Browse entries in the PDBbind-CN Database
HEADER TRANSFERASE 05-JUN-16 5B77 TITLE CRYSTAL STRUCTRUE OF MOZ DOUBLE PHD FINGER IN COMPLEX WITH HISTONE H3 TITLE 2 PROPIONYLATION AT K14 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE KAT6A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 194-323; COMPND 5 SYNONYM: MOZ; COMPND 6 EC: 2.3.1.48; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: HISTONE H3; COMPND 10 CHAIN: B; COMPND 11 FRAGMENT: UNP RESIDUES 2-26; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: MOZ; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606 KEYWDS MOZ DOUBLE PHD FINGER, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR H.LI,X.XIONG REVDAT 2 30-NOV-16 5B77 1 JRNL REVDAT 1 26-OCT-16 5B77 0 JRNL AUTH X.XIONG,T.PANCHENKO,S.YANG,S.ZHAO,P.YAN,W.ZHANG,W.XIE,Y.LI, JRNL AUTH 2 Y.ZHAO,C.D.ALLIS,H.LI JRNL TITL SELECTIVE RECOGNITION OF HISTONE CROTONYLATION BY DOUBLE PHD JRNL TITL 2 FINGERS OF MOZ AND DPF2 JRNL REF NAT.CHEM.BIOL. V. 12 1111 2016 JRNL REFN ESSN 1552-4469 JRNL PMID 27775714 JRNL DOI 10.1038/NCHEMBIO.2218 REMARK 2 REMARK 2 RESOLUTION. 1.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10_2155: ???) 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.80 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 25683 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.176 REMARK 3 R VALUE (WORKING SET) : 0.174 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1309 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 33.8553 - 3.2243 1.00 2867 149 0.1600 0.1968 REMARK 3 2 3.2243 - 2.5595 1.00 2757 146 0.1810 0.2157 REMARK 3 3 2.5595 - 2.2361 1.00 2728 137 0.1746 0.1763 REMARK 3 4 2.2361 - 2.0317 1.00 2673 166 0.1716 0.2015 REMARK 3 5 2.0317 - 1.8860 1.00 2695 140 0.1740 0.2073 REMARK 3 6 1.8860 - 1.7749 1.00 2653 143 0.1753 0.1795 REMARK 3 7 1.7749 - 1.6860 1.00 2709 127 0.1794 0.2320 REMARK 3 8 1.6860 - 1.6126 1.00 2651 141 0.2062 0.2560 REMARK 3 9 1.6126 - 1.5505 1.00 2641 160 0.2537 0.2691 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.070 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.011 1121 REMARK 3 ANGLE : 1.257 1504 REMARK 3 CHIRALITY : 0.069 159 REMARK 3 PLANARITY : 0.008 196 REMARK 3 DIHEDRAL : 16.457 712 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 197 THROUGH 312) REMARK 3 ORIGIN FOR THE GROUP (A): 19.1181 2.8072 8.6639 REMARK 3 T TENSOR REMARK 3 T11: 0.1527 T22: 0.1583 REMARK 3 T33: 0.1808 T12: -0.0412 REMARK 3 T13: -0.0109 T23: -0.0076 REMARK 3 L TENSOR REMARK 3 L11: 1.7314 L22: 2.1611 REMARK 3 L33: 2.6197 L12: -0.2133 REMARK 3 L13: -0.3330 L23: -0.9624 REMARK 3 S TENSOR REMARK 3 S11: -0.0926 S12: 0.1076 S13: -0.1188 REMARK 3 S21: 0.1304 S22: 0.0718 S23: 0.0761 REMARK 3 S31: 0.1975 S32: -0.1497 S33: 0.0148 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 25) REMARK 3 ORIGIN FOR THE GROUP (A): 27.8221 11.7325 4.7841 REMARK 3 T TENSOR REMARK 3 T11: 0.2449 T22: 0.2258 REMARK 3 T33: 0.3795 T12: -0.0152 REMARK 3 T13: -0.0308 T23: 0.0221 REMARK 3 L TENSOR REMARK 3 L11: 1.2731 L22: 3.3595 REMARK 3 L33: 2.5875 L12: 0.5561 REMARK 3 L13: -0.6455 L23: -1.4342 REMARK 3 S TENSOR REMARK 3 S11: -0.1138 S12: 0.0334 S13: 0.4254 REMARK 3 S21: 0.0705 S22: -0.0371 S23: -0.3133 REMARK 3 S31: -0.3414 S32: 0.0907 S33: 0.1603 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 5B77 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JUN-16. REMARK 100 THE DEPOSITION ID IS D_1300000654. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-JAN-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25683 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550 REMARK 200 RESOLUTION RANGE LOW (A) : 33.800 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> 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: PHASER REMARK 200 STARTING MODEL: 4LLB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 4000, LITHIUM REMARK 280 SULFATE, TRIS, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.85400 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.58400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.01400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.58400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.85400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.01400 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 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 SER A 193 REMARK 465 LEU A 194 REMARK 465 PRO A 195 REMARK 465 HIS A 196 REMARK 465 ARG A 313 REMARK 465 LYS A 314 REMARK 465 LYS A 315 REMARK 465 GLY A 316 REMARK 465 ARG A 317 REMARK 465 LYS A 318 REMARK 465 LEU A 319 REMARK 465 LEU A 320 REMARK 465 GLN A 321 REMARK 465 LYS A 322 REMARK 465 LYS A 323 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 630 O HOH A 636 1.78 REMARK 500 O HOH A 501 O HOH A 608 1.93 REMARK 500 O HOH A 606 O HOH A 607 2.02 REMARK 500 O HOH A 564 O HOH B 218 2.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 516 O HOH B 226 4455 2.05 REMARK 500 O HOH A 525 O HOH A 582 3655 2.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 207 36.83 -86.60 REMARK 500 GLN A 271 -68.21 -103.32 REMARK 500 ASP A 285 15.28 57.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 645 DISTANCE = 5.84 ANGSTROMS 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 A 403 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 209 SG REMARK 620 2 CYS A 212 SG 112.4 REMARK 620 3 HIS A 238 ND1 100.0 98.3 REMARK 620 4 CYS A 241 SG 110.9 112.7 121.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 404 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 230 SG REMARK 620 2 CYS A 233 SG 108.0 REMARK 620 3 CYS A 259 SG 111.9 116.5 REMARK 620 4 CYS A 262 SG 106.7 112.7 100.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 402 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 265 SG REMARK 620 2 CYS A 268 SG 110.2 REMARK 620 3 HIS A 289 ND1 101.2 99.0 REMARK 620 4 CYS A 292 SG 115.5 116.5 112.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 281 SG REMARK 620 2 CYS A 284 SG 107.5 REMARK 620 3 CYS A 307 SG 108.2 110.8 REMARK 620 4 CYS A 310 SG 111.7 106.8 111.8 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 A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 101 DBREF 5B77 A 194 323 UNP Q92794 KAT6A_HUMAN 194 323 DBREF 5B77 B 1 25 UNP K7EMV3 K7EMV3_HUMAN 2 26 SEQADV 5B77 SER A 193 UNP Q92794 EXPRESSION TAG SEQRES 1 A 131 SER LEU PRO HIS GLU LYS ASP LYS PRO VAL ALA GLU PRO SEQRES 2 A 131 ILE PRO ILE CYS SER PHE CYS LEU GLY THR LYS GLU GLN SEQRES 3 A 131 ASN ARG GLU LYS LYS PRO GLU GLU LEU ILE SER CYS ALA SEQRES 4 A 131 ASP CYS GLY ASN SER GLY HIS PRO SER CYS LEU LYS PHE SEQRES 5 A 131 SER PRO GLU LEU THR VAL ARG VAL LYS ALA LEU ARG TRP SEQRES 6 A 131 GLN CYS ILE GLU CYS LYS THR CYS SER SER CYS ARG ASP SEQRES 7 A 131 GLN GLY LYS ASN ALA ASP ASN MET LEU PHE CYS ASP SER SEQRES 8 A 131 CYS ASP ARG GLY PHE HIS MET GLU CYS CYS ASP PRO PRO SEQRES 9 A 131 LEU THR ARG MET PRO LYS GLY MET TRP ILE CYS GLN ILE SEQRES 10 A 131 CYS ARG PRO ARG LYS LYS GLY ARG LYS LEU LEU GLN LYS SEQRES 11 A 131 LYS SEQRES 1 B 25 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY SEQRES 2 B 25 PRK ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA MODRES 5B77 PRK B 14 LYS MODIFIED RESIDUE HET PRK B 14 13 HET ZN A 401 1 HET ZN A 402 1 HET ZN A 403 1 HET ZN A 404 1 HET SO4 A 405 5 HET SO4 B 101 5 HETNAM PRK N~6~-PROPANOYL-L-LYSINE HETNAM ZN ZINC ION HETNAM SO4 SULFATE ION HETSYN PRK N(6)-PROPIONYLLYSINE FORMUL 2 PRK C9 H18 N2 O3 FORMUL 3 ZN 4(ZN 2+) FORMUL 7 SO4 2(O4 S 2-) FORMUL 9 HOH *187(H2 O) HELIX 1 AA1 HIS A 238 LYS A 243 1 6 HELIX 2 AA2 SER A 245 ALA A 254 1 10 HELIX 3 AA3 ASN A 274 ASN A 277 5 4 HELIX 4 AA4 HIS A 289 CYS A 293 5 5 HELIX 5 AA5 LYS B 4 GLY B 12 1 9 HELIX 6 AA6 PRO B 16 ALA B 25 1 10 SHEET 1 AA1 2 ILE A 228 SER A 229 0 SHEET 2 AA1 2 SER A 236 GLY A 237 -1 O GLY A 237 N ILE A 228 SHEET 1 AA2 3 GLY A 287 PHE A 288 0 SHEET 2 AA2 3 LEU A 279 PHE A 280 -1 N LEU A 279 O PHE A 288 SHEET 3 AA2 3 ARG B 2 THR B 3 -1 O ARG B 2 N PHE A 280 LINK SG CYS A 209 ZN ZN A 403 1555 1555 2.32 LINK SG CYS A 212 ZN ZN A 403 1555 1555 2.31 LINK SG CYS A 230 ZN ZN A 404 1555 1555 2.31 LINK SG CYS A 233 ZN ZN A 404 1555 1555 2.26 LINK ND1 HIS A 238 ZN ZN A 403 1555 1555 2.10 LINK SG CYS A 241 ZN ZN A 403 1555 1555 2.28 LINK SG CYS A 259 ZN ZN A 404 1555 1555 2.28 LINK SG CYS A 262 ZN ZN A 404 1555 1555 2.27 LINK SG CYS A 265 ZN ZN A 402 1555 1555 2.33 LINK SG CYS A 268 ZN ZN A 402 1555 1555 2.28 LINK SG CYS A 281 ZN ZN A 401 1555 1555 2.33 LINK SG CYS A 284 ZN ZN A 401 1555 1555 2.31 LINK ND1 HIS A 289 ZN ZN A 402 1555 1555 2.13 LINK SG CYS A 292 ZN ZN A 402 1555 1555 2.27 LINK SG CYS A 307 ZN ZN A 401 1555 1555 2.34 LINK SG CYS A 310 ZN ZN A 401 1555 1555 2.25 LINK C GLY B 13 N PRK B 14 1555 1555 1.32 LINK C PRK B 14 N ALA B 15 1555 1555 1.33 CISPEP 1 ASP A 294 PRO A 295 0 0.61 SITE 1 AC1 4 CYS A 281 CYS A 284 CYS A 307 CYS A 310 SITE 1 AC2 4 CYS A 265 CYS A 268 HIS A 289 CYS A 292 SITE 1 AC3 4 CYS A 209 CYS A 212 HIS A 238 CYS A 241 SITE 1 AC4 4 CYS A 230 CYS A 233 CYS A 259 CYS A 262 SITE 1 AC5 4 PRO A 301 LYS A 302 GLY A 303 ALA B 1 SITE 1 AC6 4 PRO B 16 ARG B 17 HOH B 201 HOH B 208 CRYST1 47.708 48.028 75.168 90.00 90.00 90.00 P 21 21 21 4 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 0.020961 0.000000 0.000000 0.00000 SCALE2 0.000000 0.020821 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013304 0.00000 ATOM 1 N GLU A 197 6.326 4.498 14.231 1.00 61.10 N ANISOU 1 N GLU A 197 6865 8287 8062 -257 752 683 N ATOM 2 CA GLU A 197 6.713 4.696 12.835 1.00 57.24 C ANISOU 2 CA GLU A 197 6317 7831 7602 -328 599 623 C ATOM 3 C GLU A 197 5.482 4.912 11.965 1.00 59.40 C ANISOU 3 C GLU A 197 6338 8280 7951 -371 584 720 C ATOM 4 O GLU A 197 5.474 5.751 11.072 1.00 53.10 O ANISOU 4 O GLU A 197 5473 7545 7158 -322 513 721 O ATOM 5 CB GLU A 197 7.518 3.500 12.322 1.00 59.45 C ANISOU 5 CB GLU A 197 6672 8030 7885 -494 492 532 C ATOM 6 CG GLU A 197 8.838 3.255 13.066 1.00 62.11 C ANISOU 6 CG GLU A 197 7237 8208 8153 -448 485 448 C ATOM 7 CD GLU A 197 9.473 1.907 12.716 1.00 61.70 C ANISOU 7 CD GLU A 197 7254 8071 8117 -592 417 385 C ATOM 8 OE1 GLU A 197 8.752 1.007 12.233 1.00 65.73 O ANISOU 8 OE1 GLU A 197 7667 8621 8688 -739 406 410 O ATOM 9 OE2 GLU A 197 10.689 1.748 12.927 1.00 49.89 O ANISOU 9 OE2 GLU A 197 5912 6469 6577 -557 375 313 O ATOM 10 N LYS A 198 4.431 4.138 12.235 1.00 69.94 N ANISOU 10 N LYS A 198 7526 9701 9349 -467 648 814 N ATOM 11 CA LYS A 198 3.166 4.336 11.537 1.00 76.52 C ANISOU 11 CA LYS A 198 8087 10726 10260 -509 635 931 C ATOM 12 C LYS A 198 2.608 5.736 11.760 1.00 79.19 C ANISOU 12 C LYS A 198 8346 11147 10597 -283 731 1023 C ATOM 13 O LYS A 198 1.754 6.184 10.984 1.00 78.89 O ANISOU 13 O LYS A 198 8159 11224 10592 -264 668 1075 O ATOM 14 CB LYS A 198 2.145 3.291 11.999 1.00 78.83 C ANISOU 14 CB LYS A 198 8285 11055 10611 -634 690 997 C ATOM 15 CG LYS A 198 2.649 1.855 11.955 1.00 78.72 C ANISOU 15 CG LYS A 198 8368 10932 10609 -847 631 922 C ATOM 16 CD LYS A 198 1.817 0.943 12.853 1.00 78.73 C ANISOU 16 CD LYS A 198 8339 10920 10655 -921 741 994 C ATOM 17 CE LYS A 198 0.332 1.003 12.512 1.00 81.54 C ANISOU 17 CE LYS A 198 8487 11421 11076 -948 731 1072 C ATOM 18 NZ LYS A 198 -0.458 1.812 13.490 1.00 81.90 N ANISOU 18 NZ LYS A 198 8453 11547 11117 -756 899 1197 N ATOM 19 N ASP A 199 3.087 6.443 12.789 1.00 78.95 N ANISOU 19 N ASP A 199 8499 11001 10498 -96 848 996 N ATOM 20 CA ASP A 199 2.476 7.690 13.221 1.00 78.09 C ANISOU 20 CA ASP A 199 8347 10939 10383 135 981 1084 C ATOM 21 C ASP A 199 3.291 8.939 12.926 1.00 68.04 C ANISOU 21 C ASP A 199 7230 9567 9054 283 936 1007 C ATOM 22 O ASP A 199 2.726 10.036 12.952 1.00 75.97 O ANISOU 22 O ASP A 199 8180 10614 10071 468 1021 1084 O ATOM 23 CB ASP A 199 2.187 7.640 14.728 1.00 80.35 C ANISOU 23 CB ASP A 199 8732 11175 10623 253 1182 1126 C ATOM 24 CG ASP A 199 0.782 7.187 15.027 1.00 82.67 C ANISOU 24 CG ASP A 199 8834 11597 10982 228 1264 1254 C ATOM 25 OD1 ASP A 199 0.553 5.960 15.106 1.00 83.60 O ANISOU 25 OD1 ASP A 199 8903 11727 11134 38 1231 1259 O ATOM 26 OD2 ASP A 199 -0.100 8.062 15.165 1.00 85.40 O ANISOU 26 OD2 ASP A 199 9105 12005 11338 394 1341 1333 O ATOM 27 N LYS A 200 4.568 8.820 12.655 1.00 53.40 N ANISOU 27 N LYS A 200 5560 7581 7148 213 816 869 N ATOM 28 CA LYS A 200 5.245 10.111 12.575 1.00 42.13 C ANISOU 28 CA LYS A 200 4280 6052 5675 362 804 817 C ATOM 29 C LYS A 200 5.433 10.550 11.128 1.00 31.62 C ANISOU 29 C LYS A 200 2853 4781 4379 319 663 819 C ATOM 30 O LYS A 200 5.931 9.760 10.318 1.00 30.73 O ANISOU 30 O LYS A 200 2716 4689 4272 149 529 762 O ATOM 31 CB LYS A 200 6.589 10.035 13.266 1.00 40.91 C ANISOU 31 CB LYS A 200 4392 5715 5435 349 771 680 C ATOM 32 CG LYS A 200 7.124 11.382 13.666 1.00 47.43 C ANISOU 32 CG LYS A 200 5400 6414 6206 512 804 634 C ATOM 33 CD LYS A 200 7.958 11.278 14.937 1.00 51.71 C ANISOU 33 CD LYS A 200 6191 6809 6648 536 837 538 C ATOM 34 CE LYS A 200 9.078 10.276 14.764 1.00 52.08 C ANISOU 34 CE LYS A 200 6300 6808 6679 368 703 451 C ATOM 35 NZ LYS A 200 8.742 8.852 15.096 1.00 55.99 N ANISOU 35 NZ LYS A 200 6728 7358 7186 257 728 480 N ATOM 36 N PRO A 201 5.023 11.772 10.761 1.00 33.41 N ANISOU 36 N PRO A 201 3033 5037 4626 476 696 891 N ATOM 37 CA PRO A 201 5.071 12.170 9.353 1.00 27.89 C ANISOU 37 CA PRO A 201 2223 4419 3954 440 568 923 C ATOM 38 C PRO A 201 6.475 12.167 8.788 1.00 24.86 C ANISOU 38 C PRO A 201 2002 3920 3525 348 440 798 C ATOM 39 O PRO A 201 7.483 12.329 9.491 1.00 26.90 O ANISOU 39 O PRO A 201 2471 4013 3737 365 453 697 O ATOM 40 CB PRO A 201 4.492 13.587 9.357 1.00 31.35 C ANISOU 40 CB PRO A 201 2638 4858 4414 666 661 1025 C ATOM 41 CG PRO A 201 3.487 13.555 10.476 1.00 35.98 C ANISOU 41 CG PRO A 201 3168 5483 5019 788 841 1104 C ATOM 42 CD PRO A 201 4.196 12.703 11.551 1.00 35.36 C ANISOU 42 CD PRO A 201 3274 5281 4878 697 870 982 C ATOM 43 N VAL A 202 6.518 12.054 7.467 1.00 21.47 N ANISOU 43 N VAL A 202 1462 3591 3104 259 315 817 N ATOM 44 CA VAL A 202 7.746 11.874 6.690 1.00 23.44 C ANISOU 44 CA VAL A 202 1817 3777 3313 154 193 718 C ATOM 45 C VAL A 202 8.113 13.198 6.028 1.00 20.12 C ANISOU 45 C VAL A 202 1438 3319 2888 265 172 759 C ATOM 46 O VAL A 202 7.255 13.835 5.416 1.00 22.39 O ANISOU 46 O VAL A 202 1587 3719 3202 349 176 878 O ATOM 47 CB VAL A 202 7.501 10.768 5.642 1.00 26.93 C ANISOU 47 CB VAL A 202 2124 4359 3748 -25 77 707 C ATOM 48 CG1 VAL A 202 8.539 10.707 4.560 1.00 29.46 C ANISOU 48 CG1 VAL A 202 2514 4659 4019 -104 -36 637 C ATOM 49 CG2 VAL A 202 7.269 9.390 6.371 1.00 28.46 C ANISOU 49 CG2 VAL A 202 2313 4544 3954 -152 103 658 C ATOM 50 N ALA A 203 9.365 13.625 6.186 1.00 19.88 N ANISOU 50 N ALA A 203 1592 3132 2831 266 152 674 N ATOM 51 CA ALA A 203 9.877 14.876 5.634 1.00 19.43 C ANISOU 51 CA ALA A 203 1603 3004 2776 349 136 708 C ATOM 52 C ALA A 203 9.943 14.823 4.112 1.00 21.02 C ANISOU 52 C ALA A 203 1694 3333 2961 282 32 756 C ATOM 53 O ALA A 203 10.072 13.759 3.514 1.00 21.07 O ANISOU 53 O ALA A 203 1637 3434 2935 143 -46 710 O ATOM 54 CB ALA A 203 11.276 15.142 6.218 1.00 20.27 C ANISOU 54 CB ALA A 203 1918 2922 2863 320 124 599 C ATOM 55 N GLU A 204 9.930 16.005 3.479 1.00 21.59 N ANISOU 55 N GLU A 204 1769 3391 3043 383 33 846 N ATOM 56 CA GLU A 204 10.097 16.077 2.030 1.00 20.01 C ANISOU 56 CA GLU A 204 1489 3306 2807 332 -62 901 C ATOM 57 C GLU A 204 11.460 15.502 1.630 1.00 20.66 C ANISOU 57 C GLU A 204 1670 3335 2845 195 -128 791 C ATOM 58 O GLU A 204 12.495 15.974 2.117 1.00 19.43 O ANISOU 58 O GLU A 204 1659 3016 2705 200 -104 737 O ATOM 59 CB GLU A 204 9.978 17.523 1.534 1.00 22.33 C ANISOU 59 CB GLU A 204 1801 3560 3123 475 -34 1026 C ATOM 60 CG GLU A 204 10.082 17.636 0.006 1.00 22.18 C ANISOU 60 CG GLU A 204 1700 3679 3050 435 -128 1104 C ATOM 61 CD GLU A 204 9.985 19.057 -0.514 1.00 28.69 C ANISOU 61 CD GLU A 204 2548 4457 3898 579 -97 1247 C ATOM 62 OE1 GLU A 204 9.376 19.900 0.172 1.00 28.79 O ANISOU 62 OE1 GLU A 204 2583 4382 3973 736 -5 1314 O ATOM 63 OE2 GLU A 204 10.499 19.298 -1.634 1.00 30.19 O ANISOU 63 OE2 GLU A 204 2739 4697 4037 542 -158 1296 O ATOM 64 N PRO A 205 11.509 14.538 0.715 1.00 18.52 N ANISOU 64 N PRO A 205 1324 3197 2515 75 -210 759 N ATOM 65 CA PRO A 205 12.802 13.964 0.316 1.00 19.21 C ANISOU 65 CA PRO A 205 1502 3237 2559 -30 -251 662 C ATOM 66 C PRO A 205 13.576 14.887 -0.608 1.00 19.50 C ANISOU 66 C PRO A 205 1580 3257 2573 0 -267 723 C ATOM 67 O PRO A 205 13.006 15.549 -1.486 1.00 22.41 O ANISOU 67 O PRO A 205 1875 3723 2916 57 -289 837 O ATOM 68 CB PRO A 205 12.404 12.680 -0.417 1.00 22.75 C ANISOU 68 CB PRO A 205 1868 3833 2942 -151 -322 613 C ATOM 69 CG PRO A 205 10.992 12.839 -0.795 1.00 24.23 C ANISOU 69 CG PRO A 205 1901 4178 3128 -121 -352 715 C ATOM 70 CD PRO A 205 10.351 13.810 0.159 1.00 19.70 C ANISOU 70 CD PRO A 205 1308 3539 2637 23 -265 800 C ATOM 71 N ILE A 206 14.889 14.906 -0.414 1.00 20.98 N ANISOU 71 N ILE A 206 1874 3327 2769 -41 -256 659 N ATOM 72 CA ILE A 206 15.803 15.631 -1.292 1.00 21.44 C ANISOU 72 CA ILE A 206 1967 3368 2810 -40 -263 715 C ATOM 73 C ILE A 206 16.238 14.668 -2.393 1.00 21.69 C ANISOU 73 C ILE A 206 1967 3527 2747 -127 -307 673 C ATOM 74 O ILE A 206 16.833 13.634 -2.078 1.00 20.44 O ANISOU 74 O ILE A 206 1843 3344 2578 -197 -309 562 O ATOM 75 CB ILE A 206 17.024 16.131 -0.516 1.00 24.51 C ANISOU 75 CB ILE A 206 2469 3579 3264 -54 -232 676 C ATOM 76 CG1 ILE A 206 16.573 17.013 0.642 1.00 26.22 C ANISOU 76 CG1 ILE A 206 2755 3656 3553 28 -189 690 C ATOM 77 CG2 ILE A 206 17.991 16.849 -1.465 1.00 23.25 C ANISOU 77 CG2 ILE A 206 2326 3410 3097 -70 -232 750 C ATOM 78 CD1 ILE A 206 15.746 18.168 0.209 1.00 34.84 C ANISOU 78 CD1 ILE A 206 3824 4751 4662 139 -161 819 C ATOM 79 N PRO A 207 16.046 14.996 -3.660 1.00 20.30 N ANISOU 79 N PRO A 207 1744 3473 2495 -114 -335 758 N ATOM 80 CA PRO A 207 16.233 13.991 -4.716 1.00 20.75 C ANISOU 80 CA PRO A 207 1786 3664 2433 -190 -378 703 C ATOM 81 C PRO A 207 17.677 13.897 -5.192 1.00 21.88 C ANISOU 81 C PRO A 207 1997 3769 2549 -220 -340 677 C ATOM 82 O PRO A 207 17.937 13.640 -6.371 1.00 23.58 O ANISOU 82 O PRO A 207 2214 4096 2650 -239 -351 690 O ATOM 83 CB PRO A 207 15.308 14.491 -5.834 1.00 25.33 C ANISOU 83 CB PRO A 207 2288 4409 2929 -152 -431 822 C ATOM 84 CG PRO A 207 15.352 15.977 -5.690 1.00 21.89 C ANISOU 84 CG PRO A 207 1860 3890 2568 -46 -387 961 C ATOM 85 CD PRO A 207 15.394 16.219 -4.178 1.00 20.44 C ANISOU 85 CD PRO A 207 1720 3528 2517 -18 -335 911 C ATOM 86 N ILE A 208 18.615 14.046 -4.264 1.00 19.10 N ANISOU 86 N ILE A 208 1697 3268 2292 -224 -296 640 N ATOM 87 CA ILE A 208 20.041 14.038 -4.585 1.00 19.23 C ANISOU 87 CA ILE A 208 1748 3248 2311 -248 -254 636 C ATOM 88 C ILE A 208 20.723 13.144 -3.566 1.00 17.37 C ANISOU 88 C ILE A 208 1547 2921 2132 -287 -242 520 C ATOM 89 O ILE A 208 20.414 13.220 -2.375 1.00 18.78 O ANISOU 89 O ILE A 208 1746 3002 2388 -282 -252 486 O ATOM 90 CB ILE A 208 20.667 15.448 -4.543 1.00 17.30 C ANISOU 90 CB ILE A 208 1517 2913 2144 -220 -222 754 C ATOM 91 CG1 ILE A 208 20.000 16.350 -5.587 1.00 23.02 C ANISOU 91 CG1 ILE A 208 2213 3723 2810 -167 -228 891 C ATOM 92 CG2 ILE A 208 22.195 15.336 -4.793 1.00 22.86 C ANISOU 92 CG2 ILE A 208 2227 3593 2867 -262 -178 757 C ATOM 93 CD1 ILE A 208 20.203 17.825 -5.329 1.00 30.62 C ANISOU 93 CD1 ILE A 208 3206 4557 3870 -128 -200 1011 C ATOM 94 N CYS A 209 21.626 12.268 -4.020 1.00 17.23 N ANISOU 94 N CYS A 209 1542 2937 2068 -312 -213 464 N ATOM 95 CA CYS A 209 22.392 11.470 -3.077 1.00 17.77 C ANISOU 95 CA CYS A 209 1637 2919 2197 -330 -199 378 C ATOM 96 C CYS A 209 23.441 12.335 -2.354 1.00 15.47 C ANISOU 96 C CYS A 209 1339 2525 2015 -334 -189 433 C ATOM 97 O CYS A 209 24.263 13.003 -2.984 1.00 17.00 O ANISOU 97 O CYS A 209 1501 2737 2220 -336 -160 518 O ATOM 98 CB CYS A 209 23.064 10.320 -3.813 1.00 19.52 C ANISOU 98 CB CYS A 209 1876 3200 2340 -333 -158 313 C ATOM 99 SG CYS A 209 24.137 9.299 -2.772 1.00 17.72 S ANISOU 99 SG CYS A 209 1672 2875 2187 -329 -130 234 S ATOM 100 N SER A 210 23.369 12.338 -1.015 1.00 16.78 N ANISOU 100 N SER A 210 1536 2585 2257 -342 -219 389 N ATOM 101 CA SER A 210 24.282 13.125 -0.195 1.00 14.82 C ANISOU 101 CA SER A 210 1295 2232 2102 -366 -236 424 C ATOM 102 C SER A 210 25.712 12.674 -0.318 1.00 17.78 C ANISOU 102 C SER A 210 1624 2626 2506 -388 -218 431 C ATOM 103 O SER A 210 26.610 13.443 0.043 1.00 19.23 O ANISOU 103 O SER A 210 1786 2753 2767 -428 -239 487 O ATOM 104 CB SER A 210 23.897 12.991 1.271 1.00 24.03 C ANISOU 104 CB SER A 210 2523 3298 3308 -366 -274 357 C ATOM 105 OG SER A 210 22.680 13.621 1.480 1.00 27.31 O ANISOU 105 OG SER A 210 2972 3688 3716 -332 -275 371 O ATOM 106 N PHE A 211 25.937 11.442 -0.776 1.00 15.99 N ANISOU 106 N PHE A 211 1383 2469 2222 -362 -181 378 N ATOM 107 CA PHE A 211 27.305 10.948 -0.848 1.00 16.10 C ANISOU 107 CA PHE A 211 1342 2505 2269 -356 -148 394 C ATOM 108 C PHE A 211 27.957 11.223 -2.200 1.00 18.33 C ANISOU 108 C PHE A 211 1565 2886 2515 -342 -76 476 C ATOM 109 O PHE A 211 29.103 11.688 -2.237 1.00 21.59 O ANISOU 109 O PHE A 211 1898 3307 2997 -361 -58 559 O ATOM 110 CB PHE A 211 27.317 9.437 -0.533 1.00 16.69 C ANISOU 110 CB PHE A 211 1452 2580 2311 -316 -128 297 C ATOM 111 CG PHE A 211 26.809 9.119 0.833 1.00 15.76 C ANISOU 111 CG PHE A 211 1390 2370 2227 -327 -186 235 C ATOM 112 CD1 PHE A 211 27.638 9.208 1.935 1.00 19.81 C ANISOU 112 CD1 PHE A 211 1886 2826 2815 -338 -232 251 C ATOM 113 CD2 PHE A 211 25.474 8.765 1.011 1.00 19.59 C ANISOU 113 CD2 PHE A 211 1939 2840 2664 -332 -199 172 C ATOM 114 CE1 PHE A 211 27.152 8.923 3.193 1.00 20.98 C ANISOU 114 CE1 PHE A 211 2101 2898 2973 -342 -281 198 C ATOM 115 CE2 PHE A 211 24.979 8.486 2.266 1.00 22.66 C ANISOU 115 CE2 PHE A 211 2379 3152 3077 -337 -234 128 C ATOM 116 CZ PHE A 211 25.818 8.579 3.359 1.00 21.75 C ANISOU 116 CZ PHE A 211 2268 2975 3021 -337 -272 139 C ATOM 117 N CYS A 212 27.286 10.917 -3.320 1.00 16.18 N ANISOU 117 N CYS A 212 1323 2697 2127 -312 -35 460 N ATOM 118 CA CYS A 212 27.893 11.108 -4.631 1.00 20.79 C ANISOU 118 CA CYS A 212 1867 3384 2647 -286 46 536 C ATOM 119 C CYS A 212 27.314 12.265 -5.422 1.00 19.62 C ANISOU 119 C CYS A 212 1719 3277 2459 -302 40 632 C ATOM 120 O CYS A 212 27.867 12.594 -6.488 1.00 22.04 O ANISOU 120 O CYS A 212 1991 3670 2713 -284 112 721 O ATOM 121 CB CYS A 212 27.819 9.845 -5.500 1.00 18.75 C ANISOU 121 CB CYS A 212 1662 3206 2258 -230 112 451 C ATOM 122 SG CYS A 212 26.119 9.438 -6.066 1.00 19.60 S ANISOU 122 SG CYS A 212 1867 3357 2223 -248 55 359 S ATOM 123 N LEU A 213 26.248 12.914 -4.922 1.00 17.72 N ANISOU 123 N LEU A 213 1512 2978 2242 -324 -33 632 N ATOM 124 CA LEU A 213 25.602 14.061 -5.587 1.00 18.15 C ANISOU 124 CA LEU A 213 1569 3057 2268 -320 -42 737 C ATOM 125 C LEU A 213 24.899 13.664 -6.883 1.00 21.62 C ANISOU 125 C LEU A 213 2030 3640 2544 -284 -25 737 C ATOM 126 O LEU A 213 24.499 14.533 -7.675 1.00 22.82 O ANISOU 126 O LEU A 213 2177 3846 2647 -267 -23 846 O ATOM 127 CB LEU A 213 26.592 15.209 -5.840 1.00 18.92 C ANISOU 127 CB LEU A 213 1620 3122 2445 -349 -3 878 C ATOM 128 CG LEU A 213 27.239 15.719 -4.562 1.00 20.96 C ANISOU 128 CG LEU A 213 1867 3238 2858 -409 -46 877 C ATOM 129 CD1 LEU A 213 28.138 16.909 -4.919 1.00 22.31 C ANISOU 129 CD1 LEU A 213 1993 3373 3111 -464 -14 1026 C ATOM 130 CD2 LEU A 213 26.181 16.129 -3.555 1.00 23.53 C ANISOU 130 CD2 LEU A 213 2265 3451 3223 -406 -118 823 C ATOM 131 N GLY A 214 24.735 12.381 -7.126 1.00 19.45 N ANISOU 131 N GLY A 214 1790 3424 2178 -275 -19 619 N ATOM 132 CA GLY A 214 23.908 11.933 -8.227 1.00 20.52 C ANISOU 132 CA GLY A 214 1965 3687 2146 -263 -34 591 C ATOM 133 C GLY A 214 22.433 11.922 -7.880 1.00 23.14 C ANISOU 133 C GLY A 214 2301 4025 2466 -283 -130 555 C ATOM 134 O GLY A 214 22.020 12.086 -6.743 1.00 24.64 O ANISOU 134 O GLY A 214 2476 4116 2769 -296 -168 533 O ATOM 135 N THR A 215 21.639 11.771 -8.914 1.00 26.01 N ANISOU 135 N THR A 215 2680 4521 2683 -285 -168 561 N ATOM 136 CA THR A 215 20.202 11.634 -8.776 1.00 23.32 C ANISOU 136 CA THR A 215 2318 4228 2316 -311 -265 536 C ATOM 137 C THR A 215 19.816 10.175 -8.902 1.00 23.09 C ANISOU 137 C THR A 215 2344 4231 2199 -372 -299 378 C ATOM 138 O THR A 215 20.650 9.291 -9.042 1.00 25.47 O ANISOU 138 O THR A 215 2715 4500 2463 -377 -241 285 O ATOM 139 CB THR A 215 19.473 12.424 -9.846 1.00 25.60 C ANISOU 139 CB THR A 215 2574 4657 2496 -284 -311 657 C ATOM 140 OG1 THR A 215 19.763 11.849 -11.124 1.00 28.61 O ANISOU 140 OG1 THR A 215 3016 5166 2689 -294 -300 625 O ATOM 141 CG2 THR A 215 19.890 13.887 -9.828 1.00 31.28 C ANISOU 141 CG2 THR A 215 3261 5326 3300 -223 -265 824 C ATOM 142 N LYS A 216 18.508 9.924 -8.929 1.00 22.41 N ANISOU 142 N LYS A 216 2225 4214 2075 -420 -395 357 N ATOM 143 CA LYS A 216 18.040 8.577 -9.247 1.00 25.33 C ANISOU 143 CA LYS A 216 2657 4623 2344 -506 -445 213 C ATOM 144 C LYS A 216 18.491 8.130 -10.632 1.00 26.70 C ANISOU 144 C LYS A 216 2925 4900 2320 -511 -431 167 C ATOM 145 O LYS A 216 18.442 6.933 -10.931 1.00 28.46 O ANISOU 145 O LYS A 216 3247 5116 2451 -575 -445 23 O ATOM 146 CB LYS A 216 16.522 8.516 -9.170 1.00 24.84 C ANISOU 146 CB LYS A 216 2514 4649 2273 -571 -562 226 C ATOM 147 CG LYS A 216 15.849 9.331 -10.261 1.00 28.55 C ANISOU 147 CG LYS A 216 2924 5299 2626 -550 -637 347 C ATOM 148 CD LYS A 216 14.321 9.421 -10.089 1.00 34.19 C ANISOU 148 CD LYS A 216 3513 6117 3361 -598 -754 397 C ATOM 149 CE LYS A 216 13.700 10.368 -11.144 1.00 35.39 C ANISOU 149 CE LYS A 216 3592 6448 3408 -549 -826 549 C ATOM 150 NZ LYS A 216 12.207 10.461 -11.019 1.00 45.52 N ANISOU 150 NZ LYS A 216 4768 7770 4759 -565 -889 597 N ATOM 151 N GLU A 217 18.931 9.054 -11.486 1.00 26.30 N ANISOU 151 N GLU A 217 2863 4935 2196 -443 -396 288 N ATOM 152 CA GLU A 217 19.357 8.651 -12.818 1.00 26.39 C ANISOU 152 CA GLU A 217 2975 5055 1996 -436 -370 250 C ATOM 153 C GLU A 217 20.824 8.256 -12.884 1.00 26.41 C ANISOU 153 C GLU A 217 3054 4979 2003 -374 -221 206 C ATOM 154 O GLU A 217 21.239 7.685 -13.897 1.00 32.55 O ANISOU 154 O GLU A 217 3942 5825 2601 -358 -173 143 O ATOM 155 CB GLU A 217 19.068 9.772 -13.817 1.00 34.00 C ANISOU 155 CB GLU A 217 3894 6172 2851 -390 -400 414 C ATOM 156 CG GLU A 217 17.602 10.193 -13.839 1.00 38.98 C ANISOU 156 CG GLU A 217 4431 6908 3473 -430 -548 482 C ATOM 157 CD GLU A 217 16.640 9.032 -14.158 1.00 51.09 C ANISOU 157 CD GLU A 217 6007 8523 4883 -549 -675 336 C ATOM 158 OE1 GLU A 217 17.057 8.055 -14.826 1.00 50.98 O ANISOU 158 OE1 GLU A 217 6135 8524 4713 -592 -657 196 O ATOM 159 OE2 GLU A 217 15.458 9.098 -13.740 1.00 53.00 O ANISOU 159 OE2 GLU A 217 6141 8810 5185 -604 -789 363 O ATOM 160 N GLN A 218 21.626 8.512 -11.837 1.00 24.83 N ANISOU 160 N GLN A 218 2799 4641 1994 -336 -146 238 N ATOM 161 CA GLN A 218 23.052 8.221 -11.945 1.00 25.57 C ANISOU 161 CA GLN A 218 2928 4687 2100 -269 -6 228 C ATOM 162 C GLN A 218 23.657 7.974 -10.568 1.00 25.96 C ANISOU 162 C GLN A 218 2933 4578 2352 -262 27 199 C ATOM 163 O GLN A 218 23.743 8.898 -9.751 1.00 25.31 O ANISOU 163 O GLN A 218 2757 4436 2423 -263 9 296 O ATOM 164 CB GLN A 218 23.762 9.364 -12.638 1.00 36.52 C ANISOU 164 CB GLN A 218 4262 6149 3466 -208 69 397 C ATOM 165 CG GLN A 218 25.065 8.947 -13.224 1.00 42.89 C ANISOU 165 CG GLN A 218 5110 6975 4210 -137 219 392 C ATOM 166 CD GLN A 218 25.632 9.996 -14.137 1.00 52.07 C ANISOU 166 CD GLN A 218 6230 8240 5312 -88 297 566 C ATOM 167 OE1 GLN A 218 25.170 11.141 -14.157 1.00 59.28 O ANISOU 167 OE1 GLN A 218 7077 9177 6270 -106 240 702 O ATOM 168 NE2 GLN A 218 26.634 9.615 -14.908 1.00 54.94 N ANISOU 168 NE2 GLN A 218 6638 8663 5575 -16 439 571 N ATOM 169 N ASN A 219 24.107 6.753 -10.317 1.00 25.24 N ANISOU 169 N ASN A 219 2920 4413 2256 -251 77 69 N ATOM 170 CA ASN A 219 24.892 6.463 -9.123 1.00 23.85 C ANISOU 170 CA ASN A 219 2704 4106 2251 -223 121 58 C ATOM 171 C ASN A 219 26.387 6.532 -9.462 1.00 23.70 C ANISOU 171 C ASN A 219 2655 4102 2248 -132 257 122 C ATOM 172 O ASN A 219 26.763 7.064 -10.504 1.00 28.98 O ANISOU 172 O ASN A 219 3314 4878 2819 -96 319 202 O ATOM 173 CB ASN A 219 24.477 5.101 -8.548 1.00 22.41 C ANISOU 173 CB ASN A 219 2617 3824 2074 -256 97 -98 C ATOM 174 CG ASN A 219 24.796 3.946 -9.475 1.00 26.53 C ANISOU 174 CG ASN A 219 3283 4355 2442 -222 172 -218 C ATOM 175 OD1 ASN A 219 25.450 4.119 -10.485 1.00 29.15 O ANISOU 175 OD1 ASN A 219 3640 4773 2663 -156 258 -185 O ATOM 176 ND2 ASN A 219 24.354 2.747 -9.106 1.00 27.81 N ANISOU 176 ND2 ASN A 219 3552 4417 2596 -263 150 -357 N ATOM 177 N ARG A 220 27.247 5.966 -8.600 1.00 23.63 N ANISOU 177 N ARG A 220 2622 3997 2359 -89 308 99 N ATOM 178 CA ARG A 220 28.683 6.083 -8.822 1.00 24.83 C ANISOU 178 CA ARG A 220 2703 4178 2553 -1 433 185 C ATOM 179 C ARG A 220 29.157 5.238 -9.987 1.00 32.69 C ANISOU 179 C ARG A 220 3800 5236 3385 89 563 125 C ATOM 180 O ARG A 220 30.271 5.455 -10.486 1.00 31.69 O ANISOU 180 O ARG A 220 3608 5175 3258 173 690 218 O ATOM 181 CB ARG A 220 29.446 5.707 -7.552 1.00 26.15 C ANISOU 181 CB ARG A 220 2803 4242 2891 25 437 189 C ATOM 182 CG ARG A 220 29.470 6.842 -6.530 1.00 23.43 C ANISOU 182 CG ARG A 220 2340 3858 2703 -45 343 290 C ATOM 183 CD ARG A 220 30.199 6.444 -5.236 1.00 19.92 C ANISOU 183 CD ARG A 220 1838 3325 2407 -27 324 291 C ATOM 184 NE ARG A 220 30.416 7.615 -4.378 1.00 19.86 N ANISOU 184 NE ARG A 220 1728 3288 2531 -98 240 389 N ATOM 185 CZ ARG A 220 30.396 7.608 -3.048 1.00 18.73 C ANISOU 185 CZ ARG A 220 1572 3055 2490 -132 154 371 C ATOM 186 NH1 ARG A 220 30.185 6.477 -2.360 1.00 18.61 N ANISOU 186 NH1 ARG A 220 1626 2972 2475 -97 144 276 N ATOM 187 NH2 ARG A 220 30.587 8.747 -2.382 1.00 19.76 N ANISOU 187 NH2 ARG A 220 1635 3154 2718 -205 78 449 N ATOM 188 N GLU A 221 28.335 4.294 -10.437 1.00 32.71 N ANISOU 188 N GLU A 221 3964 5219 3246 69 537 -27 N ATOM 189 CA GLU A 221 28.667 3.466 -11.585 1.00 41.22 C ANISOU 189 CA GLU A 221 5184 6341 4137 150 655 -112 C ATOM 190 C GLU A 221 27.967 3.923 -12.857 1.00 40.86 C ANISOU 190 C GLU A 221 5211 6432 3883 110 623 -110 C ATOM 191 O GLU A 221 27.870 3.149 -13.817 1.00 49.53 O ANISOU 191 O GLU A 221 6476 7560 4783 143 678 -224 O ATOM 192 CB GLU A 221 28.351 2.006 -11.269 1.00 45.99 C ANISOU 192 CB GLU A 221 5950 6811 4711 154 655 -294 C ATOM 193 CG GLU A 221 29.448 1.362 -10.448 1.00 54.76 C ANISOU 193 CG GLU A 221 7020 7818 5968 265 758 -281 C ATOM 194 CD GLU A 221 28.964 0.208 -9.606 1.00 63.76 C ANISOU 194 CD GLU A 221 8272 8791 7163 236 711 -415 C ATOM 195 OE1 GLU A 221 28.087 0.430 -8.743 1.00 64.75 O ANISOU 195 OE1 GLU A 221 8357 8867 7376 119 572 -421 O ATOM 196 OE2 GLU A 221 29.463 -0.923 -9.805 1.00 70.95 O ANISOU 196 OE2 GLU A 221 9316 9613 8028 337 824 -507 O ATOM 197 N LYS A 222 27.492 5.170 -12.891 1.00 35.79 N ANISOU 197 N LYS A 222 4458 5868 3274 45 536 18 N ATOM 198 CA LYS A 222 26.887 5.753 -14.087 1.00 41.66 C ANISOU 198 CA LYS A 222 5246 6758 3826 20 502 60 C ATOM 199 C LYS A 222 25.621 5.008 -14.503 1.00 44.61 C ANISOU 199 C LYS A 222 5765 7146 4037 -67 379 -97 C ATOM 200 O LYS A 222 25.324 4.883 -15.692 1.00 44.30 O ANISOU 200 O LYS A 222 5839 7223 3770 -65 380 -133 O ATOM 201 CB LYS A 222 27.897 5.788 -15.239 1.00 50.70 C ANISOU 201 CB LYS A 222 6432 8008 4823 133 675 118 C ATOM 202 CG LYS A 222 27.775 6.988 -16.175 1.00 58.20 C ANISOU 202 CG LYS A 222 7333 9111 5670 131 676 281 C ATOM 203 CD LYS A 222 29.158 7.466 -16.618 1.00 59.62 C ANISOU 203 CD LYS A 222 7429 9351 5871 236 867 432 C ATOM 204 CE LYS A 222 29.082 8.731 -17.467 1.00 62.14 C ANISOU 204 CE LYS A 222 7694 9806 6110 230 877 621 C ATOM 205 NZ LYS A 222 30.448 9.212 -17.843 1.00 65.23 N ANISOU 205 NZ LYS A 222 7985 10255 6545 316 1070 787 N ATOM 206 N LYS A 223 24.871 4.497 -13.532 1.00 40.63 N ANISOU 206 N LYS A 223 5260 6532 3644 -151 271 -188 N ATOM 207 CA LYS A 223 23.652 3.738 -13.766 1.00 37.84 C ANISOU 207 CA LYS A 223 5021 6182 3177 -262 143 -332 C ATOM 208 C LYS A 223 22.514 4.296 -12.925 1.00 35.58 C ANISOU 208 C LYS A 223 4610 5888 3020 -365 -12 -280 C ATOM 209 O LYS A 223 22.741 4.821 -11.830 1.00 34.25 O ANISOU 209 O LYS A 223 4319 5640 3053 -348 -5 -199 O ATOM 210 CB LYS A 223 23.846 2.252 -13.419 1.00 39.55 C ANISOU 210 CB LYS A 223 5387 6246 3393 -266 188 -515 C ATOM 211 CG LYS A 223 24.773 1.503 -14.380 1.00 53.05 C ANISOU 211 CG LYS A 223 7265 7956 4934 -157 344 -601 C ATOM 212 CD LYS A 223 24.948 0.040 -13.981 1.00 60.13 C ANISOU 212 CD LYS A 223 8327 8672 5847 -148 396 -778 C ATOM 213 CE LYS A 223 25.695 -0.103 -12.651 1.00 63.30 C ANISOU 213 CE LYS A 223 8619 8935 6498 -77 463 -721 C ATOM 214 NZ LYS A 223 25.753 -1.517 -12.149 1.00 64.59 N ANISOU 214 NZ LYS A 223 8939 8906 6695 -69 503 -875 N ATOM 215 N PRO A 224 21.278 4.161 -13.393 1.00 31.54 N ANISOU 215 N PRO A 224 4129 5461 2395 -472 -152 -328 N ATOM 216 CA PRO A 224 20.133 4.582 -12.575 1.00 30.18 C ANISOU 216 CA PRO A 224 3829 5288 2350 -560 -285 -278 C ATOM 217 C PRO A 224 20.003 3.723 -11.326 1.00 28.63 C ANISOU 217 C PRO A 224 3641 4922 2314 -607 -286 -372 C ATOM 218 O PRO A 224 20.280 2.521 -11.334 1.00 29.54 O ANISOU 218 O PRO A 224 3896 4938 2390 -628 -245 -517 O ATOM 219 CB PRO A 224 18.931 4.386 -13.508 1.00 30.63 C ANISOU 219 CB PRO A 224 3924 5491 2225 -668 -432 -322 C ATOM 220 CG PRO A 224 19.494 4.170 -14.845 1.00 33.95 C ANISOU 220 CG PRO A 224 4486 6001 2410 -624 -378 -367 C ATOM 221 CD PRO A 224 20.847 3.573 -14.664 1.00 34.52 C ANISOU 221 CD PRO A 224 4657 5943 2517 -522 -200 -433 C ATOM 222 N GLU A 225 19.578 4.353 -10.238 1.00 25.86 N ANISOU 222 N GLU A 225 3154 4531 2141 -616 -325 -284 N ATOM 223 CA GLU A 225 19.387 3.638 -8.980 1.00 24.70 C ANISOU 223 CA GLU A 225 3006 4235 2142 -658 -325 -348 C ATOM 224 C GLU A 225 18.526 4.517 -8.094 1.00 24.19 C ANISOU 224 C GLU A 225 2792 4188 2211 -678 -393 -240 C ATOM 225 O GLU A 225 18.861 5.681 -7.858 1.00 24.44 O ANISOU 225 O GLU A 225 2735 4239 2313 -601 -366 -114 O ATOM 226 CB GLU A 225 20.715 3.318 -8.295 1.00 24.34 C ANISOU 226 CB GLU A 225 2998 4052 2197 -561 -199 -363 C ATOM 227 CG GLU A 225 20.515 2.548 -7.015 1.00 23.31 C ANISOU 227 CG GLU A 225 2881 3773 2202 -598 -201 -420 C ATOM 228 CD GLU A 225 21.796 2.206 -6.264 1.00 23.70 C ANISOU 228 CD GLU A 225 2954 3697 2351 -498 -94 -420 C ATOM 229 OE1 GLU A 225 22.884 2.717 -6.618 1.00 26.47 O ANISOU 229 OE1 GLU A 225 3277 4081 2698 -401 -17 -356 O ATOM 230 OE2 GLU A 225 21.691 1.437 -5.281 1.00 26.46 O ANISOU 230 OE2 GLU A 225 3340 3923 2791 -519 -90 -469 O ATOM 231 N GLU A 226 17.390 3.988 -7.646 1.00 25.13 N ANISOU 231 N GLU A 226 2885 4302 2362 -782 -475 -283 N ATOM 232 CA GLU A 226 16.479 4.772 -6.829 1.00 23.44 C ANISOU 232 CA GLU A 226 2528 4116 2265 -788 -524 -178 C ATOM 233 C GLU A 226 17.109 5.130 -5.499 1.00 24.72 C ANISOU 233 C GLU A 226 2666 4141 2587 -709 -444 -137 C ATOM 234 O GLU A 226 17.909 4.369 -4.945 1.00 24.44 O ANISOU 234 O GLU A 226 2714 3978 2595 -694 -380 -211 O ATOM 235 CB GLU A 226 15.184 3.998 -6.581 1.00 26.50 C ANISOU 235 CB GLU A 226 2881 4527 2661 -923 -613 -228 C ATOM 236 CG GLU A 226 14.330 3.860 -7.840 1.00 35.34 C ANISOU 236 CG GLU A 226 3986 5816 3625 -1020 -733 -243 C ATOM 237 CD GLU A 226 13.917 5.219 -8.391 1.00 47.05 C ANISOU 237 CD GLU A 226 5341 7462 5076 -947 -780 -87 C ATOM 238 OE1 GLU A 226 13.325 6.024 -7.639 1.00 38.78 O ANISOU 238 OE1 GLU A 226 4157 6428 4149 -897 -780 30 O ATOM 239 OE2 GLU A 226 14.205 5.489 -9.577 1.00 57.60 O ANISOU 239 OE2 GLU A 226 6724 8905 6258 -926 -805 -77 O ATOM 240 N LEU A 227 16.745 6.308 -4.989 1.00 21.95 N ANISOU 240 N LEU A 227 2210 3814 2318 -653 -451 -17 N ATOM 241 CA LEU A 227 17.243 6.796 -3.714 1.00 20.50 C ANISOU 241 CA LEU A 227 2013 3507 2268 -586 -392 22 C ATOM 242 C LEU A 227 16.404 6.260 -2.556 1.00 20.86 C ANISOU 242 C LEU A 227 2036 3492 2397 -630 -400 -4 C ATOM 243 O LEU A 227 15.223 5.934 -2.711 1.00 23.26 O ANISOU 243 O LEU A 227 2281 3873 2684 -703 -456 -3 O ATOM 244 CB LEU A 227 17.208 8.324 -3.683 1.00 23.13 C ANISOU 244 CB LEU A 227 2274 3869 2643 -505 -388 154 C ATOM 245 CG LEU A 227 18.084 9.034 -4.725 1.00 22.19 C ANISOU 245 CG LEU A 227 2169 3802 2461 -457 -366 213 C ATOM 246 CD1 LEU A 227 17.737 10.489 -4.703 1.00 21.87 C ANISOU 246 CD1 LEU A 227 2064 3781 2466 -391 -371 349 C ATOM 247 CD2 LEU A 227 19.577 8.853 -4.422 1.00 20.51 C ANISOU 247 CD2 LEU A 227 2016 3489 2289 -426 -293 181 C ATOM 248 N ILE A 228 17.007 6.214 -1.377 1.00 19.44 N ANISOU 248 N ILE A 228 1895 3185 2308 -588 -346 -15 N ATOM 249 CA ILE A 228 16.207 6.120 -0.164 1.00 19.41 C ANISOU 249 CA ILE A 228 1861 3132 2384 -597 -336 1 C ATOM 250 C ILE A 228 16.442 7.391 0.635 1.00 18.91 C ANISOU 250 C ILE A 228 1777 3020 2387 -500 -306 81 C ATOM 251 O ILE A 228 17.517 7.989 0.570 1.00 18.43 O ANISOU 251 O ILE A 228 1753 2915 2335 -450 -289 96 O ATOM 252 CB ILE A 228 16.464 4.864 0.679 1.00 26.61 C ANISOU 252 CB ILE A 228 2852 3930 3328 -639 -304 -81 C ATOM 253 CG1 ILE A 228 17.857 4.796 1.218 1.00 25.72 C ANISOU 253 CG1 ILE A 228 2818 3709 3244 -573 -259 -103 C ATOM 254 CG2 ILE A 228 16.095 3.585 -0.129 1.00 29.43 C ANISOU 254 CG2 ILE A 228 3251 4310 3621 -750 -335 -169 C ATOM 255 CD1 ILE A 228 18.002 3.590 2.200 1.00 32.88 C ANISOU 255 CD1 ILE A 228 3802 4501 4188 -597 -226 -159 C ATOM 256 N SER A 229 15.398 7.831 1.340 1.00 19.57 N ANISOU 256 N SER A 229 1802 3117 2515 -477 -296 135 N ATOM 257 CA SER A 229 15.389 9.151 1.962 1.00 17.53 C ANISOU 257 CA SER A 229 1540 2815 2305 -379 -266 210 C ATOM 258 C SER A 229 15.014 9.043 3.427 1.00 17.01 C ANISOU 258 C SER A 229 1507 2665 2290 -348 -215 202 C ATOM 259 O SER A 229 14.110 8.305 3.789 1.00 18.87 O ANISOU 259 O SER A 229 1699 2935 2535 -390 -201 197 O ATOM 260 CB SER A 229 14.373 10.064 1.261 1.00 19.49 C ANISOU 260 CB SER A 229 1685 3178 2544 -336 -285 310 C ATOM 261 OG SER A 229 14.731 10.191 -0.116 1.00 22.68 O ANISOU 261 OG SER A 229 2070 3669 2879 -360 -333 325 O ATOM 262 N CYS A 230 15.714 9.796 4.253 1.00 19.15 N ANISOU 262 N CYS A 230 1859 2829 2589 -283 -188 205 N ATOM 263 CA CYS A 230 15.444 9.826 5.682 1.00 15.50 C ANISOU 263 CA CYS A 230 1456 2283 2150 -240 -137 195 C ATOM 264 C CYS A 230 14.082 10.433 5.950 1.00 16.06 C ANISOU 264 C CYS A 230 1457 2405 2238 -172 -86 269 C ATOM 265 O CYS A 230 13.759 11.505 5.422 1.00 17.10 O ANISOU 265 O CYS A 230 1551 2567 2380 -106 -85 336 O ATOM 266 CB CYS A 230 16.518 10.672 6.385 1.00 15.50 C ANISOU 266 CB CYS A 230 1568 2162 2160 -194 -141 178 C ATOM 267 SG CYS A 230 16.285 10.846 8.172 1.00 16.57 S ANISOU 267 SG CYS A 230 1818 2191 2287 -132 -85 156 S ATOM 268 N ALA A 231 13.293 9.759 6.790 1.00 15.59 N ANISOU 268 N ALA A 231 1381 2355 2186 -178 -35 269 N ATOM 269 CA ALA A 231 11.958 10.258 7.073 1.00 17.17 C ANISOU 269 CA ALA A 231 1491 2622 2410 -103 31 354 C ATOM 270 C ALA A 231 11.993 11.490 7.956 1.00 17.88 C ANISOU 270 C ALA A 231 1679 2613 2502 35 100 376 C ATOM 271 O ALA A 231 11.018 12.227 8.019 1.00 19.10 O ANISOU 271 O ALA A 231 1767 2810 2677 137 163 457 O ATOM 272 CB ALA A 231 11.130 9.144 7.722 1.00 20.01 C ANISOU 272 CB ALA A 231 1797 3023 2782 -160 78 359 C ATOM 273 N ASP A 232 13.094 11.746 8.644 1.00 19.25 N ANISOU 273 N ASP A 232 2011 2652 2652 43 89 306 N ATOM 274 CA ASP A 232 13.121 12.909 9.528 1.00 20.65 C ANISOU 274 CA ASP A 232 2313 2717 2817 161 148 309 C ATOM 275 C ASP A 232 13.787 14.137 8.926 1.00 19.52 C ANISOU 275 C ASP A 232 2225 2501 2691 191 106 319 C ATOM 276 O ASP A 232 13.314 15.256 9.168 1.00 23.02 O ANISOU 276 O ASP A 232 2719 2883 3143 307 167 360 O ATOM 277 CB ASP A 232 13.823 12.550 10.845 1.00 20.55 C ANISOU 277 CB ASP A 232 2460 2595 2755 150 157 229 C ATOM 278 CG ASP A 232 13.006 11.627 11.680 1.00 24.35 C ANISOU 278 CG ASP A 232 2916 3121 3214 158 236 242 C ATOM 279 OD1 ASP A 232 11.952 12.027 12.195 1.00 25.72 O ANISOU 279 OD1 ASP A 232 3071 3317 3385 260 344 296 O ATOM 280 OD2 ASP A 232 13.409 10.484 11.806 1.00 28.83 O ANISOU 280 OD2 ASP A 232 3480 3701 3772 67 201 208 O ATOM 281 N CYS A 233 14.875 13.989 8.172 1.00 17.06 N ANISOU 281 N CYS A 233 1913 2184 2385 98 15 290 N ATOM 282 CA CYS A 233 15.501 15.150 7.581 1.00 15.92 C ANISOU 282 CA CYS A 233 1813 1972 2265 114 -17 317 C ATOM 283 C CYS A 233 15.367 15.227 6.070 1.00 17.63 C ANISOU 283 C CYS A 233 1898 2303 2497 90 -54 388 C ATOM 284 O CYS A 233 15.700 16.278 5.497 1.00 21.16 O ANISOU 284 O CYS A 233 2371 2701 2967 117 -65 440 O ATOM 285 CB CYS A 233 16.980 15.225 7.973 1.00 18.59 C ANISOU 285 CB CYS A 233 2263 2202 2599 36 -85 246 C ATOM 286 SG CYS A 233 18.036 13.961 7.213 1.00 18.71 S ANISOU 286 SG CYS A 233 2192 2305 2610 -90 -163 213 S ATOM 287 N GLY A 234 14.911 14.161 5.410 1.00 17.58 N ANISOU 287 N GLY A 234 1768 2440 2473 32 -77 393 N ATOM 288 CA GLY A 234 14.766 14.162 3.973 1.00 18.33 C ANISOU 288 CA GLY A 234 1754 2656 2555 3 -121 452 C ATOM 289 C GLY A 234 16.030 13.946 3.179 1.00 18.90 C ANISOU 289 C GLY A 234 1846 2726 2608 -78 -177 421 C ATOM 290 O GLY A 234 15.934 13.798 1.945 1.00 19.98 O ANISOU 290 O GLY A 234 1905 2977 2708 -106 -211 460 O ATOM 291 N ASN A 235 17.188 13.911 3.823 1.00 18.76 N ANISOU 291 N ASN A 235 1924 2598 2606 -114 -188 359 N ATOM 292 CA ASN A 235 18.415 13.680 3.058 1.00 20.69 C ANISOU 292 CA ASN A 235 2164 2856 2841 -181 -227 346 C ATOM 293 C ASN A 235 18.423 12.231 2.550 1.00 17.00 C ANISOU 293 C ASN A 235 1644 2487 2327 -242 -242 289 C ATOM 294 O ASN A 235 17.842 11.343 3.170 1.00 17.29 O ANISOU 294 O ASN A 235 1682 2530 2357 -257 -232 240 O ATOM 295 CB ASN A 235 19.643 13.997 3.923 1.00 26.59 C ANISOU 295 CB ASN A 235 3003 3476 3626 -208 -245 307 C ATOM 296 CG ASN A 235 19.887 15.520 4.080 1.00 38.34 C ANISOU 296 CG ASN A 235 4557 4852 5158 -179 -243 362 C ATOM 297 OD1 ASN A 235 19.124 16.335 3.600 1.00 44.64 O ANISOU 297 OD1 ASN A 235 5342 5658 5963 -118 -214 434 O ATOM 298 ND2 ASN A 235 20.971 15.878 4.754 1.00 50.33 N ANISOU 298 ND2 ASN A 235 6150 6263 6710 -229 -279 331 N ATOM 299 N SER A 236 19.091 12.005 1.410 1.00 18.59 N ANISOU 299 N SER A 236 1814 2756 2495 -277 -258 298 N ATOM 300 CA SER A 236 18.939 10.780 0.639 1.00 17.69 C ANISOU 300 CA SER A 236 1668 2736 2316 -326 -269 247 C ATOM 301 C SER A 236 20.283 10.156 0.291 1.00 17.76 C ANISOU 301 C SER A 236 1705 2731 2311 -351 -258 204 C ATOM 302 O SER A 236 21.329 10.800 0.303 1.00 17.87 O ANISOU 302 O SER A 236 1726 2703 2362 -340 -251 242 O ATOM 303 CB SER A 236 18.204 11.052 -0.681 1.00 17.82 C ANISOU 303 CB SER A 236 1619 2886 2265 -326 -291 304 C ATOM 304 OG SER A 236 16.929 11.619 -0.422 1.00 19.63 O ANISOU 304 OG SER A 236 1796 3149 2514 -287 -298 363 O ATOM 305 N GLY A 237 20.226 8.874 -0.039 1.00 16.10 N ANISOU 305 N GLY A 237 1510 2556 2052 -387 -255 129 N ATOM 306 CA GLY A 237 21.400 8.162 -0.521 1.00 16.15 C ANISOU 306 CA GLY A 237 1543 2559 2034 -388 -226 89 C ATOM 307 C GLY A 237 21.009 7.057 -1.471 1.00 16.23 C ANISOU 307 C GLY A 237 1580 2636 1951 -424 -222 19 C ATOM 308 O GLY A 237 19.947 6.435 -1.324 1.00 18.40 O ANISOU 308 O GLY A 237 1863 2921 2205 -473 -250 -27 O ATOM 309 N HIS A 238 21.869 6.784 -2.433 1.00 15.67 N ANISOU 309 N HIS A 238 1528 2606 1820 -404 -184 8 N ATOM 310 CA HIS A 238 21.733 5.535 -3.177 1.00 20.59 C ANISOU 310 CA HIS A 238 2222 3251 2348 -432 -168 -91 C ATOM 311 C HIS A 238 22.027 4.368 -2.233 1.00 19.42 C ANISOU 311 C HIS A 238 2140 2984 2255 -432 -142 -168 C ATOM 312 O HIS A 238 22.983 4.435 -1.451 1.00 18.39 O ANISOU 312 O HIS A 238 1998 2785 2203 -379 -111 -140 O ATOM 313 CB HIS A 238 22.724 5.443 -4.339 1.00 17.21 C ANISOU 313 CB HIS A 238 1820 2882 1837 -385 -106 -89 C ATOM 314 CG HIS A 238 22.546 6.477 -5.402 1.00 20.23 C ANISOU 314 CG HIS A 238 2155 3385 2144 -379 -119 -4 C ATOM 315 ND1 HIS A 238 23.444 7.508 -5.568 1.00 16.90 N ANISOU 315 ND1 HIS A 238 1673 2984 1764 -330 -78 106 N ATOM 316 CD2 HIS A 238 21.604 6.640 -6.354 1.00 22.11 C ANISOU 316 CD2 HIS A 238 2398 3734 2268 -418 -171 -1 C ATOM 317 CE1 HIS A 238 23.077 8.243 -6.602 1.00 21.01 C ANISOU 317 CE1 HIS A 238 2174 3613 2197 -330 -91 175 C ATOM 318 NE2 HIS A 238 21.949 7.745 -7.087 1.00 20.26 N ANISOU 318 NE2 HIS A 238 2116 3582 2002 -378 -153 113 N ATOM 319 N PRO A 239 21.249 3.283 -2.288 1.00 19.70 N ANISOU 319 N PRO A 239 2243 2991 2251 -497 -158 -258 N ATOM 320 CA PRO A 239 21.639 2.081 -1.519 1.00 18.79 C ANISOU 320 CA PRO A 239 2212 2747 2182 -486 -117 -325 C ATOM 321 C PRO A 239 23.085 1.665 -1.720 1.00 18.98 C ANISOU 321 C PRO A 239 2275 2728 2207 -388 -37 -333 C ATOM 322 O PRO A 239 23.756 1.282 -0.744 1.00 20.19 O ANISOU 322 O PRO A 239 2438 2792 2441 -334 -8 -318 O ATOM 323 CB PRO A 239 20.652 1.025 -2.041 1.00 19.99 C ANISOU 323 CB PRO A 239 2446 2886 2262 -588 -144 -426 C ATOM 324 CG PRO A 239 19.424 1.826 -2.358 1.00 21.30 C ANISOU 324 CG PRO A 239 2520 3171 2402 -663 -226 -380 C ATOM 325 CD PRO A 239 19.947 3.116 -2.957 1.00 20.45 C ANISOU 325 CD PRO A 239 2336 3165 2269 -591 -223 -292 C ATOM 326 N SER A 240 23.615 1.793 -2.941 1.00 19.79 N ANISOU 326 N SER A 240 2391 2908 2222 -351 5 -340 N ATOM 327 CA SER A 240 25.005 1.422 -3.189 1.00 20.62 C ANISOU 327 CA SER A 240 2514 2990 2331 -241 101 -332 C ATOM 328 C SER A 240 25.968 2.362 -2.469 1.00 20.46 C ANISOU 328 C SER A 240 2367 2986 2420 -183 104 -212 C ATOM 329 O SER A 240 27.010 1.919 -1.965 1.00 23.82 O ANISOU 329 O SER A 240 2779 3361 2910 -102 155 -189 O ATOM 330 CB SER A 240 25.285 1.387 -4.694 1.00 23.47 C ANISOU 330 CB SER A 240 2921 3442 2555 -211 159 -361 C ATOM 331 OG SER A 240 25.006 2.623 -5.331 1.00 23.72 O ANISOU 331 OG SER A 240 2866 3602 2545 -240 119 -280 O ATOM 332 N CYS A 241 25.623 3.644 -2.368 1.00 18.95 N ANISOU 332 N CYS A 241 2086 2857 2256 -227 43 -133 N ATOM 333 CA CYS A 241 26.463 4.570 -1.609 1.00 17.77 C ANISOU 333 CA CYS A 241 1836 2704 2213 -202 26 -32 C ATOM 334 C CYS A 241 26.317 4.371 -0.102 1.00 16.36 C ANISOU 334 C CYS A 241 1667 2428 2122 -215 -26 -39 C ATOM 335 O CYS A 241 27.264 4.648 0.654 1.00 20.02 O ANISOU 335 O CYS A 241 2074 2869 2665 -184 -39 19 O ATOM 336 CB CYS A 241 26.104 6.017 -1.952 1.00 19.10 C ANISOU 336 CB CYS A 241 1936 2938 2383 -245 -18 50 C ATOM 337 SG CYS A 241 26.593 6.542 -3.628 1.00 21.25 S ANISOU 337 SG CYS A 241 2175 3338 2560 -218 51 110 S ATOM 338 N LEU A 242 25.140 3.924 0.350 1.00 17.09 N ANISOU 338 N LEU A 242 1824 2474 2197 -266 -61 -100 N ATOM 339 CA LEU A 242 24.904 3.587 1.753 1.00 20.55 C ANISOU 339 CA LEU A 242 2290 2822 2695 -272 -94 -108 C ATOM 340 C LEU A 242 25.508 2.247 2.131 1.00 18.20 C ANISOU 340 C LEU A 242 2057 2445 2411 -219 -47 -148 C ATOM 341 O LEU A 242 25.607 1.937 3.333 1.00 20.12 O ANISOU 341 O LEU A 242 2323 2618 2704 -204 -68 -134 O ATOM 342 CB LEU A 242 23.390 3.568 2.050 1.00 17.89 C ANISOU 342 CB LEU A 242 1984 2475 2338 -344 -129 -142 C ATOM 343 CG LEU A 242 22.747 4.944 2.019 1.00 19.22 C ANISOU 343 CG LEU A 242 2090 2701 2513 -370 -172 -85 C ATOM 344 CD1 LEU A 242 21.240 4.787 1.838 1.00 19.37 C ANISOU 344 CD1 LEU A 242 2110 2752 2497 -430 -191 -110 C ATOM 345 CD2 LEU A 242 23.044 5.723 3.299 1.00 22.45 C ANISOU 345 CD2 LEU A 242 2490 3054 2986 -349 -204 -38 C ATOM 346 N LYS A 243 25.967 1.491 1.142 1.00 18.80 N ANISOU 346 N LYS A 243 2173 2529 2440 -176 22 -190 N ATOM 347 CA LYS A 243 26.565 0.170 1.331 1.00 20.61 C ANISOU 347 CA LYS A 243 2482 2668 2680 -102 88 -228 C ATOM 348 C LYS A 243 25.539 -0.817 1.868 1.00 21.56 C ANISOU 348 C LYS A 243 2717 2682 2794 -161 79 -299 C ATOM 349 O LYS A 243 25.876 -1.704 2.658 1.00 24.22 O ANISOU 349 O LYS A 243 3113 2917 3173 -111 106 -297 O ATOM 350 CB LYS A 243 27.802 0.211 2.247 1.00 21.92 C ANISOU 350 CB LYS A 243 2580 2819 2931 -11 88 -143 C ATOM 351 CG LYS A 243 28.805 1.336 1.951 1.00 25.70 C ANISOU 351 CG LYS A 243 2917 3405 3444 15 76 -49 C ATOM 352 CD LYS A 243 29.363 1.255 0.559 1.00 24.88 C ANISOU 352 CD LYS A 243 2795 3372 3288 68 168 -53 C ATOM 353 CE LYS A 243 30.451 2.354 0.278 1.00 28.20 C ANISOU 353 CE LYS A 243 3056 3901 3759 88 169 64 C ATOM 354 NZ LYS A 243 31.596 2.286 1.189 1.00 26.92 N ANISOU 354 NZ LYS A 243 2795 3738 3695 148 149 151 N ATOM 355 N PHE A 244 24.286 -0.653 1.466 1.00 20.39 N ANISOU 355 N PHE A 244 2588 2561 2597 -270 40 -347 N ATOM 356 CA PHE A 244 23.227 -1.599 1.837 1.00 19.18 C ANISOU 356 CA PHE A 244 2528 2318 2441 -355 32 -410 C ATOM 357 C PHE A 244 23.134 -2.749 0.840 1.00 23.45 C ANISOU 357 C PHE A 244 3200 2796 2913 -377 81 -517 C ATOM 358 O PHE A 244 23.164 -2.549 -0.376 1.00 24.93 O ANISOU 358 O PHE A 244 3397 3060 3015 -387 87 -562 O ATOM 359 CB PHE A 244 21.868 -0.886 1.902 1.00 20.45 C ANISOU 359 CB PHE A 244 2626 2553 2592 -468 -38 -397 C ATOM 360 CG PHE A 244 21.713 0.075 3.060 1.00 19.73 C ANISOU 360 CG PHE A 244 2452 2483 2562 -450 -74 -311 C ATOM 361 CD1 PHE A 244 22.676 0.227 4.033 1.00 19.06 C ANISOU 361 CD1 PHE A 244 2360 2353 2529 -366 -66 -258 C ATOM 362 CD2 PHE A 244 20.556 0.805 3.156 1.00 20.10 C ANISOU 362 CD2 PHE A 244 2434 2598 2607 -518 -118 -285 C ATOM 363 CE1 PHE A 244 22.496 1.121 5.100 1.00 19.05 C ANISOU 363 CE1 PHE A 244 2313 2364 2561 -359 -105 -197 C ATOM 364 CE2 PHE A 244 20.348 1.659 4.198 1.00 17.52 C ANISOU 364 CE2 PHE A 244 2059 2277 2322 -492 -135 -219 C ATOM 365 CZ PHE A 244 21.304 1.836 5.169 1.00 18.43 C ANISOU 365 CZ PHE A 244 2193 2337 2474 -418 -131 -183 C ATOM 366 N SER A 245 22.965 -3.957 1.369 1.00 24.25 N ANISOU 366 N SER A 245 3419 2750 3044 -391 116 -561 N ATOM 367 CA SER A 245 22.687 -5.115 0.535 1.00 25.71 C ANISOU 367 CA SER A 245 3763 2839 3166 -441 154 -680 C ATOM 368 C SER A 245 21.335 -4.969 -0.162 1.00 27.10 C ANISOU 368 C SER A 245 3936 3085 3277 -616 73 -742 C ATOM 369 O SER A 245 20.487 -4.181 0.270 1.00 25.13 O ANISOU 369 O SER A 245 3562 2928 3057 -692 2 -680 O ATOM 370 CB SER A 245 22.681 -6.365 1.409 1.00 31.65 C ANISOU 370 CB SER A 245 4642 3400 3983 -434 203 -694 C ATOM 371 OG SER A 245 21.529 -6.346 2.223 1.00 28.68 O ANISOU 371 OG SER A 245 4231 3011 3654 -564 145 -665 O ATOM 372 N PRO A 246 21.091 -5.731 -1.238 1.00 28.00 N ANISOU 372 N PRO A 246 4186 3158 3296 -681 81 -864 N ATOM 373 CA PRO A 246 19.756 -5.677 -1.844 1.00 28.40 C ANISOU 373 CA PRO A 246 4224 3282 3284 -869 -20 -918 C ATOM 374 C PRO A 246 18.660 -6.057 -0.859 1.00 30.09 C ANISOU 374 C PRO A 246 4406 3436 3592 -1004 -65 -888 C ATOM 375 O PRO A 246 17.604 -5.410 -0.837 1.00 30.05 O ANISOU 375 O PRO A 246 4268 3558 3592 -1113 -151 -841 O ATOM 376 CB PRO A 246 19.864 -6.667 -3.012 1.00 32.72 C ANISOU 376 CB PRO A 246 4972 3749 3710 -910 4 -1072 C ATOM 377 CG PRO A 246 21.330 -6.657 -3.359 1.00 35.04 C ANISOU 377 CG PRO A 246 5320 4020 3973 -704 122 -1070 C ATOM 378 CD PRO A 246 22.016 -6.565 -2.028 1.00 29.08 C ANISOU 378 CD PRO A 246 4488 3200 3363 -583 176 -956 C ATOM 379 N GLU A 247 18.907 -7.047 0.006 1.00 30.12 N ANISOU 379 N GLU A 247 4517 3255 3674 -985 1 -892 N ATOM 380 CA GLU A 247 17.868 -7.480 0.943 1.00 32.04 C ANISOU 380 CA GLU A 247 4737 3434 4003 -1118 -25 -852 C ATOM 381 C GLU A 247 17.564 -6.405 1.979 1.00 26.29 C ANISOU 381 C GLU A 247 3821 2822 3344 -1076 -44 -713 C ATOM 382 O GLU A 247 16.398 -6.153 2.296 1.00 28.72 O ANISOU 382 O GLU A 247 4026 3201 3685 -1199 -95 -668 O ATOM 383 CB GLU A 247 18.282 -8.777 1.643 1.00 33.88 C ANISOU 383 CB GLU A 247 5142 3432 4300 -1090 62 -872 C ATOM 384 CG GLU A 247 18.421 -9.988 0.730 1.00 40.47 C ANISOU 384 CG GLU A 247 6202 4102 5073 -1147 92 -1021 C ATOM 385 CD GLU A 247 19.730 -10.028 -0.060 1.00 48.02 C ANISOU 385 CD GLU A 247 7254 5039 5952 -962 168 -1082 C ATOM 386 OE1 GLU A 247 20.627 -9.166 0.152 1.00 36.30 O ANISOU 386 OE1 GLU A 247 5650 3664 4478 -791 198 -995 O ATOM 387 OE2 GLU A 247 19.854 -10.942 -0.918 1.00 50.45 O ANISOU 387 OE2 GLU A 247 7765 5219 6186 -993 202 -1218 O ATOM 388 N LEU A 248 18.602 -5.774 2.530 1.00 24.33 N ANISOU 388 N LEU A 248 3530 2593 3120 -903 -2 -643 N ATOM 389 CA LEU A 248 18.383 -4.710 3.498 1.00 20.92 C ANISOU 389 CA LEU A 248 2954 2257 2737 -859 -21 -529 C ATOM 390 C LEU A 248 17.670 -3.541 2.833 1.00 24.72 C ANISOU 390 C LEU A 248 3293 2922 3179 -908 -93 -507 C ATOM 391 O LEU A 248 16.802 -2.897 3.436 1.00 22.24 O ANISOU 391 O LEU A 248 2867 2682 2900 -944 -118 -434 O ATOM 392 CB LEU A 248 19.735 -4.282 4.081 1.00 21.10 C ANISOU 392 CB LEU A 248 2970 2264 2781 -683 18 -474 C ATOM 393 CG LEU A 248 19.698 -3.069 5.012 1.00 25.30 C ANISOU 393 CG LEU A 248 3383 2886 3344 -630 -9 -375 C ATOM 394 CD1 LEU A 248 18.851 -3.334 6.198 1.00 26.32 C ANISOU 394 CD1 LEU A 248 3514 2969 3517 -679 5 -322 C ATOM 395 CD2 LEU A 248 21.108 -2.700 5.504 1.00 27.16 C ANISOU 395 CD2 LEU A 248 3613 3109 3596 -483 6 -328 C ATOM 396 N THR A 249 18.048 -3.238 1.590 1.00 24.24 N ANISOU 396 N THR A 249 3236 2935 3038 -894 -118 -561 N ATOM 397 CA THR A 249 17.407 -2.160 0.848 1.00 24.05 C ANISOU 397 CA THR A 249 3087 3085 2966 -931 -189 -530 C ATOM 398 C THR A 249 15.903 -2.389 0.727 1.00 23.71 C ANISOU 398 C THR A 249 2981 3101 2927 -1095 -255 -531 C ATOM 399 O THR A 249 15.107 -1.458 0.903 1.00 25.46 O ANISOU 399 O THR A 249 3057 3446 3169 -1106 -294 -447 O ATOM 400 CB THR A 249 18.056 -2.041 -0.531 1.00 26.98 C ANISOU 400 CB THR A 249 3505 3515 3232 -899 -195 -592 C ATOM 401 OG1 THR A 249 19.439 -1.689 -0.368 1.00 25.51 O ANISOU 401 OG1 THR A 249 3332 3300 3061 -746 -130 -561 O ATOM 402 CG2 THR A 249 17.370 -0.980 -1.374 1.00 25.97 C ANISOU 402 CG2 THR A 249 3258 3569 3042 -936 -273 -550 C ATOM 403 N VAL A 250 15.494 -3.620 0.426 1.00 25.95 N ANISOU 403 N VAL A 250 3371 3294 3195 -1224 -266 -619 N ATOM 404 CA VAL A 250 14.070 -3.899 0.308 1.00 30.38 C ANISOU 404 CA VAL A 250 3856 3918 3769 -1406 -340 -613 C ATOM 405 C VAL A 250 13.370 -3.658 1.639 1.00 28.98 C ANISOU 405 C VAL A 250 3566 3741 3703 -1409 -305 -499 C ATOM 406 O VAL A 250 12.266 -3.094 1.684 1.00 30.30 O ANISOU 406 O VAL A 250 3572 4043 3896 -1462 -351 -419 O ATOM 407 CB VAL A 250 13.860 -5.335 -0.205 1.00 29.12 C ANISOU 407 CB VAL A 250 3856 3626 3583 -1530 -353 -727 C ATOM 408 CG1 VAL A 250 12.402 -5.727 -0.075 1.00 34.14 C ANISOU 408 CG1 VAL A 250 4393 4303 4277 -1655 -412 -673 C ATOM 409 CG2 VAL A 250 14.315 -5.430 -1.661 1.00 29.70 C ANISOU 409 CG2 VAL A 250 4030 3738 3518 -1528 -395 -836 C ATOM 410 N ARG A 251 13.998 -4.071 2.746 1.00 27.33 N ANISOU 410 N ARG A 251 3438 3388 3557 -1326 -216 -476 N ATOM 411 CA ARG A 251 13.361 -3.903 4.045 1.00 22.42 C ANISOU 411 CA ARG A 251 2736 2763 3020 -1322 -169 -370 C ATOM 412 C ARG A 251 13.265 -2.431 4.433 1.00 26.24 C ANISOU 412 C ARG A 251 3079 3382 3507 -1200 -168 -274 C ATOM 413 O ARG A 251 12.223 -1.997 4.935 1.00 28.74 O ANISOU 413 O ARG A 251 3267 3786 3866 -1231 -161 -188 O ATOM 414 CB ARG A 251 14.104 -4.676 5.139 1.00 28.66 C ANISOU 414 CB ARG A 251 3661 3374 3856 -1251 -80 -360 C ATOM 415 CG ARG A 251 14.154 -6.172 4.992 1.00 41.67 C ANISOU 415 CG ARG A 251 5466 4847 5520 -1357 -57 -436 C ATOM 416 CD ARG A 251 12.866 -6.835 5.462 1.00 52.65 C ANISOU 416 CD ARG A 251 6813 6213 6977 -1535 -53 -391 C ATOM 417 NE ARG A 251 12.421 -6.413 6.794 1.00 59.11 N ANISOU 417 NE ARG A 251 7540 7065 7853 -1482 13 -259 N ATOM 418 CZ ARG A 251 11.515 -5.459 7.035 1.00 59.79 C ANISOU 418 CZ ARG A 251 7442 7320 7953 -1486 1 -171 C ATOM 419 NH1 ARG A 251 10.952 -4.776 6.038 1.00 59.71 N ANISOU 419 NH1 ARG A 251 7303 7472 7914 -1539 -85 -187 N ATOM 420 NH2 ARG A 251 11.174 -5.178 8.286 1.00 59.54 N ANISOU 420 NH2 ARG A 251 7364 7299 7961 -1423 82 -61 N ATOM 421 N VAL A 252 14.319 -1.631 4.190 1.00 23.44 N ANISOU 421 N VAL A 252 2747 3047 3115 -1061 -168 -283 N ATOM 422 CA VAL A 252 14.232 -0.251 4.670 1.00 22.21 C ANISOU 422 CA VAL A 252 2487 2982 2970 -953 -161 -195 C ATOM 423 C VAL A 252 13.267 0.564 3.801 1.00 25.02 C ANISOU 423 C VAL A 252 2697 3504 3303 -995 -224 -156 C ATOM 424 O VAL A 252 12.680 1.542 4.280 1.00 24.95 O ANISOU 424 O VAL A 252 2586 3573 3323 -933 -207 -68 O ATOM 425 CB VAL A 252 15.615 0.432 4.771 1.00 21.49 C ANISOU 425 CB VAL A 252 2451 2856 2859 -812 -148 -201 C ATOM 426 CG1 VAL A 252 16.556 -0.367 5.690 1.00 21.41 C ANISOU 426 CG1 VAL A 252 2562 2701 2873 -759 -97 -219 C ATOM 427 CG2 VAL A 252 16.237 0.634 3.411 1.00 23.53 C ANISOU 427 CG2 VAL A 252 2717 3166 3056 -807 -191 -252 C ATOM 428 N LYS A 253 13.076 0.191 2.532 1.00 25.84 N ANISOU 428 N LYS A 253 2799 3668 3349 -1091 -295 -217 N ATOM 429 CA LYS A 253 12.120 0.925 1.697 1.00 29.08 C ANISOU 429 CA LYS A 253 3064 4256 3730 -1132 -370 -165 C ATOM 430 C LYS A 253 10.689 0.756 2.179 1.00 27.57 C ANISOU 430 C LYS A 253 2735 4137 3602 -1223 -377 -89 C ATOM 431 O LYS A 253 9.815 1.525 1.766 1.00 30.16 O ANISOU 431 O LYS A 253 2930 4601 3930 -1189 -414 -9 O ATOM 432 CB LYS A 253 12.212 0.489 0.222 1.00 27.98 C ANISOU 432 CB LYS A 253 2968 4174 3490 -1225 -456 -251 C ATOM 433 CG LYS A 253 13.501 0.968 -0.486 1.00 27.94 C ANISOU 433 CG LYS A 253 3052 4155 3410 -1112 -442 -291 C ATOM 434 CD LYS A 253 13.605 0.430 -1.928 1.00 27.84 C ANISOU 434 CD LYS A 253 3113 4194 3273 -1196 -511 -387 C ATOM 435 CE LYS A 253 14.707 1.195 -2.706 1.00 31.17 C ANISOU 435 CE LYS A 253 3574 4653 3617 -1070 -488 -383 C ATOM 436 NZ LYS A 253 14.917 0.693 -4.103 1.00 28.01 N ANISOU 436 NZ LYS A 253 3270 4303 3070 -1128 -533 -478 N ATOM 437 N ALA A 254 10.414 -0.260 2.994 1.00 27.14 N ANISOU 437 N ALA A 254 2727 3978 3606 -1304 -329 -103 N ATOM 438 CA ALA A 254 9.085 -0.498 3.525 1.00 28.70 C ANISOU 438 CA ALA A 254 2806 4224 3876 -1360 -310 -19 C ATOM 439 C ALA A 254 8.920 -0.012 4.953 1.00 25.38 C ANISOU 439 C ALA A 254 2328 3795 3520 -1285 -203 80 C ATOM 440 O ALA A 254 7.874 -0.253 5.555 1.00 28.42 O ANISOU 440 O ALA A 254 2612 4216 3969 -1329 -159 161 O ATOM 441 CB ALA A 254 8.754 -1.998 3.455 1.00 29.35 C ANISOU 441 CB ALA A 254 2974 4195 3983 -1509 -323 -84 C ATOM 442 N LEU A 255 9.929 0.641 5.518 1.00 24.77 N ANISOU 442 N LEU A 255 2350 3640 3423 -1119 -147 72 N ATOM 443 CA LEU A 255 9.929 1.109 6.896 1.00 24.43 C ANISOU 443 CA LEU A 255 2322 3550 3411 -997 -41 142 C ATOM 444 C LEU A 255 10.147 2.622 6.929 1.00 21.14 C ANISOU 444 C LEU A 255 1869 3192 2972 -833 -32 186 C ATOM 445 O LEU A 255 10.589 3.223 5.955 1.00 22.42 O ANISOU 445 O LEU A 255 2022 3400 3097 -806 -100 159 O ATOM 446 CB LEU A 255 11.057 0.411 7.711 1.00 25.03 C ANISOU 446 CB LEU A 255 2585 3450 3476 -958 6 84 C ATOM 447 CG LEU A 255 10.895 -1.090 7.946 1.00 26.12 C ANISOU 447 CG LEU A 255 2795 3484 3646 -1093 27 56 C ATOM 448 CD1 LEU A 255 12.148 -1.576 8.683 1.00 25.66 C ANISOU 448 CD1 LEU A 255 2916 3267 3569 -1009 68 16 C ATOM 449 CD2 LEU A 255 9.660 -1.289 8.773 1.00 31.49 C ANISOU 449 CD2 LEU A 255 3372 4211 4383 -1147 99 159 C ATOM 450 N ARG A 256 9.825 3.242 8.066 1.00 23.23 N ANISOU 450 N ARG A 256 2125 3446 3254 -721 62 257 N ATOM 451 CA ARG A 256 10.142 4.665 8.277 1.00 19.14 C ANISOU 451 CA ARG A 256 1623 2935 2714 -560 83 285 C ATOM 452 C ARG A 256 11.633 4.806 8.595 1.00 20.48 C ANISOU 452 C ARG A 256 1966 2973 2843 -501 65 206 C ATOM 453 O ARG A 256 12.055 4.980 9.739 1.00 22.13 O ANISOU 453 O ARG A 256 2279 3094 3033 -424 121 204 O ATOM 454 CB ARG A 256 9.253 5.255 9.376 1.00 23.68 C ANISOU 454 CB ARG A 256 2151 3536 3309 -455 198 377 C ATOM 455 CG ARG A 256 9.314 6.804 9.454 1.00 20.90 C ANISOU 455 CG ARG A 256 1808 3191 2940 -290 225 412 C ATOM 456 CD ARG A 256 8.552 7.383 10.664 1.00 21.48 C ANISOU 456 CD ARG A 256 1883 3262 3015 -158 364 487 C ATOM 457 NE ARG A 256 8.616 8.851 10.594 1.00 22.37 N ANISOU 457 NE ARG A 256 2025 3360 3115 -4 385 510 N ATOM 458 CZ ARG A 256 9.663 9.568 10.968 1.00 21.14 C ANISOU 458 CZ ARG A 256 2044 3075 2913 67 370 441 C ATOM 459 NH1 ARG A 256 10.750 8.973 11.466 1.00 22.18 N ANISOU 459 NH1 ARG A 256 2321 3103 3004 9 329 354 N ATOM 460 NH2 ARG A 256 9.650 10.885 10.836 1.00 22.12 N ANISOU 460 NH2 ARG A 256 2199 3170 3035 191 390 466 N ATOM 461 N TRP A 257 12.437 4.752 7.545 1.00 17.24 N ANISOU 461 N TRP A 257 1577 2561 2411 -538 -16 147 N ATOM 462 CA TRP A 257 13.881 4.695 7.707 1.00 16.22 C ANISOU 462 CA TRP A 257 1579 2328 2257 -504 -39 82 C ATOM 463 C TRP A 257 14.461 6.051 8.073 1.00 18.00 C ANISOU 463 C TRP A 257 1845 2523 2470 -390 -37 101 C ATOM 464 O TRP A 257 14.007 7.090 7.578 1.00 18.52 O ANISOU 464 O TRP A 257 1844 2651 2541 -343 -43 147 O ATOM 465 CB TRP A 257 14.510 4.172 6.419 1.00 18.98 C ANISOU 465 CB TRP A 257 1931 2695 2586 -573 -107 22 C ATOM 466 CG TRP A 257 16.019 4.088 6.447 1.00 16.78 C ANISOU 466 CG TRP A 257 1754 2332 2291 -531 -123 -28 C ATOM 467 CD1 TRP A 257 16.765 3.079 6.981 1.00 18.64 C ANISOU 467 CD1 TRP A 257 2082 2470 2529 -538 -107 -69 C ATOM 468 CD2 TRP A 257 16.944 5.020 5.896 1.00 17.45 C ANISOU 468 CD2 TRP A 257 1840 2428 2362 -476 -157 -26 C ATOM 469 NE1 TRP A 257 18.103 3.337 6.811 1.00 16.12 N ANISOU 469 NE1 TRP A 257 1807 2117 2202 -484 -131 -88 N ATOM 470 CE2 TRP A 257 18.243 4.516 6.139 1.00 14.88 C ANISOU 470 CE2 TRP A 257 1593 2026 2037 -456 -161 -64 C ATOM 471 CE3 TRP A 257 16.805 6.258 5.220 1.00 17.84 C ANISOU 471 CE3 TRP A 257 1828 2546 2406 -440 -180 19 C ATOM 472 CZ2 TRP A 257 19.397 5.180 5.746 1.00 14.52 C ANISOU 472 CZ2 TRP A 257 1548 1979 1990 -414 -188 -58 C ATOM 473 CZ3 TRP A 257 17.959 6.920 4.803 1.00 17.33 C ANISOU 473 CZ3 TRP A 257 1785 2464 2337 -404 -203 21 C ATOM 474 CH2 TRP A 257 19.245 6.396 5.088 1.00 14.93 C ANISOU 474 CH2 TRP A 257 1542 2091 2038 -397 -207 -17 C ATOM 475 N GLN A 258 15.487 6.026 8.948 1.00 15.39 N ANISOU 475 N GLN A 258 1633 2092 2124 -349 -35 69 N ATOM 476 CA GLN A 258 16.220 7.214 9.380 1.00 14.40 C ANISOU 476 CA GLN A 258 1573 1914 1984 -271 -52 69 C ATOM 477 C GLN A 258 17.674 7.093 8.966 1.00 16.14 C ANISOU 477 C GLN A 258 1833 2096 2204 -291 -118 29 C ATOM 478 O GLN A 258 18.263 5.997 9.006 1.00 16.87 O ANISOU 478 O GLN A 258 1952 2162 2295 -326 -129 -2 O ATOM 479 CB GLN A 258 16.171 7.361 10.898 1.00 15.31 C ANISOU 479 CB GLN A 258 1794 1957 2068 -211 -5 71 C ATOM 480 CG GLN A 258 14.730 7.521 11.463 1.00 18.23 C ANISOU 480 CG GLN A 258 2125 2366 2435 -167 90 125 C ATOM 481 CD GLN A 258 14.740 7.437 12.953 1.00 18.34 C ANISOU 481 CD GLN A 258 2261 2312 2394 -110 148 123 C ATOM 482 OE1 GLN A 258 15.155 6.416 13.531 1.00 20.39 O ANISOU 482 OE1 GLN A 258 2579 2535 2634 -146 145 108 O ATOM 483 NE2 GLN A 258 14.293 8.513 13.609 1.00 19.51 N ANISOU 483 NE2 GLN A 258 2466 2437 2510 -10 206 139 N ATOM 484 N CYS A 259 18.245 8.233 8.599 1.00 15.26 N ANISOU 484 N CYS A 259 1722 1976 2100 -264 -154 41 N ATOM 485 CA CYS A 259 19.669 8.283 8.285 1.00 14.75 C ANISOU 485 CA CYS A 259 1675 1885 2045 -282 -211 23 C ATOM 486 C CYS A 259 20.506 8.032 9.534 1.00 15.84 C ANISOU 486 C CYS A 259 1903 1947 2168 -268 -237 1 C ATOM 487 O CYS A 259 20.009 7.982 10.661 1.00 15.88 O ANISOU 487 O CYS A 259 1981 1912 2142 -238 -210 -4 O ATOM 488 CB CYS A 259 20.035 9.636 7.660 1.00 14.86 C ANISOU 488 CB CYS A 259 1667 1901 2078 -270 -239 56 C ATOM 489 SG CYS A 259 20.032 11.052 8.789 1.00 16.55 S ANISOU 489 SG CYS A 259 1987 2011 2290 -223 -246 62 S ATOM 490 N ILE A 260 21.826 7.898 9.314 1.00 16.94 N ANISOU 490 N ILE A 260 2032 2078 2325 -285 -291 -2 N ATOM 491 CA ILE A 260 22.755 7.599 10.416 1.00 17.62 C ANISOU 491 CA ILE A 260 2182 2115 2397 -275 -339 -10 C ATOM 492 C ILE A 260 22.597 8.614 11.541 1.00 16.55 C ANISOU 492 C ILE A 260 2145 1919 2224 -260 -367 -18 C ATOM 493 O ILE A 260 22.519 8.251 12.721 1.00 19.50 O ANISOU 493 O ILE A 260 2608 2257 2546 -236 -370 -31 O ATOM 494 CB ILE A 260 24.201 7.580 9.891 1.00 19.95 C ANISOU 494 CB ILE A 260 2415 2433 2732 -293 -396 10 C ATOM 495 CG1 ILE A 260 24.406 6.392 8.946 1.00 20.73 C ANISOU 495 CG1 ILE A 260 2453 2574 2847 -284 -350 6 C ATOM 496 CG2 ILE A 260 25.191 7.553 11.061 1.00 20.35 C ANISOU 496 CG2 ILE A 260 2514 2450 2769 -290 -474 18 C ATOM 497 CD1 ILE A 260 25.720 6.513 8.074 1.00 23.61 C ANISOU 497 CD1 ILE A 260 2728 2986 3255 -286 -371 39 C ATOM 498 N GLU A 261 22.587 9.915 11.197 1.00 15.62 N ANISOU 498 N GLU A 261 2029 1780 2125 -270 -386 -12 N ATOM 499 CA GLU A 261 22.546 10.932 12.241 1.00 17.29 C ANISOU 499 CA GLU A 261 2365 1909 2296 -258 -415 -35 C ATOM 500 C GLU A 261 21.190 11.036 12.892 1.00 17.80 C ANISOU 500 C GLU A 261 2503 1951 2309 -189 -325 -47 C ATOM 501 O GLU A 261 21.111 11.231 14.100 1.00 19.75 O ANISOU 501 O GLU A 261 2879 2140 2484 -160 -327 -77 O ATOM 502 CB GLU A 261 22.959 12.303 11.724 1.00 18.89 C ANISOU 502 CB GLU A 261 2572 2066 2541 -292 -456 -23 C ATOM 503 CG GLU A 261 24.373 12.334 11.129 1.00 24.53 C ANISOU 503 CG GLU A 261 3199 2809 3314 -368 -540 5 C ATOM 504 CD GLU A 261 25.439 11.789 12.048 1.00 29.22 C ANISOU 504 CD GLU A 261 3815 3403 3885 -401 -631 -8 C ATOM 505 OE1 GLU A 261 25.370 12.005 13.276 1.00 29.68 O ANISOU 505 OE1 GLU A 261 4002 3400 3874 -396 -672 -50 O ATOM 506 OE2 GLU A 261 26.365 11.154 11.530 1.00 27.85 O ANISOU 506 OE2 GLU A 261 3528 3297 3757 -424 -660 28 O ATOM 507 N CYS A 262 20.105 10.871 12.133 1.00 17.59 N ANISOU 507 N CYS A 262 2393 1981 2309 -161 -243 -17 N ATOM 508 CA CYS A 262 18.773 10.986 12.719 1.00 17.57 C ANISOU 508 CA CYS A 262 2427 1976 2271 -90 -146 -6 C ATOM 509 C CYS A 262 18.333 9.750 13.507 1.00 17.14 C ANISOU 509 C CYS A 262 2389 1947 2176 -83 -96 -6 C ATOM 510 O CYS A 262 17.406 9.870 14.311 1.00 19.07 O ANISOU 510 O CYS A 262 2688 2181 2376 -19 -11 5 O ATOM 511 CB CYS A 262 17.711 11.225 11.641 1.00 16.82 C ANISOU 511 CB CYS A 262 2210 1956 2225 -68 -86 44 C ATOM 512 SG CYS A 262 17.836 12.869 10.821 1.00 18.24 S ANISOU 512 SG CYS A 262 2391 2094 2446 -39 -106 74 S ATOM 513 N LYS A 263 18.995 8.612 13.326 1.00 14.61 N ANISOU 513 N LYS A 263 2031 1649 1869 -136 -137 -11 N ATOM 514 CA LYS A 263 18.538 7.344 13.901 1.00 17.02 C ANISOU 514 CA LYS A 263 2346 1967 2152 -139 -83 3 C ATOM 515 C LYS A 263 18.294 7.468 15.400 1.00 17.01 C ANISOU 515 C LYS A 263 2481 1919 2064 -80 -44 2 C ATOM 516 O LYS A 263 19.172 7.906 16.155 1.00 17.37 O ANISOU 516 O LYS A 263 2635 1913 2050 -67 -114 -28 O ATOM 517 CB LYS A 263 19.581 6.245 13.660 1.00 16.70 C ANISOU 517 CB LYS A 263 2290 1923 2133 -183 -140 -5 C ATOM 518 CG LYS A 263 18.996 4.813 13.876 1.00 18.89 C ANISOU 518 CG LYS A 263 2563 2200 2413 -203 -74 16 C ATOM 519 CD LYS A 263 18.433 4.263 12.603 1.00 19.71 C ANISOU 519 CD LYS A 263 2558 2351 2579 -264 -51 13 C ATOM 520 CE LYS A 263 19.498 3.907 11.579 1.00 17.37 C ANISOU 520 CE LYS A 263 2225 2058 2317 -291 -110 -16 C ATOM 521 NZ LYS A 263 18.738 3.651 10.299 1.00 16.33 N ANISOU 521 NZ LYS A 263 2004 1985 2217 -351 -90 -29 N ATOM 522 N THR A 264 17.095 7.088 15.835 1.00 17.58 N ANISOU 522 N THR A 264 2545 2016 2119 -50 67 39 N ATOM 523 CA THR A 264 16.766 7.045 17.251 1.00 17.01 C ANISOU 523 CA THR A 264 2604 1911 1949 14 131 50 C ATOM 524 C THR A 264 16.564 5.592 17.658 1.00 19.84 C ANISOU 524 C THR A 264 2954 2279 2303 -18 177 94 C ATOM 525 O THR A 264 16.227 4.755 16.828 1.00 21.59 O ANISOU 525 O THR A 264 3063 2534 2608 -85 192 117 O ATOM 526 CB THR A 264 15.489 7.834 17.570 1.00 22.35 C ANISOU 526 CB THR A 264 3283 2607 2603 97 255 77 C ATOM 527 OG1 THR A 264 14.467 7.469 16.638 1.00 25.21 O ANISOU 527 OG1 THR A 264 3470 3050 3058 64 316 131 O ATOM 528 CG2 THR A 264 15.723 9.332 17.406 1.00 21.27 C ANISOU 528 CG2 THR A 264 3207 2422 2454 148 222 32 C ATOM 529 N CYS A 265 16.786 5.306 18.930 1.00 17.90 N ANISOU 529 N CYS A 265 2845 1999 1957 27 195 106 N ATOM 530 CA CYS A 265 16.618 3.938 19.421 1.00 17.29 C ANISOU 530 CA CYS A 265 2782 1915 1872 5 247 165 C ATOM 531 C CYS A 265 15.157 3.533 19.331 1.00 21.42 C ANISOU 531 C CYS A 265 3216 2484 2440 -10 391 229 C ATOM 532 O CYS A 265 14.281 4.270 19.780 1.00 22.29 O ANISOU 532 O CYS A 265 3335 2624 2509 57 486 249 O ATOM 533 CB CYS A 265 17.121 3.854 20.865 1.00 21.09 C ANISOU 533 CB CYS A 265 3439 2362 2212 69 237 176 C ATOM 534 SG CYS A 265 16.832 2.302 21.721 1.00 20.58 S ANISOU 534 SG CYS A 265 3428 2279 2113 67 324 273 S ATOM 535 N SER A 266 14.887 2.373 18.723 1.00 20.40 N ANISOU 535 N SER A 266 2997 2356 2399 -100 407 263 N ATOM 536 CA SER A 266 13.497 1.943 18.564 1.00 22.60 C ANISOU 536 CA SER A 266 3163 2686 2736 -147 526 332 C ATOM 537 C SER A 266 12.817 1.658 19.899 1.00 26.02 C ANISOU 537 C SER A 266 3674 3120 3092 -92 661 414 C ATOM 538 O SER A 266 11.586 1.764 19.993 1.00 30.15 O ANISOU 538 O SER A 266 4102 3711 3644 -91 781 482 O ATOM 539 CB SER A 266 13.456 0.712 17.671 1.00 21.58 C ANISOU 539 CB SER A 266 2955 2536 2710 -276 499 336 C ATOM 540 OG SER A 266 13.549 1.099 16.327 1.00 25.85 O ANISOU 540 OG SER A 266 3387 3117 3319 -328 418 278 O ATOM 541 N SER A 267 13.583 1.312 20.935 1.00 22.77 N ANISOU 541 N SER A 267 3427 2649 2578 -40 647 421 N ATOM 542 CA SER A 267 12.998 1.032 22.246 1.00 26.14 C ANISOU 542 CA SER A 267 3948 3079 2904 22 780 506 C ATOM 543 C SER A 267 12.728 2.304 23.047 1.00 32.30 C ANISOU 543 C SER A 267 4823 3893 3558 153 838 483 C ATOM 544 O SER A 267 11.599 2.528 23.498 1.00 36.20 O ANISOU 544 O SER A 267 5282 4440 4031 205 996 551 O ATOM 545 CB SER A 267 13.909 0.093 23.037 1.00 29.22 C ANISOU 545 CB SER A 267 4485 3397 3222 31 739 537 C ATOM 546 OG SER A 267 13.387 -0.097 24.357 1.00 30.39 O ANISOU 546 OG SER A 267 4746 3555 3246 102 869 624 O ATOM 547 N CYS A 268 13.741 3.149 23.254 1.00 24.51 N ANISOU 547 N CYS A 268 3958 2870 2485 209 719 392 N ATOM 548 CA CYS A 268 13.564 4.306 24.126 1.00 26.56 C ANISOU 548 CA CYS A 268 4360 3130 2603 330 770 354 C ATOM 549 C CYS A 268 13.273 5.596 23.377 1.00 28.68 C ANISOU 549 C CYS A 268 4564 3408 2924 363 759 289 C ATOM 550 O CYS A 268 12.902 6.579 24.024 1.00 30.90 O ANISOU 550 O CYS A 268 4960 3677 3103 475 836 262 O ATOM 551 CB CYS A 268 14.790 4.504 25.036 1.00 28.07 C ANISOU 551 CB CYS A 268 4760 3269 2637 366 646 295 C ATOM 552 SG CYS A 268 16.322 5.078 24.239 1.00 25.97 S ANISOU 552 SG CYS A 268 4486 2959 2420 298 404 185 S ATOM 553 N ARG A 269 13.415 5.619 22.048 1.00 25.27 N ANISOU 553 N ARG A 269 3969 2992 2642 279 676 267 N ATOM 554 CA ARG A 269 13.089 6.759 21.194 1.00 26.06 C ANISOU 554 CA ARG A 269 3987 3106 2808 307 667 230 C ATOM 555 C ARG A 269 14.082 7.897 21.342 1.00 28.51 C ANISOU 555 C ARG A 269 4445 3339 3050 342 553 128 C ATOM 556 O ARG A 269 13.868 8.980 20.789 1.00 28.03 O ANISOU 556 O ARG A 269 4360 3264 3028 381 553 98 O ATOM 557 CB ARG A 269 11.671 7.278 21.448 1.00 32.89 C ANISOU 557 CB ARG A 269 4796 4028 3673 408 849 296 C ATOM 558 CG ARG A 269 10.608 6.229 21.235 1.00 44.63 C ANISOU 558 CG ARG A 269 6104 5605 5248 350 957 409 C ATOM 559 CD ARG A 269 10.400 6.018 19.750 1.00 56.38 C ANISOU 559 CD ARG A 269 7379 7149 6894 240 879 417 C ATOM 560 NE ARG A 269 10.073 4.629 19.421 1.00 63.99 N ANISOU 560 NE ARG A 269 8226 8149 7939 105 883 478 N ATOM 561 CZ ARG A 269 9.975 4.150 18.180 1.00 66.84 C ANISOU 561 CZ ARG A 269 8430 8549 8417 -20 801 474 C ATOM 562 NH1 ARG A 269 9.675 2.871 17.987 1.00 67.17 N ANISOU 562 NH1 ARG A 269 8402 8597 8522 -149 809 518 N ATOM 563 NH2 ARG A 269 10.175 4.944 17.131 1.00 67.75 N ANISOU 563 NH2 ARG A 269 8474 8690 8578 -18 712 426 N ATOM 564 N ASP A 270 15.196 7.658 22.023 1.00 28.02 N ANISOU 564 N ASP A 270 4526 3227 2894 319 444 83 N ATOM 565 CA ASP A 270 16.193 8.671 22.310 1.00 28.49 C ANISOU 565 CA ASP A 270 4733 3212 2878 326 319 -11 C ATOM 566 C ASP A 270 17.443 8.474 21.456 1.00 24.49 C ANISOU 566 C ASP A 270 4145 2700 2461 217 141 -40 C ATOM 567 O ASP A 270 17.669 7.419 20.861 1.00 22.87 O ANISOU 567 O ASP A 270 3812 2535 2342 154 116 4 O ATOM 568 CB ASP A 270 16.557 8.603 23.795 1.00 27.57 C ANISOU 568 CB ASP A 270 4840 3064 2571 378 311 -34 C ATOM 569 CG ASP A 270 17.191 9.855 24.297 1.00 31.79 C ANISOU 569 CG ASP A 270 5565 3515 2997 398 220 -140 C ATOM 570 OD1 ASP A 270 17.152 10.848 23.565 1.00 34.00 O ANISOU 570 OD1 ASP A 270 5813 3751 3355 393 201 -185 O ATOM 571 OD2 ASP A 270 17.701 9.843 25.421 1.00 31.65 O ANISOU 571 OD2 ASP A 270 5738 3475 2814 416 166 -175 O ATOM 572 N GLN A 271 18.280 9.516 21.402 1.00 24.99 N ANISOU 572 N GLN A 271 4288 2704 2502 195 23 -115 N ATOM 573 CA GLN A 271 19.650 9.316 20.950 1.00 23.74 C ANISOU 573 CA GLN A 271 4079 2546 2395 99 -149 -133 C ATOM 574 C GLN A 271 20.572 9.320 22.162 1.00 23.97 C ANISOU 574 C GLN A 271 4278 2550 2281 92 -263 -167 C ATOM 575 O GLN A 271 21.157 8.286 22.522 1.00 27.19 O ANISOU 575 O GLN A 271 4668 2998 2666 75 -317 -122 O ATOM 576 CB GLN A 271 20.026 10.386 19.934 1.00 22.90 C ANISOU 576 CB GLN A 271 3910 2407 2384 52 -215 -170 C ATOM 577 CG GLN A 271 19.168 10.302 18.670 1.00 22.05 C ANISOU 577 CG GLN A 271 3626 2347 2406 58 -122 -125 C ATOM 578 CD GLN A 271 19.484 11.380 17.702 1.00 27.99 C ANISOU 578 CD GLN A 271 4329 3066 3238 24 -174 -145 C ATOM 579 OE1 GLN A 271 19.816 12.501 18.100 1.00 26.10 O ANISOU 579 OE1 GLN A 271 4222 2740 2956 28 -219 -197 O ATOM 580 NE2 GLN A 271 19.402 11.065 16.422 1.00 31.29 N ANISOU 580 NE2 GLN A 271 4574 3546 3768 -15 -170 -104 N ATOM 581 N GLY A 272 20.714 10.479 22.804 1.00 23.96 N ANISOU 581 N GLY A 272 4451 2476 2178 106 -305 -245 N ATOM 582 CA GLY A 272 21.283 10.517 24.138 1.00 27.02 C ANISOU 582 CA GLY A 272 5038 2844 2384 112 -392 -284 C ATOM 583 C GLY A 272 22.797 10.464 24.148 1.00 24.67 C ANISOU 583 C GLY A 272 4714 2566 2096 3 -614 -296 C ATOM 584 O GLY A 272 23.465 10.521 23.110 1.00 23.71 O ANISOU 584 O GLY A 272 4424 2461 2124 -75 -692 -278 O ATOM 585 N LYS A 273 23.341 10.335 25.356 1.00 25.83 N ANISOU 585 N LYS A 273 5021 2721 2072 3 -714 -315 N ATOM 586 CA LYS A 273 24.789 10.444 25.524 1.00 30.56 C ANISOU 586 CA LYS A 273 5604 3348 2661 -105 -946 -325 C ATOM 587 C LYS A 273 25.536 9.288 24.868 1.00 31.39 C ANISOU 587 C LYS A 273 5481 3547 2899 -129 -1000 -219 C ATOM 588 O LYS A 273 26.687 9.462 24.457 1.00 37.99 O ANISOU 588 O LYS A 273 6205 4416 3814 -221 -1161 -206 O ATOM 589 CB LYS A 273 25.147 10.535 27.014 1.00 36.39 C ANISOU 589 CB LYS A 273 6575 4090 3163 -97 -1052 -365 C ATOM 590 CG LYS A 273 24.745 9.315 27.831 1.00 39.57 C ANISOU 590 CG LYS A 273 7022 4562 3451 6 -967 -279 C ATOM 591 CD LYS A 273 25.062 9.485 29.320 1.00 49.93 C ANISOU 591 CD LYS A 273 8587 5885 4499 21 -1071 -320 C ATOM 592 CE LYS A 273 24.331 8.442 30.155 1.00 57.02 C ANISOU 592 CE LYS A 273 9567 6830 5267 146 -924 -233 C ATOM 593 NZ LYS A 273 24.593 8.592 31.621 1.00 62.40 N ANISOU 593 NZ LYS A 273 10426 7534 5749 169 -980 -256 N ATOM 594 N ASN A 274 24.883 8.135 24.729 1.00 32.49 N ANISOU 594 N ASN A 274 5549 3724 3073 -48 -859 -140 N ATOM 595 CA ASN A 274 25.456 6.936 24.134 1.00 36.35 C ANISOU 595 CA ASN A 274 5856 4276 3680 -47 -876 -44 C ATOM 596 C ASN A 274 25.051 6.743 22.685 1.00 31.51 C ANISOU 596 C ASN A 274 5059 3657 3255 -60 -772 -30 C ATOM 597 O ASN A 274 25.084 5.614 22.191 1.00 30.09 O ANISOU 597 O ASN A 274 4768 3505 3160 -34 -718 38 O ATOM 598 CB ASN A 274 25.045 5.697 24.932 1.00 38.34 C ANISOU 598 CB ASN A 274 6170 4551 3846 40 -792 38 C ATOM 599 CG ASN A 274 25.757 5.608 26.252 1.00 53.08 C ANISOU 599 CG ASN A 274 8181 6455 5530 55 -929 57 C ATOM 600 OD1 ASN A 274 26.885 6.087 26.381 1.00 59.57 O ANISOU 600 OD1 ASN A 274 8984 7312 6337 -12 -1123 39 O ATOM 601 ND2 ASN A 274 25.107 5.004 27.250 1.00 55.02 N ANISOU 601 ND2 ASN A 274 8570 6703 5633 137 -835 101 N ATOM 602 N ALA A 275 24.675 7.814 21.991 1.00 24.80 N ANISOU 602 N ALA A 275 4191 2767 2466 -98 -745 -93 N ATOM 603 CA ALA A 275 24.150 7.674 20.632 1.00 25.41 C ANISOU 603 CA ALA A 275 4110 2850 2696 -106 -643 -79 C ATOM 604 C ALA A 275 25.153 7.016 19.688 1.00 25.74 C ANISOU 604 C ALA A 275 3974 2942 2862 -143 -708 -29 C ATOM 605 O ALA A 275 24.772 6.231 18.810 1.00 23.97 O ANISOU 605 O ALA A 275 3644 2737 2729 -127 -616 2 O ATOM 606 CB ALA A 275 23.773 9.057 20.090 1.00 26.74 C ANISOU 606 CB ALA A 275 4293 2967 2899 -136 -629 -141 C ATOM 607 N ASP A 276 26.437 7.361 19.808 1.00 23.83 N ANISOU 607 N ASP A 276 3699 2728 2628 -197 -864 -22 N ATOM 608 CA ASP A 276 27.406 6.850 18.842 1.00 23.51 C ANISOU 608 CA ASP A 276 3475 2743 2712 -217 -906 32 C ATOM 609 C ASP A 276 27.564 5.338 18.908 1.00 24.47 C ANISOU 609 C ASP A 276 3552 2895 2850 -143 -858 103 C ATOM 610 O ASP A 276 28.004 4.718 17.925 1.00 25.78 O ANISOU 610 O ASP A 276 3583 3089 3122 -129 -825 140 O ATOM 611 CB ASP A 276 28.771 7.491 19.081 1.00 32.60 C ANISOU 611 CB ASP A 276 4581 3934 3872 -292 -1087 46 C ATOM 612 CG ASP A 276 29.158 8.451 17.983 1.00 45.02 C ANISOU 612 CG ASP A 276 6042 5506 5558 -374 -1109 33 C ATOM 613 OD1 ASP A 276 28.247 8.989 17.331 1.00 50.70 O ANISOU 613 OD1 ASP A 276 6782 6175 6306 -375 -1006 -9 O ATOM 614 OD2 ASP A 276 30.375 8.645 17.769 1.00 55.02 O ANISOU 614 OD2 ASP A 276 7189 6829 6887 -435 -1227 80 O ATOM 615 N ASN A 277 27.220 4.730 20.037 1.00 24.14 N ANISOU 615 N ASN A 277 3635 2839 2699 -88 -843 125 N ATOM 616 CA ASN A 277 27.345 3.288 20.179 1.00 23.40 C ANISOU 616 CA ASN A 277 3522 2749 2618 -14 -791 202 C ATOM 617 C ASN A 277 26.029 2.560 19.954 1.00 23.93 C ANISOU 617 C ASN A 277 3632 2761 2699 15 -618 197 C ATOM 618 O ASN A 277 25.946 1.357 20.204 1.00 26.35 O ANISOU 618 O ASN A 277 3963 3042 3007 68 -559 259 O ATOM 619 CB ASN A 277 27.900 2.940 21.563 1.00 31.10 C ANISOU 619 CB ASN A 277 4599 3751 3467 30 -890 258 C ATOM 620 CG ASN A 277 29.313 3.424 21.746 1.00 40.23 C ANISOU 620 CG ASN A 277 5678 4982 4627 -7 -1081 285 C ATOM 621 OD1 ASN A 277 30.107 3.403 20.808 1.00 40.87 O ANISOU 621 OD1 ASN A 277 5592 5102 4834 -24 -1111 311 O ATOM 622 ND2 ASN A 277 29.635 3.876 22.947 1.00 44.87 N ANISOU 622 ND2 ASN A 277 6382 5597 5070 -24 -1210 281 N ATOM 623 N MET A 278 25.005 3.256 19.485 1.00 19.94 N ANISOU 623 N MET A 278 3132 2235 2208 -23 -538 136 N ATOM 624 CA MET A 278 23.757 2.618 19.101 1.00 18.72 C ANISOU 624 CA MET A 278 2976 2048 2089 -19 -387 138 C ATOM 625 C MET A 278 24.007 1.581 18.010 1.00 21.63 C ANISOU 625 C MET A 278 3242 2406 2572 -25 -346 158 C ATOM 626 O MET A 278 24.627 1.897 16.992 1.00 19.10 O ANISOU 626 O MET A 278 2817 2113 2327 -48 -387 134 O ATOM 627 CB MET A 278 22.795 3.714 18.599 1.00 19.97 C ANISOU 627 CB MET A 278 3116 2210 2261 -55 -334 79 C ATOM 628 CG MET A 278 21.399 3.224 18.301 1.00 20.09 C ANISOU 628 CG MET A 278 3111 2216 2305 -61 -191 90 C ATOM 629 SD MET A 278 20.392 4.530 17.524 1.00 19.26 S ANISOU 629 SD MET A 278 2945 2137 2236 -84 -142 43 S ATOM 630 CE MET A 278 20.356 5.793 18.815 1.00 19.17 C ANISOU 630 CE MET A 278 3091 2099 2094 -30 -166 12 C ATOM 631 N LEU A 279 23.490 0.360 18.201 1.00 18.13 N ANISOU 631 N LEU A 279 2839 1913 2137 -5 -255 199 N ATOM 632 CA LEU A 279 23.568 -0.686 17.175 1.00 17.94 C ANISOU 632 CA LEU A 279 2756 1849 2210 -15 -200 201 C ATOM 633 C LEU A 279 22.561 -0.448 16.061 1.00 19.49 C ANISOU 633 C LEU A 279 2886 2054 2465 -91 -133 142 C ATOM 634 O LEU A 279 21.438 0.012 16.307 1.00 19.07 O ANISOU 634 O LEU A 279 2844 2017 2385 -126 -81 133 O ATOM 635 CB LEU A 279 23.298 -2.081 17.770 1.00 17.61 C ANISOU 635 CB LEU A 279 2802 1725 2163 16 -124 266 C ATOM 636 CG LEU A 279 24.103 -2.464 19.024 1.00 21.60 C ANISOU 636 CG LEU A 279 3391 2223 2591 103 -180 349 C ATOM 637 CD1 LEU A 279 23.660 -3.773 19.588 1.00 19.22 C ANISOU 637 CD1 LEU A 279 3188 1830 2286 130 -85 424 C ATOM 638 CD2 LEU A 279 25.594 -2.519 18.738 1.00 28.00 C ANISOU 638 CD2 LEU A 279 4132 3068 3437 166 -282 374 C ATOM 639 N PHE A 280 22.953 -0.800 14.821 1.00 16.15 N ANISOU 639 N PHE A 280 2391 1629 2115 -109 -130 108 N ATOM 640 CA PHE A 280 22.050 -0.755 13.668 1.00 19.13 C ANISOU 640 CA PHE A 280 2710 2021 2536 -185 -80 55 C ATOM 641 C PHE A 280 21.793 -2.188 13.213 1.00 19.99 C ANISOU 641 C PHE A 280 2863 2046 2688 -212 -11 47 C ATOM 642 O PHE A 280 22.740 -2.931 12.922 1.00 20.43 O ANISOU 642 O PHE A 280 2942 2052 2770 -157 -12 50 O ATOM 643 CB PHE A 280 22.635 0.046 12.494 1.00 16.28 C ANISOU 643 CB PHE A 280 2254 1725 2205 -194 -129 13 C ATOM 644 CG PHE A 280 22.781 1.540 12.722 1.00 16.99 C ANISOU 644 CG PHE A 280 2306 1879 2270 -193 -193 13 C ATOM 645 CD1 PHE A 280 22.294 2.206 13.845 1.00 16.51 C ANISOU 645 CD1 PHE A 280 2304 1816 2153 -182 -201 29 C ATOM 646 CD2 PHE A 280 23.435 2.277 11.759 1.00 19.05 C ANISOU 646 CD2 PHE A 280 2485 2192 2562 -201 -235 -4 C ATOM 647 CE1 PHE A 280 22.453 3.582 13.998 1.00 16.70 C ANISOU 647 CE1 PHE A 280 2320 1871 2155 -182 -256 16 C ATOM 648 CE2 PHE A 280 23.598 3.675 11.901 1.00 21.26 C ANISOU 648 CE2 PHE A 280 2741 2507 2829 -211 -293 -2 C ATOM 649 CZ PHE A 280 23.106 4.323 13.021 1.00 19.55 C ANISOU 649 CZ PHE A 280 2599 2270 2560 -203 -306 1 C ATOM 650 N CYS A 281 20.516 -2.567 13.139 1.00 16.85 N ANISOU 650 N CYS A 281 2474 1627 2301 -297 51 39 N ATOM 651 CA CYS A 281 20.156 -3.919 12.745 1.00 18.35 C ANISOU 651 CA CYS A 281 2723 1717 2533 -353 111 25 C ATOM 652 C CYS A 281 20.566 -4.201 11.311 1.00 18.32 C ANISOU 652 C CYS A 281 2697 1707 2557 -376 98 -54 C ATOM 653 O CYS A 281 20.292 -3.399 10.418 1.00 18.83 O ANISOU 653 O CYS A 281 2676 1865 2614 -418 65 -99 O ATOM 654 CB CYS A 281 18.642 -4.134 12.887 1.00 22.26 C ANISOU 654 CB CYS A 281 3201 2214 3041 -467 167 38 C ATOM 655 SG CYS A 281 18.109 -5.787 12.367 1.00 21.13 S ANISOU 655 SG CYS A 281 3141 1929 2959 -582 228 12 S ATOM 656 N ASP A 282 21.195 -5.358 11.080 1.00 19.95 N ANISOU 656 N ASP A 282 2994 1799 2789 -340 135 -67 N ATOM 657 CA ASP A 282 21.620 -5.683 9.730 1.00 20.75 C ANISOU 657 CA ASP A 282 3102 1885 2899 -345 140 -150 C ATOM 658 C ASP A 282 20.523 -6.276 8.874 1.00 21.05 C ANISOU 658 C ASP A 282 3174 1882 2942 -492 162 -226 C ATOM 659 O ASP A 282 20.774 -6.537 7.693 1.00 24.45 O ANISOU 659 O ASP A 282 3631 2304 3357 -507 164 -310 O ATOM 660 CB ASP A 282 22.823 -6.618 9.784 1.00 24.74 C ANISOU 660 CB ASP A 282 3693 2282 3424 -220 180 -134 C ATOM 661 CG ASP A 282 24.081 -5.894 10.237 1.00 24.78 C ANISOU 661 CG ASP A 282 3620 2371 3424 -86 132 -68 C ATOM 662 OD1 ASP A 282 24.323 -4.770 9.764 1.00 23.51 O ANISOU 662 OD1 ASP A 282 3350 2337 3247 -92 79 -82 O ATOM 663 OD2 ASP A 282 24.842 -6.421 11.077 1.00 23.58 O ANISOU 663 OD2 ASP A 282 3511 2164 3285 21 140 8 O ATOM 664 N SER A 283 19.309 -6.444 9.407 1.00 20.91 N ANISOU 664 N SER A 283 3151 1854 2942 -605 175 -198 N ATOM 665 CA SER A 283 18.124 -6.841 8.666 1.00 22.85 C ANISOU 665 CA SER A 283 3389 2096 3198 -775 171 -255 C ATOM 666 C SER A 283 17.205 -5.666 8.329 1.00 24.06 C ANISOU 666 C SER A 283 3385 2425 3333 -843 117 -246 C ATOM 667 O SER A 283 16.703 -5.579 7.203 1.00 23.79 O ANISOU 667 O SER A 283 3309 2452 3279 -939 73 -313 O ATOM 668 CB SER A 283 17.349 -7.900 9.472 1.00 26.74 C ANISOU 668 CB SER A 283 3961 2461 3739 -867 230 -208 C ATOM 669 OG SER A 283 16.065 -8.123 8.919 1.00 29.45 O ANISOU 669 OG SER A 283 4255 2831 4102 -1056 211 -240 O ATOM 670 N CYS A 284 16.971 -4.748 9.263 1.00 21.17 N ANISOU 670 N CYS A 284 2939 2142 2964 -787 119 -165 N ATOM 671 CA CYS A 284 15.973 -3.706 9.058 1.00 22.81 C ANISOU 671 CA CYS A 284 3006 2497 3165 -836 90 -140 C ATOM 672 C CYS A 284 16.538 -2.304 9.257 1.00 20.48 C ANISOU 672 C CYS A 284 2648 2296 2836 -715 59 -114 C ATOM 673 O CYS A 284 15.810 -1.319 9.088 1.00 22.13 O ANISOU 673 O CYS A 284 2750 2618 3040 -724 41 -87 O ATOM 674 CB CYS A 284 14.781 -3.915 10.013 1.00 23.14 C ANISOU 674 CB CYS A 284 3008 2544 3239 -903 146 -59 C ATOM 675 SG CYS A 284 15.165 -3.552 11.779 1.00 21.20 S ANISOU 675 SG CYS A 284 2820 2266 2968 -763 210 37 S ATOM 676 N ASP A 285 17.820 -2.192 9.621 1.00 17.42 N ANISOU 676 N ASP A 285 2324 1862 2433 -602 50 -114 N ATOM 677 CA ASP A 285 18.517 -0.953 9.938 1.00 16.87 C ANISOU 677 CA ASP A 285 2217 1854 2337 -504 12 -91 C ATOM 678 C ASP A 285 17.897 -0.129 11.073 1.00 17.87 C ANISOU 678 C ASP A 285 2328 2016 2445 -470 31 -31 C ATOM 679 O ASP A 285 18.303 1.024 11.242 1.00 18.36 O ANISOU 679 O ASP A 285 2368 2124 2486 -409 -5 -23 O ATOM 680 CB ASP A 285 18.685 -0.064 8.692 1.00 17.20 C ANISOU 680 CB ASP A 285 2176 1990 2369 -511 -37 -126 C ATOM 681 CG ASP A 285 19.962 0.729 8.715 1.00 17.16 C ANISOU 681 CG ASP A 285 2164 2000 2355 -421 -77 -117 C ATOM 682 OD1 ASP A 285 20.992 0.143 9.072 1.00 19.45 O ANISOU 682 OD1 ASP A 285 2509 2229 2652 -366 -76 -114 O ATOM 683 OD2 ASP A 285 20.032 1.948 8.392 1.00 17.63 O ANISOU 683 OD2 ASP A 285 2161 2131 2407 -404 -112 -104 O ATOM 684 N ARG A 286 16.993 -0.665 11.905 1.00 17.04 N ANISOU 684 N ARG A 286 2247 1883 2345 -503 94 14 N ATOM 685 CA ARG A 286 16.593 0.053 13.120 1.00 18.83 C ANISOU 685 CA ARG A 286 2490 2131 2531 -440 132 70 C ATOM 686 C ARG A 286 17.767 0.183 14.085 1.00 19.46 C ANISOU 686 C ARG A 286 2674 2159 2560 -345 100 80 C ATOM 687 O ARG A 286 18.666 -0.655 14.116 1.00 19.33 O ANISOU 687 O ARG A 286 2716 2077 2552 -328 78 76 O ATOM 688 CB ARG A 286 15.435 -0.634 13.852 1.00 19.47 C ANISOU 688 CB ARG A 286 2575 2200 2625 -489 224 133 C ATOM 689 CG ARG A 286 14.135 -0.530 13.121 1.00 19.73 C ANISOU 689 CG ARG A 286 2476 2317 2706 -582 248 146 C ATOM 690 CD ARG A 286 13.112 -1.283 13.915 1.00 23.33 C ANISOU 690 CD ARG A 286 2925 2757 3183 -639 345 224 C ATOM 691 NE ARG A 286 11.765 -1.277 13.351 1.00 27.37 N ANISOU 691 NE ARG A 286 3283 3364 3752 -742 370 261 N ATOM 692 CZ ARG A 286 11.239 -2.272 12.629 1.00 27.03 C ANISOU 692 CZ ARG A 286 3194 3305 3769 -899 351 248 C ATOM 693 NH1 ARG A 286 11.959 -3.353 12.305 1.00 27.76 N ANISOU 693 NH1 ARG A 286 3402 3272 3875 -959 320 188 N ATOM 694 NH2 ARG A 286 9.969 -2.194 12.228 1.00 33.86 N ANISOU 694 NH2 ARG A 286 3898 4281 4686 -999 363 299 N ATOM 695 N GLY A 287 17.751 1.241 14.890 1.00 17.88 N ANISOU 695 N GLY A 287 2502 1988 2303 -278 94 96 N ATOM 696 CA GLY A 287 18.763 1.455 15.929 1.00 16.99 C ANISOU 696 CA GLY A 287 2493 1841 2122 -203 46 105 C ATOM 697 C GLY A 287 18.289 0.987 17.297 1.00 17.79 C ANISOU 697 C GLY A 287 2695 1911 2154 -167 117 164 C ATOM 698 O GLY A 287 17.115 1.121 17.645 1.00 19.99 O ANISOU 698 O GLY A 287 2960 2215 2421 -174 211 196 O ATOM 699 N PHE A 288 19.205 0.416 18.070 1.00 17.28 N ANISOU 699 N PHE A 288 2723 1801 2042 -122 77 191 N ATOM 700 CA PHE A 288 18.931 0.056 19.459 1.00 17.44 C ANISOU 700 CA PHE A 288 2862 1798 1968 -73 132 255 C ATOM 701 C PHE A 288 20.168 0.369 20.275 1.00 19.04 C ANISOU 701 C PHE A 288 3155 1999 2079 -5 21 256 C ATOM 702 O PHE A 288 21.245 -0.113 19.931 1.00 20.06 O ANISOU 702 O PHE A 288 3261 2112 2248 4 -59 261 O ATOM 703 CB PHE A 288 18.610 -1.444 19.619 1.00 19.40 C ANISOU 703 CB PHE A 288 3138 1980 2255 -102 211 323 C ATOM 704 CG PHE A 288 17.251 -1.847 19.131 1.00 20.62 C ANISOU 704 CG PHE A 288 3216 2136 2482 -189 322 341 C ATOM 705 CD1 PHE A 288 17.049 -2.201 17.804 1.00 20.57 C ANISOU 705 CD1 PHE A 288 3109 2123 2584 -278 308 293 C ATOM 706 CD2 PHE A 288 16.194 -1.936 20.024 1.00 24.09 C ANISOU 706 CD2 PHE A 288 3685 2591 2876 -185 438 413 C ATOM 707 CE1 PHE A 288 15.797 -2.588 17.356 1.00 22.78 C ANISOU 707 CE1 PHE A 288 3309 2418 2929 -379 386 312 C ATOM 708 CE2 PHE A 288 14.946 -2.333 19.601 1.00 25.61 C ANISOU 708 CE2 PHE A 288 3782 2802 3148 -279 534 446 C ATOM 709 CZ PHE A 288 14.744 -2.663 18.270 1.00 27.56 C ANISOU 709 CZ PHE A 288 3920 3046 3507 -384 498 395 C ATOM 710 N HIS A 289 20.022 1.100 21.380 1.00 18.42 N ANISOU 710 N HIS A 289 3184 1941 1874 45 19 258 N ATOM 711 CA HIS A 289 21.125 1.113 22.344 1.00 19.52 C ANISOU 711 CA HIS A 289 3429 2083 1906 98 -92 277 C ATOM 712 C HIS A 289 21.361 -0.282 22.893 1.00 24.45 C ANISOU 712 C HIS A 289 4104 2669 2516 131 -61 374 C ATOM 713 O HIS A 289 20.420 -1.029 23.143 1.00 22.37 O ANISOU 713 O HIS A 289 3867 2373 2259 126 71 431 O ATOM 714 CB HIS A 289 20.838 2.026 23.529 1.00 22.23 C ANISOU 714 CB HIS A 289 3918 2445 2085 145 -91 257 C ATOM 715 CG HIS A 289 20.601 3.448 23.154 1.00 22.74 C ANISOU 715 CG HIS A 289 3972 2519 2150 128 -113 165 C ATOM 716 ND1 HIS A 289 19.365 4.039 23.292 1.00 26.13 N ANISOU 716 ND1 HIS A 289 4426 2949 2551 157 21 150 N ATOM 717 CD2 HIS A 289 21.446 4.417 22.722 1.00 23.52 C ANISOU 717 CD2 HIS A 289 4046 2621 2269 94 -246 96 C ATOM 718 CE1 HIS A 289 19.448 5.303 22.907 1.00 24.03 C ANISOU 718 CE1 HIS A 289 4160 2675 2294 149 -27 72 C ATOM 719 NE2 HIS A 289 20.696 5.555 22.558 1.00 23.17 N ANISOU 719 NE2 HIS A 289 4026 2563 2216 101 -189 37 N ATOM 720 N MET A 290 22.624 -0.610 23.182 1.00 23.45 N ANISOU 720 N MET A 290 3995 2549 2365 170 -184 406 N ATOM 721 CA MET A 290 22.885 -1.913 23.780 1.00 23.88 C ANISOU 721 CA MET A 290 4112 2560 2400 224 -154 514 C ATOM 722 C MET A 290 22.084 -2.105 25.052 1.00 25.06 C ANISOU 722 C MET A 290 4408 2706 2408 262 -62 578 C ATOM 723 O MET A 290 21.607 -3.211 25.323 1.00 23.97 O ANISOU 723 O MET A 290 4312 2508 2287 275 48 669 O ATOM 724 CB MET A 290 24.369 -2.093 24.085 1.00 26.37 C ANISOU 724 CB MET A 290 4422 2909 2688 283 -311 558 C ATOM 725 CG MET A 290 25.205 -2.299 22.833 1.00 30.35 C ANISOU 725 CG MET A 290 4777 3409 3346 270 -361 533 C ATOM 726 SD MET A 290 26.958 -2.464 23.204 1.00 34.19 S ANISOU 726 SD MET A 290 5214 3962 3814 349 -541 609 S ATOM 727 CE MET A 290 27.395 -0.776 23.496 1.00 40.57 C ANISOU 727 CE MET A 290 6008 4869 4537 279 -703 522 C ATOM 728 N GLU A 291 21.951 -1.050 25.861 1.00 25.44 N ANISOU 728 N GLU A 291 4550 2809 2307 282 -99 535 N ATOM 729 CA GLU A 291 21.253 -1.226 27.129 1.00 31.00 C ANISOU 729 CA GLU A 291 5410 3520 2850 337 -2 601 C ATOM 730 C GLU A 291 19.742 -1.319 26.954 1.00 27.69 C ANISOU 730 C GLU A 291 4965 3080 2477 308 200 614 C ATOM 731 O GLU A 291 19.044 -1.714 27.899 1.00 34.09 O ANISOU 731 O GLU A 291 5880 3890 3183 350 323 697 O ATOM 732 CB GLU A 291 21.625 -0.091 28.084 1.00 32.42 C ANISOU 732 CB GLU A 291 5727 3757 2834 374 -105 541 C ATOM 733 CG GLU A 291 21.259 1.306 27.534 1.00 35.75 C ANISOU 733 CG GLU A 291 6114 4188 3280 332 -113 407 C ATOM 734 CD GLU A 291 22.361 1.993 26.713 1.00 40.57 C ANISOU 734 CD GLU A 291 6623 4812 3980 273 -294 327 C ATOM 735 OE1 GLU A 291 23.281 1.324 26.184 1.00 33.81 O ANISOU 735 OE1 GLU A 291 5661 3961 3225 257 -384 369 O ATOM 736 OE2 GLU A 291 22.295 3.248 26.597 1.00 47.29 O ANISOU 736 OE2 GLU A 291 7504 5662 4801 247 -336 225 O ATOM 737 N CYS A 292 19.240 -1.056 25.754 1.00 24.31 N ANISOU 737 N CYS A 292 4389 2643 2206 236 238 552 N ATOM 738 CA CYS A 292 17.822 -1.107 25.439 1.00 27.99 C ANISOU 738 CA CYS A 292 4786 3110 2739 195 407 570 C ATOM 739 C CYS A 292 17.423 -2.355 24.675 1.00 28.78 C ANISOU 739 C CYS A 292 4787 3150 2998 115 478 627 C ATOM 740 O CYS A 292 16.245 -2.490 24.321 1.00 30.31 O ANISOU 740 O CYS A 292 4897 3353 3267 54 603 650 O ATOM 741 CB CYS A 292 17.412 0.118 24.614 1.00 24.90 C ANISOU 741 CB CYS A 292 4295 2759 2404 169 396 467 C ATOM 742 SG CYS A 292 17.653 1.660 25.475 1.00 26.16 S ANISOU 742 SG CYS A 292 4597 2954 2386 252 341 386 S ATOM 743 N CYS A 293 18.378 -3.238 24.357 1.00 25.66 N ANISOU 743 N CYS A 293 4396 2693 2662 110 398 647 N ATOM 744 CA CYS A 293 18.060 -4.497 23.715 1.00 26.08 C ANISOU 744 CA CYS A 293 4400 2657 2850 37 468 694 C ATOM 745 C CYS A 293 17.345 -5.399 24.707 1.00 26.08 C ANISOU 745 C CYS A 293 4496 2611 2803 41 606 825 C ATOM 746 O CYS A 293 17.479 -5.258 25.926 1.00 27.53 O ANISOU 746 O CYS A 293 4802 2825 2833 129 621 892 O ATOM 747 CB CYS A 293 19.331 -5.189 23.209 1.00 24.46 C ANISOU 747 CB CYS A 293 4200 2387 2708 64 363 686 C ATOM 748 SG CYS A 293 20.072 -4.259 21.840 1.00 25.04 S ANISOU 748 SG CYS A 293 4136 2513 2863 39 233 548 S ATOM 749 N ASP A 294 16.603 -6.355 24.165 1.00 29.15 N ANISOU 749 N ASP A 294 4834 2922 3320 -62 702 865 N ATOM 750 CA ASP A 294 15.985 -7.388 24.989 1.00 32.73 C ANISOU 750 CA ASP A 294 5372 3305 3759 -81 838 1006 C ATOM 751 C ASP A 294 16.500 -8.743 24.568 1.00 31.36 C ANISOU 751 C ASP A 294 5248 2975 3693 -116 831 1045 C ATOM 752 O ASP A 294 16.116 -9.235 23.512 1.00 36.18 O ANISOU 752 O ASP A 294 5782 3516 4448 -237 846 994 O ATOM 753 CB ASP A 294 14.466 -7.310 24.865 1.00 30.69 C ANISOU 753 CB ASP A 294 5012 3089 3561 -189 981 1040 C ATOM 754 CG ASP A 294 13.752 -8.257 25.829 1.00 39.33 C ANISOU 754 CG ASP A 294 6185 4127 4633 -213 1140 1205 C ATOM 755 OD1 ASP A 294 14.414 -8.878 26.693 1.00 42.48 O ANISOU 755 OD1 ASP A 294 6737 4460 4945 -127 1142 1295 O ATOM 756 OD2 ASP A 294 12.513 -8.349 25.735 1.00 46.38 O ANISOU 756 OD2 ASP A 294 6976 5051 5593 -316 1266 1258 O ATOM 757 N PRO A 295 17.401 -9.346 25.379 1.00 27.95 N ANISOU 757 N PRO A 295 4952 2484 3183 -4 803 1135 N ATOM 758 CA PRO A 295 17.909 -8.797 26.640 1.00 30.51 C ANISOU 758 CA PRO A 295 5379 2899 3315 133 761 1194 C ATOM 759 C PRO A 295 19.037 -7.795 26.436 1.00 27.28 C ANISOU 759 C PRO A 295 4938 2583 2844 212 583 1088 C ATOM 760 O PRO A 295 19.609 -7.713 25.354 1.00 26.71 O ANISOU 760 O PRO A 295 4773 2493 2884 186 498 994 O ATOM 761 CB PRO A 295 18.413 -10.045 27.379 1.00 37.98 C ANISOU 761 CB PRO A 295 6466 3729 4234 203 795 1346 C ATOM 762 CG PRO A 295 18.825 -10.942 26.309 1.00 41.64 C ANISOU 762 CG PRO A 295 6897 4052 4873 157 776 1313 C ATOM 763 CD PRO A 295 17.992 -10.664 25.095 1.00 37.40 C ANISOU 763 CD PRO A 295 6224 3514 4474 2 807 1189 C ATOM 764 N PRO A 296 19.349 -7.022 27.470 1.00 30.53 N ANISOU 764 N PRO A 296 5432 3095 3072 302 527 1102 N ATOM 765 CA PRO A 296 20.379 -5.993 27.317 1.00 31.84 C ANISOU 765 CA PRO A 296 5567 3350 3182 349 347 1000 C ATOM 766 C PRO A 296 21.747 -6.605 27.064 1.00 28.90 C ANISOU 766 C PRO A 296 5182 2942 2857 412 219 1032 C ATOM 767 O PRO A 296 22.057 -7.720 27.494 1.00 32.30 O ANISOU 767 O PRO A 296 5688 3295 3289 471 251 1156 O ATOM 768 CB PRO A 296 20.343 -5.246 28.657 1.00 40.22 C ANISOU 768 CB PRO A 296 6762 4504 4014 424 326 1024 C ATOM 769 CG PRO A 296 19.009 -5.571 29.245 1.00 39.48 C ANISOU 769 CG PRO A 296 6727 4394 3878 406 528 1104 C ATOM 770 CD PRO A 296 18.684 -6.944 28.785 1.00 34.68 C ANISOU 770 CD PRO A 296 6084 3665 3428 350 631 1198 C ATOM 771 N LEU A 297 22.567 -5.842 26.349 1.00 25.80 N ANISOU 771 N LEU A 297 4687 2607 2509 406 80 929 N ATOM 772 CA LEU A 297 23.888 -6.279 25.935 1.00 26.74 C ANISOU 772 CA LEU A 297 4750 2715 2695 468 -38 954 C ATOM 773 C LEU A 297 24.923 -5.457 26.685 1.00 28.42 C ANISOU 773 C LEU A 297 4980 3050 2769 528 -220 956 C ATOM 774 O LEU A 297 24.823 -4.233 26.752 1.00 30.59 O ANISOU 774 O LEU A 297 5242 3404 2976 480 -287 856 O ATOM 775 CB LEU A 297 24.078 -6.114 24.425 1.00 25.75 C ANISOU 775 CB LEU A 297 4475 2567 2740 406 -48 847 C ATOM 776 CG LEU A 297 23.213 -7.056 23.570 1.00 26.34 C ANISOU 776 CG LEU A 297 4538 2515 2955 336 102 837 C ATOM 777 CD1 LEU A 297 23.443 -6.765 22.102 1.00 25.18 C ANISOU 777 CD1 LEU A 297 4261 2369 2939 281 76 722 C ATOM 778 CD2 LEU A 297 23.515 -8.512 23.870 1.00 29.49 C ANISOU 778 CD2 LEU A 297 5028 2785 3392 406 165 959 C ATOM 779 N THR A 298 25.883 -6.139 27.278 1.00 36.15 N ANISOU 779 N THR A 298 5994 4039 3704 630 -300 1074 N ATOM 780 CA THR A 298 26.977 -5.427 27.911 1.00 44.16 C ANISOU 780 CA THR A 298 6999 5181 4599 671 -503 1083 C ATOM 781 C THR A 298 28.057 -5.072 26.907 1.00 43.04 C ANISOU 781 C THR A 298 6676 5086 4591 660 -624 1032 C ATOM 782 O THR A 298 28.727 -4.049 27.052 1.00 38.89 O ANISOU 782 O THR A 298 6099 4670 4008 623 -788 978 O ATOM 783 CB THR A 298 27.556 -6.288 29.031 1.00 48.67 C ANISOU 783 CB THR A 298 7672 5768 5053 792 -552 1252 C ATOM 784 OG1 THR A 298 26.529 -6.561 30.000 1.00 53.35 O ANISOU 784 OG1 THR A 298 8440 6325 5504 800 -427 1307 O ATOM 785 CG2 THR A 298 28.720 -5.591 29.692 1.00 53.56 C ANISOU 785 CG2 THR A 298 8269 6537 5543 821 -788 1269 C ATOM 786 N ARG A 299 28.240 -5.905 25.890 1.00 37.49 N ANISOU 786 N ARG A 299 5882 4299 4063 688 -542 1050 N ATOM 787 CA ARG A 299 29.319 -5.749 24.935 1.00 31.66 C ANISOU 787 CA ARG A 299 4971 3605 3452 706 -627 1030 C ATOM 788 C ARG A 299 28.754 -5.779 23.532 1.00 32.33 C ANISOU 788 C ARG A 299 4982 3610 3692 636 -503 921 C ATOM 789 O ARG A 299 27.677 -6.324 23.283 1.00 32.29 O ANISOU 789 O ARG A 299 5053 3494 3722 595 -352 896 O ATOM 790 CB ARG A 299 30.369 -6.870 25.062 1.00 28.44 C ANISOU 790 CB ARG A 299 4527 3182 3096 857 -653 1181 C ATOM 791 CG ARG A 299 31.205 -6.880 26.330 1.00 38.46 C ANISOU 791 CG ARG A 299 5828 4563 4223 943 -813 1312 C ATOM 792 CD ARG A 299 32.372 -5.902 26.189 1.00 45.76 C ANISOU 792 CD ARG A 299 6584 5652 5150 915 -1020 1292 C ATOM 793 NE ARG A 299 33.336 -5.969 27.284 1.00 46.79 N ANISOU 793 NE ARG A 299 6709 5910 5160 994 -1204 1428 N ATOM 794 CZ ARG A 299 33.141 -5.452 28.499 1.00 48.21 C ANISOU 794 CZ ARG A 299 7022 6163 5131 956 -1317 1433 C ATOM 795 NH1 ARG A 299 31.996 -4.844 28.786 1.00 52.03 N ANISOU 795 NH1 ARG A 299 7659 6598 5514 855 -1241 1312 N ATOM 796 NH2 ARG A 299 34.088 -5.552 29.434 1.00 47.09 N ANISOU 796 NH2 ARG A 299 6848 6157 4886 1014 -1488 1554 N ATOM 797 N MET A 300 29.518 -5.198 22.634 1.00 28.26 N ANISOU 797 N MET A 300 4313 3160 3263 617 -576 868 N ATOM 798 CA MET A 300 29.172 -5.167 21.226 1.00 31.86 C ANISOU 798 CA MET A 300 4690 3564 3851 561 -480 769 C ATOM 799 C MET A 300 29.045 -6.586 20.690 1.00 25.80 C ANISOU 799 C MET A 300 3967 2656 3178 633 -339 810 C ATOM 800 O MET A 300 29.945 -7.409 20.910 1.00 29.48 O ANISOU 800 O MET A 300 4425 3102 3672 764 -352 919 O ATOM 801 CB MET A 300 30.263 -4.438 20.455 1.00 39.05 C ANISOU 801 CB MET A 300 5427 4579 4832 558 -582 744 C ATOM 802 CG MET A 300 30.157 -2.969 20.560 1.00 51.20 C ANISOU 802 CG MET A 300 6927 6210 6315 445 -687 663 C ATOM 803 SD MET A 300 28.991 -2.599 19.273 1.00 51.59 S ANISOU 803 SD MET A 300 6965 6197 6441 342 -552 529 S ATOM 804 CE MET A 300 29.974 -3.079 17.845 1.00 35.61 C ANISOU 804 CE MET A 300 4788 4181 4562 399 -516 538 C ATOM 805 N PRO A 301 27.987 -6.893 19.955 1.00 27.35 N ANISOU 805 N PRO A 301 4210 2752 3430 551 -209 727 N ATOM 806 CA PRO A 301 27.910 -8.192 19.283 1.00 24.98 C ANISOU 806 CA PRO A 301 3966 2300 3226 598 -83 739 C ATOM 807 C PRO A 301 28.942 -8.306 18.174 1.00 25.94 C ANISOU 807 C PRO A 301 3977 2439 3442 673 -87 715 C ATOM 808 O PRO A 301 29.422 -7.317 17.610 1.00 28.74 O ANISOU 808 O PRO A 301 4196 2916 3809 642 -162 662 O ATOM 809 CB PRO A 301 26.486 -8.225 18.713 1.00 30.11 C ANISOU 809 CB PRO A 301 4668 2874 3900 452 22 638 C ATOM 810 CG PRO A 301 25.800 -6.962 19.226 1.00 32.62 C ANISOU 810 CG PRO A 301 4955 3308 4131 358 -37 595 C ATOM 811 CD PRO A 301 26.853 -6.013 19.635 1.00 30.49 C ANISOU 811 CD PRO A 301 4604 3175 3807 411 -181 617 C ATOM 812 N LYS A 302 29.288 -9.545 17.867 1.00 25.95 N ANISOU 812 N LYS A 302 4044 2306 3510 779 7 762 N ATOM 813 CA LYS A 302 30.296 -9.827 16.859 1.00 26.61 C ANISOU 813 CA LYS A 302 4041 2390 3677 886 36 753 C ATOM 814 C LYS A 302 29.611 -10.266 15.575 1.00 29.14 C ANISOU 814 C LYS A 302 4428 2589 4056 811 160 620 C ATOM 815 O LYS A 302 28.668 -11.061 15.612 1.00 27.19 O ANISOU 815 O LYS A 302 4330 2183 3815 746 250 589 O ATOM 816 CB LYS A 302 31.270 -10.905 17.339 1.00 33.72 C ANISOU 816 CB LYS A 302 4977 3223 4612 1088 64 899 C ATOM 817 CG LYS A 302 32.528 -10.960 16.481 1.00 48.91 C ANISOU 817 CG LYS A 302 6763 5206 6613 1230 76 922 C ATOM 818 CD LYS A 302 33.601 -11.861 17.063 1.00 53.47 C ANISOU 818 CD LYS A 302 7334 5758 7226 1455 84 1095 C ATOM 819 CE LYS A 302 34.734 -12.103 16.060 1.00 53.93 C ANISOU 819 CE LYS A 302 7269 5848 7376 1616 149 1116 C ATOM 820 NZ LYS A 302 35.391 -10.829 15.649 1.00 58.16 N ANISOU 820 NZ LYS A 302 7570 6610 7916 1559 36 1098 N ATOM 821 N GLY A 303 30.100 -9.761 14.435 1.00 28.87 N ANISOU 821 N GLY A 303 4282 2631 4057 815 162 545 N ATOM 822 CA GLY A 303 29.550 -10.171 13.158 1.00 27.66 C ANISOU 822 CA GLY A 303 4198 2376 3935 753 267 414 C ATOM 823 C GLY A 303 28.213 -9.506 12.896 1.00 22.76 C ANISOU 823 C GLY A 303 3591 1781 3276 547 247 305 C ATOM 824 O GLY A 303 27.863 -8.509 13.516 1.00 27.29 O ANISOU 824 O GLY A 303 4092 2474 3805 469 157 321 O ATOM 825 N MET A 304 27.472 -10.053 11.930 1.00 27.28 N ANISOU 825 N MET A 304 4258 2244 3864 461 330 193 N ATOM 826 CA AMET A 304 26.161 -9.502 11.612 0.50 25.70 C ANISOU 826 CA AMET A 304 4054 2078 3635 267 309 102 C ATOM 827 CA BMET A 304 26.156 -9.527 11.600 0.50 26.17 C ANISOU 827 CA BMET A 304 4116 2134 3695 267 311 101 C ATOM 828 C MET A 304 25.270 -9.575 12.840 1.00 21.77 C ANISOU 828 C MET A 304 3606 1551 3117 193 295 167 C ATOM 829 O MET A 304 25.306 -10.548 13.595 1.00 24.69 O ANISOU 829 O MET A 304 4089 1790 3502 247 345 244 O ATOM 830 CB AMET A 304 25.508 -10.274 10.460 0.50 30.04 C ANISOU 830 CB AMET A 304 4714 2502 4198 177 387 -21 C ATOM 831 CB BMET A 304 25.555 -10.370 10.464 0.50 30.27 C ANISOU 831 CB BMET A 304 4753 2518 4229 187 393 -18 C ATOM 832 CG AMET A 304 26.185 -10.112 9.125 0.50 33.13 C ANISOU 832 CG AMET A 304 5071 2936 4580 233 412 -104 C ATOM 833 CG BMET A 304 24.480 -9.712 9.635 0.50 27.85 C ANISOU 833 CG BMET A 304 4400 2291 3893 7 359 -126 C ATOM 834 SD AMET A 304 25.983 -8.448 8.486 0.50 38.87 S ANISOU 834 SD AMET A 304 5610 3896 5262 144 317 -146 S ATOM 835 SD BMET A 304 23.894 -10.802 8.302 0.50 34.43 S ANISOU 835 SD BMET A 304 5394 2963 4725 -94 434 -274 S ATOM 836 CE AMET A 304 27.709 -8.041 8.267 0.50 38.90 C ANISOU 836 CE AMET A 304 5492 4002 5285 339 317 -74 C ATOM 837 CE BMET A 304 22.304 -10.063 7.950 0.50 29.14 C ANISOU 837 CE BMET A 304 4642 2404 4026 -334 361 -337 C ATOM 838 N TRP A 305 24.471 -8.536 13.048 1.00 21.57 N ANISOU 838 N TRP A 305 3498 1644 3052 81 239 147 N ATOM 839 CA TRP A 305 23.600 -8.489 14.213 1.00 23.10 C ANISOU 839 CA TRP A 305 3730 1832 3215 21 241 212 C ATOM 840 C TRP A 305 22.166 -8.217 13.785 1.00 21.40 C ANISOU 840 C TRP A 305 3491 1635 3003 -151 264 145 C ATOM 841 O TRP A 305 21.919 -7.268 13.039 1.00 21.12 O ANISOU 841 O TRP A 305 3353 1716 2957 -206 219 76 O ATOM 842 CB TRP A 305 24.078 -7.408 15.199 1.00 20.77 C ANISOU 842 CB TRP A 305 3360 1675 2856 85 152 278 C ATOM 843 CG TRP A 305 23.163 -7.314 16.403 1.00 22.12 C ANISOU 843 CG TRP A 305 3586 1847 2971 39 171 340 C ATOM 844 CD1 TRP A 305 23.091 -8.188 17.457 1.00 24.31 C ANISOU 844 CD1 TRP A 305 3976 2034 3227 85 219 442 C ATOM 845 CD2 TRP A 305 22.161 -6.316 16.633 1.00 19.28 C ANISOU 845 CD2 TRP A 305 3175 1583 2569 -51 162 314 C ATOM 846 NE1 TRP A 305 22.115 -7.777 18.342 1.00 24.57 N ANISOU 846 NE1 TRP A 305 4029 2109 3198 26 243 479 N ATOM 847 CE2 TRP A 305 21.533 -6.632 17.856 1.00 20.05 C ANISOU 847 CE2 TRP A 305 3355 1649 2614 -52 213 399 C ATOM 848 CE3 TRP A 305 21.743 -5.178 15.925 1.00 19.40 C ANISOU 848 CE3 TRP A 305 3084 1705 2584 -117 124 236 C ATOM 849 CZ2 TRP A 305 20.506 -5.854 18.396 1.00 21.77 C ANISOU 849 CZ2 TRP A 305 3550 1943 2779 -108 238 404 C ATOM 850 CZ3 TRP A 305 20.723 -4.399 16.462 1.00 25.41 C ANISOU 850 CZ3 TRP A 305 3823 2532 3299 -169 142 243 C ATOM 851 CH2 TRP A 305 20.108 -4.755 17.687 1.00 23.47 C ANISOU 851 CH2 TRP A 305 3660 2256 3002 -161 204 325 C ATOM 852 N ILE A 306 21.237 -9.026 14.292 1.00 24.56 N ANISOU 852 N ILE A 306 3978 1932 3422 -233 332 181 N ATOM 853 CA ILE A 306 19.816 -8.947 13.989 1.00 26.89 C ANISOU 853 CA ILE A 306 4238 2244 3735 -405 359 145 C ATOM 854 C ILE A 306 19.088 -8.558 15.264 1.00 25.93 C ANISOU 854 C ILE A 306 4101 2178 3574 -418 385 243 C ATOM 855 O ILE A 306 19.284 -9.185 16.309 1.00 28.67 O ANISOU 855 O ILE A 306 4544 2445 3904 -357 429 340 O ATOM 856 CB ILE A 306 19.296 -10.296 13.465 1.00 35.94 C ANISOU 856 CB ILE A 306 5498 3213 4945 -515 427 109 C ATOM 857 CG1 ILE A 306 20.155 -10.795 12.303 1.00 40.48 C ANISOU 857 CG1 ILE A 306 6134 3708 5539 -467 422 11 C ATOM 858 CG2 ILE A 306 17.855 -10.200 13.076 1.00 40.70 C ANISOU 858 CG2 ILE A 306 6035 3856 5574 -712 434 77 C ATOM 859 CD1 ILE A 306 20.282 -9.792 11.202 1.00 38.16 C ANISOU 859 CD1 ILE A 306 5721 3565 5215 -483 353 -85 C ATOM 860 N CYS A 307 18.205 -7.570 15.163 1.00 23.83 N ANISOU 860 N CYS A 307 3721 2045 3289 -490 368 224 N ATOM 861 CA CYS A 307 17.531 -6.974 16.299 1.00 24.53 C ANISOU 861 CA CYS A 307 3786 2210 3325 -478 402 306 C ATOM 862 C CYS A 307 16.386 -7.859 16.790 1.00 26.64 C ANISOU 862 C CYS A 307 4087 2404 3631 -588 505 380 C ATOM 863 O CYS A 307 15.991 -8.847 16.153 1.00 26.08 O ANISOU 863 O CYS A 307 4047 2226 3637 -706 534 355 O ATOM 864 CB CYS A 307 17.006 -5.581 15.938 1.00 24.63 C ANISOU 864 CB CYS A 307 3665 2380 3312 -495 362 263 C ATOM 865 SG CYS A 307 15.421 -5.566 15.018 1.00 23.31 S ANISOU 865 SG CYS A 307 3368 2273 3215 -674 395 236 S ATOM 866 N GLN A 308 15.823 -7.452 17.937 1.00 28.58 N ANISOU 866 N GLN A 308 4331 2712 3818 -555 563 472 N ATOM 867 CA GLN A 308 14.784 -8.235 18.591 1.00 29.94 C ANISOU 867 CA GLN A 308 4528 2828 4019 -645 678 573 C ATOM 868 C GLN A 308 13.498 -8.301 17.779 1.00 31.74 C ANISOU 868 C GLN A 308 4624 3099 4336 -825 705 551 C ATOM 869 O GLN A 308 12.687 -9.223 17.995 1.00 33.52 O ANISOU 869 O GLN A 308 4862 3248 4626 -951 788 622 O ATOM 870 CB GLN A 308 14.506 -7.652 19.978 1.00 30.92 C ANISOU 870 CB GLN A 308 4678 3031 4037 -548 743 674 C ATOM 871 CG GLN A 308 13.902 -6.236 19.970 1.00 32.05 C ANISOU 871 CG GLN A 308 4701 3344 4135 -520 738 644 C ATOM 872 CD GLN A 308 14.154 -5.520 21.278 1.00 33.75 C ANISOU 872 CD GLN A 308 5000 3618 4207 -375 766 698 C ATOM 873 OE1 GLN A 308 15.306 -5.334 21.684 1.00 33.49 O ANISOU 873 OE1 GLN A 308 5066 3565 4095 -267 684 677 O ATOM 874 NE2 GLN A 308 13.085 -5.166 21.974 1.00 37.61 N ANISOU 874 NE2 GLN A 308 5454 4181 4657 -372 884 773 N ATOM 875 N ILE A 309 13.278 -7.341 16.884 1.00 32.53 N ANISOU 875 N ILE A 309 4592 3325 4443 -846 635 466 N ATOM 876 CA ILE A 309 12.108 -7.365 16.021 1.00 31.33 C ANISOU 876 CA ILE A 309 4298 3237 4369 -1015 634 447 C ATOM 877 C ILE A 309 12.294 -8.359 14.887 1.00 32.78 C ANISOU 877 C ILE A 309 4529 3302 4622 -1148 578 357 C ATOM 878 O ILE A 309 11.373 -9.114 14.563 1.00 33.69 O ANISOU 878 O ILE A 309 4609 3377 4814 -1330 602 374 O ATOM 879 CB ILE A 309 11.803 -5.954 15.502 1.00 35.47 C ANISOU 879 CB ILE A 309 4671 3941 4866 -970 580 406 C ATOM 880 CG1 ILE A 309 11.492 -5.014 16.674 1.00 37.27 C ANISOU 880 CG1 ILE A 309 4877 4263 5021 -841 656 491 C ATOM 881 CG2 ILE A 309 10.691 -5.979 14.473 1.00 31.95 C ANISOU 881 CG2 ILE A 309 4064 3579 4495 -1139 551 388 C ATOM 882 CD1 ILE A 309 11.560 -3.540 16.308 1.00 39.02 C ANISOU 882 CD1 ILE A 309 5011 4615 5200 -745 602 442 C ATOM 883 N CYS A 310 13.488 -8.415 14.294 1.00 27.48 N ANISOU 883 N CYS A 310 3948 2569 3926 -1064 509 262 N ATOM 884 CA CYS A 310 13.653 -9.302 13.151 1.00 30.84 C ANISOU 884 CA CYS A 310 4437 2882 4398 -1176 466 161 C ATOM 885 C CYS A 310 13.893 -10.753 13.546 1.00 37.49 C ANISOU 885 C CYS A 310 5457 3501 5288 -1214 533 191 C ATOM 886 O CYS A 310 13.610 -11.655 12.748 1.00 42.22 O ANISOU 886 O CYS A 310 6122 3981 5940 -1361 522 120 O ATOM 887 CB CYS A 310 14.808 -8.847 12.289 1.00 22.76 C ANISOU 887 CB CYS A 310 3439 1879 3331 -1064 389 55 C ATOM 888 SG CYS A 310 14.647 -7.175 11.664 1.00 24.89 S ANISOU 888 SG CYS A 310 3526 2379 3551 -1021 308 18 S ATOM 889 N ARG A 311 14.457 -10.995 14.723 1.00 36.75 N ANISOU 889 N ARG A 311 5457 3340 5167 -1081 596 289 N ATOM 890 CA ARG A 311 14.644 -12.352 15.214 1.00 41.96 C ANISOU 890 CA ARG A 311 6288 3782 5872 -1101 672 347 C ATOM 891 C ARG A 311 13.333 -13.134 15.135 1.00 47.96 C ANISOU 891 C ARG A 311 7027 4479 6717 -1328 719 382 C ATOM 892 O ARG A 311 12.315 -12.675 15.674 1.00 51.46 O ANISOU 892 O ARG A 311 7340 5045 7167 -1402 760 470 O ATOM 893 CB ARG A 311 15.082 -12.330 16.675 1.00 47.43 C ANISOU 893 CB ARG A 311 7046 4467 6509 -945 734 488 C ATOM 894 CG ARG A 311 16.514 -12.037 16.986 1.00 49.62 C ANISOU 894 CG ARG A 311 7386 4750 6717 -725 688 487 C ATOM 895 CD ARG A 311 16.770 -12.667 18.360 1.00 53.89 C ANISOU 895 CD ARG A 311 8051 5201 7224 -629 764 640 C ATOM 896 NE ARG A 311 17.177 -11.713 19.382 1.00 57.29 N ANISOU 896 NE ARG A 311 8447 5781 7540 -482 735 707 N ATOM 897 CZ ARG A 311 16.416 -11.292 20.391 1.00 57.64 C ANISOU 897 CZ ARG A 311 8466 5914 7522 -491 794 801 C ATOM 898 NH1 ARG A 311 16.914 -10.416 21.253 1.00 55.25 N ANISOU 898 NH1 ARG A 311 8163 5733 7096 -351 753 837 N ATOM 899 NH2 ARG A 311 15.172 -11.729 20.543 1.00 56.33 N ANISOU 899 NH2 ARG A 311 8275 5719 7410 -640 894 861 N ATOM 900 N PRO A 312 13.314 -14.317 14.500 1.00 62.61 N ANISOU 900 N PRO A 312 8969 6191 8629 -1402 691 318 N ATOM 901 CA PRO A 312 12.132 -15.180 14.649 1.00 71.38 C ANISOU 901 CA PRO A 312 10037 7263 9820 -1575 708 376 C ATOM 902 C PRO A 312 11.997 -15.704 16.076 1.00 73.26 C ANISOU 902 C PRO A 312 10335 7433 10066 -1525 814 548 C ATOM 903 O PRO A 312 13.016 -16.101 16.645 1.00 71.19 O ANISOU 903 O PRO A 312 10225 7056 9768 -1364 854 585 O ATOM 904 CB PRO A 312 12.402 -16.341 13.680 1.00 74.39 C ANISOU 904 CB PRO A 312 10548 7472 10245 -1633 659 258 C ATOM 905 CG PRO A 312 13.455 -15.839 12.741 1.00 72.82 C ANISOU 905 CG PRO A 312 10400 7288 9981 -1521 604 118 C ATOM 906 CD PRO A 312 14.283 -14.858 13.532 1.00 66.30 C ANISOU 906 CD PRO A 312 9564 6536 9090 -1340 644 186 C TER 907 PRO A 312 ATOM 908 N ALA B 1 29.162 -6.126 13.979 1.00 37.82 N ANISOU 908 N ALA B 1 4714 4807 4849 488 325 191 N ATOM 909 CA ALA B 1 27.918 -5.371 14.060 1.00 25.12 C ANISOU 909 CA ALA B 1 3175 3227 3142 412 278 56 C ATOM 910 C ALA B 1 28.256 -3.951 13.782 1.00 24.27 C ANISOU 910 C ALA B 1 2968 3130 3125 368 154 44 C ATOM 911 O ALA B 1 29.396 -3.539 13.951 1.00 29.76 O ANISOU 911 O ALA B 1 3551 3825 3932 378 56 129 O ATOM 912 CB ALA B 1 27.288 -5.494 15.400 1.00 26.38 C ANISOU 912 CB ALA B 1 3430 3413 3180 415 206 -2 C ATOM 913 N ARG B 2 27.261 -3.190 13.365 1.00 21.78 N ANISOU 913 N ARG B 2 2684 2822 2769 315 153 -48 N ATOM 914 CA ARG B 2 27.458 -1.778 13.068 1.00 20.76 C ANISOU 914 CA ARG B 2 2484 2684 2720 273 47 -64 C ATOM 915 C ARG B 2 26.895 -0.952 14.196 1.00 21.50 C ANISOU 915 C ARG B 2 2645 2779 2747 260 -73 -153 C ATOM 916 O ARG B 2 25.831 -1.272 14.735 1.00 21.99 O ANISOU 916 O ARG B 2 2801 2858 2696 275 -24 -224 O ATOM 917 CB ARG B 2 26.746 -1.352 11.792 1.00 24.68 C ANISOU 917 CB ARG B 2 2976 3176 3226 232 124 -90 C ATOM 918 CG ARG B 2 27.266 -1.930 10.507 1.00 27.57 C ANISOU 918 CG ARG B 2 3316 3522 3638 226 251 -17 C ATOM 919 CD ARG B 2 26.369 -1.430 9.377 1.00 21.88 C ANISOU 919 CD ARG B 2 2622 2806 2886 166 290 -49 C ATOM 920 NE ARG B 2 25.052 -2.006 9.528 1.00 21.41 N ANISOU 920 NE ARG B 2 2648 2782 2705 141 331 -113 N ATOM 921 CZ ARG B 2 23.911 -1.376 9.313 1.00 19.39 C ANISOU 921 CZ ARG B 2 2391 2559 2417 104 293 -153 C ATOM 922 NH1 ARG B 2 23.890 -0.100 8.899 1.00 19.46 N ANISOU 922 NH1 ARG B 2 2338 2556 2498 96 217 -145 N ATOM 923 NH2 ARG B 2 22.768 -2.024 9.523 1.00 19.88 N ANISOU 923 NH2 ARG B 2 2504 2663 2385 77 334 -189 N ATOM 924 N THR B 3 27.590 0.130 14.531 1.00 21.38 N ANISOU 924 N THR B 3 2589 2735 2798 226 -217 -148 N ATOM 925 CA THR B 3 27.023 1.164 15.373 1.00 20.55 C ANISOU 925 CA THR B 3 2581 2597 2631 205 -309 -247 C ATOM 926 C THR B 3 26.935 2.423 14.541 1.00 19.83 C ANISOU 926 C THR B 3 2443 2458 2632 169 -331 -262 C ATOM 927 O THR B 3 27.418 2.476 13.417 1.00 20.47 O ANISOU 927 O THR B 3 2418 2541 2818 151 -295 -189 O ATOM 928 CB THR B 3 27.889 1.465 16.599 1.00 23.80 C ANISOU 928 CB THR B 3 3040 2991 3013 169 -484 -240 C ATOM 929 OG1 THR B 3 29.176 1.937 16.160 1.00 24.41 O ANISOU 929 OG1 THR B 3 2981 3058 3237 112 -594 -144 O ATOM 930 CG2 THR B 3 28.115 0.216 17.448 1.00 26.09 C ANISOU 930 CG2 THR B 3 3372 3328 3215 208 -481 -198 C ATOM 931 N LYS B 4 26.297 3.439 15.110 1.00 20.28 N ANISOU 931 N LYS B 4 2600 2460 2645 165 -374 -353 N ATOM 932 CA LYS B 4 26.269 4.734 14.441 1.00 20.49 C ANISOU 932 CA LYS B 4 2603 2418 2764 135 -406 -362 C ATOM 933 C LYS B 4 27.678 5.188 14.090 1.00 24.32 C ANISOU 933 C LYS B 4 2991 2878 3373 56 -522 -280 C ATOM 934 O LYS B 4 27.951 5.601 12.959 1.00 22.43 O ANISOU 934 O LYS B 4 2656 2625 3242 34 -491 -219 O ATOM 935 CB LYS B 4 25.548 5.746 15.338 1.00 21.35 C ANISOU 935 CB LYS B 4 2866 2442 2804 153 -431 -471 C ATOM 936 CG LYS B 4 25.240 7.057 14.654 1.00 22.35 C ANISOU 936 CG LYS B 4 2990 2481 3020 150 -427 -482 C ATOM 937 CD LYS B 4 24.482 7.986 15.628 1.00 23.89 C ANISOU 937 CD LYS B 4 3369 2568 3140 192 -412 -595 C ATOM 938 CE LYS B 4 23.042 7.472 15.880 1.00 23.04 C ANISOU 938 CE LYS B 4 3287 2509 2957 304 -249 -631 C ATOM 939 NZ LYS B 4 22.003 8.580 15.553 1.00 23.00 N ANISOU 939 NZ LYS B 4 3307 2419 3014 388 -156 -650 N ATOM 940 N GLN B 5 28.605 5.054 15.042 1.00 23.61 N ANISOU 940 N GLN B 5 2916 2788 3267 7 -658 -261 N ATOM 941 CA GLN B 5 29.979 5.481 14.831 1.00 25.74 C ANISOU 941 CA GLN B 5 3066 3045 3670 -83 -787 -163 C ATOM 942 C GLN B 5 30.655 4.665 13.736 1.00 27.46 C ANISOU 942 C GLN B 5 3098 3327 4009 -53 -687 -29 C ATOM 943 O GLN B 5 31.311 5.223 12.847 1.00 27.72 O ANISOU 943 O GLN B 5 3016 3337 4179 -100 -685 48 O ATOM 944 CB GLN B 5 30.736 5.359 16.148 1.00 29.68 C ANISOU 944 CB GLN B 5 3615 3552 4111 -147 -971 -153 C ATOM 945 CG GLN B 5 32.178 5.715 16.082 1.00 35.53 C ANISOU 945 CG GLN B 5 4204 4299 4998 -256 -1134 -28 C ATOM 946 CD GLN B 5 32.855 5.471 17.417 1.00 46.59 C ANISOU 946 CD GLN B 5 5654 5728 6323 -328 -1341 -1 C ATOM 947 OE1 GLN B 5 32.470 4.567 18.164 1.00 50.79 O ANISOU 947 OE1 GLN B 5 6271 6306 6720 -260 -1318 -24 O ATOM 948 NE2 GLN B 5 33.853 6.281 17.733 1.00 51.75 N ANISOU 948 NE2 GLN B 5 6259 6350 7052 -479 -1555 56 N ATOM 949 N THR B 6 30.540 3.333 13.792 1.00 24.10 N ANISOU 949 N THR B 6 2656 2969 3532 24 -586 5 N ATOM 950 CA THR B 6 31.257 2.558 12.790 1.00 23.24 C ANISOU 950 CA THR B 6 2402 2895 3534 60 -467 131 C ATOM 951 C THR B 6 30.617 2.693 11.421 1.00 23.99 C ANISOU 951 C THR B 6 2503 2972 3639 75 -308 116 C ATOM 952 O THR B 6 31.322 2.624 10.406 1.00 28.08 O ANISOU 952 O THR B 6 2918 3486 4267 71 -223 214 O ATOM 953 CB THR B 6 31.404 1.071 13.184 1.00 24.09 C ANISOU 953 CB THR B 6 2507 3053 3592 142 -388 183 C ATOM 954 OG1 THR B 6 30.158 0.385 13.064 1.00 23.95 O ANISOU 954 OG1 THR B 6 2620 3045 3435 192 -253 90 O ATOM 955 CG2 THR B 6 32.005 0.897 14.594 1.00 32.27 C ANISOU 955 CG2 THR B 6 3547 4115 4598 126 -566 214 C ATOM 956 N ALA B 7 29.296 2.930 11.364 1.00 20.11 N ANISOU 956 N ALA B 7 2131 2472 3037 88 -267 6 N ATOM 957 CA ALA B 7 28.614 3.072 10.089 1.00 19.64 C ANISOU 957 CA ALA B 7 2081 2408 2972 87 -151 5 C ATOM 958 C ALA B 7 29.008 4.372 9.404 1.00 19.68 C ANISOU 958 C ALA B 7 2034 2357 3086 31 -204 39 C ATOM 959 O ALA B 7 29.124 4.415 8.176 1.00 23.84 O ANISOU 959 O ALA B 7 2527 2879 3652 17 -112 100 O ATOM 960 CB ALA B 7 27.105 3.023 10.313 1.00 23.41 C ANISOU 960 CB ALA B 7 2663 2904 3328 114 -118 -93 C ATOM 961 N ARG B 8 29.231 5.437 10.187 1.00 20.68 N ANISOU 961 N ARG B 8 2177 2430 3250 -10 -349 1 N ATOM 962 CA ARG B 8 29.776 6.671 9.637 1.00 22.60 C ANISOU 962 CA ARG B 8 2374 2603 3610 -78 -408 43 C ATOM 963 C ARG B 8 31.049 6.397 8.861 1.00 23.46 C ANISOU 963 C ARG B 8 2336 2729 3849 -112 -364 180 C ATOM 964 O ARG B 8 31.233 6.900 7.746 1.00 24.38 O ANISOU 964 O ARG B 8 2413 2815 4034 -140 -298 241 O ATOM 965 CB ARG B 8 30.105 7.655 10.751 1.00 31.10 C ANISOU 965 CB ARG B 8 3507 3608 4703 -142 -581 -12 C ATOM 966 CG ARG B 8 29.043 8.580 11.068 1.00 33.22 C ANISOU 966 CG ARG B 8 3917 3799 4908 -122 -597 -119 C ATOM 967 CD ARG B 8 29.544 9.592 12.070 1.00 30.22 C ANISOU 967 CD ARG B 8 3627 3317 4537 -208 -758 -174 C ATOM 968 NE ARG B 8 28.412 9.930 12.889 1.00 29.40 N ANISOU 968 NE ARG B 8 3703 3158 4311 -145 -738 -303 N ATOM 969 CZ ARG B 8 28.337 9.707 14.189 1.00 37.48 C ANISOU 969 CZ ARG B 8 4853 4172 5216 -150 -804 -386 C ATOM 970 NH1 ARG B 8 27.235 10.058 14.837 1.00 34.00 N ANISOU 970 NH1 ARG B 8 4580 3668 4668 -76 -740 -499 N ATOM 971 NH2 ARG B 8 29.377 9.185 14.840 1.00 39.23 N ANISOU 971 NH2 ARG B 8 5034 4442 5429 -228 -932 -345 N ATOM 972 N LYS B 9 31.967 5.641 9.485 1.00 24.73 N ANISOU 972 N LYS B 9 2409 2934 4051 -107 -399 242 N ATOM 973 CA LYS B 9 33.291 5.395 8.918 1.00 26.29 C ANISOU 973 CA LYS B 9 2433 3149 4407 -125 -354 396 C ATOM 974 C LYS B 9 33.198 4.460 7.734 1.00 25.28 C ANISOU 974 C LYS B 9 2299 3044 4263 -51 -123 450 C ATOM 975 O LYS B 9 33.834 4.680 6.698 1.00 29.57 O ANISOU 975 O LYS B 9 2762 3565 4907 -69 -18 549 O ATOM 976 CB LYS B 9 34.228 4.768 9.959 1.00 33.47 C ANISOU 976 CB LYS B 9 3237 4108 5370 -122 -458 470 C ATOM 977 CG LYS B 9 34.774 5.674 11.030 1.00 44.59 C ANISOU 977 CG LYS B 9 4625 5495 6822 -236 -707 465 C ATOM 978 CD LYS B 9 36.041 5.051 11.628 1.00 52.40 C ANISOU 978 CD LYS B 9 5429 6550 7929 -247 -800 620 C ATOM 979 CE LYS B 9 36.291 5.509 13.069 1.00 56.91 C ANISOU 979 CE LYS B 9 6055 7124 8447 -353 -1077 584 C ATOM 980 NZ LYS B 9 35.537 6.742 13.444 1.00 57.27 N ANISOU 980 NZ LYS B 9 6303 7074 8384 -447 -1186 419 N ATOM 981 N SER B 10 32.434 3.382 7.883 1.00 23.05 N ANISOU 981 N SER B 10 2118 2796 3845 23 -33 387 N ATOM 982 CA SER B 10 32.448 2.364 6.841 1.00 26.12 C ANISOU 982 CA SER B 10 2535 3188 4201 79 188 436 C ATOM 983 C SER B 10 31.694 2.824 5.601 1.00 26.39 C ANISOU 983 C SER B 10 2667 3196 4165 40 273 403 C ATOM 984 O SER B 10 32.031 2.426 4.476 1.00 28.35 O ANISOU 984 O SER B 10 2934 3423 4416 49 447 469 O ATOM 985 CB SER B 10 31.887 1.055 7.394 1.00 23.71 C ANISOU 985 CB SER B 10 2324 2914 3771 149 251 382 C ATOM 986 OG SER B 10 30.578 1.217 7.880 1.00 27.09 O ANISOU 986 OG SER B 10 2876 3359 4059 131 176 252 O ATOM 987 N THR B 11 30.722 3.717 5.776 1.00 25.98 N ANISOU 987 N THR B 11 2681 3136 4053 0 158 314 N ATOM 988 CA THR B 11 29.966 4.210 4.639 1.00 24.23 C ANISOU 988 CA THR B 11 2540 2898 3769 -36 208 306 C ATOM 989 C THR B 11 30.815 5.097 3.738 1.00 24.65 C ANISOU 989 C THR B 11 2525 2901 3941 -85 236 405 C ATOM 990 O THR B 11 30.734 4.984 2.511 1.00 27.80 O ANISOU 990 O THR B 11 2984 3288 4291 -104 362 451 O ATOM 991 CB THR B 11 28.720 4.941 5.142 1.00 23.23 C ANISOU 991 CB THR B 11 2476 2774 3577 -42 85 210 C ATOM 992 OG1 THR B 11 27.949 4.007 5.925 1.00 21.68 O ANISOU 992 OG1 THR B 11 2338 2629 3272 0 90 132 O ATOM 993 CG2 THR B 11 27.915 5.407 3.996 1.00 22.59 C ANISOU 993 CG2 THR B 11 2456 2688 3439 -74 117 228 C ATOM 994 N GLY B 12 31.682 5.939 4.319 1.00 22.81 N ANISOU 994 N GLY B 12 2176 2636 3855 -118 124 445 N ATOM 995 CA GLY B 12 32.439 6.947 3.612 1.00 25.12 C ANISOU 995 CA GLY B 12 2396 2873 4274 -183 127 538 C ATOM 996 C GLY B 12 31.807 8.313 3.775 1.00 23.80 C ANISOU 996 C GLY B 12 2285 2645 4113 -232 -14 483 C ATOM 997 O GLY B 12 30.609 8.449 4.026 1.00 23.57 O ANISOU 997 O GLY B 12 2361 2620 3975 -201 -62 389 O ATOM 998 N GLY B 13 32.615 9.348 3.618 1.00 23.87 N ANISOU 998 N GLY B 13 2219 2588 4261 -309 -70 554 N ATOM 999 CA GLY B 13 32.125 10.692 3.850 1.00 25.39 C ANISOU 999 CA GLY B 13 2481 2692 4473 -355 -197 505 C ATOM 1000 C GLY B 13 31.017 11.229 2.950 1.00 24.73 C ANISOU 1000 C GLY B 13 2513 2576 4306 -328 -154 494 C ATOM 1001 O GLY B 13 30.953 10.918 1.769 1.00 23.67 O ANISOU 1001 O GLY B 13 2397 2468 4129 -325 -31 566 O HETATM 1002 C PRK B 14 30.000 13.813 1.836 1.00 25.79 C ANISOU 1002 C PRK B 14 2796 2510 4495 -364 -225 549 C HETATM 1003 N PRK B 14 30.161 12.057 3.520 1.00 23.71 N ANISOU 1003 N PRK B 14 2470 2385 4153 -308 -256 413 N HETATM 1004 O PRK B 14 31.123 14.280 2.153 1.00 25.97 O ANISOU 1004 O PRK B 14 2751 2472 4643 -451 -269 582 O HETATM 1005 CA PRK B 14 29.244 12.833 2.695 1.00 23.81 C ANISOU 1005 CA PRK B 14 2563 2349 4134 -284 -240 439 C HETATM 1006 CB PRK B 14 28.195 13.598 3.460 1.00 23.90 C ANISOU 1006 CB PRK B 14 2662 2292 4126 -223 -321 351 C HETATM 1007 CD PRK B 14 26.062 12.939 4.457 1.00 27.18 C ANISOU 1007 CD PRK B 14 3151 2791 4384 -56 -318 215 C HETATM 1008 CE PRK B 14 25.323 11.817 5.177 1.00 26.96 C ANISOU 1008 CE PRK B 14 3122 2872 4250 7 -291 137 C HETATM 1009 CG PRK B 14 27.477 12.540 4.265 1.00 29.68 C ANISOU 1009 CG PRK B 14 3404 3123 4750 -149 -312 256 C HETATM 1010 NZ PRK B 14 24.034 11.812 4.559 1.00 27.18 N ANISOU 1010 NZ PRK B 14 3146 2950 4233 68 -260 179 N HETATM 1011 CAA PRK B 14 21.112 9.697 3.877 1.00 22.92 C ANISOU 1011 CAA PRK B 14 2521 2718 3470 129 -192 230 C HETATM 1012 OAD PRK B 14 23.485 9.788 5.410 1.00 21.67 O ANISOU 1012 OAD PRK B 14 2427 2424 3382 93 -202 87 O HETATM 1013 CAF PRK B 14 21.895 10.963 3.964 1.00 29.74 C ANISOU 1013 CAF PRK B 14 3417 3442 4442 143 -222 234 C HETATM 1014 CAL PRK B 14 23.201 10.760 4.703 1.00 22.40 C ANISOU 1014 CAL PRK B 14 2517 2461 3531 100 -223 155 C ATOM 1015 N ALA B 15 29.404 14.156 0.697 1.00 25.12 N ANISOU 1015 N ALA B 15 2768 2415 4364 -350 -172 622 N ATOM 1016 CA ALA B 15 29.981 15.172 -0.178 1.00 26.37 C ANISOU 1016 CA ALA B 15 2933 2475 4611 -421 -150 735 C ATOM 1017 C ALA B 15 29.889 16.574 0.448 1.00 27.37 C ANISOU 1017 C ALA B 15 3113 2446 4841 -440 -261 705 C ATOM 1018 O ALA B 15 29.074 16.817 1.318 1.00 27.81 O ANISOU 1018 O ALA B 15 3230 2468 4870 -370 -331 605 O ATOM 1019 CB ALA B 15 29.310 15.147 -1.535 1.00 26.60 C ANISOU 1019 CB ALA B 15 3034 2536 4538 -403 -78 827 C ATOM 1020 N PRO B 16 30.756 17.494 0.039 1.00 28.71 N ANISOU 1020 N PRO B 16 3272 2507 5131 -538 -263 790 N ATOM 1021 CA PRO B 16 30.709 18.842 0.622 1.00 29.93 C ANISOU 1021 CA PRO B 16 3511 2484 5379 -573 -362 757 C ATOM 1022 C PRO B 16 29.326 19.457 0.463 1.00 29.94 C ANISOU 1022 C PRO B 16 3633 2421 5322 -451 -370 742 C ATOM 1023 O PRO B 16 28.736 19.430 -0.618 1.00 31.31 O ANISOU 1023 O PRO B 16 3821 2636 5439 -402 -313 840 O ATOM 1024 CB PRO B 16 31.775 19.603 -0.172 1.00 33.58 C ANISOU 1024 CB PRO B 16 3937 2856 5965 -703 -329 890 C ATOM 1025 CG PRO B 16 32.789 18.524 -0.458 1.00 31.06 C ANISOU 1025 CG PRO B 16 3463 2675 5664 -754 -247 949 C ATOM 1026 CD PRO B 16 31.968 17.282 -0.757 1.00 29.40 C ANISOU 1026 CD PRO B 16 3262 2618 5290 -633 -169 912 C ATOM 1027 N ARG B 17 28.808 20.010 1.563 1.00 37.54 N ANISOU 1027 N ARG B 17 4687 3280 6298 -400 -440 627 N ATOM 1028 CA ARG B 17 27.425 20.484 1.575 1.00 41.36 C ANISOU 1028 CA ARG B 17 5258 3711 6744 -250 -427 616 C ATOM 1029 C ARG B 17 27.204 21.608 0.583 1.00 41.09 C ANISOU 1029 C ARG B 17 5288 3548 6776 -239 -405 750 C ATOM 1030 O ARG B 17 26.143 21.682 -0.052 1.00 40.85 O ANISOU 1030 O ARG B 17 5261 3553 6706 -123 -379 829 O ATOM 1031 CB ARG B 17 27.038 20.968 2.958 1.00 51.42 C ANISOU 1031 CB ARG B 17 6648 4863 8028 -197 -469 470 C ATOM 1032 CG ARG B 17 26.326 19.959 3.793 1.00 58.88 C ANISOU 1032 CG ARG B 17 7565 5938 8869 -101 -457 362 C ATOM 1033 CD ARG B 17 26.397 20.448 5.204 1.00 67.57 C ANISOU 1033 CD ARG B 17 8806 6899 9967 -106 -500 212 C ATOM 1034 NE ARG B 17 27.786 20.785 5.501 1.00 73.01 N ANISOU 1034 NE ARG B 17 9514 7511 10715 -294 -591 195 N ATOM 1035 CZ ARG B 17 28.191 21.390 6.610 1.00 75.09 C ANISOU 1035 CZ ARG B 17 9927 7625 10980 -374 -668 81 C ATOM 1036 NH1 ARG B 17 27.306 21.730 7.531 1.00 76.77 N ANISOU 1036 NH1 ARG B 17 10309 7732 11127 -263 -633 -39 N ATOM 1037 NH2 ARG B 17 29.479 21.648 6.795 1.00 75.58 N ANISOU 1037 NH2 ARG B 17 9973 7640 11105 -571 -775 92 N ATOM 1038 N LYS B 18 28.187 22.505 0.458 1.00 35.52 N ANISOU 1038 N LYS B 18 4628 2691 6176 -366 -425 788 N ATOM 1039 CA LYS B 18 28.115 23.560 -0.546 1.00 41.47 C ANISOU 1039 CA LYS B 18 5448 3313 6994 -373 -397 931 C ATOM 1040 C LYS B 18 27.929 22.978 -1.932 1.00 38.60 C ANISOU 1040 C LYS B 18 5011 3101 6552 -360 -339 1078 C ATOM 1041 O LYS B 18 27.244 23.566 -2.774 1.00 45.78 O ANISOU 1041 O LYS B 18 5975 3965 7455 -292 -325 1202 O ATOM 1042 CB LYS B 18 29.379 24.421 -0.522 1.00 46.70 C ANISOU 1042 CB LYS B 18 6148 3814 7781 -551 -422 959 C ATOM 1043 CG LYS B 18 29.468 25.394 0.621 1.00 51.38 C ANISOU 1043 CG LYS B 18 6891 4186 8444 -587 -489 841 C ATOM 1044 CD LYS B 18 30.797 26.117 0.605 1.00 54.68 C ANISOU 1044 CD LYS B 18 7324 4469 8984 -807 -535 880 C ATOM 1045 CE LYS B 18 30.920 27.028 1.813 1.00 58.74 C ANISOU 1045 CE LYS B 18 8025 4754 9540 -877 -620 742 C ATOM 1046 NZ LYS B 18 29.785 27.996 1.906 1.00 66.71 N ANISOU 1046 NZ LYS B 18 9241 5559 10547 -714 -567 720 N ATOM 1047 N GLN B 19 28.543 21.826 -2.195 1.00 35.88 N ANISOU 1047 N GLN B 19 4559 2929 6143 -427 -301 1075 N ATOM 1048 CA GLN B 19 28.327 21.179 -3.483 1.00 34.14 C ANISOU 1048 CA GLN B 19 4315 2845 5810 -424 -233 1194 C ATOM 1049 C GLN B 19 26.919 20.572 -3.565 1.00 33.96 C ANISOU 1049 C GLN B 19 4295 2947 5662 -293 -262 1181 C ATOM 1050 O GLN B 19 26.291 20.627 -4.626 1.00 40.37 O ANISOU 1050 O GLN B 19 5142 3804 6392 -268 -259 1308 O ATOM 1051 CB GLN B 19 29.442 20.151 -3.734 1.00 31.72 C ANISOU 1051 CB GLN B 19 3917 2657 5478 -525 -151 1195 C ATOM 1052 CG GLN B 19 30.839 20.834 -4.050 1.00 33.13 C ANISOU 1052 CG GLN B 19 4065 2726 5798 -668 -103 1282 C ATOM 1053 CD GLN B 19 32.011 19.828 -4.095 1.00 40.99 C ANISOU 1053 CD GLN B 19 4929 3831 6813 -745 -8 1291 C ATOM 1054 OE1 GLN B 19 31.894 18.751 -4.675 1.00 37.14 O ANISOU 1054 OE1 GLN B 19 4431 3478 6202 -710 89 1307 O ATOM 1055 NE2 GLN B 19 33.133 20.179 -3.461 1.00 41.15 N ANISOU 1055 NE2 GLN B 19 4852 3787 6994 -853 -38 1288 N ATOM 1056 N LEU B 20 26.392 20.028 -2.448 1.00 30.45 N ANISOU 1056 N LEU B 20 3813 2557 5199 -217 -298 1042 N ATOM 1057 CA LEU B 20 25.012 19.521 -2.419 1.00 31.54 C ANISOU 1057 CA LEU B 20 3929 2807 5246 -98 -326 1039 C ATOM 1058 C LEU B 20 23.998 20.645 -2.542 1.00 39.75 C ANISOU 1058 C LEU B 20 5015 3736 6354 21 -364 1123 C ATOM 1059 O LEU B 20 22.936 20.442 -3.129 1.00 42.11 O ANISOU 1059 O LEU B 20 5280 4131 6589 91 -395 1220 O ATOM 1060 CB LEU B 20 24.742 18.727 -1.137 1.00 35.83 C ANISOU 1060 CB LEU B 20 4427 3421 5765 -46 -336 876 C ATOM 1061 CG LEU B 20 23.338 18.138 -0.860 1.00 34.84 C ANISOU 1061 CG LEU B 20 4257 3414 5569 71 -354 858 C ATOM 1062 CD1 LEU B 20 22.924 17.053 -1.851 1.00 29.00 C ANISOU 1062 CD1 LEU B 20 3476 2859 4685 25 -353 932 C ATOM 1063 CD2 LEU B 20 23.256 17.499 0.533 1.00 32.12 C ANISOU 1063 CD2 LEU B 20 3891 3101 5211 112 -345 692 C ATOM 1064 N ALA B 21 24.312 21.828 -2.004 1.00 42.48 N ANISOU 1064 N ALA B 21 5438 3873 6829 39 -364 1099 N ATOM 1065 CA ALA B 21 23.452 22.994 -2.198 1.00 46.22 C ANISOU 1065 CA ALA B 21 5973 4204 7387 163 -374 1199 C ATOM 1066 C ALA B 21 23.523 23.487 -3.634 1.00 45.87 C ANISOU 1066 C ALA B 21 5954 4145 7329 120 -383 1399 C ATOM 1067 O ALA B 21 22.493 23.790 -4.247 1.00 51.04 O ANISOU 1067 O ALA B 21 6592 4824 7975 226 -416 1542 O ATOM 1068 CB ALA B 21 23.845 24.113 -1.235 1.00 46.25 C ANISOU 1068 CB ALA B 21 6098 3957 7517 177 -356 1105 C ATOM 1069 N THR B 22 24.736 23.599 -4.185 1.00 48.50 N ANISOU 1069 N THR B 22 6323 4439 7666 -35 -354 1428 N ATOM 1070 CA THR B 22 24.876 23.991 -5.586 1.00 53.82 C ANISOU 1070 CA THR B 22 7043 5106 8302 -90 -346 1620 C ATOM 1071 C THR B 22 24.053 23.085 -6.488 1.00 59.82 C ANISOU 1071 C THR B 22 7757 6077 8894 -70 -381 1715 C ATOM 1072 O THR B 22 23.508 23.535 -7.505 1.00 62.11 O ANISOU 1072 O THR B 22 8091 6368 9141 -47 -420 1895 O ATOM 1073 CB THR B 22 26.348 23.935 -6.005 1.00 52.61 C ANISOU 1073 CB THR B 22 6906 4923 8161 -268 -278 1628 C ATOM 1074 OG1 THR B 22 27.074 24.980 -5.343 1.00 47.49 O ANISOU 1074 OG1 THR B 22 6312 4058 7675 -317 -273 1581 O ATOM 1075 CG2 THR B 22 26.490 24.090 -7.517 1.00 53.28 C ANISOU 1075 CG2 THR B 22 7051 5034 8160 -332 -243 1821 C ATOM 1076 N LYS B 23 23.950 21.808 -6.123 1.00 53.93 N ANISOU 1076 N LYS B 23 6938 5508 8047 -89 -377 1603 N ATOM 1077 CA LYS B 23 23.162 20.850 -6.879 1.00 56.84 C ANISOU 1077 CA LYS B 23 7280 6073 8242 -99 -421 1670 C ATOM 1078 C LYS B 23 21.686 20.883 -6.493 1.00 57.22 C ANISOU 1078 C LYS B 23 7247 6184 8310 46 -511 1703 C ATOM 1079 O LYS B 23 20.827 20.716 -7.365 1.00 64.34 O ANISOU 1079 O LYS B 23 8137 7195 9115 49 -594 1851 O ATOM 1080 CB LYS B 23 23.766 19.450 -6.685 1.00 51.91 C ANISOU 1080 CB LYS B 23 6631 5589 7506 -191 -359 1540 C ATOM 1081 CG LYS B 23 23.031 18.289 -7.338 1.00 55.67 C ANISOU 1081 CG LYS B 23 7110 6258 7784 -231 -396 1571 C ATOM 1082 CD LYS B 23 23.273 18.176 -8.833 1.00 55.51 C ANISOU 1082 CD LYS B 23 7215 6274 7602 -346 -378 1714 C ATOM 1083 CE LYS B 23 22.810 16.808 -9.361 1.00 52.50 C ANISOU 1083 CE LYS B 23 6881 6069 6996 -430 -392 1695 C ATOM 1084 NZ LYS B 23 22.607 16.803 -10.847 1.00 53.92 N ANISOU 1084 NZ LYS B 23 7213 6292 6980 -536 -426 1857 N ATOM 1085 N ALA B 24 21.360 21.136 -5.223 1.00 60.10 N ANISOU 1085 N ALA B 24 7559 6479 8798 162 -497 1584 N ATOM 1086 CA ALA B 24 19.956 21.176 -4.811 1.00 63.12 C ANISOU 1086 CA ALA B 24 7845 6916 9222 317 -549 1626 C ATOM 1087 C ALA B 24 19.204 22.366 -5.378 1.00 67.71 C ANISOU 1087 C ALA B 24 8430 7395 9901 435 -594 1827 C ATOM 1088 O ALA B 24 17.986 22.459 -5.179 1.00 70.14 O ANISOU 1088 O ALA B 24 8630 7755 10266 576 -634 1912 O ATOM 1089 CB ALA B 24 19.841 21.177 -3.285 1.00 63.36 C ANISOU 1089 CB ALA B 24 7849 6878 9349 419 -488 1445 C ATOM 1090 N ALA B 25 19.880 23.267 -6.076 1.00 70.27 N ANISOU 1090 N ALA B 25 8865 7575 10259 385 -582 1922 N ATOM 1091 CA ALA B 25 19.209 24.394 -6.697 1.00 75.51 C ANISOU 1091 CA ALA B 25 9545 8132 11012 497 -625 2135 C ATOM 1092 C ALA B 25 20.023 24.910 -7.881 1.00 79.46 C ANISOU 1092 C ALA B 25 10172 8562 11457 370 -631 2265 C ATOM 1093 O ALA B 25 20.633 24.126 -8.613 1.00 80.24 O ANISOU 1093 O ALA B 25 10309 8785 11392 205 -635 2261 O ATOM 1094 CB ALA B 25 18.978 25.494 -5.680 1.00 77.33 C ANISOU 1094 CB ALA B 25 9810 8129 11443 670 -549 2085 C TER 1095 ALA B 25 HETATM 1096 ZN ZN A 401 15.814 -5.559 12.716 1.00 21.56 ZN HETATM 1097 ZN ZN A 402 17.486 3.172 23.785 1.00 24.97 ZN HETATM 1098 ZN ZN A 403 25.144 8.083 -4.476 1.00 19.35 ZN HETATM 1099 ZN ZN A 404 18.078 12.220 8.658 1.00 18.06 ZN HETATM 1100 S SO4 A 405 32.557 -7.420 13.822 1.00 86.02 S HETATM 1101 O1 SO4 A 405 33.514 -6.413 13.376 1.00 89.75 O HETATM 1102 O2 SO4 A 405 31.726 -7.789 12.676 1.00 86.51 O HETATM 1103 O3 SO4 A 405 33.296 -8.574 14.334 1.00 84.52 O HETATM 1104 O4 SO4 A 405 31.720 -6.851 14.880 1.00 86.77 O HETATM 1105 S SO4 B 101 31.483 19.963 4.213 1.00 98.50 S HETATM 1106 O1 SO4 B 101 32.329 18.772 4.178 1.00101.43 O HETATM 1107 O2 SO4 B 101 31.773 20.791 3.045 1.00 99.35 O HETATM 1108 O3 SO4 B 101 31.754 20.712 5.436 1.00100.11 O HETATM 1109 O4 SO4 B 101 30.081 19.566 4.197 1.00 98.43 O HETATM 1110 O HOH A 501 11.801 11.465 14.407 1.00 62.32 O HETATM 1111 O HOH A 502 11.675 7.634 -8.214 1.00 47.68 O HETATM 1112 O HOH A 503 10.980 7.992 15.221 1.00 40.81 O HETATM 1113 O HOH A 504 11.308 16.031 10.256 1.00 47.57 O HETATM 1114 O HOH A 505 11.615 -6.088 26.143 1.00 65.46 O HETATM 1115 O HOH A 506 24.912 -2.001 27.842 1.00 49.36 O HETATM 1116 O HOH A 507 26.149 10.330 17.648 1.00 39.96 O HETATM 1117 O HOH A 508 23.058 -9.679 -0.215 1.00 45.37 O HETATM 1118 O HOH A 509 10.429 21.150 -3.338 1.00 45.37 O HETATM 1119 O HOH A 510 16.268 5.031 -10.997 1.00 34.22 O HETATM 1120 O HOH A 511 14.582 7.730 -6.210 1.00 24.82 O HETATM 1121 O HOH A 512 26.812 4.318 -6.052 1.00 25.20 O HETATM 1122 O HOH A 513 24.878 -4.441 7.264 1.00 40.49 O HETATM 1123 O HOH A 514 12.479 17.940 -2.633 1.00 31.54 O HETATM 1124 O HOH A 515 10.780 14.350 12.308 1.00 38.41 O HETATM 1125 O HOH A 516 11.501 15.192 -3.584 1.00 32.57 O HETATM 1126 O HOH A 517 19.204 11.503 26.765 1.00 29.14 O HETATM 1127 O HOH A 518 23.100 14.578 3.953 1.00 53.25 O HETATM 1128 O HOH A 519 24.632 1.110 22.473 1.00 30.04 O HETATM 1129 O HOH A 520 15.343 2.843 15.223 1.00 17.68 O HETATM 1130 O HOH A 521 12.641 -9.275 23.257 1.00 52.37 O HETATM 1131 O HOH A 522 10.153 -2.588 0.159 1.00 40.10 O HETATM 1132 O HOH A 523 13.800 -3.526 24.261 1.00 37.38 O HETATM 1133 O HOH A 524 22.369 3.154 8.804 1.00 25.46 O HETATM 1134 O HOH A 525 13.249 18.013 3.655 1.00 36.83 O HETATM 1135 O HOH A 526 17.056 -5.338 19.672 1.00 30.26 O HETATM 1136 O HOH A 527 25.452 -1.911 -1.590 1.00 37.06 O HETATM 1137 O HOH A 528 24.839 -4.548 13.232 1.00 23.25 O HETATM 1138 O HOH A 529 12.510 6.608 5.087 1.00 21.90 O HETATM 1139 O HOH A 530 27.340 -8.977 23.086 1.00 27.21 O HETATM 1140 O HOH A 531 12.700 5.659 17.728 1.00 37.78 O HETATM 1141 O HOH A 532 23.902 12.679 15.434 1.00 46.11 O HETATM 1142 O HOH A 533 14.706 3.879 12.733 1.00 20.41 O HETATM 1143 O HOH A 534 25.995 -10.528 16.203 1.00 23.71 O HETATM 1144 O HOH A 535 13.124 9.615 -2.207 1.00 27.96 O HETATM 1145 O HOH A 536 20.342 14.303 0.097 1.00 20.97 O HETATM 1146 O HOH A 537 19.651 -8.473 22.759 1.00 36.25 O HETATM 1147 O HOH A 538 11.330 6.098 12.101 1.00 22.91 O HETATM 1148 O HOH A 539 11.618 2.913 15.201 1.00 36.04 O HETATM 1149 O HOH A 540 23.378 5.174 -17.569 1.00 54.71 O HETATM 1150 O HOH A 541 12.636 2.390 11.135 1.00 27.76 O HETATM 1151 O HOH A 542 21.409 -9.588 29.375 1.00 30.86 O HETATM 1152 O HOH A 543 21.691 -8.634 3.711 1.00 39.59 O HETATM 1153 O HOH A 544 31.060 8.540 0.303 1.00 19.80 O HETATM 1154 O HOH A 545 15.386 11.680 14.661 1.00 29.16 O HETATM 1155 O HOH A 546 31.414 11.842 -0.775 1.00 21.35 O HETATM 1156 O HOH A 547 17.380 1.589 -4.909 1.00 28.95 O HETATM 1157 O HOH A 548 17.071 -7.570 5.338 1.00 33.78 O HETATM 1158 O HOH A 549 14.678 1.179 9.326 1.00 20.17 O HETATM 1159 O HOH A 550 14.533 -8.164 2.023 1.00 35.34 O HETATM 1160 O HOH A 551 28.339 -0.411 -2.617 1.00 42.36 O HETATM 1161 O HOH A 552 11.863 11.623 3.418 1.00 21.30 O HETATM 1162 O HOH A 553 25.219 3.468 5.601 1.00 21.74 O HETATM 1163 O HOH A 554 25.584 2.142 24.888 1.00 59.15 O HETATM 1164 O HOH A 555 22.889 -6.187 5.944 1.00 31.15 O HETATM 1165 O HOH A 556 26.572 11.517 8.794 1.00 28.55 O HETATM 1166 O HOH A 557 22.832 -1.003 -5.932 1.00 44.04 O HETATM 1167 O HOH A 558 16.575 11.753 -7.878 1.00 25.82 O HETATM 1168 O HOH A 559 27.436 -5.750 10.353 1.00 31.93 O HETATM 1169 O HOH A 560 18.846 -9.468 19.037 1.00 39.21 O HETATM 1170 O HOH A 561 15.956 3.404 10.402 1.00 19.02 O HETATM 1171 O HOH A 562 19.365 7.674 26.050 1.00 47.68 O HETATM 1172 O HOH A 563 19.450 -0.258 -5.200 1.00 27.19 O HETATM 1173 O HOH A 564 26.179 0.137 5.417 1.00 36.27 O HETATM 1174 O HOH A 565 13.137 7.537 -3.723 1.00 30.31 O HETATM 1175 O HOH A 566 12.551 1.793 -5.208 1.00 51.57 O HETATM 1176 O HOH A 567 5.633 7.072 8.529 1.00 34.02 O HETATM 1177 O HOH A 568 21.936 -2.783 -2.970 1.00 31.77 O HETATM 1178 O HOH A 569 15.105 -2.175 -3.869 1.00 37.28 O HETATM 1179 O HOH A 570 27.036 -4.138 1.631 1.00 56.25 O HETATM 1180 O HOH A 571 29.631 -9.940 22.280 1.00 28.72 O HETATM 1181 O HOH A 572 27.514 9.343 21.682 1.00 38.53 O HETATM 1182 O HOH A 573 23.777 -4.410 4.127 1.00 25.93 O HETATM 1183 O HOH A 574 12.223 4.295 3.441 1.00 24.99 O HETATM 1184 O HOH A 575 11.995 10.236 18.940 1.00 55.63 O HETATM 1185 O HOH A 576 21.496 10.147 27.613 1.00 37.50 O HETATM 1186 O HOH A 577 21.018 0.138 -9.811 1.00 47.81 O HETATM 1187 O HOH A 578 25.261 12.489 21.889 1.00 28.72 O HETATM 1188 O HOH A 579 29.641 3.692 -3.105 1.00 27.69 O HETATM 1189 O HOH A 580 9.906 -5.807 3.497 1.00 41.90 O HETATM 1190 O HOH A 581 28.156 -3.126 3.864 1.00 54.37 O HETATM 1191 O HOH A 582 35.137 -5.121 32.156 1.00 38.32 O HETATM 1192 O HOH A 583 17.191 -4.009 -3.405 1.00 34.04 O HETATM 1193 O HOH A 584 12.914 4.498 -1.551 1.00 37.49 O HETATM 1194 O HOH A 585 9.917 18.584 4.925 1.00 29.31 O HETATM 1195 O HOH A 586 12.554 5.679 14.732 1.00 32.85 O HETATM 1196 O HOH A 587 16.780 1.175 -8.352 1.00 28.77 O HETATM 1197 O HOH A 588 8.612 20.362 3.003 1.00 35.99 O HETATM 1198 O HOH A 589 8.332 -4.334 10.971 1.00 40.82 O HETATM 1199 O HOH A 590 19.863 -8.510 5.620 1.00 46.02 O HETATM 1200 O HOH A 591 12.853 9.566 24.420 1.00 54.00 O HETATM 1201 O HOH A 592 21.861 13.444 16.030 1.00 32.40 O HETATM 1202 O HOH A 593 21.562 -9.714 20.617 1.00 37.48 O HETATM 1203 O HOH A 594 32.857 -6.746 21.595 1.00 47.03 O HETATM 1204 O HOH A 595 25.069 -2.379 5.572 1.00 34.34 O HETATM 1205 O HOH A 596 22.898 12.762 -11.595 1.00 37.56 O HETATM 1206 O HOH A 597 18.094 -7.526 20.906 1.00 31.61 O HETATM 1207 O HOH A 598 24.903 -9.048 27.982 1.00 32.06 O HETATM 1208 O HOH A 599 9.792 0.445 15.962 1.00 47.16 O HETATM 1209 O HOH A 600 9.585 14.690 9.661 1.00 62.59 O HETATM 1210 O HOH A 601 11.374 -2.348 23.219 1.00 48.32 O HETATM 1211 O HOH A 602 14.528 0.311 -7.340 1.00 50.01 O HETATM 1212 O HOH A 603 32.130 7.627 -8.842 1.00 39.52 O HETATM 1213 O HOH A 604 12.088 7.516 0.860 1.00 33.42 O HETATM 1214 O HOH A 605 13.056 5.431 1.085 1.00 33.99 O HETATM 1215 O HOH A 606 10.858 11.893 -8.291 1.00 99.82 O HETATM 1216 O HOH A 607 12.757 11.442 -7.790 1.00 68.14 O HETATM 1217 O HOH A 608 12.178 10.204 15.825 1.00 72.93 O HETATM 1218 O HOH A 609 10.752 8.974 2.878 1.00 27.38 O HETATM 1219 O HOH A 610 16.676 -8.330 -2.709 1.00 49.19 O HETATM 1220 O HOH A 611 23.193 12.463 19.406 1.00 33.49 O HETATM 1221 O HOH A 612 27.219 -9.427 25.872 1.00 28.60 O HETATM 1222 O HOH A 613 38.197 -13.057 16.467 1.00 53.38 O HETATM 1223 O HOH A 614 30.078 -10.331 9.274 1.00 56.11 O HETATM 1224 O HOH A 615 8.862 -0.778 17.568 1.00 53.14 O HETATM 1225 O HOH A 616 21.824 10.901 30.390 1.00 46.59 O HETATM 1226 O HOH A 617 19.684 -2.778 -4.050 1.00 34.13 O HETATM 1227 O HOH A 618 16.419 2.329 -11.127 1.00 39.73 O HETATM 1228 O HOH A 619 29.067 2.566 -5.673 1.00 37.79 O HETATM 1229 O HOH A 620 27.794 -4.620 7.988 1.00 51.27 O HETATM 1230 O HOH A 621 23.575 18.700 3.917 1.00 58.88 O HETATM 1231 O HOH A 622 26.124 -5.632 3.076 1.00 50.94 O HETATM 1232 O HOH A 623 8.793 -4.966 0.836 1.00 43.35 O HETATM 1233 O HOH A 624 16.416 -6.323 -4.596 1.00 41.24 O HETATM 1234 O HOH A 625 15.349 -9.088 5.018 1.00 48.00 O HETATM 1235 O HOH A 626 13.757 11.601 -4.044 1.00 33.06 O HETATM 1236 O HOH A 627 33.542 -8.542 24.029 1.00 44.71 O HETATM 1237 O HOH A 628 33.259 5.624 -7.531 1.00 37.46 O HETATM 1238 O HOH A 629 17.843 5.612 26.897 1.00 39.49 O HETATM 1239 O HOH A 630 17.328 14.108 12.598 1.00 66.77 O HETATM 1240 O HOH A 631 14.688 19.273 -2.941 1.00 49.61 O HETATM 1241 O HOH A 632 15.540 13.173 -9.956 1.00 42.63 O HETATM 1242 O HOH A 633 31.401 2.575 -6.836 1.00 50.69 O HETATM 1243 O HOH A 634 22.883 4.713 6.470 1.00 20.97 O HETATM 1244 O HOH A 635 25.192 16.592 3.535 1.00 35.69 O HETATM 1245 O HOH A 636 15.868 13.939 13.609 1.00 30.83 O HETATM 1246 O HOH A 637 14.920 -9.182 -0.616 1.00 38.22 O HETATM 1247 O HOH A 638 18.665 -0.856 -7.754 1.00 42.44 O HETATM 1248 O HOH A 639 14.521 10.656 -6.569 1.00 25.59 O HETATM 1249 O HOH A 640 11.872 -8.151 2.624 1.00 46.35 O HETATM 1250 O HOH A 641 34.654 8.683 -16.176 1.00 49.02 O HETATM 1251 O HOH A 642 18.924 -11.594 3.771 1.00 63.09 O HETATM 1252 O HOH A 643 15.530 -11.023 3.309 1.00 55.84 O HETATM 1253 O HOH A 644 20.093 -4.013 -6.258 1.00 41.02 O HETATM 1254 O HOH A 645 17.466 -3.036 -7.800 1.00 57.42 O HETATM 1255 O HOH B 201 30.713 22.609 1.960 1.00 37.58 O HETATM 1256 O HOH B 202 29.257 25.110 -4.389 1.00 49.75 O HETATM 1257 O HOH B 203 30.289 -0.156 10.551 1.00 31.95 O HETATM 1258 O HOH B 204 30.780 18.511 -7.030 1.00 42.81 O HETATM 1259 O HOH B 205 33.018 14.262 3.958 1.00 40.67 O HETATM 1260 O HOH B 206 32.962 7.497 13.212 1.00 38.86 O HETATM 1261 O HOH B 207 30.845 2.331 18.258 1.00 35.36 O HETATM 1262 O HOH B 208 29.085 17.047 4.327 1.00 32.30 O HETATM 1263 O HOH B 209 29.541 6.116 0.347 1.00 20.64 O HETATM 1264 O HOH B 210 22.890 10.617 17.164 1.00 31.88 O HETATM 1265 O HOH B 211 35.715 6.280 5.474 1.00 35.46 O HETATM 1266 O HOH B 212 33.696 16.656 -4.781 1.00 25.28 O HETATM 1267 O HOH B 213 26.420 16.081 1.029 1.00 23.21 O HETATM 1268 O HOH B 214 29.340 8.508 6.488 1.00 24.70 O HETATM 1269 O HOH B 215 22.405 7.468 6.584 1.00 18.65 O HETATM 1270 O HOH B 216 26.618 26.327 -2.760 1.00 45.30 O HETATM 1271 O HOH B 217 33.018 8.916 6.870 1.00 40.64 O HETATM 1272 O HOH B 218 25.830 1.169 7.257 1.00 35.10 O HETATM 1273 O HOH B 219 30.363 12.854 6.247 1.00 31.62 O HETATM 1274 O HOH B 220 33.837 1.243 10.470 1.00 34.43 O HETATM 1275 O HOH B 221 23.834 10.690 8.126 1.00 19.62 O HETATM 1276 O HOH B 222 32.228 9.604 14.432 1.00 53.46 O HETATM 1277 O HOH B 223 23.840 20.939 1.849 1.00 41.86 O HETATM 1278 O HOH B 224 27.651 24.483 5.882 1.00 56.13 O HETATM 1279 O HOH B 225 33.093 13.974 -0.624 1.00 27.20 O HETATM 1280 O HOH B 226 35.744 10.568 4.582 1.00 41.28 O HETATM 1281 O HOH B 227 33.578 8.704 10.476 1.00 44.40 O HETATM 1282 O HOH B 228 34.553 14.938 1.120 1.00 33.13 O HETATM 1283 O HOH B 229 30.208 24.016 4.081 1.00 53.71 O HETATM 1284 O HOH B 230 35.381 1.206 8.226 1.00 38.57 O HETATM 1285 O HOH B 231 22.233 12.950 7.772 1.00 26.14 O HETATM 1286 O HOH B 232 29.445 -2.534 7.956 1.00 45.31 O HETATM 1287 O HOH B 233 31.924 25.721 4.456 1.00 62.68 O HETATM 1288 O HOH B 234 30.879 15.474 6.269 1.00 41.73 O HETATM 1289 O HOH B 235 35.670 8.476 6.477 1.00 39.57 O HETATM 1290 O HOH B 236 33.704 -1.270 11.119 1.00 47.00 O HETATM 1291 O HOH B 237 31.809 11.083 8.888 1.00 39.08 O HETATM 1292 O HOH B 238 25.893 26.712 0.042 1.00 47.90 O HETATM 1293 O HOH B 239 33.895 12.799 6.104 1.00 50.82 O HETATM 1294 O HOH B 240 29.019 10.949 7.798 1.00 30.21 O HETATM 1295 O HOH B 241 24.956 25.526 6.514 1.00 53.40 O HETATM 1296 O HOH B 242 35.236 1.509 12.952 1.00 41.53 O CONECT 99 1098 CONECT 122 1098 CONECT 267 1099 CONECT 286 1099 CONECT 315 1098 CONECT 337 1098 CONECT 489 1099 CONECT 512 1099 CONECT 534 1097 CONECT 552 1097 CONECT 655 1096 CONECT 675 1096 CONECT 716 1097 CONECT 742 1097 CONECT 865 1096 CONECT 888 1096 CONECT 1000 1003 CONECT 1002 1004 1005 1015 CONECT 1003 1000 1005 CONECT 1004 1002 CONECT 1005 1002 1003 1006 CONECT 1006 1005 1009 CONECT 1007 1008 1009 CONECT 1008 1007 1010 CONECT 1009 1006 1007 CONECT 1010 1008 1014 CONECT 1011 1013 CONECT 1012 1014 CONECT 1013 1011 1014 CONECT 1014 1010 1012 1013 CONECT 1015 1002 CONECT 1096 655 675 865 888 CONECT 1097 534 552 716 742 CONECT 1098 99 122 315 337 CONECT 1099 267 286 489 512 CONECT 1100 1101 1102 1103 1104 CONECT 1101 1100 CONECT 1102 1100 CONECT 1103 1100 CONECT 1104 1100 CONECT 1105 1106 1107 1108 1109 CONECT 1106 1105 CONECT 1107 1105 CONECT 1108 1105 CONECT 1109 1105 MASTER 383 0 7 6 5 0 6 6 1289 2 45 13 END
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Related entries of code: 5b77
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
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Protein Sequence Similarity
3v43
RCSB PDB
PDBbind
112aa, >3V43_1|Chain... at 98%
5b75
RCSB PDB
PDBbind
131aa, >5B75_1|Chain... *
5b76
RCSB PDB
PDBbind
131aa, >5B76_1|Chain... at 100%
5b78
RCSB PDB
PDBbind
131aa, >5B78_1|Chain... at 98%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
5b77
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
MOZ double PHD finger, MOZDPF
Ligand Name
histone H3 propionylation at K14, H3(1-25)K14pr
EC.Number
E.C.2.3.1.48
Resolution
1.55(Å)
Affinity (Kd/Ki/IC50)
Kd=10.8uM
Release Year
2016
Protein/NA Sequence
Check fasta file
Primary Reference
(2016) Nat.Chem.Biol. Vol. 12: pp. 1111-1118
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):
Q92794
K7EMV3
Entrez Gene ID
NCBI Entrez Gene ID:
7994
ASD
Information of known allosteric effects of PDB entries
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