| content |
HEADER HYDROLASE 03-OCT-19 6T0E
TITLE THE GLUCURONOYL ESTERASE OTCE15A S267A VARIANT FROM OPITUTUS TERRAE IN
TITLE 2 COMPLEX WITH BENZYL D-GLUCURONOATE AND D-GLUCURONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE (STRAIN DSM 11246 / JCM 15787 /
SOURCE 3 PB90-1);
SOURCE 4 ORGANISM_TAXID: 452637;
SOURCE 5 STRAIN: DSM 11246 / JCM 15787 / PB90-1;
SOURCE 6 GENE: OTER_0116;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ESTERASE, COMPLEX, BIOMASS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 27-NOV-19 6T0E 0
JRNL AUTH S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
JRNL TITL THE GLUCURONOYL ESTERASE OTCE15A S267A VARIANT FROM OPITUTUS
JRNL TITL 2 TERRAE IN COMPLEX WITH BENZYL D-GLUCURONOATE AND
JRNL TITL 3 D-GLUCURONATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.89 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 63362
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1988
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 44.4500 - 4.5500 1.00 4725 155 0.1677 0.2271
REMARK 3 2 4.5500 - 3.6100 1.00 4528 147 0.1252 0.1629
REMARK 3 3 3.6100 - 3.1600 1.00 4476 145 0.1362 0.1790
REMARK 3 4 3.1600 - 2.8700 1.00 4448 145 0.1491 0.1979
REMARK 3 5 2.8700 - 2.6600 0.99 4402 141 0.1572 0.2532
REMARK 3 6 2.6600 - 2.5100 1.00 4400 143 0.1623 0.2347
REMARK 3 7 2.5100 - 2.3800 0.99 4384 142 0.1678 0.2110
REMARK 3 8 2.3800 - 2.2800 1.00 4429 143 0.1682 0.2099
REMARK 3 9 2.2800 - 2.1900 1.00 4376 141 0.1783 0.2481
REMARK 3 10 2.1900 - 2.1100 1.00 4397 143 0.1915 0.2917
REMARK 3 11 2.1100 - 2.0500 1.00 4379 141 0.2146 0.2487
REMARK 3 12 2.0500 - 1.9900 1.00 4360 142 0.2485 0.2729
REMARK 3 13 1.9900 - 1.9400 1.00 4406 143 0.2804 0.3733
REMARK 3 14 1.9400 - 1.8900 0.84 3664 117 0.3399 0.3654
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) : 0.253
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.558
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.74
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 6649
REMARK 3 ANGLE : 1.121 8976
REMARK 3 CHIRALITY : 0.062 930
REMARK 3 PLANARITY : 0.008 1175
REMARK 3 DIHEDRAL : 22.805 2389
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 6T0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104635.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63514
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 44.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 13.60
REMARK 200 R MERGE (I) : 0.15890
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.840
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.15.2_3472
REMARK 200 STARTING MODEL: 6GS0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME MIXED 50/50 WITH RESERVOIR
REMARK 280 SOLUTION CONTAINING JCSG+ SCREEN SOLUTION G4: 0.2 M
REMARK 280 TRIMETHYLAMINE N-OXIDE, 0.1 M TRIS PH 8.5, AND 20 % W/V PEG 2000
REMARK 280 MME, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 25.85950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.95500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.80550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.95500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.85950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.80550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 12
REMARK 465 GLY A 13
REMARK 465 SER A 14
REMARK 465 SER A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 GLU A 24
REMARK 465 ASN A 25
REMARK 465 LEU A 26
REMARK 465 TYR A 27
REMARK 465 PHE A 28
REMARK 465 GLN A 29
REMARK 465 GLY A 30
REMARK 465 HIS A 31
REMARK 465 SER A 32
REMARK 465 ALA A 33
REMARK 465 TYR A 34
REMARK 465 THR A 35
REMARK 465 SER A 428
REMARK 465 ALA A 429
REMARK 465 LEU A 430
REMARK 465 PRO A 431
REMARK 465 ALA A 432
REMARK 465 MET B 12
REMARK 465 GLY B 13
REMARK 465 SER B 14
REMARK 465 SER B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 465 HIS B 19
REMARK 465 HIS B 20
REMARK 465 HIS B 21
REMARK 465 SER B 22
REMARK 465 SER B 23
REMARK 465 GLU B 24
REMARK 465 ASN B 25
REMARK 465 LEU B 26
REMARK 465 TYR B 27
REMARK 465 PHE B 28
REMARK 465 GLN B 29
REMARK 465 GLY B 30
REMARK 465 HIS B 31
REMARK 465 SER B 32
REMARK 465 ALA B 33
REMARK 465 TYR B 34
REMARK 465 ALA B 429
REMARK 465 LEU B 430
REMARK 465 PRO B 431
REMARK 465 ALA B 432
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 ARG A 57 -54.56 -123.16
REMARK 500 VAL A 70 -71.41 -120.06
REMARK 500 ASP A 150 103.35 -30.33
REMARK 500 ALA A 267 -126.20 57.65
REMARK 500 HIS A 328 43.23 -150.34
REMARK 500 ASP A 356 65.98 -104.23
REMARK 500 ASP A 357 11.10 -68.49
REMARK 500 TRP A 358 -30.47 -171.52
REMARK 500 ASP A 360 75.18 59.50
REMARK 500 LEU A 426 60.04 -108.26
REMARK 500 LEU B 40 33.06 -95.68
REMARK 500 VAL B 70 -69.34 -122.12
REMARK 500 ASP B 150 108.37 -35.44
REMARK 500 ALA B 267 -124.34 58.31
REMARK 500 ILE B 302 40.26 37.93
REMARK 500 ASP B 327 29.99 49.88
REMARK 500 HIS B 328 46.60 -152.59
REMARK 500 ASP B 356 57.16 -105.28
REMARK 500 TRP B 358 -22.82 70.57
REMARK 500 ASP B 360 78.20 59.32
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 MG A 532 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 101.0
REMARK 620 3 HOH A 739 O 99.6 92.3
REMARK 620 4 HOH A 781 O 99.0 83.8 161.3
REMARK 620 5 HOH A 654 O 90.6 159.0 103.0 77.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GCU A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue M55 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 529
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO A 533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO A 534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO A 535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GCU B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO B 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO B 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO B 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO B 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 526
DBREF 6T0E A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
DBREF 6T0E B 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 6T0E MET A 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 6T0E GLY A 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER A 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER A 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS A 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS A 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS A 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS A 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS A 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS A 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER A 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER A 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E GLU A 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E ASN A 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E LEU A 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E TYR A 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E PHE A 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E GLN A 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E GLY A 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS A 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER A 32 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E ALA A 267 UNP B1ZMF4 SER 267 ENGINEERED MUTATION
SEQADV 6T0E MET B 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 6T0E GLY B 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER B 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER B 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS B 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS B 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS B 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS B 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS B 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS B 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER B 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER B 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E GLU B 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E ASN B 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E LEU B 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E TYR B 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E PHE B 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E GLN B 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E GLY B 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E HIS B 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E SER B 32 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0E ALA B 267 UNP B1ZMF4 SER 267 ENGINEERED MUTATION
SEQRES 1 A 421 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 421 ASN LEU TYR PHE GLN GLY HIS SER ALA TYR THR LEU PRO
SEQRES 3 A 421 ASP PRO LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP
SEQRES 4 A 421 ARG ALA THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU
SEQRES 5 A 421 GLN LEU PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU
SEQRES 6 A 421 GLY ARG PRO GLU GLY MET VAL PHE LYS VAL THR THR MET
SEQRES 7 A 421 GLU HIS ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU
SEQRES 8 A 421 VAL THR VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER
SEQRES 9 A 421 MET GLN LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA
SEQRES 10 A 421 ARG ALA GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE
SEQRES 11 A 421 TYR GLY ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA
SEQRES 12 A 421 LEU SER ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY
SEQRES 13 A 421 ALA ASN HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP
SEQRES 14 A 421 ALA GLN LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY
SEQRES 15 A 421 TYR ALA VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO
SEQRES 16 A 421 ASP ARG PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP
SEQRES 17 A 421 LEU ASP ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA
SEQRES 18 A 421 TRP GLY ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG
SEQRES 19 A 421 ALA LEU ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA
SEQRES 20 A 421 SER ARG VAL ALA VAL HIS GLY HIS ALA ARG LEU GLY LYS
SEQRES 21 A 421 ALA ALA LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA
SEQRES 22 A 421 LEU VAL ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA
SEQRES 23 A 421 LEU SER LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE
SEQRES 24 A 421 ASN THR VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG
SEQRES 25 A 421 ARG TYR ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN
SEQRES 26 A 421 HIS GLU LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR
SEQRES 27 A 421 VAL ALA SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG
SEQRES 28 A 421 GLY GLU PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE
SEQRES 29 A 421 ARG LEU PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL
SEQRES 30 A 421 PRO ARG VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR
SEQRES 31 A 421 HIS ILE ARG PRO GLY PRO HIS GLY MET THR ALA GLN ASP
SEQRES 32 A 421 TRP ALA PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS
SEQRES 33 A 421 SER ALA LEU PRO ALA
SEQRES 1 B 421 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 B 421 ASN LEU TYR PHE GLN GLY HIS SER ALA TYR THR LEU PRO
SEQRES 3 B 421 ASP PRO LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP
SEQRES 4 B 421 ARG ALA THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU
SEQRES 5 B 421 GLN LEU PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU
SEQRES 6 B 421 GLY ARG PRO GLU GLY MET VAL PHE LYS VAL THR THR MET
SEQRES 7 B 421 GLU HIS ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU
SEQRES 8 B 421 VAL THR VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER
SEQRES 9 B 421 MET GLN LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA
SEQRES 10 B 421 ARG ALA GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE
SEQRES 11 B 421 TYR GLY ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA
SEQRES 12 B 421 LEU SER ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY
SEQRES 13 B 421 ALA ASN HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP
SEQRES 14 B 421 ALA GLN LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY
SEQRES 15 B 421 TYR ALA VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO
SEQRES 16 B 421 ASP ARG PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP
SEQRES 17 B 421 LEU ASP ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA
SEQRES 18 B 421 TRP GLY ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG
SEQRES 19 B 421 ALA LEU ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA
SEQRES 20 B 421 SER ARG VAL ALA VAL HIS GLY HIS ALA ARG LEU GLY LYS
SEQRES 21 B 421 ALA ALA LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA
SEQRES 22 B 421 LEU VAL ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA
SEQRES 23 B 421 LEU SER LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE
SEQRES 24 B 421 ASN THR VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG
SEQRES 25 B 421 ARG TYR ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN
SEQRES 26 B 421 HIS GLU LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR
SEQRES 27 B 421 VAL ALA SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG
SEQRES 28 B 421 GLY GLU PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE
SEQRES 29 B 421 ARG LEU PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL
SEQRES 30 B 421 PRO ARG VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR
SEQRES 31 B 421 HIS ILE ARG PRO GLY PRO HIS GLY MET THR ALA GLN ASP
SEQRES 32 B 421 TRP ALA PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS
SEQRES 33 B 421 SER ALA LEU PRO ALA
HET GCU A 501 22
HET CL A 502 1
HET M55 A 503 36
HET PG4 A 504 31
HET EDO A 505 10
HET EDO A 506 10
HET EDO A 507 10
HET EDO A 508 10
HET EDO A 509 10
HET EDO A 510 10
HET EDO A 511 10
HET EDO A 512 10
HET EDO A 513 10
HET EDO A 514 10
HET EDO A 515 10
HET EDO A 516 10
HET EDO A 517 10
HET EDO A 518 10
HET EDO A 519 10
HET EDO A 520 10
HET EDO A 521 10
HET EDO A 522 10
HET EDO A 523 10
HET PEG A 524 17
HET PEG A 525 17
HET PEG A 526 17
HET PEG A 527 17
HET PGE A 528 24
HET PGE A 529 24
HET PGE A 530 24
HET PGE A 531 24
HET MG A 532 1
HET TMO A 533 14
HET TMO A 534 14
HET TMO A 535 14
HET DMS A 536 10
HET DMS A 537 10
HET GCU B 501 22
HET EDO B 502 10
HET EDO B 503 10
HET EDO B 504 10
HET EDO B 505 10
HET EDO B 506 10
HET EDO B 507 10
HET EDO B 508 10
HET EDO B 509 10
HET EDO B 510 10
HET EDO B 511 10
HET EDO B 512 10
HET EDO B 513 10
HET EDO B 514 10
HET EDO B 515 10
HET EDO B 516 10
HET PEG B 517 17
HET PEG B 518 17
HET PGE B 519 24
HET TMO B 520 14
HET TMO B 521 14
HET TMO B 522 14
HET TMO B 523 14
HET DMS B 524 10
HET DMS B 525 10
HET DMS B 526 10
HETNAM GCU D-GLUCURONIC ACID
HETNAM CL CHLORIDE ION
HETNAM M55 BENZYL D-GLUCURONOATE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM MG MAGNESIUM ION
HETNAM TMO TRIMETHYLAMINE OXIDE
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 GCU 2(C6 H10 O7)
FORMUL 4 CL CL 1-
FORMUL 5 M55 C13 H16 O7
FORMUL 6 PG4 C8 H18 O5
FORMUL 7 EDO 34(C2 H6 O2)
FORMUL 26 PEG 6(C4 H10 O3)
FORMUL 30 PGE 5(C6 H14 O4)
FORMUL 34 MG MG 2+
FORMUL 35 TMO 7(C3 H9 N O)
FORMUL 38 DMS 5(C2 H6 O S)
FORMUL 66 HOH *412(H2 O)
HELIX 1 AA1 ASP A 50 ARG A 57 1 8
HELIX 2 AA2 ARG A 57 VAL A 70 1 14
HELIX 3 AA3 LEU A 94 GLY A 96 5 3
HELIX 4 AA4 ASN A 124 ARG A 129 1 6
HELIX 5 AA5 GLY A 143 VAL A 147 5 5
HELIX 6 AA6 THR A 173 ARG A 177 5 5
HELIX 7 AA7 ASP A 180 TRP A 184 5 5
HELIX 8 AA8 PRO A 185 ARG A 192 1 8
HELIX 9 AA9 GLY A 202 LEU A 204 5 3
HELIX 10 AB1 ASP A 210 ALA A 214 5 5
HELIX 11 AB2 SER A 215 ASP A 221 1 7
HELIX 12 AB3 ALA A 224 ARG A 228 5 5
HELIX 13 AB4 GLY A 234 GLU A 251 1 18
HELIX 14 AB5 ALA A 267 ASP A 280 1 14
HELIX 15 AB6 THR A 306 PHE A 314 1 9
HELIX 16 AB7 ALA A 319 ASP A 326 5 8
HELIX 17 AB8 HIS A 328 LEU A 332 5 5
HELIX 18 AB9 ASP A 335 LEU A 342 1 8
HELIX 19 AC1 ASP A 356 ALA A 359 5 4
HELIX 20 AC2 ASP A 360 PHE A 378 1 19
HELIX 21 AC3 THR A 411 LEU A 426 1 16
HELIX 22 AC4 ASP B 50 ARG B 57 1 8
HELIX 23 AC5 ARG B 57 VAL B 70 1 14
HELIX 24 AC6 ASN B 124 ARG B 129 1 6
HELIX 25 AC7 GLY B 143 VAL B 147 5 5
HELIX 26 AC8 THR B 173 ARG B 177 5 5
HELIX 27 AC9 ASP B 180 TRP B 184 5 5
HELIX 28 AD1 PRO B 185 ARG B 192 1 8
HELIX 29 AD2 CYS B 201 CYS B 205 1 5
HELIX 30 AD3 ASP B 210 ALA B 214 5 5
HELIX 31 AD4 SER B 215 ASP B 221 1 7
HELIX 32 AD5 ALA B 224 ARG B 228 5 5
HELIX 33 AD6 GLY B 234 GLU B 251 1 18
HELIX 34 AD7 ALA B 267 ASP B 280 1 14
HELIX 35 AD8 LEU B 298 ILE B 302 5 5
HELIX 36 AD9 THR B 306 PHE B 314 1 9
HELIX 37 AE1 ALA B 319 ASP B 326 5 8
HELIX 38 AE2 HIS B 328 LEU B 332 5 5
HELIX 39 AE3 ASP B 335 LEU B 342 1 8
HELIX 40 AE4 ASP B 360 PHE B 378 1 19
HELIX 41 AE5 THR B 411 LEU B 426 1 16
SHEET 1 AA1 9 VAL A 83 ALA A 93 0
SHEET 2 AA1 9 ALA A 98 ARG A 106 -1 O ARG A 106 N VAL A 83
SHEET 3 AA1 9 SER A 115 PRO A 123 -1 O LEU A 118 N VAL A 103
SHEET 4 AA1 9 ALA A 195 TYR A 200 -1 O THR A 198 N LEU A 119
SHEET 5 AA1 9 ALA A 133 ASN A 140 1 N PRO A 134 O ALA A 195
SHEET 6 AA1 9 VAL A 256 HIS A 266 1 O ALA A 262 N VAL A 135
SHEET 7 AA1 9 LEU A 285 ASN A 289 1 O ASN A 289 N GLY A 265
SHEET 8 AA1 9 LEU A 348 ALA A 353 1 O TYR A 349 N SER A 288
SHEET 9 AA1 9 LEU A 399 ARG A 404 1 O ARG A 400 N LEU A 348
SHEET 1 AA210 VAL B 83 ALA B 93 0
SHEET 2 AA210 ALA B 98 ARG B 106 -1 O ARG B 100 N GLU B 90
SHEET 3 AA210 SER B 115 PRO B 123 -1 O LEU B 118 N VAL B 103
SHEET 4 AA210 ALA B 195 TYR B 200 -1 O THR B 198 N LEU B 119
SHEET 5 AA210 ALA B 133 ASN B 140 1 N PRO B 134 O ALA B 195
SHEET 6 AA210 VAL B 256 HIS B 266 1 O ALA B 262 N VAL B 135
SHEET 7 AA210 LEU B 285 ASN B 289 1 O ASN B 289 N GLY B 265
SHEET 8 AA210 LEU B 348 ALA B 353 1 O TYR B 349 N SER B 288
SHEET 9 AA210 LEU B 399 ARG B 404 1 O ARG B 400 N VAL B 350
SHEET 10 AA210 SER B 395 GLY B 396 -1 N SER B 395 O TYR B 401
LINK O HIS A 303 MG MG A 532 1555 1555 2.23
LINK O GLU A 305 MG MG A 532 1555 1555 2.38
LINK MG MG A 532 O HOH A 739 1555 1555 2.60
LINK MG MG A 532 O HOH A 781 1555 1555 2.54
LINK MG MG A 532 O HOH A 654 1555 1555 2.36
CISPEP 1 ALA A 344 PRO A 345 0 1.34
CISPEP 2 ALA B 344 PRO B 345 0 2.58
SITE 1 AC1 8 ALA A 267 ARG A 268 LYS A 271 GLU A 305
SITE 2 AC1 8 PHE A 314 TRP A 358 HIS A 408 HOH A 650
SITE 1 AC2 5 GLN A 188 ARG A 192 HOH A 784 GLN B 188
SITE 2 AC2 5 ARG B 192
SITE 1 AC3 11 ASP A 207 PRO A 209 ARG A 268 THR A 312
SITE 2 AC3 11 VAL A 313 PHE A 314 HIS A 316 EDO A 519
SITE 3 AC3 11 ALA B 52 HIS B 56 ARG B 57
SITE 1 AC4 6 ARG A 192 HOH A 725 HOH A 765 ALA B 191
SITE 2 AC4 6 ARG B 192 HOH B 675
SITE 1 AC5 6 LEU A 212 ASP A 221 ALA A 223 ARG A 228
SITE 2 AC5 6 HOH A 602 HOH A 686
SITE 1 AC6 6 ALA A 43 ARG A 58 LEU A 65 PRO A 333
SITE 2 AC6 6 HOH A 646 HOH A 653
SITE 1 AC7 2 HIS A 91 ASN A 124
SITE 1 AC8 2 GLN A 182 EDO B 516
SITE 1 AC9 5 ARG A 192 TYR A 194 LEU A 426 LYS A 427
SITE 2 AC9 5 HOH A 622
SITE 1 AD1 5 ARG A 78 PRO A 79 MET A 82 ASP A 387
SITE 2 AD1 5 HOH A 794
SITE 1 AD2 1 GLU A 131
SITE 1 AD3 3 ASN A 321 ARG A 324 EDO A 513
SITE 1 AD4 4 ARG A 68 GLU A 69 ASN A 321 EDO A 512
SITE 1 AD5 2 SER A 218 ALA A 222
SITE 1 AD6 4 ARG A 132 GLU A 251 THR A 252 PRO A 254
SITE 1 AD7 3 ASN A 112 SER A 215 HOH A 722
SITE 1 AD8 1 ARG A 208
SITE 1 AD9 4 PRO A 373 HOH A 604 HOH A 618 HOH A 749
SITE 1 AE1 3 GLU A 163 ARG A 268 M55 A 503
SITE 1 AE2 4 GLU A 372 ARG A 376 HOH A 611 HOH A 625
SITE 1 AE3 6 ASP A 44 PRO A 79 GLU A 80 TRP A 219
SITE 2 AE3 6 TMO A 533 HOH A 601
SITE 1 AE4 2 VAL A 86 PGE A 529
SITE 1 AE5 1 ASP A 50
SITE 1 AE6 6 ALA A 93 LEU A 94 ARG A 100 ASP A 150
SITE 2 AE6 6 HOH A 636 HOH A 796
SITE 1 AE7 5 ARG A 68 GLU A 69 TYR A 325 ALA A 331
SITE 2 AE7 5 PRO A 333
SITE 1 AE8 6 ASP A 110 ARG A 301 ILE A 302 HIS A 303
SITE 2 AE8 6 TMO A 533 HOH A 734
SITE 1 AE9 5 GLN A 182 PRO A 407 THR A 411 LEU B 94
SITE 2 AE9 5 GLU B 187
SITE 1 AF1 8 PRO A 373 ARG A 376 HOH A 625 HOH A 775
SITE 2 AF1 8 ASP B 210 ASN B 213 ALA B 224 ASP B 226
SITE 1 AF2 7 LYS A 85 GLU A 354 ASP A 355 PRO A 405
SITE 2 AF2 7 EDO A 522 ALA B 92 GLY B 96
SITE 1 AF3 8 THR A 74 LEU A 76 GLY A 77 ARG A 245
SITE 2 AF3 8 GLN A 279 ASP A 280 TMO A 534 HOH A 672
SITE 1 AF4 6 LEU A 36 PRO A 39 ARG A 68 ARG A 73
SITE 2 AF4 6 ALA A 370 HOH A 694
SITE 1 AF5 5 HIS A 303 GLU A 305 HOH A 654 HOH A 739
SITE 2 AF5 5 HOH A 781
SITE 1 AF6 6 ASP A 44 THR A 46 ARG A 57 TRP A 219
SITE 2 AF6 6 EDO A 521 PEG A 526
SITE 1 AF7 5 ALA A 67 THR A 74 GLN A 279 PGE A 530
SITE 2 AF7 5 HOH A 789
SITE 1 AF8 2 PRO A 345 PRO A 347
SITE 1 AF9 6 VAL A 86 MET A 89 HOH A 680 HIS B 91
SITE 2 AF9 6 THR B 99 ILE B 127
SITE 1 AG1 4 ARG A 376 ARG B 208 HOH B 694 HOH B 784
SITE 1 AG2 9 ALA B 267 ARG B 268 LYS B 271 GLU B 305
SITE 2 AG2 9 ILE B 310 TRP B 358 HIS B 408 PGE B 519
SITE 3 AG2 9 HOH B 611
SITE 1 AG3 2 GLU B 424 TRP B 425
SITE 1 AG4 5 ASP B 221 ALA B 223 GLY B 225 ARG B 228
SITE 2 AG4 5 HOH B 655
SITE 1 AG5 6 TYR B 349 PRO B 394 ARG B 400 PHE B 417
SITE 2 AG5 6 ALA B 420 PHE B 421
SITE 1 AG6 1 ASN B 166
SITE 1 AG7 4 ARG B 68 GLU B 69 TYR B 325 HOH B 617
SITE 1 AG8 8 ARG B 132 LEU B 250 GLU B 251 ASP B 253
SITE 2 AG8 8 VAL B 256 ASP B 257 ALA B 258 HOH B 636
SITE 1 AG9 4 ARG B 59 ALA B 278 GLN B 279 ASP B 281
SITE 1 AH1 4 PRO B 394 SER B 395 GLY B 396 ARG B 400
SITE 1 AH2 3 ARG B 324 HIS B 328 ALA B 331
SITE 1 AH3 4 VAL B 41 GLY B 42 ARG B 58 HOH B 642
SITE 1 AH4 3 GLU B 354 VAL B 388 PRO B 389
SITE 1 AH5 2 THR B 35 HOH B 657
SITE 1 AH6 3 LYS B 101 TYR B 249 THR B 252
SITE 1 AH7 3 GLU B 69 ARG B 324 HOH B 654
SITE 1 AH8 7 EDO A 508 HOH A 606 PRO B 185 VAL B 186
SITE 2 AH8 7 GLU B 187 GLN B 188 HOH B 603
SITE 1 AH9 9 GLU A 187 GLN B 182 LYS B 183 GLY B 409
SITE 2 AH9 9 MET B 410 THR B 411 ALA B 412 HOH B 605
SITE 3 AH9 9 HOH B 765
SITE 1 AI1 8 PRO B 134 ARG B 192 GLY B 193 TYR B 194
SITE 2 AI1 8 LEU B 426 LYS B 427 HOH B 643 HOH B 690
SITE 1 AI2 9 TYR B 142 PRO B 165 SER B 179 ASP B 180
SITE 2 AI2 9 GLN B 182 LYS B 183 HIS B 266 HIS B 408
SITE 3 AI2 9 GCU B 501
SITE 1 AI3 10 GLY A 397 GLU A 424 TRP A 425 HOH A 619
SITE 2 AI3 10 ALA B 157 ARG B 158 TRP B 159 ARG B 171
SITE 3 AI3 10 HOH B 644 HOH B 713
SITE 1 AI4 3 ASP A 357 TRP A 358 ARG B 51
SITE 1 AI5 4 TRP B 219 LEU B 220 ASP B 221 ALA B 222
SITE 1 AI6 5 ALA B 67 ARG B 73 THR B 74 GLN B 279
SITE 2 AI6 5 HOH B 745
SITE 1 AI7 5 SER B 244 ARG B 245 GLN B 279 ASP B 280
SITE 2 AI7 5 HOH B 734
SITE 1 AI8 4 VAL B 86 THR B 87 THR B 88 MET B 89
SITE 1 AI9 2 GLU B 80 TRP B 219
CRYST1 51.719 87.611 173.910 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 0.019335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005750 0.00000
TER 6028 LYS A 427
TER 12065 SER B 428
MASTER 576 0 63 41 19 0 100 6 6837 2 828 66
END |