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test.pdb
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test.pdb
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HEADER VIRAL PROTEIN/HYDROLASE 21-FEB-20 6M0J
TITLE CRYSTAL STRUCTURE OF 2019-NCOV SPIKE RECEPTOR-BINDING DOMAIN BOUND
TITLE 2 WITH ACE2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACE-RELATED CARBOXYPEPTIDASE,ANGIOTENSIN-CONVERTING ENZYME
COMPND 5 HOMOLOG,ACEH,METALLOPROTEASE MPROT15;
COMPND 6 EC: 3.4.17.23;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 2019-NCOV RECEPTOR-BINDING DOMAIN;
COMPND 10 CHAIN: E;
COMPND 11 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: ACE2, UNQ868/PRO1885;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 10 2;
SOURCE 11 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2;
SOURCE 12 ORGANISM_TAXID: 2697049;
SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS SPIKE, RECEPTOR BINDING, VIRAL PROTEIN-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.WANG,J.LAN,J.GE,J.YU,S.SHAN
REVDAT 1 18-MAR-20 6M0J 0
JRNL AUTH X.WANG
JRNL TITL CRYSTAL STRUCTURE OF 2019-NCOV SPIKE RECEPTOR-BINDING DOMAIN
JRNL TITL 2 BOUND WITH ACE2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 47555
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2426
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 53.1000 - 6.2965 0.99 2877 160 0.1746 0.2312
REMARK 3 2 6.2965 - 4.9989 1.00 2725 163 0.1838 0.2013
REMARK 3 3 4.9989 - 4.3674 1.00 2676 156 0.1495 0.1925
REMARK 3 4 4.3674 - 3.9682 1.00 2691 148 0.1655 0.2034
REMARK 3 5 3.9682 - 3.6838 1.00 2674 133 0.1853 0.2157
REMARK 3 6 3.6838 - 3.4667 1.00 2665 132 0.2100 0.2611
REMARK 3 7 3.4667 - 3.2931 1.00 2637 138 0.2196 0.2507
REMARK 3 8 3.2931 - 3.1498 1.00 2619 159 0.2313 0.2704
REMARK 3 9 3.1498 - 3.0285 1.00 2644 135 0.2316 0.3022
REMARK 3 10 3.0285 - 2.9240 1.00 2622 124 0.2324 0.2737
REMARK 3 11 2.9240 - 2.8326 1.00 2630 138 0.2368 0.2840
REMARK 3 12 2.8326 - 2.7516 1.00 2612 141 0.2315 0.2491
REMARK 3 13 2.7516 - 2.6792 1.00 2620 148 0.2453 0.2893
REMARK 3 14 2.6792 - 2.6138 1.00 2615 140 0.2488 0.3438
REMARK 3 15 2.6138 - 2.5544 1.00 2600 133 0.2695 0.3352
REMARK 3 16 2.5544 - 2.5001 1.00 2606 141 0.2908 0.3840
REMARK 3 17 2.5001 - 2.4501 1.00 2616 137 0.2806 0.3210
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.83
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6M0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-20.
REMARK 100 THE DEPOSITION ID IS D_1300015820.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-20
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) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47679
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 95.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 26.10
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.75000
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: 2AJF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, PEG5000MME, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.36000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.33500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.33500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.18000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.33500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.33500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 171.54000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.33500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.33500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.18000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.33500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.33500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 171.54000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 114.36000
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: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 HIS A 616
REMARK 465 HIS A 617
REMARK 465 HIS A 618
REMARK 465 HIS A 619
REMARK 465 HIS A 620
REMARK 465 HIS A 621
REMARK 465 ARG E 319
REMARK 465 VAL E 320
REMARK 465 GLN E 321
REMARK 465 PRO E 322
REMARK 465 THR E 323
REMARK 465 GLU E 324
REMARK 465 SER E 325
REMARK 465 ILE E 326
REMARK 465 VAL E 327
REMARK 465 ARG E 328
REMARK 465 PHE E 329
REMARK 465 PRO E 330
REMARK 465 ASN E 331
REMARK 465 ILE E 332
REMARK 465 PRO E 527
REMARK 465 LYS E 528
REMARK 465 LYS E 529
REMARK 465 SER E 530
REMARK 465 THR E 531
REMARK 465 ASN E 532
REMARK 465 LEU E 533
REMARK 465 VAL E 534
REMARK 465 LYS E 535
REMARK 465 ASN E 536
REMARK 465 LYS E 537
REMARK 465 CYS E 538
REMARK 465 VAL E 539
REMARK 465 ASN E 540
REMARK 465 PHE E 541
REMARK 465 HIS E 542
REMARK 465 HIS E 543
REMARK 465 HIS E 544
REMARK 465 HIS E 545
REMARK 465 HIS E 546
REMARK 465 HIS E 547
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 ND1 HIS A 540 O HOH A 1001 2.00
REMARK 500 O GLY A 130 O HOH A 1002 2.11
REMARK 500 OD1 ASN A 121 O HOH A 1003 2.12
REMARK 500 NE ARG A 245 O HOH A 1004 2.13
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 ASN A 53 81.71 -160.11
REMARK 500 SER A 106 0.55 -59.43
REMARK 500 PRO A 138 37.09 -69.86
REMARK 500 GLN A 139 -3.38 -155.67
REMARK 500 HIS A 195 31.84 70.10
REMARK 500 ASP A 198 -178.29 -170.86
REMARK 500 ASP A 427 28.58 -73.74
REMARK 500 ALA E 352 51.27 -116.87
REMARK 500 PHE E 377 75.25 -160.04
REMARK 500 SER E 383 137.23 -38.94
REMARK 500 ASP E 389 72.32 -103.72
REMARK 500 ASN E 422 -54.57 -126.52
REMARK 500 PHE E 464 17.08 56.59
REMARK 500 LEU E 518 -149.42 -143.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 378 NE2
REMARK 620 2 GLU A 402 OE1 82.4
REMARK 620 N 1
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 902 bound
REMARK 800 to ASN A 90
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 904 bound
REMARK 800 to ASN A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 903 bound
REMARK 800 to ASN A 546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG E 601 bound
REMARK 800 to ASN E 343
DBREF 6M0J A 19 615 UNP Q9BYF1 ACE2_HUMAN 19 615
DBREF 6M0J E 319 547 PDB 6M0J 6M0J 319 547
SEQADV 6M0J HIS A 616 UNP Q9BYF1 EXPRESSION TAG
SEQADV 6M0J HIS A 617 UNP Q9BYF1 EXPRESSION TAG
SEQADV 6M0J HIS A 618 UNP Q9BYF1 EXPRESSION TAG
SEQADV 6M0J HIS A 619 UNP Q9BYF1 EXPRESSION TAG
SEQADV 6M0J HIS A 620 UNP Q9BYF1 EXPRESSION TAG
SEQADV 6M0J HIS A 621 UNP Q9BYF1 EXPRESSION TAG
SEQRES 1 A 603 SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS
SEQRES 2 A 603 PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER
SEQRES 3 A 603 LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU
SEQRES 4 A 603 ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER
SEQRES 5 A 603 ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR
SEQRES 6 A 603 PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN
SEQRES 7 A 603 LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER
SEQRES 8 A 603 GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR
SEQRES 9 A 603 MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO
SEQRES 10 A 603 ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU
SEQRES 11 A 603 ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG
SEQRES 12 A 603 LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS
SEQRES 13 A 603 GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS
SEQRES 14 A 603 ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY
SEQRES 15 A 603 ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP
SEQRES 16 A 603 GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL
SEQRES 17 A 603 GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS
SEQRES 18 A 603 LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR
SEQRES 19 A 603 PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS
SEQRES 20 A 603 LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU
SEQRES 21 A 603 TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE
SEQRES 22 A 603 ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA
SEQRES 23 A 603 GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER
SEQRES 24 A 603 VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN
SEQRES 25 A 603 SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL
SEQRES 26 A 603 CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE
SEQRES 27 A 603 ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE
SEQRES 28 A 603 LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP
SEQRES 29 A 603 MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY
SEQRES 30 A 603 ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET
SEQRES 31 A 603 SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE
SEQRES 32 A 603 GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR
SEQRES 33 A 603 GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL
SEQRES 34 A 603 GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG
SEQRES 35 A 603 TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP
SEQRES 36 A 603 MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY
SEQRES 37 A 603 VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP
SEQRES 38 A 603 PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE
SEQRES 39 A 603 ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE
SEQRES 40 A 603 GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO
SEQRES 41 A 603 LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY
SEQRES 42 A 603 GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU
SEQRES 43 A 603 PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS
SEQRES 44 A 603 ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO
SEQRES 45 A 603 LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE
SEQRES 46 A 603 VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA ASP HIS
SEQRES 47 A 603 HIS HIS HIS HIS HIS
SEQRES 1 E 229 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN
SEQRES 2 E 229 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA
SEQRES 3 E 229 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG
SEQRES 4 E 229 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN
SEQRES 5 E 229 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER
SEQRES 6 E 229 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR
SEQRES 7 E 229 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN
SEQRES 8 E 229 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN
SEQRES 9 E 229 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA
SEQRES 10 E 229 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN
SEQRES 11 E 229 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU
SEQRES 12 E 229 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN
SEQRES 13 E 229 ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN
SEQRES 14 E 229 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR
SEQRES 15 E 229 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU
SEQRES 16 E 229 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY
SEQRES 17 E 229 PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL
SEQRES 18 E 229 ASN PHE HIS HIS HIS HIS HIS HIS
HET ZN A 901 1
HET NAG A 902 14
HET NAG A 903 14
HET NAG A 904 14
HET NAG E 601 14
HETNAM ZN ZINC ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 ZN ZN 2+
FORMUL 4 NAG 4(C8 H15 N O6)
FORMUL 8 HOH *80(H2 O)
HELIX 1 AA1 THR A 20 ASN A 53 1 34
HELIX 2 AA2 THR A 55 GLN A 81 1 27
HELIX 3 AA3 MET A 82 TYR A 83 5 2
HELIX 4 AA4 PRO A 84 ILE A 88 5 5
HELIX 5 AA5 ASN A 90 GLN A 101 1 12
HELIX 6 AA6 ASN A 103 LEU A 108 5 6
HELIX 7 AA7 SER A 109 GLY A 130 1 22
HELIX 8 AA8 PRO A 146 SER A 155 1 10
HELIX 9 AA9 ASP A 157 VAL A 172 1 16
HELIX 10 AB1 VAL A 172 ASN A 194 1 23
HELIX 11 AB2 ASP A 198 GLY A 205 1 8
HELIX 12 AB3 ASP A 206 GLU A 208 5 3
HELIX 13 AB4 SER A 218 GLU A 232 1 15
HELIX 14 AB5 ILE A 233 TYR A 252 1 20
HELIX 15 AB6 HIS A 265 LEU A 267 5 3
HELIX 16 AB7 TRP A 275 ASN A 277 5 3
HELIX 17 AB8 LEU A 278 VAL A 283 1 6
HELIX 18 AB9 VAL A 293 GLN A 300 1 8
HELIX 19 AC1 ASP A 303 VAL A 318 1 16
HELIX 20 AC2 THR A 324 SER A 331 1 8
HELIX 21 AC3 THR A 365 TYR A 385 1 21
HELIX 22 AC4 PRO A 389 ARG A 393 5 5
HELIX 23 AC5 GLY A 399 THR A 414 1 16
HELIX 24 AC6 THR A 414 ILE A 421 1 8
HELIX 25 AC7 ASP A 431 VAL A 447 1 17
HELIX 26 AC8 GLY A 448 LYS A 465 1 18
HELIX 27 AC9 PRO A 469 ASP A 471 5 3
HELIX 28 AD1 GLN A 472 ILE A 484 1 13
HELIX 29 AD2 CYS A 498 SER A 502 5 5
HELIX 30 AD3 LEU A 503 ASN A 508 1 6
HELIX 31 AD4 ILE A 513 ALA A 533 1 21
HELIX 32 AD5 PRO A 538 CYS A 542 5 5
HELIX 33 AD6 SER A 547 ARG A 559 1 13
HELIX 34 AD7 PRO A 565 GLY A 575 1 11
HELIX 35 AD8 VAL A 581 ASN A 599 1 19
HELIX 36 AD9 LYS A 600 SER A 602 5 3
HELIX 37 AE1 PHE E 338 ASN E 343 1 6
HELIX 38 AE2 SER E 349 TRP E 353 5 5
HELIX 39 AE3 ASP E 364 ASN E 370 1 7
HELIX 40 AE4 SER E 383 ASN E 388 1 6
HELIX 41 AE5 ASP E 405 ILE E 410 5 6
HELIX 42 AE6 GLY E 416 ASN E 422 1 7
HELIX 43 AE7 SER E 438 SER E 443 1 6
HELIX 44 AE8 GLY E 502 TYR E 505 5 4
SHEET 1 AA1 2 LYS A 131 CYS A 133 0
SHEET 2 AA1 2 CYS A 141 LEU A 143 -1 O LEU A 142 N VAL A 132
SHEET 1 AA2 2 LEU A 262 PRO A 263 0
SHEET 2 AA2 2 VAL A 487 VAL A 488 1 O VAL A 488 N LEU A 262
SHEET 1 AA3 2 THR A 347 GLY A 352 0
SHEET 2 AA3 2 ASP A 355 LEU A 359 -1 O ARG A 357 N TRP A 349
SHEET 1 AA4 5 ASN E 354 ILE E 358 0
SHEET 2 AA4 5 ASN E 394 ARG E 403 -1 O VAL E 395 N ILE E 358
SHEET 3 AA4 5 PRO E 507 GLU E 516 -1 O VAL E 512 N ASP E 398
SHEET 4 AA4 5 CYS E 432 ASN E 437 -1 N ILE E 434 O VAL E 511
SHEET 5 AA4 5 THR E 376 CYS E 379 -1 N LYS E 378 O VAL E 433
SHEET 1 AA5 2 CYS E 361 VAL E 362 0
SHEET 2 AA5 2 VAL E 524 CYS E 525 1 O CYS E 525 N CYS E 361
SHEET 1 AA6 2 LEU E 452 ARG E 454 0
SHEET 2 AA6 2 LEU E 492 SER E 494 -1 O GLN E 493 N TYR E 453
SHEET 1 AA7 2 TYR E 473 GLN E 474 0
SHEET 2 AA7 2 CYS E 488 TYR E 489 -1 O TYR E 489 N TYR E 473
SSBOND 1 CYS A 133 CYS A 141 1555 1555 2.05
SSBOND 2 CYS A 344 CYS A 361 1555 1555 2.05
SSBOND 3 CYS A 530 CYS A 542 1555 1555 2.02
SSBOND 4 CYS E 336 CYS E 361 1555 1555 2.04
SSBOND 5 CYS E 379 CYS E 432 1555 1555 2.05
SSBOND 6 CYS E 391 CYS E 525 1555 1555 2.04
SSBOND 7 CYS E 480 CYS E 488 1555 1555 2.06
LINK ND2 ASN A 90 C1 NAG A 902 1555 1555 1.45
LINK ND2 ASN A 322 C1 NAG A 904 1555 1555 1.45
LINK NE2 HIS A 378 ZN ZN A 901 1555 1555 2.29
LINK OE1 GLU A 402 ZN ZN A 901 1555 1555 2.08
LINK ND2 ASN A 546 C1 NAG A 903 1555 1555 1.45
LINK ND2 ASN E 343 C1 NAG E 601 1555 1555 1.45
CISPEP 1 GLU A 145 PRO A 146 0 6.12
SITE 1 AC1 4 HIS A 374 GLU A 375 HIS A 378 GLU A 402
SITE 1 AC2 2 LYS A 26 ASN A 90
SITE 1 AC3 1 ASN A 322
SITE 1 AC4 2 SER A 420 ASN A 546
SITE 1 AC5 2 GLY E 339 ASN E 343
CRYST1 104.670 104.670 228.720 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009554 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004372 0.00000
ATOM 1 N SER A 19 -31.582 49.526 2.485 1.00 76.82 N
ATOM 2 CA SER A 19 -31.419 50.898 2.017 1.00 82.31 C
ATOM 3 C SER A 19 -31.115 50.917 0.529 1.00 82.97 C
ATOM 4 O SER A 19 -31.982 51.268 -0.273 1.00 87.50 O
ATOM 5 CB SER A 19 -30.312 51.628 2.791 1.00 79.38 C
ATOM 6 OG SER A 19 -30.868 52.517 3.747 1.00 94.98 O
ATOM 7 N THR A 20 -29.890 50.537 0.159 1.00 82.57 N
ATOM 8 CA THR A 20 -29.485 50.566 -1.243 1.00 77.87 C
ATOM 9 C THR A 20 -30.258 49.521 -2.042 1.00 76.03 C
ATOM 10 O THR A 20 -30.945 48.660 -1.491 1.00 81.26 O
ATOM 11 CB THR A 20 -27.987 50.300 -1.393 1.00 76.68 C
ATOM 12 OG1 THR A 20 -27.749 48.892 -1.297 1.00 78.19 O
ATOM 13 CG2 THR A 20 -27.199 51.008 -0.307 1.00 77.81 C
ATOM 14 N ILE A 21 -30.117 49.583 -3.365 1.00 79.49 N
ATOM 15 CA ILE A 21 -30.789 48.600 -4.208 1.00 77.44 C
ATOM 16 C ILE A 21 -30.106 47.236 -4.100 1.00 77.36 C
ATOM 17 O ILE A 21 -30.774 46.196 -4.103 1.00 75.38 O
ATOM 18 CB ILE A 21 -30.861 49.106 -5.659 1.00 80.26 C
ATOM 19 CG1 ILE A 21 -31.919 50.205 -5.769 1.00 78.26 C
ATOM 20 CG2 ILE A 21 -31.181 47.966 -6.620 1.00 80.54 C
ATOM 21 CD1 ILE A 21 -31.383 51.524 -6.287 1.00 83.91 C
ATOM 22 N GLU A 22 -28.776 47.212 -3.973 1.00 78.07 N
ATOM 23 CA GLU A 22 -28.089 45.932 -3.820 1.00 73.15 C
ATOM 24 C GLU A 22 -28.469 45.254 -2.512 1.00 77.00 C
ATOM 25 O GLU A 22 -28.677 44.034 -2.473 1.00 76.18 O
ATOM 26 CB GLU A 22 -26.575 46.121 -3.906 1.00 70.99 C
ATOM 27 CG GLU A 22 -25.766 44.864 -3.605 1.00 81.29 C
ATOM 28 CD GLU A 22 -24.266 45.043 -3.844 1.00 82.14 C
ATOM 29 OE1 GLU A 22 -23.907 45.683 -4.848 1.00 81.45 O
ATOM 30 OE2 GLU A 22 -23.449 44.551 -3.026 1.00 82.94 O
ATOM 31 N GLU A 23 -28.576 46.026 -1.426 1.00 80.63 N
ATOM 32 CA GLU A 23 -28.953 45.428 -0.149 1.00 74.30 C
ATOM 33 C GLU A 23 -30.349 44.829 -0.210 1.00 71.49 C
ATOM 34 O GLU A 23 -30.605 43.791 0.411 1.00 73.78 O
ATOM 35 CB GLU A 23 -28.860 46.467 0.966 1.00 74.77 C
ATOM 36 CG GLU A 23 -27.459 47.014 1.162 1.00 76.51 C
ATOM 37 CD GLU A 23 -27.385 48.109 2.217 1.00 86.28 C
ATOM 38 OE1 GLU A 23 -26.371 48.141 2.949 1.00 94.26 O
ATOM 39 OE2 GLU A 23 -28.326 48.937 2.316 1.00 83.18 O
ATOM 40 N GLN A 24 -31.256 45.458 -0.960 1.00 69.98 N
ATOM 41 CA GLN A 24 -32.610 44.932 -1.085 1.00 73.41 C
ATOM 42 C GLN A 24 -32.636 43.684 -1.947 1.00 71.95 C
ATOM 43 O GLN A 24 -33.381 42.737 -1.656 1.00 75.00 O
ATOM 44 CB GLN A 24 -33.536 45.997 -1.665 1.00 70.85 C
ATOM 45 CG GLN A 24 -33.582 47.249 -0.841 1.00 75.01 C
ATOM 46 CD GLN A 24 -34.162 48.407 -1.610 1.00 77.95 C
ATOM 47 OE1 GLN A 24 -35.129 48.246 -2.353 1.00 75.95 O
ATOM 48 NE2 GLN A 24 -33.564 49.584 -1.450 1.00 74.84 N
ATOM 49 N ALA A 25 -31.844 43.678 -3.024 1.00 73.62 N
ATOM 50 CA ALA A 25 -31.748 42.498 -3.874 1.00 73.61 C
ATOM 51 C ALA A 25 -31.179 41.314 -3.103 1.00 68.09 C
ATOM 52 O ALA A 25 -31.672 40.186 -3.237 1.00 65.31 O
ATOM 53 CB ALA A 25 -30.897 42.809 -5.104 1.00 70.91 C
ATOM 54 N LYS A 26 -30.146 41.557 -2.284 1.00 67.12 N
ATOM 55 CA LYS A 26 -29.628 40.539 -1.372 1.00 67.83 C
ATOM 56 C LYS A 26 -30.738 39.957 -0.504 1.00 69.52 C
ATOM 57 O LYS A 26 -30.827 38.737 -0.319 1.00 68.94 O
ATOM 58 CB LYS A 26 -28.527 41.129 -0.486 1.00 64.05 C
ATOM 59 CG LYS A 26 -27.122 41.108 -1.084 1.00 69.06 C
ATOM 60 CD LYS A 26 -26.147 41.921 -0.215 1.00 74.62 C
ATOM 61 CE LYS A 26 -24.670 41.584 -0.477 1.00 76.55 C
ATOM 62 NZ LYS A 26 -24.237 40.285 0.152 1.00 74.06 N
ATOM 63 N THR A 27 -31.591 40.824 0.047 1.00 69.01 N
ATOM 64 CA THR A 27 -32.678 40.349 0.892 1.00 63.87 C
ATOM 65 C THR A 27 -33.742 39.646 0.066 1.00 65.18 C
ATOM 66 O THR A 27 -34.318 38.644 0.507 1.00 62.58 O
ATOM 67 CB THR A 27 -33.282 41.523 1.667 1.00 69.36 C
ATOM 68 OG1 THR A 27 -32.230 42.325 2.227 1.00 67.64 O
ATOM 69 CG2 THR A 27 -34.195 41.026 2.782 1.00 63.39 C
ATOM 70 N PHE A 28 -34.000 40.146 -1.141 1.00 64.25 N
ATOM 71 CA PHE A 28 -34.919 39.465 -2.045 1.00 63.66 C
ATOM 72 C PHE A 28 -34.430 38.059 -2.382 1.00 62.96 C
ATOM 73 O PHE A 28 -35.211 37.102 -2.359 1.00 65.69 O
ATOM 74 CB PHE A 28 -35.104 40.296 -3.311 1.00 65.39 C
ATOM 75 CG PHE A 28 -35.840 39.580 -4.388 1.00 63.63 C
ATOM 76 CD1 PHE A 28 -37.172 39.251 -4.225 1.00 62.80 C
ATOM 77 CD2 PHE A 28 -35.200 39.219 -5.557 1.00 63.72 C
ATOM 78 CE1 PHE A 28 -37.855 38.577 -5.203 1.00 63.43 C
ATOM 79 CE2 PHE A 28 -35.876 38.551 -6.541 1.00 64.20 C
ATOM 80 CZ PHE A 28 -37.210 38.228 -6.367 1.00 68.03 C
ATOM 81 N LEU A 29 -33.139 37.911 -2.690 1.00 62.54 N
ATOM 82 CA LEU A 29 -32.598 36.588 -2.996 1.00 67.77 C
ATOM 83 C LEU A 29 -32.616 35.688 -1.771 1.00 66.32 C
ATOM 84 O LEU A 29 -32.816 34.472 -1.889 1.00 61.58 O
ATOM 85 CB LEU A 29 -31.176 36.711 -3.543 1.00 63.72 C
ATOM 86 CG LEU A 29 -31.084 37.411 -4.898 1.00 68.07 C
ATOM 87 CD1 LEU A 29 -29.647 37.825 -5.205 1.00 65.35 C
ATOM 88 CD2 LEU A 29 -31.647 36.506 -5.986 1.00 67.34 C
ATOM 89 N ASP A 30 -32.389 36.269 -0.591 1.00 65.49 N
ATOM 90 CA ASP A 30 -32.484 35.517 0.650 1.00 62.77 C
ATOM 91 C ASP A 30 -33.846 34.846 0.768 1.00 69.15 C
ATOM 92 O ASP A 30 -33.942 33.650 1.070 1.00 68.39 O
ATOM 93 CB ASP A 30 -32.227 36.456 1.827 1.00 74.30 C
ATOM 94 CG ASP A 30 -31.312 35.853 2.862 1.00 73.32 C
ATOM 95 OD1 ASP A 30 -31.249 34.612 2.920 1.00 74.96 O
ATOM 96 OD2 ASP A 30 -30.664 36.613 3.619 1.00 75.15 O
ATOM 97 N LYS A 31 -34.917 35.606 0.509 1.00 69.84 N
ATOM 98 CA LYS A 31 -36.260 35.036 0.548 1.00 67.57 C
ATOM 99 C LYS A 31 -36.451 34.005 -0.557 1.00 56.95 C
ATOM 100 O LYS A 31 -37.021 32.935 -0.325 1.00 62.67 O
ATOM 101 CB LYS A 31 -37.318 36.137 0.430 1.00 62.00 C
ATOM 102 CG LYS A 31 -38.760 35.605 0.424 1.00 58.78 C
ATOM 103 CD LYS A 31 -39.281 35.398 1.858 1.00 76.99 C
ATOM 104 CE LYS A 31 -40.316 34.282 1.949 1.00 70.48 C
ATOM 105 NZ LYS A 31 -41.314 34.329 0.850 1.00 76.48 N
ATOM 106 N PHE A 32 -36.010 34.327 -1.775 1.00 62.56 N
ATOM 107 CA PHE A 32 -36.187 33.412 -2.898 1.00 58.66 C
ATOM 108 C PHE A 32 -35.549 32.063 -2.616 1.00 62.49 C
ATOM 109 O PHE A 32 -36.186 31.015 -2.802 1.00 61.72 O
ATOM 110 CB PHE A 32 -35.588 33.989 -4.173 1.00 58.47 C
ATOM 111 CG PHE A 32 -35.520 32.992 -5.288 1.00 63.16 C
ATOM 112 CD1 PHE A 32 -36.613 32.795 -6.120 1.00 62.61 C
ATOM 113 CD2 PHE A 32 -34.372 32.224 -5.487 1.00 58.38 C
ATOM 114 CE1 PHE A 32 -36.561 31.867 -7.145 1.00 64.74 C
ATOM 115 CE2 PHE A 32 -34.313 31.292 -6.495 1.00 61.40 C
ATOM 116 CZ PHE A 32 -35.412 31.108 -7.331 1.00 64.78 C
ATOM 117 N ASN A 33 -34.275 32.074 -2.200 1.00 56.62 N
ATOM 118 CA ASN A 33 -33.530 30.840 -1.953 1.00 57.22 C
ATOM 119 C ASN A 33 -34.300 29.886 -1.050 1.00 62.99 C
ATOM 120 O ASN A 33 -34.397 28.685 -1.337 1.00 57.35 O
ATOM 121 CB ASN A 33 -32.171 31.163 -1.330 1.00 55.01 C
ATOM 122 CG ASN A 33 -31.227 31.813 -2.311 1.00 61.68 C
ATOM 123 OD1 ASN A 33 -31.362 31.640 -3.519 1.00 60.67 O
ATOM 124 ND2 ASN A 33 -30.264 32.566 -1.799 1.00 57.80 N
ATOM 125 N HIS A 34 -34.862 30.406 0.049 1.00 61.93 N
ATOM 126 CA HIS A 34 -35.517 29.531 1.014 1.00 63.46 C
ATOM 127 C HIS A 34 -36.861 29.045 0.480 1.00 68.91 C
ATOM 128 O HIS A 34 -37.196 27.856 0.597 1.00 64.02 O
ATOM 129 CB HIS A 34 -35.655 30.252 2.360 1.00 65.40 C
ATOM 130 CG HIS A 34 -34.334 30.618 2.984 1.00 74.75 C
ATOM 131 ND1 HIS A 34 -33.572 31.688 2.554 1.00 67.12 N
ATOM 132 CD2 HIS A 34 -33.628 30.039 3.989 1.00 74.35 C
ATOM 133 CE1 HIS A 34 -32.464 31.757 3.275 1.00 66.34 C
ATOM 134 NE2 HIS A 34 -32.478 30.774 4.159 1.00 67.62 N
ATOM 135 N GLU A 35 -37.621 29.930 -0.159 1.00 61.76 N
ATOM 136 CA GLU A 35 -38.860 29.485 -0.781 1.00 63.43 C
ATOM 137 C GLU A 35 -38.577 28.505 -1.915 1.00 64.68 C
ATOM 138 O GLU A 35 -39.246 27.470 -2.036 1.00 65.09 O
ATOM 139 CB GLU A 35 -39.654 30.695 -1.279 1.00 65.86 C
ATOM 140 CG GLU A 35 -41.162 30.612 -1.051 1.00 72.30 C
ATOM 141 CD GLU A 35 -41.538 30.419 0.425 1.00 86.54 C
ATOM 142 OE1 GLU A 35 -41.530 29.260 0.907 1.00 84.06 O
ATOM 143 OE2 GLU A 35 -41.837 31.427 1.109 1.00 82.67 O
ATOM 144 N ALA A 36 -37.574 28.804 -2.746 1.00 62.87 N
ATOM 145 CA ALA A 36 -37.310 27.962 -3.909 1.00 61.37 C
ATOM 146 C ALA A 36 -36.902 26.554 -3.493 1.00 60.72 C
ATOM 147 O ALA A 36 -37.371 25.562 -4.066 1.00 54.79 O
ATOM 148 CB ALA A 36 -36.228 28.602 -4.776 1.00 63.56 C
ATOM 149 N GLU A 37 -36.036 26.451 -2.486 1.00 61.50 N
ATOM 150 CA GLU A 37 -35.552 25.147 -2.056 1.00 58.80 C
ATOM 151 C GLU A 37 -36.709 24.204 -1.750 1.00 56.53 C
ATOM 152 O GLU A 37 -36.712 23.048 -2.185 1.00 58.66 O
ATOM 153 CB GLU A 37 -34.640 25.322 -0.846 1.00 55.41 C
ATOM 154 CG GLU A 37 -33.980 24.060 -0.356 1.00 69.25 C
ATOM 155 CD GLU A 37 -32.468 24.065 -0.564 1.00 77.89 C
ATOM 156 OE1 GLU A 37 -31.971 23.205 -1.339 1.00 70.81 O
ATOM 157 OE2 GLU A 37 -31.784 24.931 0.041 1.00 75.53 O
ATOM 158 N ASP A 38 -37.726 24.686 -1.046 1.00 61.61 N
ATOM 159 CA ASP A 38 -38.801 23.780 -0.682 1.00 60.09 C
ATOM 160 C ASP A 38 -39.723 23.497 -1.861 1.00 58.64 C
ATOM 161 O ASP A 38 -40.138 22.348 -2.064 1.00 56.99 O
ATOM 162 CB ASP A 38 -39.594 24.335 0.493 1.00 61.19 C
ATOM 163 CG ASP A 38 -40.581 23.324 1.025 1.00 64.04 C
ATOM 164 OD1 ASP A 38 -40.141 22.260 1.542 1.00 64.91 O
ATOM 165 OD2 ASP A 38 -41.793 23.574 0.874 1.00 65.04 O
ATOM 166 N LEU A 39 -40.049 24.527 -2.646 1.00 54.22 N
ATOM 167 CA LEU A 39 -40.905 24.317 -3.806 1.00 62.98 C
ATOM 168 C LEU A 39 -40.231 23.425 -4.836 1.00 60.51 C
ATOM 169 O LEU A 39 -40.872 22.533 -5.403 1.00 58.79 O
ATOM 170 CB LEU A 39 -41.301 25.656 -4.421 1.00 68.34 C
ATOM 171 CG LEU A 39 -42.600 26.176 -3.817 1.00 72.27 C
ATOM 172 CD1 LEU A 39 -42.810 27.644 -4.181 1.00 66.79 C
ATOM 173 CD2 LEU A 39 -43.737 25.295 -4.320 1.00 71.64 C
ATOM 174 N PHE A 40 -38.938 23.641 -5.085 1.00 56.84 N
ATOM 175 CA PHE A 40 -38.227 22.754 -5.995 1.00 60.93 C
ATOM 176 C PHE A 40 -38.193 21.335 -5.447 1.00 56.99 C
ATOM 177 O PHE A 40 -38.316 20.363 -6.206 1.00 58.16 O
ATOM 178 CB PHE A 40 -36.808 23.267 -6.258 1.00 58.16 C
ATOM 179 CG PHE A 40 -36.032 22.422 -7.237 1.00 56.47 C
ATOM 180 CD1 PHE A 40 -36.116 22.662 -8.603 1.00 54.98 C
ATOM 181 CD2 PHE A 40 -35.223 21.380 -6.788 1.00 51.26 C
ATOM 182 CE1 PHE A 40 -35.403 21.872 -9.513 1.00 55.60 C
ATOM 183 CE2 PHE A 40 -34.510 20.596 -7.676 1.00 53.45 C
ATOM 184 CZ PHE A 40 -34.602 20.834 -9.052 1.00 46.59 C
ATOM 185 N TYR A 41 -38.054 21.198 -4.129 1.00 54.47 N
ATOM 186 CA TYR A 41 -37.951 19.871 -3.534 1.00 56.61 C
ATOM 187 C TYR A 41 -39.253 19.091 -3.690 1.00 58.15 C
ATOM 188 O TYR A 41 -39.231 17.889 -3.981 1.00 56.03 O
ATOM 189 CB TYR A 41 -37.553 19.980 -2.065 1.00 51.43 C
ATOM 190 CG TYR A 41 -37.215 18.638 -1.458 1.00 59.73 C
ATOM 191 CD1 TYR A 41 -35.934 18.120 -1.565 1.00 59.23 C
ATOM 192 CD2 TYR A 41 -38.178 17.878 -0.796 1.00 55.14 C
ATOM 193 CE1 TYR A 41 -35.610 16.898 -1.021 1.00 60.35 C
ATOM 194 CE2 TYR A 41 -37.861 16.644 -0.246 1.00 58.14 C
ATOM 195 CZ TYR A 41 -36.569 16.157 -0.360 1.00 57.79 C
ATOM 196 OH TYR A 41 -36.224 14.923 0.161 1.00 52.63 O
ATOM 197 N GLN A 42 -40.401 19.756 -3.519 1.00 58.71 N
ATOM 198 CA GLN A 42 -41.675 19.061 -3.704 1.00 56.44 C
ATOM 199 C GLN A 42 -41.846 18.618 -5.150 1.00 60.90 C
ATOM 200 O GLN A 42 -42.228 17.471 -5.421 1.00 63.80 O
ATOM 201 CB GLN A 42 -42.839 19.956 -3.271 1.00 61.57 C
ATOM 202 CG GLN A 42 -42.804 20.410 -1.798 1.00 62.32 C
ATOM 203 CD GLN A 42 -43.140 19.296 -0.806 1.00 72.63 C
ATOM 204 OE1 GLN A 42 -42.991 18.108 -1.103 1.00 72.21 O
ATOM 205 NE2 GLN A 42 -43.606 19.683 0.386 1.00 82.04 N
ATOM 206 N SER A 43 -41.546 19.512 -6.092 1.00 60.17 N
ATOM 207 CA SER A 43 -41.617 19.171 -7.506 1.00 58.91 C
ATOM 208 C SER A 43 -40.732 17.970 -7.837 1.00 61.89 C
ATOM 209 O SER A 43 -41.197 16.998 -8.446 1.00 55.36 O
ATOM 210 CB SER A 43 -41.219 20.381 -8.342 1.00 57.89 C
ATOM 211 OG SER A 43 -41.539 20.153 -9.704 1.00 67.86 O
ATOM 212 N SER A 44 -39.446 18.022 -7.447 1.00 60.61 N
ATOM 213 CA SER A 44 -38.529 16.914 -7.726 1.00 50.53 C
ATOM 214 C SER A 44 -39.037 15.622 -7.112 1.00 56.02 C
ATOM 215 O SER A 44 -38.902 14.545 -7.702 1.00 58.18 O
ATOM 216 CB SER A 44 -37.133 17.225 -7.186 1.00 51.34 C
ATOM 217 OG SER A 44 -36.639 18.447 -7.693 1.00 57.52 O
ATOM 218 N LEU A 45 -39.632 15.716 -5.928 1.00 59.27 N
ATOM 219 CA LEU A 45 -40.164 14.535 -5.263 1.00 59.06 C
ATOM 220 C LEU A 45 -41.371 13.979 -6.007 1.00 61.90 C
ATOM 221 O LEU A 45 -41.489 12.763 -6.183 1.00 65.85 O
ATOM 222 CB LEU A 45 -40.524 14.892 -3.830 1.00 57.33 C
ATOM 223 CG LEU A 45 -40.756 13.756 -2.857 1.00 66.80 C
ATOM 224 CD1 LEU A 45 -39.777 12.635 -3.137 1.00 64.61 C
ATOM 225 CD2 LEU A 45 -40.556 14.333 -1.475 1.00 61.13 C
ATOM 226 N ALA A 46 -42.281 14.849 -6.447 1.00 61.69 N
ATOM 227 CA ALA A 46 -43.415 14.381 -7.234 1.00 58.50 C
ATOM 228 C ALA A 46 -42.949 13.856 -8.586 1.00 62.08 C
ATOM 229 O ALA A 46 -43.468 12.852 -9.088 1.00 65.09 O
ATOM 230 CB ALA A 46 -44.437 15.508 -7.399 1.00 58.04 C
ATOM 231 N SER A 47 -41.960 14.513 -9.186 1.00 60.07 N
ATOM 232 CA SER A 47 -41.399 13.991 -10.423 1.00 64.57 C
ATOM 233 C SER A 47 -40.745 12.630 -10.207 1.00 67.93 C
ATOM 234 O SER A 47 -40.835 11.749 -11.073 1.00 59.94 O
ATOM 235 CB SER A 47 -40.394 14.985 -10.985 1.00 60.12 C
ATOM 236 OG SER A 47 -39.839 14.468 -12.174 1.00 70.67 O
ATOM 237 N TRP A 48 -40.100 12.437 -9.050 1.00 62.53 N
ATOM 238 CA TRP A 48 -39.454 11.165 -8.755 1.00 60.00 C
ATOM 239 C TRP A 48 -40.462 10.030 -8.661 1.00 64.49 C
ATOM 240 O TRP A 48 -40.215 8.934 -9.177 1.00 62.86 O
ATOM 241 CB TRP A 48 -38.656 11.262 -7.455 1.00 58.36 C
ATOM 242 CG TRP A 48 -38.104 9.930 -7.025 1.00 59.58 C
ATOM 243 CD1 TRP A 48 -38.697 9.028 -6.188 1.00 58.94 C
ATOM 244 CD2 TRP A 48 -36.862 9.338 -7.437 1.00 54.40 C
ATOM 245 NE1 TRP A 48 -37.894 7.919 -6.043 1.00 62.03 N
ATOM 246 CE2 TRP A 48 -36.768 8.082 -6.809 1.00 56.32 C
ATOM 247 CE3 TRP A 48 -35.820 9.753 -8.270 1.00 55.33 C
ATOM 248 CZ2 TRP A 48 -35.667 7.245 -6.979 1.00 57.61 C
ATOM 249 CZ3 TRP A 48 -34.733 8.918 -8.439 1.00 51.54 C
ATOM 250 CH2 TRP A 48 -34.660 7.685 -7.798 1.00 54.93 C
ATOM 251 N ASN A 49 -41.591 10.261 -7.979 1.00 68.46 N
ATOM 252 CA ASN A 49 -42.563 9.190 -7.770 1.00 64.82 C
ATOM 253 C ASN A 49 -43.244 8.796 -9.068 1.00 70.21 C
ATOM 254 O ASN A 49 -43.593 7.624 -9.250 1.00 70.76 O
ATOM 255 CB ASN A 49 -43.589 9.609 -6.732 1.00 58.26 C
ATOM 256 CG ASN A 49 -42.968 9.818 -5.381 1.00 70.33 C
ATOM 257 OD1 ASN A 49 -42.015 9.129 -5.018 1.00 73.63 O
ATOM 258 ND2 ASN A 49 -43.475 10.786 -4.635 1.00 73.92 N
ATOM 259 N TYR A 50 -43.437 9.748 -9.979 1.00 65.73 N
ATOM 260 CA TYR A 50 -43.922 9.379 -11.297 1.00 68.25 C
ATOM 261 C TYR A 50 -42.891 8.534 -12.034 1.00 69.15 C
ATOM 262 O TYR A 50 -43.221 7.492 -12.608 1.00 67.18 O
ATOM 263 CB TYR A 50 -44.274 10.628 -12.108 1.00 71.99 C
ATOM 264 CG TYR A 50 -44.551 10.302 -13.556 1.00 66.94 C
ATOM 265 CD1 TYR A 50 -45.716 9.634 -13.926 1.00 74.04 C
ATOM 266 CD2 TYR A 50 -43.638 10.625 -14.545 1.00 72.99 C
ATOM 267 CE1 TYR A 50 -45.971 9.304 -15.248 1.00 73.70 C
ATOM 268 CE2 TYR A 50 -43.880 10.303 -15.871 1.00 74.74 C
ATOM 269 CZ TYR A 50 -45.052 9.650 -16.215 1.00 78.16 C
ATOM 270 OH TYR A 50 -45.286 9.338 -17.534 1.00 85.51 O
ATOM 271 N ASN A 51 -41.627 8.960 -12.015 1.00 67.13 N
ATOM 272 CA ASN A 51 -40.639 8.322 -12.874 1.00 69.76 C
ATOM 273 C ASN A 51 -40.235 6.937 -12.383 1.00 66.76 C
ATOM 274 O ASN A 51 -39.678 6.160 -13.163 1.00 69.99 O
ATOM 275 CB ASN A 51 -39.413 9.224 -13.019 1.00 70.33 C
ATOM 276 CG ASN A 51 -39.546 10.203 -14.188 1.00 64.89 C
ATOM 277 OD1 ASN A 51 -39.147 9.902 -15.311 1.00 59.23 O
ATOM 278 ND2 ASN A 51 -40.115 11.370 -13.924 1.00 67.34 N
ATOM 279 N THR A 52 -40.529 6.601 -11.131 1.00 62.73 N
ATOM 280 CA THR A 52 -40.285 5.269 -10.597 1.00 66.88 C
ATOM 281 C THR A 52 -41.559 4.447 -10.476 1.00 71.03 C
ATOM 282 O THR A 52 -41.496 3.279 -10.086 1.00 76.46 O
ATOM 283 CB THR A 52 -39.611 5.371 -9.229 1.00 63.41 C
ATOM 284 OG1 THR A 52 -40.427 6.166 -8.356 1.00 62.69 O
ATOM 285 CG2 THR A 52 -38.232 6.031 -9.366 1.00 63.20 C
ATOM 286 N ASN A 53 -42.707 5.031 -10.807 1.00 71.09 N
ATOM 287 CA ASN A 53 -44.006 4.413 -10.586 1.00 74.82 C
ATOM 288 C ASN A 53 -45.008 5.100 -11.502 1.00 73.54 C
ATOM 289 O ASN A 53 -45.720 6.013 -11.079 1.00 78.62 O
ATOM 290 CB ASN A 53 -44.416 4.527 -9.110 1.00 70.87 C
ATOM 291 CG ASN A 53 -45.638 3.696 -8.772 1.00 77.54 C
ATOM 292 OD1 ASN A 53 -46.145 2.963 -9.619 1.00 82.44 O
ATOM 293 ND2 ASN A 53 -46.115 3.798 -7.522 1.00 80.15 N
ATOM 294 N ILE A 54 -45.051 4.689 -12.765 1.00 72.74 N
ATOM 295 CA ILE A 54 -45.840 5.386 -13.776 1.00 77.18 C
ATOM 296 C ILE A 54 -47.323 5.087 -13.592 1.00 81.11 C
ATOM 297 O ILE A 54 -47.797 3.995 -13.923 1.00 77.53 O
ATOM 298 CB ILE A 54 -45.371 5.004 -15.189 1.00 79.08 C
ATOM 299 CG1 ILE A 54 -43.903 5.404 -15.376 1.00 77.63 C
ATOM 300 CG2 ILE A 54 -46.264 5.649 -16.252 1.00 75.09 C
ATOM 301 CD1 ILE A 54 -43.326 5.013 -16.713 1.00 72.01 C
ATOM 302 N THR A 55 -48.062 6.052 -13.047 1.00 80.20 N
ATOM 303 CA THR A 55 -49.501 5.936 -12.861 1.00 80.79 C
ATOM 304 C THR A 55 -50.157 7.255 -13.254 1.00 87.17 C
ATOM 305 O THR A 55 -49.495 8.285 -13.403 1.00 85.41 O
ATOM 306 CB THR A 55 -49.869 5.585 -11.416 1.00 76.06 C
ATOM 307 OG1 THR A 55 -49.543 6.684 -10.555 1.00 74.50 O
ATOM 308 CG2 THR A 55 -49.122 4.347 -10.948 1.00 78.29 C
ATOM 309 N GLU A 56 -51.482 7.223 -13.415 1.00 89.28 N
ATOM 310 CA GLU A 56 -52.204 8.458 -13.701 1.00 86.96 C
ATOM 311 C GLU A 56 -52.253 9.363 -12.472 1.00 88.71 C
ATOM 312 O GLU A 56 -52.112 10.586 -12.587 1.00 87.15 O
ATOM 313 CB GLU A 56 -53.613 8.144 -14.211 1.00 90.51 C
ATOM 314 CG GLU A 56 -54.379 9.362 -14.749 1.00 91.37 C
ATOM 315 CD GLU A 56 -53.696 10.028 -15.948 1.00 99.18 C
ATOM 316 OE1 GLU A 56 -53.924 11.239 -16.170 1.00 97.52 O
ATOM 317 OE2 GLU A 56 -52.934 9.346 -16.672 1.00100.02 O
ATOM 318 N GLU A 57 -52.441 8.791 -11.281 1.00 84.58 N
ATOM 319 CA GLU A 57 -52.379 9.627 -10.090 1.00 83.86 C
ATOM 320 C GLU A 57 -51.017 10.297 -9.951 1.00 89.27 C
ATOM 321 O GLU A 57 -50.932 11.434 -9.470 1.00 88.65 O
ATOM 322 CB GLU A 57 -52.690 8.817 -8.832 1.00 85.85 C
ATOM 323 CG GLU A 57 -52.895 9.708 -7.605 1.00 88.58 C
ATOM 324 CD GLU A 57 -52.814 8.962 -6.286 1.00 92.86 C
ATOM 325 OE1 GLU A 57 -53.069 9.595 -5.241 1.00 98.30 O
ATOM 326 OE2 GLU A 57 -52.493 7.754 -6.287 1.00 95.88 O
ATOM 327 N ASN A 58 -49.943 9.619 -10.377 1.00 88.39 N
ATOM 328 CA ASN A 58 -48.601 10.174 -10.215 1.00 80.34 C
ATOM 329 C ASN A 58 -48.290 11.220 -11.279 1.00 80.35 C
ATOM 330 O ASN A 58 -47.652 12.239 -10.980 1.00 77.20 O
ATOM 331 CB ASN A 58 -47.554 9.060 -10.244 1.00 74.83 C
ATOM 332 CG ASN A 58 -47.413 8.368 -8.914 1.00 74.23 C
ATOM 333 OD1 ASN A 58 -47.651 8.975 -7.868 1.00 83.36 O
ATOM 334 ND2 ASN A 58 -47.014 7.098 -8.934 1.00 71.36 N
ATOM 335 N VAL A 59 -48.728 11.000 -12.522 1.00 78.45 N
ATOM 336 CA VAL A 59 -48.474 12.012 -13.543 1.00 75.55 C
ATOM 337 C VAL A 59 -49.173 13.318 -13.181 1.00 82.64 C
ATOM 338 O VAL A 59 -48.682 14.404 -13.517 1.00 81.52 O
ATOM 339 CB VAL A 59 -48.878 11.506 -14.944 1.00 77.29 C
ATOM 340 CG1 VAL A 59 -50.342 11.172 -14.999 1.00 87.53 C
ATOM 341 CG2 VAL A 59 -48.552 12.540 -16.001 1.00 78.05 C
ATOM 342 N GLN A 60 -50.290 13.254 -12.445 1.00 82.43 N
ATOM 343 CA GLN A 60 -50.978 14.498 -12.130 1.00 80.54 C
ATOM 344 C GLN A 60 -50.383 15.181 -10.909 1.00 79.16 C
ATOM 345 O GLN A 60 -50.241 16.407 -10.909 1.00 82.06 O
ATOM 346 CB GLN A 60 -52.477 14.271 -11.948 1.00 85.72 C
ATOM 347 CG GLN A 60 -53.292 15.124 -12.919 1.00 90.61 C
ATOM 348 CD GLN A 60 -54.566 15.668 -12.313 1.00101.56 C
ATOM 349 OE1 GLN A 60 -55.619 15.031 -12.395 1.00111.35 O
ATOM 350 NE2 GLN A 60 -54.482 16.857 -11.706 1.00 95.89 N
ATOM 351 N ASN A 61 -50.038 14.424 -9.856 1.00 80.46 N
ATOM 352 CA ASN A 61 -49.287 15.024 -8.753 1.00 74.59 C
ATOM 353 C ASN A 61 -48.036 15.709 -9.283 1.00 80.09 C
ATOM 354 O ASN A 61 -47.662 16.800 -8.825 1.00 76.06 O
ATOM 355 CB ASN A 61 -48.883 13.976 -7.719 1.00 66.57 C
ATOM 356 CG ASN A 61 -50.042 13.456 -6.926 1.00 81.29 C
ATOM 357 OD1 ASN A 61 -50.315 13.934 -5.826 1.00 84.44 O
ATOM 358 ND2 ASN A 61 -50.721 12.446 -7.459 1.00 87.92 N
ATOM 359 N MET A 62 -47.380 15.074 -10.260 1.00 73.15 N
ATOM 360 CA MET A 62 -46.194 15.661 -10.863 1.00 72.92 C
ATOM 361 C MET A 62 -46.536 16.963 -11.570 1.00 72.78 C
ATOM 362 O MET A 62 -45.788 17.942 -11.480 1.00 75.38 O
ATOM 363 CB MET A 62 -45.554 14.672 -11.837 1.00 66.58 C
ATOM 364 CG MET A 62 -44.280 15.194 -12.427 1.00 57.83 C
ATOM 365 SD MET A 62 -43.590 14.185 -13.750 1.00 69.90 S
ATOM 366 CE MET A 62 -42.153 15.184 -14.168 1.00 77.00 C
ATOM 367 N ASN A 63 -47.674 17.001 -12.263 1.00 77.45 N
ATOM 368 CA ASN A 63 -48.036 18.207 -12.997 1.00 75.82 C
ATOM 369 C ASN A 63 -48.395 19.349 -12.058 1.00 73.23 C
ATOM 370 O ASN A 63 -47.993 20.494 -12.296 1.00 74.51 O
ATOM 371 CB ASN A 63 -49.176 17.907 -13.962 1.00 75.26 C
ATOM 372 CG ASN A 63 -48.698 17.183 -15.200 1.00 84.39 C
ATOM 373 OD1 ASN A 63 -49.263 16.161 -15.597 1.00 87.27 O
ATOM 374 ND2 ASN A 63 -47.634 17.704 -15.814 1.00 79.37 N
ATOM 375 N ASN A 64 -49.123 19.059 -10.973 1.00 70.11 N
ATOM 376 CA ASN A 64 -49.520 20.113 -10.038 1.00 78.01 C
ATOM 377 C ASN A 64 -48.308 20.718 -9.330 1.00 79.09 C
ATOM 378 O ASN A 64 -48.153 21.944 -9.288 1.00 79.53 O
ATOM 379 CB ASN A 64 -50.529 19.576 -9.016 1.00 74.99 C
ATOM 380 CG ASN A 64 -51.801 19.035 -9.667 1.00 84.70 C
ATOM 381 OD1 ASN A 64 -52.134 19.377 -10.807 1.00 85.48 O
ATOM 382 ND2 ASN A 64 -52.510 18.175 -8.944 1.00 84.73 N
ATOM 383 N ALA A 65 -47.436 19.877 -8.762 1.00 78.18 N
ATOM 384 CA ALA A 65 -46.248 20.398 -8.089 1.00 70.44 C
ATOM 385 C ALA A 65 -45.332 21.127 -9.066 1.00 71.59 C
ATOM 386 O ALA A 65 -44.716 22.138 -8.715 1.00 74.55 O
ATOM 387 CB ALA A 65 -45.496 19.268 -7.390 1.00 65.18 C
ATOM 388 N GLY A 66 -45.231 20.634 -10.300 1.00 68.68 N
ATOM 389 CA GLY A 66 -44.473 21.359 -11.306 1.00 66.27 C
ATOM 390 C GLY A 66 -45.118 22.685 -11.660 1.00 77.15 C
ATOM 391 O GLY A 66 -44.424 23.684 -11.890 1.00 73.79 O
ATOM 392 N ASP A 67 -46.456 22.714 -11.706 1.00 77.15 N
ATOM 393 CA ASP A 67 -47.167 23.956 -11.992 1.00 76.98 C
ATOM 394 C ASP A 67 -46.914 24.992 -10.900 1.00 76.72 C
ATOM 395 O ASP A 67 -46.572 26.146 -11.190 1.00 75.97 O
ATOM 396 CB ASP A 67 -48.663 23.679 -12.152 1.00 80.69 C
ATOM 397 CG ASP A 67 -49.019 23.130 -13.534 1.00 86.95 C
ATOM 398 OD1 ASP A 67 -48.127 23.078 -14.417 1.00 87.40 O
ATOM 399 OD2 ASP A 67 -50.199 22.754 -13.733 1.00 82.86 O
ATOM 400 N LYS A 68 -47.056 24.593 -9.633 1.00 67.25 N
ATOM 401 CA LYS A 68 -46.743 25.504 -8.539 1.00 72.70 C
ATOM 402 C LYS A 68 -45.331 26.066 -8.681 1.00 75.47 C
ATOM 403 O LYS A 68 -45.108 27.270 -8.489 1.00 71.58 O
ATOM 404 CB LYS A 68 -46.912 24.793 -7.189 1.00 69.73 C
ATOM 405 CG LYS A 68 -48.299 24.206 -6.971 1.00 77.65 C
ATOM 406 CD LYS A 68 -48.522 23.722 -5.547 1.00 84.23 C
ATOM 407 CE LYS A 68 -49.955 23.193 -5.369 1.00 88.76 C
ATOM 408 NZ LYS A 68 -50.254 22.841 -3.944 1.00 90.40 N
ATOM 409 N TRP A 69 -44.367 25.209 -9.042 1.00 73.68 N
ATOM 410 CA TRP A 69 -42.981 25.656 -9.153 1.00 72.44 C
ATOM 411 C TRP A 69 -42.797 26.597 -10.338 1.00 69.99 C
ATOM 412 O TRP A 69 -42.112 27.619 -10.218 1.00 68.36 O
ATOM 413 CB TRP A 69 -42.055 24.439 -9.246 1.00 72.42 C
ATOM 414 CG TRP A 69 -40.639 24.719 -9.700 1.00 70.06 C
ATOM 415 CD1 TRP A 69 -40.063 24.293 -10.858 1.00 68.63 C
ATOM 416 CD2 TRP A 69 -39.625 25.467 -9.000 1.00 66.62 C
ATOM 417 NE1 TRP A 69 -38.761 24.731 -10.934 1.00 64.48 N
ATOM 418 CE2 TRP A 69 -38.463 25.451 -9.809 1.00 65.04 C
ATOM 419 CE3 TRP A 69 -39.590 26.156 -7.780 1.00 58.82 C
ATOM 420 CZ2 TRP A 69 -37.275 26.092 -9.435 1.00 56.86 C
ATOM 421 CZ3 TRP A 69 -38.411 26.796 -7.408 1.00 59.35 C
ATOM 422 CH2 TRP A 69 -37.267 26.757 -8.235 1.00 63.26 C
ATOM 423 N SER A 70 -43.413 26.283 -11.483 1.00 68.46 N
ATOM 424 CA SER A 70 -43.374 27.207 -12.615 1.00 68.71 C
ATOM 425 C SER A 70 -44.022 28.538 -12.258 1.00 70.98 C
ATOM 426 O SER A 70 -43.492 29.606 -12.589 1.00 70.64 O
ATOM 427 CB SER A 70 -44.063 26.592 -13.833 1.00 68.91 C
ATOM 428 OG SER A 70 -43.220 25.679 -14.514 1.00 75.03 O
ATOM 429 N ALA A 71 -45.167 28.494 -11.572 1.00 72.41 N
ATOM 430 CA ALA A 71 -45.832 29.723 -11.152 1.00 71.29 C
ATOM 431 C ALA A 71 -44.948 30.529 -10.207 1.00 68.44 C
ATOM 432 O ALA A 71 -44.783 31.743 -10.388 1.00 66.96 O
ATOM 433 CB ALA A 71 -47.174 29.393 -10.496 1.00 59.62 C
ATOM 434 N PHE A 72 -44.352 29.870 -9.211 1.00 62.19 N
ATOM 435 CA PHE A 72 -43.445 30.569 -8.304 1.00 65.32 C
ATOM 436 C PHE A 72 -42.345 31.293 -9.077 1.00 68.93 C
ATOM 437 O PHE A 72 -41.997 32.438 -8.757 1.00 64.49 O
ATOM 438 CB PHE A 72 -42.867 29.573 -7.297 1.00 62.72 C
ATOM 439 CG PHE A 72 -41.730 30.112 -6.473 1.00 65.56 C
ATOM 440 CD1 PHE A 72 -41.949 31.071 -5.504 1.00 59.51 C
ATOM 441 CD2 PHE A 72 -40.442 29.631 -6.654 1.00 64.09 C