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HEADER HYDROLASE 04-DEC-10 3PUH
TITLE COCAINE ESTERASE, WILD-TYPE BIOLOGICALLY ACTIVE DIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COCAINE ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 104109;
SOURCE 4 STRAIN: MB1 BRESLER;
SOURCE 5 GENE: COCE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B (+)
KEYWDS ALPHA/BETA HYDROLASE, JELLY-ROLL BETA-BARREL, CLEAVAGE OF COCAINE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.NANCE,J.J.G.TESMER
REVDAT 1 21-SEP-11 3PUH 0
JRNL AUTH D.NARASIMHAN,G.T.COLLINS,M.R.NANCE,J.NICHOLS,E.EDWALD,
JRNL AUTH 2 J.CHAN,M.C.KO,J.H.WOODS,J.J.TESMER,R.K.SUNAHARA
JRNL TITL SUBUNIT STABILIZATION AND PEGYLATION OF COCAINE ESTERASE
JRNL TITL 2 IMPROVES IN VIVO RESIDENCE TIME.
JRNL REF MOL.PHARMACOL. 2011
JRNL REFN ESSN 1521-0111
JRNL PMID 21890748
JRNL DOI 10.1124/MOL.111.074997
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 78375
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3947
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.35
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5221
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 320
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8741
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 778
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.80000
REMARK 3 B22 (A**2) : 0.17000
REMARK 3 B33 (A**2) : -0.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.210
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.957
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9076 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12423 ; 1.384 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1163 ; 5.151 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 405 ;33.470 ;23.728
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1335 ;13.318 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 65 ;14.546 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1391 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7071 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5749 ; 0.302 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9286 ; 0.565 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3327 ; 0.715 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3137 ; 1.238 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 600 4
REMARK 3 1 B 1 B 600 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 4305 ; 0.200 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4305 ; 0.240 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3PUH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-10.
REMARK 100 THE RCSB ID CODE IS RCSB062826.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78491
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 100 MM MES PH 6.0, 1 M
REMARK 280 NACL, VAPOR 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 36.67250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.25900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.72100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.25900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.67250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.72100
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER OF COCE, CONSISTING
REMARK 300 OF CHAIN A AND CHAIN B.
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: 3850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 ASP A 3
REMARK 465 LYS A 575
REMARK 465 LEU A 576
REMARK 465 ALA A 577
REMARK 465 ALA A 578
REMARK 465 ALA A 579
REMARK 465 LEU A 580
REMARK 465 GLU A 581
REMARK 465 HIS A 582
REMARK 465 HIS A 583
REMARK 465 HIS A 584
REMARK 465 HIS A 585
REMARK 465 HIS A 586
REMARK 465 HIS A 587
REMARK 465 LYS B 575
REMARK 465 LEU B 576
REMARK 465 ALA B 577
REMARK 465 ALA B 578
REMARK 465 ALA B 579
REMARK 465 LEU B 580
REMARK 465 GLU B 581
REMARK 465 HIS B 582
REMARK 465 HIS B 583
REMARK 465 HIS B 584
REMARK 465 HIS B 585
REMARK 465 HIS B 586
REMARK 465 HIS B 587
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 ASP A 45 110.30 80.23
REMARK 500 SER A 56 -87.36 -133.81
REMARK 500 PHE A 78 -108.07 52.25
REMARK 500 HIS A 87 -39.63 76.80
REMARK 500 SER A 117 -114.60 64.71
REMARK 500 TYR A 152 -120.36 -121.27
REMARK 500 ASP A 198 86.31 -154.06
REMARK 500 ASP A 232 -156.15 -97.04
REMARK 500 PRO A 284 45.02 -95.29
REMARK 500 THR A 371 160.38 72.59
REMARK 500 ASN A 413 59.71 -145.25
REMARK 500 HIS A 422 30.02 -91.63
REMARK 500 LEU A 476 -70.03 -116.75
REMARK 500 LEU A 508 -119.94 57.06
REMARK 500 SER A 525 -159.88 -158.80
REMARK 500 ASN A 528 83.50 -167.33
REMARK 500 ASP B 45 111.89 76.57
REMARK 500 SER B 56 -91.80 -133.61
REMARK 500 PHE B 78 -106.65 52.39
REMARK 500 HIS B 87 -39.91 73.58
REMARK 500 SER B 117 -116.18 68.57
REMARK 500 ALA B 138 78.63 -151.29
REMARK 500 TYR B 152 -120.25 -120.61
REMARK 500 ASP B 198 76.22 -155.67
REMARK 500 ASP B 232 -151.28 -94.25
REMARK 500 ALA B 248 48.32 -147.36
REMARK 500 PRO B 284 46.98 -94.98
REMARK 500 ASP B 355 42.05 -103.55
REMARK 500 THR B 371 169.56 67.70
REMARK 500 ASN B 410 58.69 38.93
REMARK 500 ASN B 413 58.62 -145.91
REMARK 500 LEU B 476 -62.88 -120.36
REMARK 500 LEU B 508 -118.07 62.61
REMARK 500 SER B 525 -157.46 -156.36
REMARK 500 ASN B 528 85.44 -168.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 HIS A 422 24.7 L L OUTSIDE RANGE
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 GOL A 588
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 589
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 590
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 591
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 592
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 588
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 589
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I2F RELATED DB: PDB
REMARK 900 RELATED ID: 3I2G RELATED DB: PDB
REMARK 900 RELATED ID: 3I2H RELATED DB: PDB
REMARK 900 RELATED ID: 3I2I RELATED DB: PDB
REMARK 900 RELATED ID: 3I2J RELATED DB: PDB
REMARK 900 RELATED ID: 1JU3 RELATED DB: PDB
REMARK 900 RELATED ID: 3IDA RELATED DB: PDB
REMARK 900 RELATED ID: 1JU4 RELATED DB: PDB
REMARK 900 RELATED ID: 3PUI RELATED DB: PDB
DBREF 3PUH A 1 574 UNP Q9L9D7 COCE_RHOSM 1 574
DBREF 3PUH B 1 574 UNP Q9L9D7 COCE_RHOSM 1 574
SEQADV 3PUH LYS A 575 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH LEU A 576 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH ALA A 577 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH ALA A 578 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH ALA A 579 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH LEU A 580 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH GLU A 581 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS A 582 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS A 583 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS A 584 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS A 585 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS A 586 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS A 587 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH LYS B 575 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH LEU B 576 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH ALA B 577 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH ALA B 578 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH ALA B 579 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH LEU B 580 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH GLU B 581 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS B 582 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS B 583 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS B 584 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS B 585 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS B 586 UNP Q9L9D7 EXPRESSION TAG
SEQADV 3PUH HIS B 587 UNP Q9L9D7 EXPRESSION TAG
SEQRES 1 A 587 MET VAL ASP GLY ASN TYR SER VAL ALA SER ASN VAL MET
SEQRES 2 A 587 VAL PRO MET ARG ASP GLY VAL ARG LEU ALA VAL ASP LEU
SEQRES 3 A 587 TYR ARG PRO ASP ALA ASP GLY PRO VAL PRO VAL LEU LEU
SEQRES 4 A 587 VAL ARG ASN PRO TYR ASP LYS PHE ASP VAL PHE ALA TRP
SEQRES 5 A 587 SER THR GLN SER THR ASN TRP LEU GLU PHE VAL ARG ASP
SEQRES 6 A 587 GLY TYR ALA VAL VAL ILE GLN ASP THR ARG GLY LEU PHE
SEQRES 7 A 587 ALA SER GLU GLY GLU PHE VAL PRO HIS VAL ASP ASP GLU
SEQRES 8 A 587 ALA ASP ALA GLU ASP THR LEU SER TRP ILE LEU GLU GLN
SEQRES 9 A 587 ALA TRP CYS ASP GLY ASN VAL GLY MET PHE GLY VAL SER
SEQRES 10 A 587 TYR LEU GLY VAL THR GLN TRP GLN ALA ALA VAL SER GLY
SEQRES 11 A 587 VAL GLY GLY LEU LYS ALA ILE ALA PRO SER MET ALA SER
SEQRES 12 A 587 ALA ASP LEU TYR ARG ALA PRO TRP TYR GLY PRO GLY GLY
SEQRES 13 A 587 ALA LEU SER VAL GLU ALA LEU LEU GLY TRP SER ALA LEU
SEQRES 14 A 587 ILE GLY THR GLY LEU ILE THR SER ARG SER ASP ALA ARG
SEQRES 15 A 587 PRO GLU ASP ALA ALA ASP PHE VAL GLN LEU ALA ALA ILE
SEQRES 16 A 587 LEU ASN ASP VAL ALA GLY ALA ALA SER VAL THR PRO LEU
SEQRES 17 A 587 ALA GLU GLN PRO LEU LEU GLY ARG LEU ILE PRO TRP VAL
SEQRES 18 A 587 ILE ASP GLN VAL VAL ASP HIS PRO ASP ASN ASP GLU SER
SEQRES 19 A 587 TRP GLN SER ILE SER LEU PHE GLU ARG LEU GLY GLY LEU
SEQRES 20 A 587 ALA THR PRO ALA LEU ILE THR ALA GLY TRP TYR ASP GLY
SEQRES 21 A 587 PHE VAL GLY GLU SER LEU ARG THR PHE VAL ALA VAL LYS
SEQRES 22 A 587 ASP ASN ALA ASP ALA ARG LEU VAL VAL GLY PRO TRP SER
SEQRES 23 A 587 HIS SER ASN LEU THR GLY ARG ASN ALA ASP ARG LYS PHE
SEQRES 24 A 587 GLY ILE ALA ALA THR TYR PRO ILE GLN GLU ALA THR THR
SEQRES 25 A 587 MET HIS LYS ALA PHE PHE ASP ARG HIS LEU ARG GLY GLU
SEQRES 26 A 587 THR ASP ALA LEU ALA GLY VAL PRO LYS VAL ARG LEU PHE
SEQRES 27 A 587 VAL MET GLY ILE ASP GLU TRP ARG ASP GLU THR ASP TRP
SEQRES 28 A 587 PRO LEU PRO ASP THR ALA TYR THR PRO PHE TYR LEU GLY
SEQRES 29 A 587 GLY SER GLY ALA ALA ASN THR SER THR GLY GLY GLY THR
SEQRES 30 A 587 LEU SER THR SER ILE SER GLY THR GLU SER ALA ASP THR
SEQRES 31 A 587 TYR LEU TYR ASP PRO ALA ASP PRO VAL PRO SER LEU GLY
SEQRES 32 A 587 GLY THR LEU LEU PHE HIS ASN GLY ASP ASN GLY PRO ALA
SEQRES 33 A 587 ASP GLN ARG PRO ILE HIS ASP ARG ASP ASP VAL LEU CYS
SEQRES 34 A 587 TYR SER THR GLU VAL LEU THR ASP PRO VAL GLU VAL THR
SEQRES 35 A 587 GLY THR VAL SER ALA ARG LEU PHE VAL SER SER SER ALA
SEQRES 36 A 587 VAL ASP THR ASP PHE THR ALA LYS LEU VAL ASP VAL PHE
SEQRES 37 A 587 PRO ASP GLY ARG ALA ILE ALA LEU CYS ASP GLY ILE VAL
SEQRES 38 A 587 ARG MET ARG TYR ARG GLU THR LEU VAL ASN PRO THR LEU
SEQRES 39 A 587 ILE GLU ALA GLY GLU ILE TYR GLU VAL ALA ILE ASP MET
SEQRES 40 A 587 LEU ALA THR SER ASN VAL PHE LEU PRO GLY HIS ARG ILE
SEQRES 41 A 587 MET VAL GLN VAL SER SER SER ASN PHE PRO LYS TYR ASP
SEQRES 42 A 587 ARG ASN SER ASN THR GLY GLY VAL ILE ALA ARG GLU GLN
SEQRES 43 A 587 LEU GLU GLU MET CYS THR ALA VAL ASN ARG ILE HIS ARG
SEQRES 44 A 587 GLY PRO GLU HIS PRO SER HIS ILE VAL LEU PRO ILE ILE
SEQRES 45 A 587 LYS ARG LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 46 A 587 HIS HIS
SEQRES 1 B 587 MET VAL ASP GLY ASN TYR SER VAL ALA SER ASN VAL MET
SEQRES 2 B 587 VAL PRO MET ARG ASP GLY VAL ARG LEU ALA VAL ASP LEU
SEQRES 3 B 587 TYR ARG PRO ASP ALA ASP GLY PRO VAL PRO VAL LEU LEU
SEQRES 4 B 587 VAL ARG ASN PRO TYR ASP LYS PHE ASP VAL PHE ALA TRP
SEQRES 5 B 587 SER THR GLN SER THR ASN TRP LEU GLU PHE VAL ARG ASP
SEQRES 6 B 587 GLY TYR ALA VAL VAL ILE GLN ASP THR ARG GLY LEU PHE
SEQRES 7 B 587 ALA SER GLU GLY GLU PHE VAL PRO HIS VAL ASP ASP GLU
SEQRES 8 B 587 ALA ASP ALA GLU ASP THR LEU SER TRP ILE LEU GLU GLN
SEQRES 9 B 587 ALA TRP CYS ASP GLY ASN VAL GLY MET PHE GLY VAL SER
SEQRES 10 B 587 TYR LEU GLY VAL THR GLN TRP GLN ALA ALA VAL SER GLY
SEQRES 11 B 587 VAL GLY GLY LEU LYS ALA ILE ALA PRO SER MET ALA SER
SEQRES 12 B 587 ALA ASP LEU TYR ARG ALA PRO TRP TYR GLY PRO GLY GLY
SEQRES 13 B 587 ALA LEU SER VAL GLU ALA LEU LEU GLY TRP SER ALA LEU
SEQRES 14 B 587 ILE GLY THR GLY LEU ILE THR SER ARG SER ASP ALA ARG
SEQRES 15 B 587 PRO GLU ASP ALA ALA ASP PHE VAL GLN LEU ALA ALA ILE
SEQRES 16 B 587 LEU ASN ASP VAL ALA GLY ALA ALA SER VAL THR PRO LEU
SEQRES 17 B 587 ALA GLU GLN PRO LEU LEU GLY ARG LEU ILE PRO TRP VAL
SEQRES 18 B 587 ILE ASP GLN VAL VAL ASP HIS PRO ASP ASN ASP GLU SER
SEQRES 19 B 587 TRP GLN SER ILE SER LEU PHE GLU ARG LEU GLY GLY LEU
SEQRES 20 B 587 ALA THR PRO ALA LEU ILE THR ALA GLY TRP TYR ASP GLY
SEQRES 21 B 587 PHE VAL GLY GLU SER LEU ARG THR PHE VAL ALA VAL LYS
SEQRES 22 B 587 ASP ASN ALA ASP ALA ARG LEU VAL VAL GLY PRO TRP SER
SEQRES 23 B 587 HIS SER ASN LEU THR GLY ARG ASN ALA ASP ARG LYS PHE
SEQRES 24 B 587 GLY ILE ALA ALA THR TYR PRO ILE GLN GLU ALA THR THR
SEQRES 25 B 587 MET HIS LYS ALA PHE PHE ASP ARG HIS LEU ARG GLY GLU
SEQRES 26 B 587 THR ASP ALA LEU ALA GLY VAL PRO LYS VAL ARG LEU PHE
SEQRES 27 B 587 VAL MET GLY ILE ASP GLU TRP ARG ASP GLU THR ASP TRP
SEQRES 28 B 587 PRO LEU PRO ASP THR ALA TYR THR PRO PHE TYR LEU GLY
SEQRES 29 B 587 GLY SER GLY ALA ALA ASN THR SER THR GLY GLY GLY THR
SEQRES 30 B 587 LEU SER THR SER ILE SER GLY THR GLU SER ALA ASP THR
SEQRES 31 B 587 TYR LEU TYR ASP PRO ALA ASP PRO VAL PRO SER LEU GLY
SEQRES 32 B 587 GLY THR LEU LEU PHE HIS ASN GLY ASP ASN GLY PRO ALA
SEQRES 33 B 587 ASP GLN ARG PRO ILE HIS ASP ARG ASP ASP VAL LEU CYS
SEQRES 34 B 587 TYR SER THR GLU VAL LEU THR ASP PRO VAL GLU VAL THR
SEQRES 35 B 587 GLY THR VAL SER ALA ARG LEU PHE VAL SER SER SER ALA
SEQRES 36 B 587 VAL ASP THR ASP PHE THR ALA LYS LEU VAL ASP VAL PHE
SEQRES 37 B 587 PRO ASP GLY ARG ALA ILE ALA LEU CYS ASP GLY ILE VAL
SEQRES 38 B 587 ARG MET ARG TYR ARG GLU THR LEU VAL ASN PRO THR LEU
SEQRES 39 B 587 ILE GLU ALA GLY GLU ILE TYR GLU VAL ALA ILE ASP MET
SEQRES 40 B 587 LEU ALA THR SER ASN VAL PHE LEU PRO GLY HIS ARG ILE
SEQRES 41 B 587 MET VAL GLN VAL SER SER SER ASN PHE PRO LYS TYR ASP
SEQRES 42 B 587 ARG ASN SER ASN THR GLY GLY VAL ILE ALA ARG GLU GLN
SEQRES 43 B 587 LEU GLU GLU MET CYS THR ALA VAL ASN ARG ILE HIS ARG
SEQRES 44 B 587 GLY PRO GLU HIS PRO SER HIS ILE VAL LEU PRO ILE ILE
SEQRES 45 B 587 LYS ARG LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 46 B 587 HIS HIS
HET GOL A 588 6
HET GOL A 589 6
HET SO4 A 590 5
HET SO4 A 591 5
HET SO4 A 592 5
HET GOL B 588 6
HET SO4 B 589 5
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 10 HOH *778(H2 O)
HELIX 1 1 VAL A 49 THR A 54 1 6
HELIX 2 2 TRP A 59 ASP A 65 1 7
HELIX 3 3 ASP A 89 GLN A 104 1 16
HELIX 4 4 SER A 117 VAL A 128 1 12
HELIX 5 5 SER A 159 SER A 177 1 19
HELIX 6 6 GLU A 184 ASP A 198 1 15
HELIX 7 7 ASP A 198 SER A 204 1 7
HELIX 8 8 LEU A 213 ILE A 218 1 6
HELIX 9 9 PRO A 219 GLN A 224 1 6
HELIX 10 10 ASP A 232 SER A 237 1 6
HELIX 11 11 ILE A 238 SER A 239 5 2
HELIX 12 12 LEU A 240 LEU A 244 5 5
HELIX 13 13 PHE A 261 LYS A 273 1 13
HELIX 14 14 GLY A 300 THR A 304 5 5
HELIX 15 15 PRO A 306 ARG A 323 1 18
HELIX 16 16 ARG A 484 ARG A 486 5 3
HELIX 17 17 VAL A 541 GLU A 545 5 5
HELIX 18 18 GLN A 546 MET A 550 5 5
HELIX 19 19 VAL B 49 THR B 54 1 6
HELIX 20 20 TRP B 59 ASP B 65 1 7
HELIX 21 21 ASP B 89 GLU B 103 1 15
HELIX 22 22 SER B 117 VAL B 128 1 12
HELIX 23 23 SER B 159 SER B 177 1 19
HELIX 24 24 GLU B 184 ASN B 197 1 14
HELIX 25 25 ASP B 198 ALA B 203 1 6
HELIX 26 26 LEU B 213 ILE B 218 1 6
HELIX 27 27 PRO B 219 GLN B 224 1 6
HELIX 28 28 ASP B 232 SER B 237 1 6
HELIX 29 29 ILE B 238 SER B 239 5 2
HELIX 30 30 LEU B 240 LEU B 247 5 8
HELIX 31 31 PHE B 261 LYS B 273 1 13
HELIX 32 32 GLY B 300 THR B 304 5 5
HELIX 33 33 PRO B 306 LEU B 322 1 17
HELIX 34 34 GLN B 418 HIS B 422 5 5
HELIX 35 35 ARG B 484 ARG B 486 5 3
HELIX 36 36 VAL B 541 GLU B 545 5 5
HELIX 37 37 GLN B 546 MET B 550 5 5
SHEET 1 A12 LEU A 134 ALA A 136 0
SHEET 2 A12 CYS A 107 MET A 113 1 N VAL A 111 O LYS A 135
SHEET 3 A12 VAL A 35 ASN A 42 1 N VAL A 35 O ASP A 108
SHEET 4 A12 ALA A 68 ASP A 73 1 O VAL A 70 N LEU A 38
SHEET 5 A12 ARG A 21 PRO A 29 -1 N TYR A 27 O VAL A 69
SHEET 6 A12 TYR A 6 PRO A 15 -1 N ALA A 9 O LEU A 26
SHEET 7 A12 TYR B 6 PRO B 15 -1 O TYR B 6 N VAL A 8
SHEET 8 A12 ARG B 21 PRO B 29 -1 O LEU B 22 N VAL B 14
SHEET 9 A12 ALA B 68 ASP B 73 -1 O VAL B 69 N TYR B 27
SHEET 10 A12 VAL B 35 ASN B 42 1 N LEU B 38 O VAL B 70
SHEET 11 A12 CYS B 107 MET B 113 1 O ASP B 108 N VAL B 35
SHEET 12 A12 LEU B 134 ALA B 136 1 O LYS B 135 N VAL B 111
SHEET 1 B 2 GLY A 115 VAL A 116 0
SHEET 2 B 2 PRO A 139 SER A 140 1 O SER A 140 N GLY A 115
SHEET 1 C 4 LEU A 252 GLY A 256 0
SHEET 2 C 4 ARG A 279 GLY A 283 1 O ARG A 279 N ILE A 253
SHEET 3 C 4 VAL A 335 VAL A 339 1 O ARG A 336 N VAL A 282
SHEET 4 C 4 GLU A 344 GLU A 348 -1 O GLU A 344 N VAL A 339
SHEET 1 D 2 ARG A 293 ASN A 294 0
SHEET 2 D 2 ARG A 297 LYS A 298 -1 O ARG A 297 N ASN A 294
SHEET 1 E10 SER A 387 TYR A 393 0
SHEET 2 E10 ALA A 553 ARG A 559 -1 O ARG A 559 N SER A 387
SHEET 3 E10 VAL A 439 SER A 453 -1 N PHE A 450 O HIS A 558
SHEET 4 E10 HIS A 566 ILE A 572 -1 O VAL A 568 N SER A 446
SHEET 5 E10 ALA A 357 GLY A 364 -1 N THR A 359 O LEU A 569
SHEET 6 E10 GLY A 376 SER A 379 -1 O SER A 379 N TYR A 362
SHEET 7 E10 LEU A 428 SER A 431 1 O SER A 431 N GLY A 376
SHEET 8 E10 ARG A 519 SER A 525 -1 O VAL A 524 N LEU A 428
SHEET 9 E10 ASP A 459 VAL A 467 -1 N VAL A 465 O MET A 521
SHEET 10 E10 ALA A 473 ARG A 482 -1 O ILE A 474 N ASP A 466
SHEET 1 F 4 SER A 387 TYR A 393 0
SHEET 2 F 4 ALA A 553 ARG A 559 -1 O ARG A 559 N SER A 387
SHEET 3 F 4 VAL A 439 SER A 453 -1 N PHE A 450 O HIS A 558
SHEET 4 F 4 TYR A 501 PHE A 514 -1 O TYR A 501 N VAL A 451
SHEET 1 G 2 GLY B 115 VAL B 116 0
SHEET 2 G 2 PRO B 139 SER B 140 1 O SER B 140 N GLY B 115
SHEET 1 H 4 ALA B 251 GLY B 256 0
SHEET 2 H 4 ALA B 278 GLY B 283 1 O ARG B 279 N ILE B 253
SHEET 3 H 4 VAL B 335 VAL B 339 1 O ARG B 336 N VAL B 282
SHEET 4 H 4 GLU B 344 GLU B 348 -1 O GLU B 348 N VAL B 335
SHEET 1 I 6 THR B 377 SER B 379 0
SHEET 2 I 6 ALA B 357 GLY B 364 -1 N TYR B 362 O SER B 379
SHEET 3 I 6 HIS B 566 ILE B 572 -1 O LEU B 569 N THR B 359
SHEET 4 I 6 VAL B 439 SER B 453 -1 N ARG B 448 O HIS B 566
SHEET 5 I 6 ALA B 553 ARG B 559 -1 O HIS B 558 N PHE B 450
SHEET 6 I 6 SER B 387 TYR B 393 -1 N SER B 387 O ARG B 559
SHEET 1 J 5 THR B 377 SER B 379 0
SHEET 2 J 5 ALA B 357 GLY B 364 -1 N TYR B 362 O SER B 379
SHEET 3 J 5 HIS B 566 ILE B 572 -1 O LEU B 569 N THR B 359
SHEET 4 J 5 VAL B 439 SER B 453 -1 N ARG B 448 O HIS B 566
SHEET 5 J 5 TYR B 501 PHE B 514 -1 O PHE B 514 N VAL B 439
SHEET 1 K 4 LEU B 428 SER B 431 0
SHEET 2 K 4 ARG B 519 SER B 525 -1 O VAL B 522 N TYR B 430
SHEET 3 K 4 ASP B 459 VAL B 467 -1 N THR B 461 O SER B 525
SHEET 4 K 4 ALA B 473 ARG B 482 -1 O ILE B 474 N ASP B 466
CISPEP 1 ALA A 149 PRO A 150 0 10.61
CISPEP 2 THR A 206 PRO A 207 0 -1.26
CISPEP 3 TRP A 351 PRO A 352 0 -5.33
CISPEP 4 PHE A 529 PRO A 530 0 6.60
CISPEP 5 ALA B 149 PRO B 150 0 11.69
CISPEP 6 THR B 206 PRO B 207 0 -4.28
CISPEP 7 TRP B 351 PRO B 352 0 -3.34
CISPEP 8 PHE B 529 PRO B 530 0 5.53
SITE 1 AC1 9 ASN A 197 VAL A 199 PHE A 408 HIS A 409
SITE 2 AC1 9 ASN A 410 HOH A 657 HOH A 740 ARG B 293
SITE 3 AC1 9 LYS B 298
SITE 1 AC2 7 VAL A 554 ARG A 556 HOH A 707 HOH A 972
SITE 2 AC2 7 SER B 452 SER B 454 VAL B 554
SITE 1 AC3 1 GLU B 103
SITE 1 AC4 2 ASP A 296 ASP B 296
SITE 1 AC5 3 ASP A 319 ARG A 323 GLU A 325
SITE 1 AC6 7 ARG A 293 LYS A 298 LEU B 196 VAL B 199
SITE 2 AC6 7 PHE B 408 HIS B 409 ASN B 410
SITE 1 AC7 3 ASP B 65 ASP B 319 GLU B 325
CRYST1 73.345 105.442 224.518 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 0.013634 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009484 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004454 0.00000
TER 4389 ARG A 574
TER 8821 ARG B 574
MASTER 391 0 7 37 55 0 11 6 9557 2 38 92
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