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HEADER HYDROLASE 22-NOV-13 3WMR
TITLE CRYSTAL STRUCTURE OF VINJ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE IMINOPEPTIDASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES HALSTEDII;
SOURCE 3 ORGANISM_TAXID: 1944;
SOURCE 4 GENE: VINJ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SHINOHARA,A.MIYANAGA,F.KUDO,T.EGUCHI
REVDAT 1 05-FEB-14 3WMR 0
JRNL AUTH Y.SHINOHARA,A.MIYANAGA,F.KUDO,T.EGUCHI
JRNL TITL THE CRYSTAL STRUCTURE OF THE AMIDOHYDROLASE VINJ SHOWS A
JRNL TITL 2 UNIQUE HYDROPHOBIC TUNNEL FOR ITS INTERACTION WITH
JRNL TITL 3 POLYKETIDE SUBSTRATES
JRNL REF FEBS LETT. 2014
JRNL REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.8
REMARK 3 NUMBER OF REFLECTIONS : 60460
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3198
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3298
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 180
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7047
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 504
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.91000
REMARK 3 B22 (A**2) : -1.94000
REMARK 3 B33 (A**2) : -1.82000
REMARK 3 B12 (A**2) : 0.37000
REMARK 3 B13 (A**2) : -0.22000
REMARK 3 B23 (A**2) : -0.08000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.533
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7298 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6750 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9960 ; 1.214 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15540 ; 0.774 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 885 ; 5.808 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 345 ;34.230 ;23.478
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1101 ;12.298 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;17.491 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1080 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8226 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1698 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 299
REMARK 3 RESIDUE RANGE : A 401 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4737 36.0685 -20.0853
REMARK 3 T TENSOR
REMARK 3 T11: 0.0209 T22: 0.0714
REMARK 3 T33: 0.1092 T12: -0.0153
REMARK 3 T13: -0.0121 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.1097 L22: 1.9198
REMARK 3 L33: 0.4087 L12: -0.1506
REMARK 3 L13: -0.0642 L23: -0.5311
REMARK 3 S TENSOR
REMARK 3 S11: -0.0163 S12: 0.0009 S13: -0.0344
REMARK 3 S21: -0.1018 S22: 0.0273 S23: 0.0661
REMARK 3 S31: 0.0337 S32: -0.0235 S33: -0.0110
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 299
REMARK 3 RESIDUE RANGE : B 400 B 402
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5659 72.7610 -1.2960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0176 T22: 0.0781
REMARK 3 T33: 0.0910 T12: 0.0034
REMARK 3 T13: 0.0047 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.1176 L22: 0.2732
REMARK 3 L33: 1.4327 L12: -0.1038
REMARK 3 L13: -0.0339 L23: -0.0695
REMARK 3 S TENSOR
REMARK 3 S11: 0.0229 S12: -0.0017 S13: 0.0135
REMARK 3 S21: 0.0237 S22: 0.0553 S23: 0.0077
REMARK 3 S31: 0.0172 S32: -0.0223 S33: -0.0783
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 299
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4649 40.3046 26.8518
REMARK 3 T TENSOR
REMARK 3 T11: 0.0224 T22: 0.0922
REMARK 3 T33: 0.0733 T12: -0.0132
REMARK 3 T13: 0.0061 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.3115 L22: 1.0205
REMARK 3 L33: 0.5158 L12: -0.1977
REMARK 3 L13: 0.0606 L23: 0.3816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0282 S12: -0.0257 S13: -0.0169
REMARK 3 S21: -0.1031 S22: 0.0670 S23: -0.0346
REMARK 3 S31: -0.0399 S32: 0.0672 S33: -0.0389
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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
REMARK 4
REMARK 4 3WMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB096530.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63636
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.8
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3NWO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM ACETATE, 20% POLYETHYLENE
REMARK 280 GLYCOL 3350, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 -15
REMARK 465 ASN A -14
REMARK 465 HIS A -13
REMARK 465 LYS A -12
REMARK 465 VAL A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 ILE A -4
REMARK 465 GLU A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 MET B -15
REMARK 465 ASN B -14
REMARK 465 HIS B -13
REMARK 465 LYS B -12
REMARK 465 VAL B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 ILE B -4
REMARK 465 GLU B -3
REMARK 465 GLY B -2
REMARK 465 ARG B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 MET C -15
REMARK 465 ASN C -14
REMARK 465 HIS C -13
REMARK 465 LYS C -12
REMARK 465 VAL C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 ILE C -4
REMARK 465 GLU C -3
REMARK 465 GLY C -2
REMARK 465 ARG C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 3
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 103 111.27 -168.34
REMARK 500 SER A 110 -135.69 67.22
REMARK 500 ASN A 215 -63.18 -102.93
REMARK 500 SER A 276 -109.49 -112.88
REMARK 500 ASP B 103 110.14 -167.11
REMARK 500 SER B 110 -127.08 57.06
REMARK 500 ASN B 215 -63.70 -104.68
REMARK 500 SER B 276 -103.88 -118.71
REMARK 500 ASP C 103 106.15 -165.78
REMARK 500 SER C 110 -127.80 60.15
REMARK 500 ASN C 215 -61.40 -96.84
REMARK 500 SER C 276 -106.92 -116.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 644 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 648 DISTANCE = 5.18 ANGSTROMS
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P4G A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P4G B 402
DBREF 3WMR A 1 299 UNP Q76KY6 Q76KY6_STRHA 1 299
DBREF 3WMR B 1 299 UNP Q76KY6 Q76KY6_STRHA 1 299
DBREF 3WMR C 1 299 UNP Q76KY6 Q76KY6_STRHA 1 299
SEQADV 3WMR MET A -15 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ASN A -14 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS A -13 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR LYS A -12 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR VAL A -11 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS A -10 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS A -9 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS A -8 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS A -7 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS A -6 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS A -5 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ILE A -4 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR GLU A -3 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR GLY A -2 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ARG A -1 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS A 0 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR MET B -15 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ASN B -14 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS B -13 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR LYS B -12 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR VAL B -11 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS B -10 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS B -9 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS B -8 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS B -7 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS B -6 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS B -5 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ILE B -4 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR GLU B -3 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR GLY B -2 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ARG B -1 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS B 0 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR MET C -15 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ASN C -14 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS C -13 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR LYS C -12 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR VAL C -11 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS C -10 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS C -9 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS C -8 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS C -7 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS C -6 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS C -5 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ILE C -4 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR GLU C -3 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR GLY C -2 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR ARG C -1 UNP Q76KY6 EXPRESSION TAG
SEQADV 3WMR HIS C 0 UNP Q76KY6 EXPRESSION TAG
SEQRES 1 A 315 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 A 315 GLY ARG HIS MET SER LYS PRO PRO SER ALA LYS GLY THR
SEQRES 3 A 315 VAL PRO PHE GLY GLN TYR ARG THR TRP TYR ARG VAL THR
SEQRES 4 A 315 GLY ASP LEU HIS SER GLY LYS PRO PRO VAL VAL LEU LEU
SEQRES 5 A 315 HIS GLY GLY PRO GLY SER THR HIS ASP TYR LEU LEU ALA
SEQRES 6 A 315 MET THR SER LEU THR GLU ALA GLY TRP PRO VAL VAL HIS
SEQRES 7 A 315 TYR ASP GLN LEU GLY ASN GLY GLY SER THR HIS LEU PRO
SEQRES 8 A 315 GLU LYS GLY GLU ASP PHE TRP THR VAL GLN LEU PHE GLU
SEQRES 9 A 315 ASP GLU LEU ASP ASN LEU LEU ASN GLN LEU GLY ILE ALA
SEQRES 10 A 315 GLY ASP TYR VAL LEU PHE GLY GLN SER TRP GLY GLY MET
SEQRES 11 A 315 LEU GLY SER VAL HIS ALA ALA ARG ARG PRO ALA GLY LEU
SEQRES 12 A 315 ARG GLY LEU VAL VAL ALA ASN ALA PRO ALA SER MET LYS
SEQRES 13 A 315 ILE TRP LEU GLN GLU MET ALA ARG LEU ARG ALA LEU LEU
SEQRES 14 A 315 PRO PRO ASP VAL GLN GLU THR LEU LEU LYS HIS GLU ALA
SEQRES 15 A 315 ALA ARG THR THR ASP THR GLU GLU TYR PHE HIS ALA MET
SEQRES 16 A 315 ARG ALA PHE TYR ASP ARG HIS VAL CYS ARG ILE VAL PRO
SEQRES 17 A 315 TRP PRO ARG ASP PHE ALA ALA THR PHE MET GLU ILE TYR
SEQRES 18 A 315 ASN ASP PRO THR VAL TYR THR THR MET ASN GLY PRO ASN
SEQRES 19 A 315 GLU PHE HIS VAL ILE GLY THR LEU ARG ASP TRP SER VAL
SEQRES 20 A 315 GLU ASP CYS LEU PRO ASP ILE GLN VAL PRO THR MET VAL
SEQRES 21 A 315 LEU ILE GLY ARG HIS ASP GLU ALA THR PRO ALA THR VAL
SEQRES 22 A 315 LYS PRO PHE LEU ASP LEU VAL PRO ASP VAL ARG TYR GLU
SEQRES 23 A 315 VAL LEU GLU ASN SER SER HIS VAL PRO HIS LEU GLU GLU
SEQRES 24 A 315 PRO GLU ARG PHE HIS GLU VAL MET ILE ASP TYR LEU GLU
SEQRES 25 A 315 SER LEU VAL
SEQRES 1 B 315 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 B 315 GLY ARG HIS MET SER LYS PRO PRO SER ALA LYS GLY THR
SEQRES 3 B 315 VAL PRO PHE GLY GLN TYR ARG THR TRP TYR ARG VAL THR
SEQRES 4 B 315 GLY ASP LEU HIS SER GLY LYS PRO PRO VAL VAL LEU LEU
SEQRES 5 B 315 HIS GLY GLY PRO GLY SER THR HIS ASP TYR LEU LEU ALA
SEQRES 6 B 315 MET THR SER LEU THR GLU ALA GLY TRP PRO VAL VAL HIS
SEQRES 7 B 315 TYR ASP GLN LEU GLY ASN GLY GLY SER THR HIS LEU PRO
SEQRES 8 B 315 GLU LYS GLY GLU ASP PHE TRP THR VAL GLN LEU PHE GLU
SEQRES 9 B 315 ASP GLU LEU ASP ASN LEU LEU ASN GLN LEU GLY ILE ALA
SEQRES 10 B 315 GLY ASP TYR VAL LEU PHE GLY GLN SER TRP GLY GLY MET
SEQRES 11 B 315 LEU GLY SER VAL HIS ALA ALA ARG ARG PRO ALA GLY LEU
SEQRES 12 B 315 ARG GLY LEU VAL VAL ALA ASN ALA PRO ALA SER MET LYS
SEQRES 13 B 315 ILE TRP LEU GLN GLU MET ALA ARG LEU ARG ALA LEU LEU
SEQRES 14 B 315 PRO PRO ASP VAL GLN GLU THR LEU LEU LYS HIS GLU ALA
SEQRES 15 B 315 ALA ARG THR THR ASP THR GLU GLU TYR PHE HIS ALA MET
SEQRES 16 B 315 ARG ALA PHE TYR ASP ARG HIS VAL CYS ARG ILE VAL PRO
SEQRES 17 B 315 TRP PRO ARG ASP PHE ALA ALA THR PHE MET GLU ILE TYR
SEQRES 18 B 315 ASN ASP PRO THR VAL TYR THR THR MET ASN GLY PRO ASN
SEQRES 19 B 315 GLU PHE HIS VAL ILE GLY THR LEU ARG ASP TRP SER VAL
SEQRES 20 B 315 GLU ASP CYS LEU PRO ASP ILE GLN VAL PRO THR MET VAL
SEQRES 21 B 315 LEU ILE GLY ARG HIS ASP GLU ALA THR PRO ALA THR VAL
SEQRES 22 B 315 LYS PRO PHE LEU ASP LEU VAL PRO ASP VAL ARG TYR GLU
SEQRES 23 B 315 VAL LEU GLU ASN SER SER HIS VAL PRO HIS LEU GLU GLU
SEQRES 24 B 315 PRO GLU ARG PHE HIS GLU VAL MET ILE ASP TYR LEU GLU
SEQRES 25 B 315 SER LEU VAL
SEQRES 1 C 315 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 C 315 GLY ARG HIS MET SER LYS PRO PRO SER ALA LYS GLY THR
SEQRES 3 C 315 VAL PRO PHE GLY GLN TYR ARG THR TRP TYR ARG VAL THR
SEQRES 4 C 315 GLY ASP LEU HIS SER GLY LYS PRO PRO VAL VAL LEU LEU
SEQRES 5 C 315 HIS GLY GLY PRO GLY SER THR HIS ASP TYR LEU LEU ALA
SEQRES 6 C 315 MET THR SER LEU THR GLU ALA GLY TRP PRO VAL VAL HIS
SEQRES 7 C 315 TYR ASP GLN LEU GLY ASN GLY GLY SER THR HIS LEU PRO
SEQRES 8 C 315 GLU LYS GLY GLU ASP PHE TRP THR VAL GLN LEU PHE GLU
SEQRES 9 C 315 ASP GLU LEU ASP ASN LEU LEU ASN GLN LEU GLY ILE ALA
SEQRES 10 C 315 GLY ASP TYR VAL LEU PHE GLY GLN SER TRP GLY GLY MET
SEQRES 11 C 315 LEU GLY SER VAL HIS ALA ALA ARG ARG PRO ALA GLY LEU
SEQRES 12 C 315 ARG GLY LEU VAL VAL ALA ASN ALA PRO ALA SER MET LYS
SEQRES 13 C 315 ILE TRP LEU GLN GLU MET ALA ARG LEU ARG ALA LEU LEU
SEQRES 14 C 315 PRO PRO ASP VAL GLN GLU THR LEU LEU LYS HIS GLU ALA
SEQRES 15 C 315 ALA ARG THR THR ASP THR GLU GLU TYR PHE HIS ALA MET
SEQRES 16 C 315 ARG ALA PHE TYR ASP ARG HIS VAL CYS ARG ILE VAL PRO
SEQRES 17 C 315 TRP PRO ARG ASP PHE ALA ALA THR PHE MET GLU ILE TYR
SEQRES 18 C 315 ASN ASP PRO THR VAL TYR THR THR MET ASN GLY PRO ASN
SEQRES 19 C 315 GLU PHE HIS VAL ILE GLY THR LEU ARG ASP TRP SER VAL
SEQRES 20 C 315 GLU ASP CYS LEU PRO ASP ILE GLN VAL PRO THR MET VAL
SEQRES 21 C 315 LEU ILE GLY ARG HIS ASP GLU ALA THR PRO ALA THR VAL
SEQRES 22 C 315 LYS PRO PHE LEU ASP LEU VAL PRO ASP VAL ARG TYR GLU
SEQRES 23 C 315 VAL LEU GLU ASN SER SER HIS VAL PRO HIS LEU GLU GLU
SEQRES 24 C 315 PRO GLU ARG PHE HIS GLU VAL MET ILE ASP TYR LEU GLU
SEQRES 25 C 315 SER LEU VAL
HET GOL A 401 6
HET P4G A 402 11
HET GOL B 400 6
HET GOL B 401 6
HET P4G B 402 11
HETNAM GOL GLYCEROL
HETNAM P4G 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 P4G 2(C8 H18 O3)
FORMUL 9 HOH *504(H2 O)
HELIX 1 1 HIS A 44 GLY A 57 5 14
HELIX 2 2 THR A 83 LEU A 98 1 16
HELIX 3 3 SER A 110 ARG A 122 1 13
HELIX 4 4 SER A 138 ALA A 151 1 14
HELIX 5 5 PRO A 154 ARG A 168 1 15
HELIX 6 6 THR A 172 VAL A 187 1 16
HELIX 7 7 PRO A 194 ASP A 207 1 14
HELIX 8 8 PRO A 208 ASN A 215 1 8
HELIX 9 9 VAL A 231 ILE A 238 5 8
HELIX 10 10 THR A 253 VAL A 264 1 12
HELIX 11 11 VAL A 278 GLU A 283 1 6
HELIX 12 12 GLU A 283 SER A 297 1 15
HELIX 13 13 HIS B 44 GLY B 57 5 14
HELIX 14 14 THR B 83 LEU B 98 1 16
HELIX 15 15 SER B 110 ARG B 122 1 13
HELIX 16 16 SER B 138 LEU B 152 1 15
HELIX 17 17 PRO B 154 ARG B 168 1 15
HELIX 18 18 THR B 172 VAL B 187 1 16
HELIX 19 19 PRO B 194 ASP B 207 1 14
HELIX 20 20 PRO B 208 ASN B 215 1 8
HELIX 21 21 VAL B 231 ILE B 238 5 8
HELIX 22 22 THR B 253 VAL B 264 1 12
HELIX 23 23 VAL B 278 GLU B 283 1 6
HELIX 24 24 GLU B 283 SER B 297 1 15
HELIX 25 25 HIS C 44 GLY C 57 5 14
HELIX 26 26 THR C 83 LEU C 98 1 16
HELIX 27 27 SER C 110 ARG C 122 1 13
HELIX 28 28 SER C 138 ALA C 151 1 14
HELIX 29 29 PRO C 154 ALA C 167 1 14
HELIX 30 30 THR C 172 VAL C 187 1 16
HELIX 31 31 PRO C 194 ASP C 207 1 14
HELIX 32 32 PRO C 208 ASN C 215 1 8
HELIX 33 33 VAL C 231 ILE C 238 5 8
HELIX 34 34 THR C 253 VAL C 264 1 12
HELIX 35 35 VAL C 278 GLU C 283 1 6
HELIX 36 36 GLU C 283 LEU C 298 1 16
SHEET 1 A 8 ALA A 7 PHE A 13 0
SHEET 2 A 8 TYR A 16 THR A 23 -1 O TYR A 16 N PHE A 13
SHEET 3 A 8 VAL A 60 ASP A 64 -1 O VAL A 60 N THR A 23
SHEET 4 A 8 VAL A 33 LEU A 36 1 N LEU A 35 O VAL A 61
SHEET 5 A 8 TYR A 104 GLN A 109 1 O PHE A 107 N LEU A 36
SHEET 6 A 8 LEU A 127 ALA A 133 1 O VAL A 131 N LEU A 106
SHEET 7 A 8 THR A 242 GLY A 247 1 O MET A 243 N VAL A 132
SHEET 8 A 8 VAL A 267 LEU A 272 1 O ARG A 268 N VAL A 244
SHEET 1 B 8 ALA B 7 PHE B 13 0
SHEET 2 B 8 TYR B 16 THR B 23 -1 O VAL B 22 N ALA B 7
SHEET 3 B 8 VAL B 60 ASP B 64 -1 O VAL B 60 N THR B 23
SHEET 4 B 8 VAL B 33 LEU B 36 1 N VAL B 33 O VAL B 61
SHEET 5 B 8 TYR B 104 GLN B 109 1 O VAL B 105 N VAL B 34
SHEET 6 B 8 LEU B 127 ALA B 133 1 O VAL B 131 N GLY B 108
SHEET 7 B 8 THR B 242 GLY B 247 1 O MET B 243 N VAL B 132
SHEET 8 B 8 VAL B 267 LEU B 272 1 O ARG B 268 N VAL B 244
SHEET 1 C 8 ALA C 7 PHE C 13 0
SHEET 2 C 8 TYR C 16 THR C 23 -1 O TYR C 16 N PHE C 13
SHEET 3 C 8 VAL C 60 TYR C 63 -1 O VAL C 60 N THR C 23
SHEET 4 C 8 VAL C 33 LEU C 36 1 N LEU C 35 O VAL C 61
SHEET 5 C 8 TYR C 104 GLN C 109 1 O VAL C 105 N VAL C 34
SHEET 6 C 8 LEU C 127 ALA C 133 1 O VAL C 131 N GLY C 108
SHEET 7 C 8 THR C 242 GLY C 247 1 O MET C 243 N VAL C 132
SHEET 8 C 8 VAL C 267 LEU C 272 1 O ARG C 268 N VAL C 244
CISPEP 1 GLY A 39 PRO A 40 0 -4.03
CISPEP 2 VAL A 191 PRO A 192 0 -3.73
CISPEP 3 GLY B 39 PRO B 40 0 -2.06
CISPEP 4 VAL B 191 PRO B 192 0 3.81
CISPEP 5 GLY C 39 PRO C 40 0 -2.48
CISPEP 6 VAL C 191 PRO C 192 0 0.89
SITE 1 AC1 10 GLY A 102 ASP A 103 ALA A 125 GLY A 126
SITE 2 AC1 10 LEU A 127 ARG A 128 HOH A 578 HOH A 613
SITE 3 AC1 10 HOH A 651 ALA B 151
SITE 1 AC2 4 THR A 225 TRP A 229 SER A 230 HOH A 638
SITE 1 AC3 8 THR B 242 ASP B 266 VAL B 267 ARG B 268
SITE 2 AC3 8 TYR B 294 SER B 297 ARG C 248 GLU C 273
SITE 1 AC4 7 ARG B 150 PHE B 220 HIS B 221 HOH B 633
SITE 2 AC4 7 MET C 202 ASN C 206 HOH C 392
SITE 1 AC5 4 VAL B 84 TRP B 229 SER B 230 ASP B 233
CRYST1 52.870 72.620 75.450 114.02 98.39 98.50 P 1 3
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 0.018914 0.002827 0.004481 0.00000
SCALE2 0.000000 0.013923 0.006785 0.00000
SCALE3 0.000000 0.000000 0.014903 0.00000
TER 2350 VAL A 299
TER 4700 VAL B 299
TER 7050 VAL C 299
MASTER 427 0 5 36 24 0 9 6 7591 3 40 75
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