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HEADER LYASE 23-JUN-14 3WWO
TITLE S-SELECTIVE HYDROXYNITRILE LYASE FROM BALIOSPERMUM MONTANUM (APO1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BALIOSPERMUM MONTANUM;
SOURCE 3 ORGANISM_TAXID: 316758;
SOURCE 4 GENE: BMHNL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCOLDI
KEYWDS ALPHA/BETA HYDROLASE FOLD, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NAKANO,M.DADASHIPOUR,Y.ASANO
REVDAT 1 22-OCT-14 3WWO 0
JRNL AUTH S.NAKANO,M.DADASHIPOUR,Y.ASANO
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF HYDROXYNITRILE LYASE
JRNL TITL 2 FROM BALIOSPERMUM MONTANUM WITH CRYSTAL STRUCTURE, MOLECULAR
JRNL TITL 3 DYNAMICS AND ENZYME KINETICS
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1844 2059 2014
JRNL REFN ISSN 0006-3002
JRNL PMID 25220808
JRNL DOI 10.1016/J.BBAPAP.2014.09.004
REMARK 2
REMARK 2 RESOLUTION. 2.55 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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 17362
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 937
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) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1214
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4078
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 43
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.00000
REMARK 3 B33 (A**2) : 0.01000
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): 1.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.299
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.205
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.434
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4210 ; 0.003 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3942 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5730 ; 1.104 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9077 ; 0.682 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 511 ; 5.495 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 201 ;37.721 ;25.124
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 682 ;18.563 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;25.073 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 636 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4765 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 971 ; 0.002 ; 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 256 B 3 256 16145 0.09 0.05
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 : 1.20
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 3WWO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUL-14.
REMARK 100 THE RCSB ID CODE IS RCSB096886.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18347
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 23.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
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) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 0.1M SODIUM ACETIC ACID,
REMARK 280 0.02M CALCIUM CHLORIDE, PH 4.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 24.22500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.05800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.26450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.05800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.22500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.26450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 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 -24
REMARK 465 ASN A -23
REMARK 465 HIS A -22
REMARK 465 LYS A -21
REMARK 465 VAL A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 ILE A -13
REMARK 465 GLU A -12
REMARK 465 GLY A -11
REMARK 465 ARG A -10
REMARK 465 HIS A -9
REMARK 465 MET A -8
REMARK 465 GLU A -7
REMARK 465 LEU A -6
REMARK 465 GLY A -5
REMARK 465 THR A -4
REMARK 465 LEU A -3
REMARK 465 GLU A -2
REMARK 465 GLY A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 ASP A 258
REMARK 465 LEU A 259
REMARK 465 LEU A 260
REMARK 465 ALA A 261
REMARK 465 VAL A 262
REMARK 465 ALA A 263
REMARK 465 MET B -24
REMARK 465 ASN B -23
REMARK 465 HIS B -22
REMARK 465 LYS B -21
REMARK 465 VAL B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 ILE B -13
REMARK 465 GLU B -12
REMARK 465 GLY B -11
REMARK 465 ARG B -10
REMARK 465 HIS B -9
REMARK 465 MET B -8
REMARK 465 GLU B -7
REMARK 465 LEU B -6
REMARK 465 GLY B -5
REMARK 465 THR B -4
REMARK 465 LEU B -3
REMARK 465 GLU B -2
REMARK 465 GLY B -1
REMARK 465 PHE B 0
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 LEU B 260
REMARK 465 ALA B 261
REMARK 465 VAL B 262
REMARK 465 ALA B 263
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU B 259 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 410 O HOH A 417 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 111 NZ LYS A 241 3545 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS A 13 -18.57 71.82
REMARK 500 HIS A 14 -166.52 -100.77
REMARK 500 GLU A 70 -147.25 46.72
REMARK 500 SER A 80 -129.92 48.18
REMARK 500 ASN A 104 48.67 38.15
REMARK 500 PRO A 108 -176.01 -67.63
REMARK 500 LYS A 129 -116.11 50.76
REMARK 500 PHE A 158 38.93 -95.30
REMARK 500 TYR A 222 84.42 -157.79
REMARK 500 LYS A 236 69.23 -100.42
REMARK 500 LYS A 241 59.02 -149.95
REMARK 500 CYS B 13 -19.60 71.71
REMARK 500 HIS B 14 -166.61 -100.95
REMARK 500 SER B 80 -129.23 48.88
REMARK 500 ASN B 104 47.53 39.10
REMARK 500 LYS B 129 -118.76 50.63
REMARK 500 PHE B 158 37.22 -94.58
REMARK 500 TYR B 222 85.27 -158.32
REMARK 500 LYS B 241 59.89 -151.49
REMARK 500 ASP B 258 36.98 74.74
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 CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WWP RELATED DB: PDB
DBREF 3WWO A 1 263 UNP D1MX73 D1MX73_9ROSI 1 263
DBREF 3WWO B 1 263 UNP D1MX73 D1MX73_9ROSI 1 263
SEQADV 3WWO MET A -24 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO ASN A -23 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS A -22 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO LYS A -21 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO VAL A -20 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS A -19 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS A -18 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS A -17 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS A -16 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS A -15 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS A -14 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO ILE A -13 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLU A -12 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLY A -11 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO ARG A -10 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS A -9 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO MET A -8 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLU A -7 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO LEU A -6 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLY A -5 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO THR A -4 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO LEU A -3 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLU A -2 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLY A -1 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO PHE A 0 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO MET B -24 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO ASN B -23 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS B -22 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO LYS B -21 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO VAL B -20 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS B -19 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS B -18 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS B -17 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS B -16 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS B -15 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS B -14 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO ILE B -13 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLU B -12 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLY B -11 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO ARG B -10 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO HIS B -9 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO MET B -8 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLU B -7 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO LEU B -6 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLY B -5 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO THR B -4 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO LEU B -3 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLU B -2 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO GLY B -1 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWO PHE B 0 UNP D1MX73 EXPRESSION TAG
SEQRES 1 A 288 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 A 288 GLY ARG HIS MET GLU LEU GLY THR LEU GLU GLY PHE MET
SEQRES 3 A 288 VAL SER ALA HIS PHE ILE LEU ILE HIS THR ILE CYS HIS
SEQRES 4 A 288 GLY ALA TRP LEU TRP TYR LYS LEU ILE PRO LEU LEU GLN
SEQRES 5 A 288 SER ALA GLY HIS ASN ALA THR ALA ILE ASP LEU VAL ALA
SEQRES 6 A 288 SER GLY ILE ASP PRO ARG GLN LEU GLU GLN ILE GLY THR
SEQRES 7 A 288 TRP GLU GLN TYR SER GLU PRO LEU PHE THR LEU ILE GLU
SEQRES 8 A 288 SER ILE PRO GLU GLY LYS LYS VAL ILE LEU VAL GLY GLU
SEQRES 9 A 288 SER GLY GLY GLY ILE ASN ILE ALA LEU ALA ALA GLU LYS
SEQRES 10 A 288 TYR PRO GLU LYS VAL SER ALA LEU VAL PHE HIS ASN ALA
SEQRES 11 A 288 LEU MET PRO ASP ILE ASP HIS SER PRO ALA PHE VAL TYR
SEQRES 12 A 288 LYS LYS PHE SER GLU VAL PHE THR ASP TRP LYS ASP SER
SEQRES 13 A 288 ILE PHE SER ASN TYR THR TYR GLY ASN ASP THR VAL THR
SEQRES 14 A 288 ALA VAL GLU LEU GLY ASP ARG THR LEU ALA GLU ASN ILE
SEQRES 15 A 288 PHE SER ASN SER PRO ILE GLU ASP VAL GLU LEU ALA LYS
SEQRES 16 A 288 HIS LEU VAL ARG LYS GLY SER PHE PHE GLU GLN ASP LEU
SEQRES 17 A 288 ASP THR LEU PRO ASN PHE THR SER GLU GLY TYR GLY SER
SEQRES 18 A 288 ILE ARG ARG VAL TYR VAL TYR GLY GLU GLU ASP GLN ILE
SEQRES 19 A 288 PHE SER ARG ASP PHE GLN LEU TRP GLN ILE ASN ASN TYR
SEQRES 20 A 288 LYS PRO ASP LYS VAL TYR CYS VAL PRO SER ALA ASP HIS
SEQRES 21 A 288 LYS ILE GLN ILE SER LYS VAL ASN GLU LEU ALA GLN ILE
SEQRES 22 A 288 LEU GLN GLU VAL ALA ASN SER ALA SER ASP LEU LEU ALA
SEQRES 23 A 288 VAL ALA
SEQRES 1 B 288 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 B 288 GLY ARG HIS MET GLU LEU GLY THR LEU GLU GLY PHE MET
SEQRES 3 B 288 VAL SER ALA HIS PHE ILE LEU ILE HIS THR ILE CYS HIS
SEQRES 4 B 288 GLY ALA TRP LEU TRP TYR LYS LEU ILE PRO LEU LEU GLN
SEQRES 5 B 288 SER ALA GLY HIS ASN ALA THR ALA ILE ASP LEU VAL ALA
SEQRES 6 B 288 SER GLY ILE ASP PRO ARG GLN LEU GLU GLN ILE GLY THR
SEQRES 7 B 288 TRP GLU GLN TYR SER GLU PRO LEU PHE THR LEU ILE GLU
SEQRES 8 B 288 SER ILE PRO GLU GLY LYS LYS VAL ILE LEU VAL GLY GLU
SEQRES 9 B 288 SER GLY GLY GLY ILE ASN ILE ALA LEU ALA ALA GLU LYS
SEQRES 10 B 288 TYR PRO GLU LYS VAL SER ALA LEU VAL PHE HIS ASN ALA
SEQRES 11 B 288 LEU MET PRO ASP ILE ASP HIS SER PRO ALA PHE VAL TYR
SEQRES 12 B 288 LYS LYS PHE SER GLU VAL PHE THR ASP TRP LYS ASP SER
SEQRES 13 B 288 ILE PHE SER ASN TYR THR TYR GLY ASN ASP THR VAL THR
SEQRES 14 B 288 ALA VAL GLU LEU GLY ASP ARG THR LEU ALA GLU ASN ILE
SEQRES 15 B 288 PHE SER ASN SER PRO ILE GLU ASP VAL GLU LEU ALA LYS
SEQRES 16 B 288 HIS LEU VAL ARG LYS GLY SER PHE PHE GLU GLN ASP LEU
SEQRES 17 B 288 ASP THR LEU PRO ASN PHE THR SER GLU GLY TYR GLY SER
SEQRES 18 B 288 ILE ARG ARG VAL TYR VAL TYR GLY GLU GLU ASP GLN ILE
SEQRES 19 B 288 PHE SER ARG ASP PHE GLN LEU TRP GLN ILE ASN ASN TYR
SEQRES 20 B 288 LYS PRO ASP LYS VAL TYR CYS VAL PRO SER ALA ASP HIS
SEQRES 21 B 288 LYS ILE GLN ILE SER LYS VAL ASN GLU LEU ALA GLN ILE
SEQRES 22 B 288 LEU GLN GLU VAL ALA ASN SER ALA SER ASP LEU LEU ALA
SEQRES 23 B 288 VAL ALA
HET CA A 301 1
HET MPD A 302 8
HET MPD A 303 8
HET CA B 301 1
HET MPD B 302 8
HET MPD B 303 8
HETNAM CA CALCIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 CA 2(CA 2+)
FORMUL 4 MPD 4(C6 H14 O2)
FORMUL 9 HOH *43(H2 O)
HELIX 1 1 GLY A 15 TYR A 20 5 6
HELIX 2 2 LYS A 21 ALA A 29 1 9
HELIX 3 3 GLN A 47 ILE A 51 5 5
HELIX 4 4 THR A 53 SER A 58 1 6
HELIX 5 5 SER A 58 SER A 67 1 10
HELIX 6 6 GLY A 81 TYR A 93 1 13
HELIX 7 7 ALA A 115 PHE A 125 1 11
HELIX 8 8 GLY A 149 ASN A 156 1 8
HELIX 9 9 PRO A 162 HIS A 171 1 10
HELIX 10 10 PHE A 179 LEU A 186 1 8
HELIX 11 11 GLY A 193 ILE A 197 5 5
HELIX 12 12 SER A 211 TYR A 222 1 12
HELIX 13 13 LYS A 236 LYS A 241 1 6
HELIX 14 14 LYS A 241 SER A 257 1 17
HELIX 15 15 GLY B 15 TYR B 20 5 6
HELIX 16 16 LYS B 21 ALA B 29 1 9
HELIX 17 17 GLN B 47 ILE B 51 5 5
HELIX 18 18 THR B 53 SER B 58 1 6
HELIX 19 19 SER B 58 SER B 67 1 10
HELIX 20 20 GLY B 81 TYR B 93 1 13
HELIX 21 21 ALA B 115 PHE B 125 1 11
HELIX 22 22 GLY B 149 ASN B 156 1 8
HELIX 23 23 PRO B 162 HIS B 171 1 10
HELIX 24 24 PHE B 179 LEU B 186 1 8
HELIX 25 25 GLY B 193 ILE B 197 5 5
HELIX 26 26 SER B 211 TYR B 222 1 12
HELIX 27 27 LYS B 236 LYS B 241 1 6
HELIX 28 28 LYS B 241 SER B 257 1 17
SHEET 1 A 6 ASN A 32 ALA A 35 0
SHEET 2 A 6 HIS A 5 ILE A 9 1 N PHE A 6 O ASN A 32
SHEET 3 A 6 VAL A 74 GLU A 79 1 O VAL A 77 N ILE A 9
SHEET 4 A 6 VAL A 97 HIS A 103 1 O VAL A 101 N LEU A 76
SHEET 5 A 6 ARG A 198 GLY A 204 1 O VAL A 200 N PHE A 102
SHEET 6 A 6 LYS A 226 VAL A 230 1 O LYS A 226 N TYR A 201
SHEET 1 B 3 ILE A 132 TYR A 138 0
SHEET 2 B 3 ASP A 141 GLU A 147 -1 O VAL A 143 N TYR A 136
SHEET 3 B 3 GLY A 176 SER A 177 -1 O GLY A 176 N VAL A 146
SHEET 1 C 6 ASN B 32 ALA B 35 0
SHEET 2 C 6 HIS B 5 ILE B 9 1 N PHE B 6 O ASN B 32
SHEET 3 C 6 VAL B 74 GLU B 79 1 O VAL B 77 N ILE B 9
SHEET 4 C 6 VAL B 97 HIS B 103 1 O VAL B 101 N LEU B 76
SHEET 5 C 6 ARG B 198 GLY B 204 1 O ARG B 198 N LEU B 100
SHEET 6 C 6 LYS B 226 VAL B 230 1 O LYS B 226 N TYR B 201
SHEET 1 D 3 ILE B 132 TYR B 138 0
SHEET 2 D 3 ASP B 141 GLU B 147 -1 O VAL B 143 N TYR B 136
SHEET 3 D 3 GLY B 176 SER B 177 -1 O GLY B 176 N VAL B 146
LINK CA CA B 301 O2 MPD B 302 1555 1555 2.54
LINK CA CA A 301 O2 MPD A 302 1555 1555 3.16
SITE 1 AC1 5 THR A 11 SER A 80 HIS A 235 LYS A 236
SITE 2 AC1 5 MPD A 302
SITE 1 AC2 5 THR A 11 SER A 80 GLY A 81 ILE A 209
SITE 2 AC2 5 CA A 301
SITE 1 AC3 8 ILE A 12 TYR A 118 PHE A 133 THR A 144
SITE 2 AC3 8 ALA A 145 SER A 177 PHE A 178 HOH A 407
SITE 1 AC4 4 THR B 11 HIS B 235 LYS B 236 MPD B 302
SITE 1 AC5 7 THR B 11 ILE B 12 SER B 80 GLY B 81
SITE 2 AC5 7 LEU B 106 CA B 301 MPD B 303
SITE 1 AC6 6 TYR B 118 PHE B 133 THR B 144 ALA B 145
SITE 2 AC6 6 PHE B 178 MPD B 302
CRYST1 48.450 68.529 162.116 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 0.020640 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014592 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006168 0.00000
TER 2037 SER A 257
TER 4080 LEU B 259
MASTER 413 0 6 28 18 0 11 6 4155 2 34 46
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