLU B 16 12.401 22.770 29.701 1.00 20.20 C ANISOU 1349 CB GLU B 16 2134 2667 2875 258 93 114 C ATOM 1350 CG GLU B 16 13.082 21.632 28.959 1.00 32.15 C ANISOU 1350 CG GLU B 16 3615 4279 4321 315 76 70 C ATOM 1351 CD GLU B 16 12.669 20.268 29.477 1.00 52.10 C ANISOU 1351 CD GLU B 16 6194 6756 6846 329 49 -32 C ATOM 1352 OE1 GLU B 16 12.048 20.205 30.557 1.00 53.50 O ANISOU 1352 OE1 GLU B 16 6432 6827 7070 289 47 -56 O ATOM 1353 OE2 GLU B 16 12.964 19.258 28.805 1.00 75.01 O ANISOU 1353 OE2 GLU B 16 9071 9727 9701 384 28 -87 O ATOM 1354 N GLU B 17 9.508 21.588 30.241 1.00 27.08 N ANISOU 1354 N GLU B 17 3095 3436 3759 261 82 -19 N ATOM 1355 CA GLU B 17 8.550 20.491 30.315 1.00 27.80 C ANISOU 1355 CA GLU B 17 3211 3504 3846 273 67 -97 C ATOM 1356 C GLU B 17 7.276 20.829 29.550 1.00 32.60 C ANISOU 1356 C GLU B 17 3797 4148 4442 290 79 -99 C ATOM 1357 O GLU B 17 6.696 19.975 28.879 1.00 26.90 O ANISOU 1357 O GLU B 17 3056 3469 3696 324 64 -160 O ATOM 1358 CB GLU B 17 8.210 20.179 31.774 1.00 26.90 C ANISOU 1358 CB GLU B 17 3163 3281 3779 228 64 -123 C ATOM 1359 CG GLU B 17 9.295 19.421 32.512 1.00 29.31 C ANISOU 1359 CG GLU B 17 3492 3555 4087 225 46 -143 C ATOM 1360 CD GLU B 17 9.385 17.974 32.076 1.00 29.36 C ANISOU 1360 CD GLU B 17 3496 3580 4080 261 20 -209 C ATOM 1361 OE1 GLU B 17 8.379 17.440 31.566 1.00 36.76 O ANISOU 1361 OE1 GLU B 17 4426 4521 5021 273 13 -251 O ATOM 1362 OE2 GLU B 17 10.460 17.368 32.247 1.00 26.29 O ANISOU 1362 OE2 GLU B 17 3111 3198 3681 279 3 -223 O ATOM 1363 N ASN B 18 6.842 22.079 29.663 1.00 26.95 N ANISOU 1363 N ASN B 18 3080 3414 3746 270 101 -37 N ATOM 1364 CA ASN B 18 5.647 22.536 28.969 1.00 30.73 C ANISOU 1364 CA ASN B 18 3535 3929 4210 290 113 -29 C ATOM 1365 C ASN B 18 5.795 22.383 27.460 1.00 36.43 C ANISOU 1365 C ASN B 18 4189 4784 4869 353 113 -21 C ATOM 1366 O ASN B 18 4.906 21.861 26.789 1.00 31.99 O ANISOU 1366 O ASN B 18 3605 4274 4277 388 105 -75 O ATOM 1367 CB ASN B 18 5.350 23.995 29.316 1.00 28.71 C ANISOU 1367 CB ASN B 18 3288 3629 3993 264 134 44 C ATOM 1368 CG ASN B 18 3.939 24.404 28.946 1.00 29.78 C ANISOU 1368 CG ASN B 18 3415 3778 4121 280 145 41 C ATOM 1369 OD1 ASN B 18 3.726 25.151 27.990 1.00 28.00 O ANISOU 1369 OD1 ASN B 18 3147 3618 3874 313 159 98 O ATOM 1370 ND2 ASN B 18 2.964 23.908 29.698 1.00 21.88 N ANISOU 1370 ND2 ASN B 18 2453 2723 3138 258 139 -21 N ATOM 1371 N ALA B 19 6.927 22.841 26.936 1.00 35.38 N ANISOU 1371 N ALA B 19 4016 4713 4713 370 121 45 N ATOM 1372 CA ALA B 19 7.197 22.770 25.505 1.00 36.76 C ANISOU 1372 CA ALA B 19 4115 5036 4814 438 125 66 C ATOM 1373 C ALA B 19 7.181 21.327 25.011 1.00 33.63 C ANISOU 1373 C ALA B 19 3703 4701 4373 487 92 -45 C ATOM 1374 O ALA B 19 6.626 21.028 23.955 1.00 32.20 O ANISOU 1374 O ALA B 19 3472 4626 4136 548 85 -80 O ATOM 1375 CB ALA B 19 8.532 23.426 25.185 1.00 30.36 C ANISOU 1375 CB ALA B 19 3263 4280 3994 440 140 161 C ATOM 1376 N TYR B 20 7.791 20.438 25.787 1.00 37.69 N ANISOU 1376 N TYR B 20 4259 5147 4915 464 70 -102 N ATOM 1377 CA TYR B 20 7.872 19.029 25.422 1.00 39.13 C ANISOU 1377 CA TYR B 20 4431 5363 5073 508 32 -211 C ATOM 1378 C TYR B 20 6.492 18.418 25.191 1.00 40.36 C ANISOU 1378 C TYR B 20 4590 5504 5241 519 14 -296 C ATOM 1379 O TYR B 20 6.242 17.809 24.152 1.00 41.96 O ANISOU 1379 O TYR B 20 4740 5806 5397 584 -9 -365 O ATOM 1380 CB TYR B 20 8.621 18.242 26.500 1.00 45.08 C ANISOU 1380 CB TYR B 20 5240 6017 5872 473 12 -247 C ATOM 1381 CG TYR B 20 8.658 16.751 26.254 1.00 54.46 C ANISOU 1381 CG TYR B 20 6426 7209 7058 514 -33 -361 C ATOM 1382 CD1 TYR B 20 9.487 16.208 25.282 1.00 58.12 C ANISOU 1382 CD1 TYR B 20 6833 7790 7461 588 -57 -401 C ATOM 1383 CD2 TYR B 20 7.867 15.885 26.999 1.00 56.50 C ANISOU 1383 CD2 TYR B 20 6734 7352 7380 480 -52 -428 C ATOM 1384 CE1 TYR B 20 9.525 14.845 25.054 1.00 64.54 C ANISOU 1384 CE1 TYR B 20 7643 8597 8283 631 -105 -517 C ATOM 1385 CE2 TYR B 20 7.899 14.520 26.779 1.00 60.67 C ANISOU 1385 CE2 TYR B 20 7259 7865 7928 514 -98 -531 C ATOM 1386 CZ TYR B 20 8.730 14.006 25.805 1.00 64.73 C ANISOU 1386 CZ TYR B 20 7720 8487 8386 592 -127 -581 C ATOM 1387 OH TYR B 20 8.767 12.649 25.581 1.00 55.97 O ANISOU 1387 OH TYR B 20 6606 7355 7304 632 -180 -695 O ATOM 1388 N TYR B 21 5.600 18.587 26.161 1.00 34.67 N ANISOU 1388 N TYR B 21 3924 4667 4581 457 25 -294 N ATOM 1389 CA TYR B 21 4.263 18.006 26.075 1.00 37.10 C ANISOU 1389 CA TYR B 21 4234 4951 4910 455 10 -370 C ATOM 1390 C TYR B 21 3.344 18.794 25.146 1.00 39.91 C ANISOU 1390 C TYR B 21 4541 5399 5223 490 27 -348 C ATOM 1391 O TYR B 21 2.342 18.267 24.661 1.00 34.22 O ANISOU 1391 O TYR B 21 3796 4708 4499 512 9 -424 O ATOM 1392 CB TYR B 21 3.635 17.888 27.467 1.00 30.38 C ANISOU 1392 CB TYR B 21 3452 3959 4134 380 18 -369 C ATOM 1393 CG TYR B 21 4.268 16.821 28.332 1.00 28.08 C ANISOU 1393 CG TYR B 21 3203 3578 3887 355 -5 -407 C ATOM 1394 CD1 TYR B 21 5.232 17.146 29.277 1.00 27.07 C ANISOU 1394 CD1 TYR B 21 3116 3396 3773 324 8 -350 C ATOM 1395 CD2 TYR B 21 3.904 15.487 28.201 1.00 31.49 C ANISOU 1395 CD2 TYR B 21 3631 3980 4354 364 -41 -499 C ATOM 1396 CE1 TYR B 21 5.814 16.174 30.069 1.00 30.91 C ANISOU 1396 CE1 TYR B 21 3641 3810 4295 308 -12 -378 C ATOM 1397 CE2 TYR B 21 4.479 14.508 28.988 1.00 39.44 C ANISOU 1397 CE2 TYR B 21 4678 4900 5409 345 -62 -523 C ATOM 1398 CZ TYR B 21 5.434 14.857 29.920 1.00 39.26 C ANISOU 1398 CZ TYR B 21 4696 4833 5387 319 -46 -459 C ATOM 1399 OH TYR B 21 6.011 13.886 30.706 1.00 36.44 O ANISOU 1399 OH TYR B 21 4378 4397 5073 307 -66 -476 O ATOM 1400 N ARG B 22 3.689 20.053 24.897 1.00 36.35 N ANISOU 1400 N ARG B 22 4074 4993 4743 496 60 -243 N ATOM 1401 CA ARG B 22 2.876 20.912 24.045 1.00 39.13 C ANISOU 1401 CA ARG B 22 4381 5431 5054 533 80 -202 C ATOM 1402 C ARG B 22 2.976 20.488 22.583 1.00 47.51 C ANISOU 1402 C ARG B 22 5361 6660 6032 623 64 -242 C ATOM 1403 O ARG B 22 1.964 20.352 21.896 1.00 54.09 O ANISOU 1403 O ARG B 22 6157 7562 6834 664 55 -292 O ATOM 1404 CB ARG B 22 3.295 22.377 24.197 1.00 41.10 C ANISOU 1404 CB ARG B 22 4634 5670 5312 514 118 -69 C ATOM 1405 CG ARG B 22 2.161 23.367 23.990 1.00 40.84 C ANISOU 1405 CG ARG B 22 4593 5644 5280 520 140 -22 C ATOM 1406 CD ARG B 22 2.625 24.806 24.161 1.00 50.97 C ANISOU 1406 CD ARG B 22 5879 6896 6591 500 170 109 C ATOM 1407 NE ARG B 22 3.047 25.406 22.898 1.00 66.62 N ANISOU 1407 NE ARG B 22 7787 9014 8513 562 189 198 N ATOM 1408 CZ ARG B 22 4.312 25.537 22.512 1.00 70.52 C ANISOU 1408 CZ ARG B 22 8245 9563 8987 573 196 263 C ATOM 1409 NH1 ARG B 22 4.593 26.098 21.343 1.00 72.18 N ANISOU 1409 NH1 ARG B 22 8378 9909 9136 633 217 356 N ATOM 1410 NH2 ARG B 22 5.296 25.109 23.291 1.00 65.23 N ANISOU 1410 NH2 ARG B 22 7609 8822 8353 527 184 242 N TER 1411 ARG B 22 HETATM 1412 ZN ZN A 2 3.087 20.853 61.799 1.00 71.00 ZN ANISOU 1412 ZN ZN A 2 8704 9897 8376 818 182 -73 ZN HETATM 1413 ZN ZN A 3 -13.006 33.872 39.847 1.00 48.54 ZN ANISOU 1413 ZN ZN A 3 5914 6002 6526 523 124 -399 ZN HETATM 1414 ZN ZN A 4 -4.958 9.039 23.518 1.00 46.56 ZN ANISOU 1414 ZN ZN A 4 5146 5907 6638 418 -356 -1391 ZN HETATM 1415 C ACT A1428 -13.872 36.522 38.015 1.00 49.88 C ANISOU 1415 C ACT A1428 6077 6092 6783 654 83 -361 C HETATM 1416 O ACT A1428 -14.681 36.663 37.072 1.00 51.91 O ANISOU 1416 O ACT A1428 6310 6397 7016 685 96 -336 O HETATM 1417 OXT ACT A1428 -13.650 35.347 38.369 1.00 42.78 O ANISOU 1417 OXT ACT A1428 5175 5239 5841 598 107 -367 O HETATM 1418 CH3 ACT A1428 -13.204 37.688 38.683 1.00 30.13 C ANISOU 1418 CH3 ACT A1428 3602 3483 4362 684 38 -386 C HETATM 1419 ZN ZN B 23 12.463 18.148 31.542 1.00 34.32 ZN ANISOU 1419 ZN ZN B 23 4064 4329 4645 308 5 -165 ZN HETATM 1420 O HOH A 1 -2.570 12.523 31.140 1.00 25.24 O ANISOU 1420 O HOH A 1 2872 2805 3914 101 -47 -626 O HETATM 1421 O HOH A 5 0.000 35.743 47.628 0.50 24.72 O ANISOU 1421 O HOH A 5 3020 2457 3914 401 0 0 O HETATM 1422 O HOH A 6 -6.283 17.189 23.545 1.00 33.22 O ANISOU 1422 O HOH A 6 3516 4646 4460 484 -37 -789 O HETATM 1423 O HOH A 7 -0.118 24.984 29.737 1.00 32.28 O ANISOU 1423 O HOH A 7 3772 4032 4460 271 160 -39 O HETATM 1424 O HOH A 8 -5.618 6.853 24.738 1.00 54.57 O ANISOU 1424 O HOH A 8 6178 6623 7933 287 -419 -1467 O HETATM 1425 O HOH A 9 7.041 38.854 31.896 1.00 29.15 O ANISOU 1425 O HOH A 9 3248 2744 5082 22 62 705 O HETATM 1426 O HOH A 11 -18.367 24.255 48.710 1.00 60.90 O ANISOU 1426 O HOH A 11 7099 8426 7613 232 448 -144 O HETATM 1427 O HOH A 12 -9.821 19.029 29.290 1.00 46.17 O ANISOU 1427 O HOH A 12 5340 5926 6277 184 104 -563 O HETATM 1428 O HOH A 13 3.569 29.236 28.276 1.00 30.69 O ANISOU 1428 O HOH A 13 3478 3823 4362 281 195 337 O HETATM 1429 O HOH A 14 14.902 13.733 48.198 1.00 45.98 O ANISOU 1429 O HOH A 14 5949 5452 6068 345 -9 -37 O HETATM 1430 O HOH A 15 0.886 15.497 25.880 1.00 36.90 O ANISOU 1430 O HOH A 15 4189 4835 4997 435 -62 -636 O HETATM 1431 O HOH A 16 -4.067 10.461 30.075 1.00 52.55 O ANISOU 1431 O HOH A 16 6241 6209 7517 82 -125 -802 O HETATM 1432 O HOH A 17 19.951 15.875 35.893 1.00 46.03 O ANISOU 1432 O HOH A 17 5602 5817 6069 368 -91 -210 O HETATM 1433 O HOH A 19 4.480 33.492 50.149 1.00 46.47 O ANISOU 1433 O HOH A 19 5757 5332 6566 355 -230 -781 O HETATM 1434 O HOH A 21 -11.036 20.043 38.424 1.00 36.17 O ANISOU 1434 O HOH A 21 4258 4433 5054 -36 258 -258 O HETATM 1435 O HOH A 23 -1.476 8.136 47.588 1.00 60.64 O ANISOU 1435 O HOH A 23 7624 6886 8532 -171 265 469 O HETATM 1436 O HOH A 24 -1.407 8.503 32.966 1.00 60.21 O ANISOU 1436 O HOH A 24 7365 6886 8626 20 -129 -644 O HETATM 1437 O HOH A 25 13.629 9.470 60.889 1.00 66.52 O ANISOU 1437 O HOH A 25 8455 8778 8040 865 187 695 O HETATM 1438 O HOH A 26 10.041 34.857 31.811 1.00 34.33 O ANISOU 1438 O HOH A 26 3880 3728 5436 -18 105 611 O HETATM 1439 O HOH A 29 -14.277 31.535 40.593 1.00 42.54 O ANISOU 1439 O HOH A 29 5101 5411 5650 452 186 -409 O HETATM 1440 O HOH A 30 -12.589 34.224 35.122 1.00 33.18 O ANISOU 1440 O HOH A 30 3935 4041 4633 538 153 -211 O HETATM 1441 O HOH A 31 0.000 35.743 35.764 0.50 31.06 O ANISOU 1441 O HOH A 31 3752 3162 4887 221 0 0 O HETATM 1442 O HOH A 33 0.000 18.646 59.717 0.50 43.96 O ANISOU 1442 O HOH A 33 5307 6268 5126 0 327 0 O HETATM 1443 O HOH A 34 23.856 28.399 42.335 1.00 51.73 O ANISOU 1443 O HOH A 34 6028 6216 7412 -117 -195 -186 O HETATM 1444 O HOH A 35 7.868 35.883 46.342 1.00 33.11 O ANISOU 1444 O HOH A 35 4012 3243 5324 140 -281 -599 O HETATM 1445 O HOH A 36 14.305 8.471 33.528 1.00 59.65 O ANISOU 1445 O HOH A 36 7455 7173 8038 521 -245 -560 O HETATM 1446 O HOH A 37 16.586 21.114 52.820 1.00 55.44 O ANISOU 1446 O HOH A 37 6963 6967 7134 408 -124 -399 O HETATM 1447 O HOH A 39 -16.023 34.652 35.705 1.00 53.33 O ANISOU 1447 O HOH A 39 6421 6772 7068 641 160 -322 O HETATM 1448 O HOH A 40 12.223 30.677 55.476 1.00 56.86 O ANISOU 1448 O HOH A 40 6952 7032 7619 475 -370 -1033 O HETATM 1449 O HOH A 41 20.670 9.101 42.873 1.00 58.53 O ANISOU 1449 O HOH A 41 7509 7028 7701 560 -184 -213 O HETATM 1450 O HOH A 42 1.376 36.017 38.528 1.00 38.35 O ANISOU 1450 O HOH A 42 4711 3973 5888 182 -28 -66 O HETATM 1451 O HOH A 43 3.047 35.180 41.299 1.00 45.12 O ANISOU 1451 O HOH A 43 5592 4830 6721 155 -82 -238 O HETATM 1452 O HOH A 44 23.400 18.822 42.577 1.00 50.85 O ANISOU 1452 O HOH A 44 6226 6377 6717 268 -134 -236 O HETATM 1453 O HOH A 46 8.197 37.350 43.820 1.00 35.37 O ANISOU 1453 O HOH A 46 4262 3357 5821 55 -266 -412 O HETATM 1454 O HOH A 47 -2.632 16.232 24.638 1.00 54.80 O ANISOU 1454 O HOH A 47 6358 7227 7237 455 -52 -715 O HETATM 1455 O HOH A 48 -1.618 8.943 28.390 1.00 39.61 O ANISOU 1455 O HOH A 48 4580 4596 5871 223 -235 -966 O HETATM 1456 O HOH A 49 14.551 28.650 56.783 1.00 59.83 O ANISOU 1456 O HOH A 49 7310 7603 7820 537 -363 -1006 O HETATM 1457 O HOH A 50 -0.541 33.594 32.757 1.00 40.85 O ANISOU 1457 O HOH A 50 4933 4660 5926 251 133 212 O HETATM 1458 O HOH A 51 8.229 14.168 33.019 1.00 48.40 O ANISOU 1458 O HOH A 51 5981 5820 6590 267 -46 -368 O HETATM 1459 O HOH A 52 5.141 19.288 55.157 1.00 42.03 O ANISOU 1459 O HOH A 52 5281 5436 5253 412 157 -23 O HETATM 1460 O HOH A 53 -9.205 17.733 50.225 1.00 42.52 O ANISOU 1460 O HOH A 53 5074 5497 5586 -4 432 240 O HETATM 1461 O HOH A 55 18.133 15.020 32.080 1.00 37.71 O ANISOU 1461 O HOH A 55 4459 4908 4962 463 -97 -271 O HETATM 1462 O HOH A 56 -4.456 6.967 46.259 1.00 46.86 O ANISOU 1462 O HOH A 56 5767 5031 7007 -323 269 460 O HETATM 1463 O HOH A 57 -5.284 2.257 45.016 1.00 56.86 O ANISOU 1463 O HOH A 57 6956 5809 8838 -496 166 518 O HETATM 1464 O HOH A 58 -16.352 10.322 39.055 1.00 55.09 O ANISOU 1464 O HOH A 58 6262 6530 8138 -560 250 -178 O HETATM 1465 O HOH A 59 -12.390 31.282 34.420 1.00 48.86 O ANISOU 1465 O HOH A 59 5887 6138 6541 434 196 -225 O HETATM 1466 O HOH A 60 20.864 14.842 32.099 1.00 40.89 O ANISOU 1466 O HOH A 60 4797 5450 5291 519 -118 -263 O HETATM 1467 O HOH A 61 9.676 39.114 45.177 1.00 37.92 O ANISOU 1467 O HOH A 61 4520 3527 6360 35 -389 -563 O HETATM 1468 O HOH A 62 -10.771 33.569 32.784 1.00 61.63 O ANISOU 1468 O HOH A 62 7519 7645 8253 504 174 -81 O HETATM 1469 O HOH A 63 18.271 12.962 47.338 1.00 56.04 O ANISOU 1469 O HOH A 63 7204 6781 7308 424 -74 -100 O HETATM 1470 O HOH A 64 -2.953 27.432 53.423 1.00 47.49 O HETATM 1471 O HOH A 328 3.677 15.184 60.815 1.00 50.94 O ANISOU 1471 O HOH A 328 6261 7091 6003 634 340 513 O HETATM 1472 O HOH A 329 10.318 26.202 52.468 1.00 36.74 O ANISOU 1472 O HOH A 329 4568 4455 4936 345 -124 -557 O HETATM 1473 O HOH A 330 17.606 13.804 50.551 1.00 44.73 O ANISOU 1473 O HOH A 330 5769 5456 5770 467 -48 -60 O HETATM 1474 O HOH B 24 16.858 24.203 29.752 1.00 36.29 O ANISOU 1474 O HOH B 24 4031 4816 4942 205 98 287 O HETATM 1475 O HOH B 25 11.172 20.719 25.545 1.00 36.55 O ANISOU 1475 O HOH B 25 4047 5120 4719 484 75 7 O HETATM 1476 O HOH B 26 11.989 34.952 46.664 1.00 51.10 O ANISOU 1476 O HOH B 26 6221 5553 7641 44 -314 -593 O HETATM 1477 O HOH B 27 10.377 20.862 22.771 1.00 39.92 O ANISOU 1477 O HOH B 27 4325 5847 4994 631 86 24 O HETATM 1478 O HOH B 28 13.380 15.995 30.305 1.00 32.30 O ANISOU 1478 O HOH B 28 3769 4173 4330 416 -51 -280 O HETATM 1479 O HOH B 29 11.920 30.018 30.948 1.00 51.41 O ANISOU 1479 O HOH B 29 6039 6272 7224 55 137 470 O HETATM 1480 O HOH B 32 6.414 26.464 26.474 1.00 41.89 O ANISOU 1480 O HOH B 32 4796 5508 5612 342 184 301 O HETATM 1481 O HOH B 38 18.928 29.388 38.103 1.00 47.87 O ANISOU 1481 O HOH B 38 5614 5619 6955 -123 -54 103 O HETATM 1482 O HOH B 45 14.293 30.814 34.283 1.00 38.51 O ANISOU 1482 O HOH B 45 4441 4420 5769 -67 55 345 O HETATM 1483 O HOH B 54 10.803 14.818 32.333 1.00 39.70 O ANISOU 1483 O HOH B 54 4836 4848 5400 328 -54 -336 O CONECT 417 1419 CONECT 548 1412 CONECT 555 1412 CONECT 1049 1413 CONECT 1197 1414 CONECT 1212 1414 CONECT 1213 1414 CONECT 1352 1419 CONECT 1362 1419 CONECT 1412 548 555 CONECT 1413 1049 1417 CONECT 1414 1197 1212 1213 1424 CONECT 1415 1416 1417 1418 CONECT 1416 1415 CONECT 1417 1413 1415 CONECT 1418 1415 CONECT 1419 417 1352 1362 1478 CONECT 1424 1414 CONECT 1478 1419 MASTER 342 0 5 9 0 0 6 6 1481 2 19 15 END
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Complexes with the same small molecule ligand
PDB Code
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Ligand Name
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Entry Information
PDB ID
3kj2
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Induced myeloid leukemia cell differentiation protein Mcl-1
Ligand Name
22-mer
EC.Number
E.C.-.-.-.-
Resolution
2.35(Å)
Affinity (Kd/Ki/IC50)
Kd=2nM
Release Year
2010
Protein/NA Sequence
Check fasta file
Primary Reference
(2010) Protein Sci. Vol. 19: pp. 507-519
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):
O43521
Q07820
Entrez Gene ID
NCBI Entrez Gene ID:
10018
4170
ASD
Information of known allosteric effects of PDB entries
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