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HEADER HYDROLASE 28-MAR-18 6G4O
TITLE NON-AGED FORM OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITED BY
TITLE 2 TABUN ANALOG NEDPA BOUND TO UNCHARGED REACTIVATOR 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787
KEYWDS ACETYLCHOLINESTERASE, TABUN, NERVE AGENT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SANTONI,E.DE LA MORA,J.DE SOUZA,I.SILMAN,J.SUSSMAN,R.BAATI,M.WEIK,
AUTHOR 2 F.NACHON
REVDAT 1 29-AUG-18 6G4O 0
JRNL AUTH G.SANTONI,J.DE SOUSA,E.DE LA MORA,J.DIAS,L.JEAN,J.L.SUSSMAN,
JRNL AUTH 2 I.SILMAN,P.Y.RENARD,R.C.D.BROWN,M.WEIK,R.BAATI,F.NACHON
JRNL TITL STRUCTURE-BASED OPTIMIZATION OF NON-QUATERNARY REACTIVATORS
JRNL TITL 2 OF ACETYLCHOLINESTERASE INHIBITED BY ORGANOPHOSPHORUS NERVE
JRNL TITL 3 AGENTS.
JRNL REF J. MED. CHEM. 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 30125110
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00592
REMARK 2
REMARK 2 RESOLUTION. 2.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_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) : 2.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 37171
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1863
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 45.9872 - 6.5310 0.98 2875 154 0.1895 0.2312
REMARK 3 2 6.5310 - 5.1861 0.99 2769 161 0.1720 0.2297
REMARK 3 3 5.1861 - 4.5312 0.98 2744 141 0.1406 0.2175
REMARK 3 4 4.5312 - 4.1172 0.98 2698 141 0.1479 0.2318
REMARK 3 5 4.1172 - 3.8223 0.98 2680 150 0.1573 0.2350
REMARK 3 6 3.8223 - 3.5970 0.99 2716 144 0.1774 0.2631
REMARK 3 7 3.5970 - 3.4169 0.99 2709 129 0.1908 0.2841
REMARK 3 8 3.4169 - 3.2682 0.99 2712 137 0.2123 0.3292
REMARK 3 9 3.2682 - 3.1424 0.98 2678 149 0.2283 0.3466
REMARK 3 10 3.1424 - 3.0340 0.99 2669 149 0.2323 0.3020
REMARK 3 11 3.0340 - 2.9392 0.99 2696 130 0.2445 0.3328
REMARK 3 12 2.9392 - 2.8552 0.99 2694 137 0.2616 0.3791
REMARK 3 13 2.8552 - 2.7800 0.98 2668 141 0.2771 0.3381
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) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.020
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 : 0.009 8872
REMARK 3 ANGLE : 1.087 12047
REMARK 3 CHIRALITY : 0.061 1263
REMARK 3 PLANARITY : 0.008 1555
REMARK 3 DIHEDRAL : 19.511 5212
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2853 -2.4775 -6.3288
REMARK 3 T TENSOR
REMARK 3 T11: 0.2580 T22: 0.4192
REMARK 3 T33: 0.2943 T12: 0.0341
REMARK 3 T13: 0.0090 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 2.4323 L22: 1.0790
REMARK 3 L33: 1.4304 L12: -0.5781
REMARK 3 L13: 0.5012 L23: -0.2195
REMARK 3 S TENSOR
REMARK 3 S11: -0.1313 S12: -0.0062 S13: 0.3447
REMARK 3 S21: 0.0434 S22: 0.0373 S23: -0.0641
REMARK 3 S31: -0.1085 S32: -0.0840 S33: 0.0935
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6246 -1.8731 53.6768
REMARK 3 T TENSOR
REMARK 3 T11: 0.2253 T22: 0.4471
REMARK 3 T33: 0.2506 T12: -0.0067
REMARK 3 T13: 0.0015 T23: -0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 0.7518 L22: 1.1491
REMARK 3 L33: 1.4177 L12: -0.2832
REMARK 3 L13: 0.1851 L23: 0.1315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: 0.1138 S13: -0.0529
REMARK 3 S21: -0.0217 S22: -0.0596 S23: -0.0112
REMARK 3 S31: 0.1509 S32: -0.0767 S33: 0.0407
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 6G4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37192
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.780
REMARK 200 RESOLUTION RANGE LOW (A) : 45.981
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
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 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: 1EA5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150MM MES 36% PEG 200, PH 5.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 45.77150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.26650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.17550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.26650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.77150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.17550
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: 5230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 ALA A 0
REMARK 465 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 486
REMARK 465 SER A 487
REMARK 465 GLN A 488
REMARK 465 GLU A 489
REMARK 465 ALA A 536
REMARK 465 CYS A 537
REMARK 465 ALA B 0
REMARK 465 ASP B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 536
REMARK 465 CYS B 537
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 TRP B 473 O HOH B 701 1.99
REMARK 500 OD1 ASP B 397 NH1 ARG B 517 2.00
REMARK 500 O SER B 125 O HOH B 702 2.00
REMARK 500 OD1 ASN A 310 NZ LYS A 410 2.03
REMARK 500 O PHE A 339 O HOH A 701 2.06
REMARK 500 O SER B 487 NZ LYS B 491 2.13
REMARK 500 O HOH B 817 O HOH B 822 2.14
REMARK 500 NH1 ARG B 515 O HOH B 703 2.14
REMARK 500 N SER A 108 O HOH A 702 2.17
REMARK 500 O VAL B 293 O HOH B 704 2.18
REMARK 500 OE2 GLU A 463 NH1 ARG A 467 2.18
REMARK 500 OD1 ASP A 369 NZ LYS B 530 2.18
REMARK 500 ND2 ASN B 324 OE1 GLU B 443 2.19
REMARK 500 OE2 GLU A 37 N LYS A 52 2.19
REMARK 500 O PRO B 229 O HOH B 705 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O VAL A 71 NZ LYS B 192 2554 2.12
REMARK 500 NZ LYS A 192 OE1 GLU B 73 2454 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 SER A 25 -159.82 -134.54
REMARK 500 ASN A 59 97.71 -59.45
REMARK 500 ALA A 60 62.38 -109.70
REMARK 500 SER A 108 79.30 48.62
REMARK 500 PHE A 120 12.78 58.56
REMARK 500 PHE A 155 22.09 -141.59
REMARK 500 ASN A 167 9.04 58.73
REMARK 500 SER A 200 -113.77 60.36
REMARK 500 ASN A 251 0.92 -69.42
REMARK 500 ASN A 253 73.76 51.89
REMARK 500 SER A 258 -143.41 -153.48
REMARK 500 ASN A 280 10.25 -69.98
REMARK 500 SER A 286 -57.98 59.81
REMARK 500 ILE A 287 -28.38 68.95
REMARK 500 GLU A 299 -45.78 -145.71
REMARK 500 THR A 317 -145.83 -147.05
REMARK 500 PRO A 361 -49.15 -24.30
REMARK 500 ASP A 380 59.56 -155.28
REMARK 500 VAL A 400 -75.37 -135.96
REMARK 500 ARG A 515 84.34 54.21
REMARK 500 GLN A 526 -50.11 -120.21
REMARK 500 VAL B 22 119.52 -171.80
REMARK 500 PHE B 45 -3.41 78.41
REMARK 500 ALA B 60 49.48 -107.44
REMARK 500 SER B 91 143.46 -176.75
REMARK 500 ASP B 93 89.27 -65.17
REMARK 500 CYS B 94 -2.38 -143.98
REMARK 500 PRO B 106 -178.23 -64.30
REMARK 500 ASP B 128 -32.48 -37.06
REMARK 500 LEU B 146 -165.45 -110.11
REMARK 500 SER B 200 -118.27 67.40
REMARK 500 CYS B 231 150.18 -37.99
REMARK 500 GLU B 299 -70.21 -118.95
REMARK 500 THR B 317 -145.77 -150.22
REMARK 500 ASP B 326 65.24 -103.02
REMARK 500 VAL B 360 66.62 -117.49
REMARK 500 ASP B 380 60.99 -170.03
REMARK 500 VAL B 400 -58.17 -134.89
REMARK 500 ASN B 457 63.04 61.68
REMARK 500 PRO B 485 171.68 -58.85
REMARK 500 HIS B 486 -49.97 76.83
REMARK 500 ASN B 506 -166.78 -163.43
REMARK 500 ARG B 515 88.13 54.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 286 ILE B 287 149.70
REMARK 500 LYS B 498 GLU B 499 127.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ELT A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DQ5 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ELT B 603 and SER B
REMARK 800 200
DBREF 6G4O A 0 537 UNP P04058 ACES_TETCF 21 558
DBREF 6G4O B 0 537 UNP P04058 ACES_TETCF 21 558
SEQRES 1 A 538 ALA ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER
SEQRES 2 A 538 GLY LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER
SEQRES 3 A 538 HIS ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 538 PRO VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS
SEQRES 5 A 538 LYS PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO
SEQRES 6 A 538 ASN ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY
SEQRES 7 A 538 PHE SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET
SEQRES 8 A 538 SER GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER
SEQRES 9 A 538 PRO ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR
SEQRES 10 A 538 GLY GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL
SEQRES 11 A 538 TYR ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL
SEQRES 12 A 538 LEU VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE
SEQRES 13 A 538 LEU ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL
SEQRES 14 A 538 GLY LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS
SEQRES 15 A 538 ASP ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL
SEQRES 16 A 538 THR ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY
SEQRES 17 A 538 MET HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG
SEQRES 18 A 538 ARG ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP
SEQRES 19 A 538 ALA SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL
SEQRES 20 A 538 GLU LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP
SEQRES 21 A 538 GLU GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN
SEQRES 22 A 538 GLU LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP
SEQRES 23 A 538 SER ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY
SEQRES 24 A 538 GLU PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER
SEQRES 25 A 538 GLY ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN
SEQRES 26 A 538 LYS ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO
SEQRES 27 A 538 GLY PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU
SEQRES 28 A 538 ASP PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA
SEQRES 29 A 538 ASN ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR
SEQRES 30 A 538 ASP TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP
SEQRES 31 A 538 GLY LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS
SEQRES 32 A 538 PRO LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY
SEQRES 33 A 538 ASN GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER
SEQRES 34 A 538 ASN LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY
SEQRES 35 A 538 TYR GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS
SEQRES 36 A 538 GLU LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG
SEQRES 37 A 538 ARG ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY
SEQRES 38 A 538 ASN PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO
SEQRES 39 A 538 LEU PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN
SEQRES 40 A 538 THR GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN
SEQRES 41 A 538 MET CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU
SEQRES 42 A 538 ASN ALA THR ALA CYS
SEQRES 1 B 538 ALA ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER
SEQRES 2 B 538 GLY LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER
SEQRES 3 B 538 HIS ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 B 538 PRO VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS
SEQRES 5 B 538 LYS PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO
SEQRES 6 B 538 ASN ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY
SEQRES 7 B 538 PHE SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET
SEQRES 8 B 538 SER GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER
SEQRES 9 B 538 PRO ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR
SEQRES 10 B 538 GLY GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL
SEQRES 11 B 538 TYR ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL
SEQRES 12 B 538 LEU VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE
SEQRES 13 B 538 LEU ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL
SEQRES 14 B 538 GLY LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS
SEQRES 15 B 538 ASP ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL
SEQRES 16 B 538 THR ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY
SEQRES 17 B 538 MET HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG
SEQRES 18 B 538 ARG ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP
SEQRES 19 B 538 ALA SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL
SEQRES 20 B 538 GLU LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP
SEQRES 21 B 538 GLU GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN
SEQRES 22 B 538 GLU LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP
SEQRES 23 B 538 SER ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY
SEQRES 24 B 538 GLU PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER
SEQRES 25 B 538 GLY ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN
SEQRES 26 B 538 LYS ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO
SEQRES 27 B 538 GLY PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU
SEQRES 28 B 538 ASP PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA
SEQRES 29 B 538 ASN ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR
SEQRES 30 B 538 ASP TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP
SEQRES 31 B 538 GLY LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS
SEQRES 32 B 538 PRO LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY
SEQRES 33 B 538 ASN GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER
SEQRES 34 B 538 ASN LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY
SEQRES 35 B 538 TYR GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS
SEQRES 36 B 538 GLU LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG
SEQRES 37 B 538 ARG ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY
SEQRES 38 B 538 ASN PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO
SEQRES 39 B 538 LEU PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN
SEQRES 40 B 538 THR GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN
SEQRES 41 B 538 MET CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU
SEQRES 42 B 538 ASN ALA THR ALA CYS
HET NAG A 601 14
HET NAG A 602 14
HET ELT A 603 8
HET DQ5 A 604 29
HET CL A 605 1
HET CL A 606 1
HET PG4 A 607 13
HET CL A 608 1
HET CL A 609 1
HET CL A 610 1
HET NAG B 601 14
HET NAG B 602 14
HET ELT B 603 8
HET NAG B 604 14
HET CL B 605 1
HET NA B 606 1
HET CL B 607 1
HET CL B 608 1
HET P6G B 609 19
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM ELT ETHOXY-~{N},~{N}-DIMETHYL-PHOSPHONAMIDIC ACID
HETNAM DQ5 2-[(~{E})-HYDROXYIMINOMETHYL]-6-[4-(1,2,3,4-
HETNAM 2 DQ5 TETRAHYDROACRIDIN-9-YLAMINO)BUTYL]PYRIDIN-3-OL
HETNAM CL CHLORIDE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM NA SODIUM ION
HETNAM P6G HEXAETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 5 ELT 2(C4 H12 N O3 P)
FORMUL 6 DQ5 C23 H26 N4 O2
FORMUL 7 CL 8(CL 1-)
FORMUL 9 PG4 C8 H18 O5
FORMUL 18 NA NA 1+
FORMUL 21 P6G C12 H26 O7
FORMUL 22 HOH *233(H2 O)
HELIX 1 AA1 VAL A 40 ARG A 44 5 5
HELIX 2 AA2 PHE A 78 MET A 83 1 6
HELIX 3 AA3 GLY A 132 GLU A 140 1 9
HELIX 4 AA4 GLY A 151 LEU A 156 1 6
HELIX 5 AA5 ASN A 167 ILE A 184 1 18
HELIX 6 AA6 GLN A 185 PHE A 187 5 3
HELIX 7 AA7 SER A 200 SER A 212 1 13
HELIX 8 AA8 SER A 212 ASP A 217 1 6
HELIX 9 AA9 SER A 237 ASN A 251 1 15
HELIX 10 AB1 ASP A 259 GLU A 268 1 10
HELIX 11 AB2 LYS A 270 GLU A 278 1 9
HELIX 12 AB3 TRP A 279 LEU A 282 5 4
HELIX 13 AB4 SER A 304 GLY A 312 1 9
HELIX 14 AB5 GLY A 328 ALA A 336 1 9
HELIX 15 AB6 SER A 348 VAL A 360 1 13
HELIX 16 AB7 ASN A 364 THR A 376 1 13
HELIX 17 AB8 ASN A 383 VAL A 400 1 18
HELIX 18 AB9 VAL A 400 GLY A 415 1 16
HELIX 19 AC1 PRO A 433 GLY A 437 5 5
HELIX 20 AC2 GLU A 443 PHE A 448 1 6
HELIX 21 AC3 GLY A 449 ASN A 457 5 9
HELIX 22 AC4 THR A 459 GLY A 480 1 22
HELIX 23 AC5 ARG A 517 GLN A 526 1 10
HELIX 24 AC6 GLN A 526 THR A 535 1 10
HELIX 25 AC7 VAL B 40 ARG B 44 5 5
HELIX 26 AC8 PHE B 78 MET B 83 1 6
HELIX 27 AC9 LEU B 127 ASN B 131 5 5
HELIX 28 AD1 GLY B 132 GLU B 140 1 9
HELIX 29 AD2 VAL B 150 LEU B 156 1 7
HELIX 30 AD3 ASN B 167 ILE B 184 1 18
HELIX 31 AD4 GLN B 185 PHE B 187 5 3
HELIX 32 AD5 SER B 200 SER B 212 1 13
HELIX 33 AD6 SER B 212 ASP B 217 1 6
HELIX 34 AD7 VAL B 238 ASN B 251 1 14
HELIX 35 AD8 SER B 258 LYS B 269 1 12
HELIX 36 AD9 LYS B 270 GLU B 278 1 9
HELIX 37 AE1 TRP B 279 LEU B 282 5 4
HELIX 38 AE2 SER B 304 GLY B 312 1 9
HELIX 39 AE3 GLY B 328 ALA B 336 1 9
HELIX 40 AE4 SER B 348 VAL B 360 1 13
HELIX 41 AE5 ASN B 364 THR B 376 1 13
HELIX 42 AE6 ASN B 383 VAL B 400 1 18
HELIX 43 AE7 VAL B 400 GLY B 415 1 16
HELIX 44 AE8 PRO B 433 GLY B 437 5 5
HELIX 45 AE9 GLU B 443 PHE B 448 1 6
HELIX 46 AF1 GLY B 449 ASN B 457 5 9
HELIX 47 AF2 THR B 459 GLY B 480 1 22
HELIX 48 AF3 ARG B 517 GLN B 526 1 10
HELIX 49 AF4 GLN B 526 THR B 535 1 10
SHEET 1 AA1 3 LEU A 7 THR A 10 0
SHEET 2 AA1 3 GLY A 13 MET A 16 -1 O VAL A 15 N VAL A 8
SHEET 3 AA1 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 AA211 THR A 18 VAL A 22 0
SHEET 2 AA211 SER A 25 PRO A 34 -1 O SER A 25 N VAL A 22
SHEET 3 AA211 TYR A 96 PRO A 102 -1 O ILE A 99 N PHE A 30
SHEET 4 AA211 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AA211 THR A 109 ILE A 115 1 N TRP A 114 O VAL A 144
SHEET 6 AA211 GLY A 189 GLU A 199 1 O PHE A 197 N VAL A 113
SHEET 7 AA211 ARG A 221 GLN A 225 1 O ILE A 223 N ILE A 196
SHEET 8 AA211 ILE A 319 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AA211 THR A 418 PHE A 423 1 O TYR A 419 N LEU A 321
SHEET 10 AA211 LYS A 501 LEU A 505 1 O ILE A 503 N PHE A 422
SHEET 11 AA211 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AA3 2 ASN A 66 CYS A 67 0
SHEET 2 AA3 2 MET A 90 SER A 91 1 O SER A 91 N ASN A 66
SHEET 1 AA4 3 LEU B 7 ASN B 9 0
SHEET 2 AA4 3 LYS B 14 MET B 16 -1 O VAL B 15 N VAL B 8
SHEET 3 AA4 3 VAL B 57 ASN B 59 1 O TRP B 58 N MET B 16
SHEET 1 AA511 THR B 18 VAL B 22 0
SHEET 2 AA511 SER B 25 PRO B 34 -1 O ILE B 27 N VAL B 20
SHEET 3 AA511 TYR B 96 VAL B 101 -1 O VAL B 101 N SER B 28
SHEET 4 AA511 VAL B 142 SER B 145 -1 O LEU B 143 N TRP B 100
SHEET 5 AA511 THR B 109 ILE B 115 1 N TRP B 114 O VAL B 144
SHEET 6 AA511 GLY B 189 GLU B 199 1 O THR B 195 N VAL B 111
SHEET 7 AA511 ARG B 221 GLN B 225 1 O GLN B 225 N GLY B 198
SHEET 8 AA511 ILE B 319 ASN B 324 1 O GLY B 322 N LEU B 224
SHEET 9 AA511 THR B 418 PHE B 423 1 O PHE B 423 N VAL B 323
SHEET 10 AA511 LYS B 501 LEU B 505 1 O ILE B 503 N PHE B 422
SHEET 11 AA511 VAL B 512 GLN B 514 -1 O HIS B 513 N PHE B 502
SHEET 1 AA6 2 VAL B 236 SER B 237 0
SHEET 2 AA6 2 VAL B 295 ILE B 296 1 O ILE B 296 N VAL B 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.06
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.04
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.05
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.04
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.06
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.11
LINK ND2 ASN A 59 C1 NAG A 601 1555 1555 1.46
LINK OG SER A 200 P01 ELT A 603 1555 1555 1.61
LINK ND2 ASN A 416 C1 NAG A 602 1555 1555 1.46
LINK ND2 ASN B 59 C1 NAG B 601 1555 1555 1.45
LINK OG SER B 200 P01 ELT B 603 1555 1555 1.57
LINK OD2 ASP B 259 NA NA B 606 1555 1555 2.35
LINK ND2 ASN B 416 C1 NAG B 602 1555 1555 1.45
LINK ND2 ASN B 457 C1 NAG B 604 1555 1555 1.44
CISPEP 1 SER A 103 PRO A 104 0 -1.41
CISPEP 2 SER B 103 PRO B 104 0 3.45
SITE 1 AC1 8 GLY A 118 GLY A 119 SER A 200 ALA A 201
SITE 2 AC1 8 TRP A 233 PHE A 290 HIS A 440 PG4 A 607
SITE 1 AC2 8 TYR A 70 TYR A 121 TRP A 279 ILE A 287
SITE 2 AC2 8 TYR A 334 PG4 A 607 GLN B 185 PRO B 191
SITE 1 AC3 1 GLN A 500
SITE 1 AC4 10 TRP A 84 GLY A 117 GLY A 118 GLU A 199
SITE 2 AC4 10 SER A 200 PHE A 330 TYR A 334 HIS A 440
SITE 3 AC4 10 ELT A 603 DQ5 A 604
SITE 1 AC5 1 HIS A 264
SITE 1 AC6 1 LYS B 133
SITE 1 AC7 1 ASP B 259
SITE 1 AC8 1 LEU B 256
SITE 1 AC9 1 THR B 497
SITE 1 AD1 8 TRP B 84 TYR B 121 GLU B 199 TRP B 279
SITE 2 AD1 8 PHE B 330 PHE B 331 HIS B 440 ELT B 603
SITE 1 AD2 2 ASN A 59 SER A 61
SITE 1 AD3 1 ASN A 416
SITE 1 AD4 2 ASN B 59 SER B 61
SITE 1 AD5 2 ASN B 416 HOH B 752
SITE 1 AD6 2 GLU B 455 ASN B 457
SITE 1 AD7 16 GLY B 117 GLY B 118 GLY B 119 GLU B 199
SITE 2 AD7 16 ALA B 201 GLY B 202 GLY B 203 ALA B 204
SITE 3 AD7 16 GLN B 225 SER B 226 GLY B 227 TRP B 233
SITE 4 AD7 16 PHE B 288 PHE B 290 HIS B 440 P6G B 609
CRYST1 91.543 106.351 150.533 90.00 90.00 90.00 P 21 21 21 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 0.010924 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009403 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006643 0.00000
TER 4216 THR A 535
TER 8469 THR B 535
MASTER 445 0 19 49 32 0 24 6 8843 2 168 84
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