HEADER TRANSFERASE 24-DEC-03 1V7V
TITLE CRYSTAL STRUCTURE OF VIBRIO PROTEOLYTICUS CHITOBIOSE PHOSPHORYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHITOBIOSE PHOSPHORYLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.4.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO PROTEOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 671;
SOURCE 4 GENE: CHBP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21GOLD(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30B-CHBP
KEYWDS BETA-SANDWICH, (ALPHA/ALPHA)6 BARREL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HIDAKA,Y.HONDA,S.NIRASAWA,M.KITAOKA,K.HAYASHI,T.WAKAGI,H.SHOUN,
AUTHOR 2 S.FUSHINOBU
REVDAT 4 27-DEC-23 1V7V 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1V7V 1 VERSN
REVDAT 2 24-FEB-09 1V7V 1 VERSN
REVDAT 1 22-JUN-04 1V7V 0
JRNL AUTH M.HIDAKA,Y.HONDA,M.KITAOKA,S.NIRASAWA,K.HAYASHI,T.WAKAGI,
JRNL AUTH 2 H.SHOUN,S.FUSHINOBU
JRNL TITL CHITOBIOSE PHOSPHORYLASE FROM VIBRIO PROTEOLYTICUS, A MEMBER
JRNL TITL 2 OF GLYCOSYL TRANSFERASE FAMILY 36, HAS A CLAN GH-L-LIKE
JRNL TITL 3 (ALPHA/ALPHA)(6) BARREL FOLD.
JRNL REF STRUCTURE V. 12 937 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15274915
JRNL DOI 10.1016/J.STR.2004.03.027
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.HONDA,M.KITAOKA,K.HAYASHI
REMARK 1 TITL REACTION MECHANISM OF CHITOBIOSE PHOSPHORYLASE FROM VIBRIO
REMARK 1 TITL 2 PROTEOLYTICUS: IDENTIFICATION OF FAMILY 36
REMARK 1 TITL 3 GLYCOSYLTRANSFERASE IN VIBRIO
REMARK 1 REF BIOCHEM.J. V. 377 225 2004
REMARK 1 REFN ISSN 0264-6021
REMARK 1 DOI 10.1042/BJ20031171
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2109709.680
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 70781
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 SET) : 0.162
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3588
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10863
REMARK 3 BIN R VALUE (WORKING SET) : 0.1850
REMARK 3 BIN FREE R VALUE : 0.2250
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 571
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6222
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 676
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.38000
REMARK 3 B22 (A**2) : 3.32000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : 0.07
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.370 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.870 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.450 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.540 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 51.55
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000006316.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000, 0.97120, 0.97848,
REMARK 200 0.97960
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ACSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70781
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.22800
REMARK 200 R SYM FOR SHELL (I) : 0.22800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.330
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, HEPES, CALCIUM CHLORIDE, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 70.47300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.29000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.47300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.29000
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 DIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: 1-X, Y, 1-Z.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 129.25278
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 79.18630
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 GLU A 395
REMARK 465 LYS A 396
REMARK 465 GLU A 397
REMARK 465 ASP A 398
REMARK 465 VAL A 399
REMARK 465 ALA A 400
REMARK 465 PRO A 401
REMARK 465 SER A 402
REMARK 465 LYS A 403
REMARK 465 SER A 404
REMARK 465 PRO A 405
REMARK 465 THR A 406
REMARK 465 VAL A 407
REMARK 465 VAL A 408
REMARK 465 PRO A 409
REMARK 465 THR A 410
REMARK 465 PRO A 411
REMARK 465 SER A 412
REMARK 465 ASP A 413
REMARK 465 GLU A 414
REMARK 465 ASP A 415
REMARK 465 LYS A 416
REMARK 465 HIS A 802
REMARK 465 HIS A 803
REMARK 465 HIS A 804
REMARK 465 HIS A 805
REMARK 465 HIS A 806
REMARK 465 HIS A 807
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 19 44.41 -85.55
REMARK 500 GLU A 31 -82.21 -121.12
REMARK 500 ASN A 48 -62.43 65.11
REMARK 500 PRO A 67 -167.48 -79.76
REMARK 500 ASN A 114 51.54 39.16
REMARK 500 ASP A 129 67.94 -106.21
REMARK 500 SER A 158 -47.23 82.55
REMARK 500 PRO A 180 115.02 -38.29
REMARK 500 PHE A 194 -68.21 -94.20
REMARK 500 ALA A 238 123.99 -171.60
REMARK 500 CYS A 241 160.42 81.25
REMARK 500 TYR A 242 -164.22 72.52
REMARK 500 ALA A 319 -74.30 -154.04
REMARK 500 SER A 332 -156.49 70.89
REMARK 500 SER A 336 -154.52 -150.35
REMARK 500 ASP A 492 69.76 -69.65
REMARK 500 LYS A 636 -129.77 45.66
REMARK 500 ARG A 658 78.87 -108.93
REMARK 500 ILE A 682 -55.41 73.14
REMARK 500 HIS A 700 123.45 -37.80
REMARK 500 HIS A 705 74.63 72.45
REMARK 500 TRP A 707 -78.09 66.77
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 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 127 O
REMARK 620 2 GLY A 791 O 154.4
REMARK 620 3 ASP A 793 OD2 89.2 90.2
REMARK 620 4 HOH A1048 O 63.5 141.4 80.4
REMARK 620 5 HOH A1088 O 82.5 72.0 84.1 142.5
REMARK 620 6 HOH A1341 O 90.4 83.6 164.7 112.9 80.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 140 O
REMARK 620 2 GLU A 459 OE1 78.6
REMARK 620 3 GLU A 459 OE2 80.3 52.8
REMARK 620 4 HOH A1279 O 86.8 146.7 153.0
REMARK 620 5 HOH A1412 O 91.1 142.2 89.7 66.8
REMARK 620 6 HOH A1435 O 163.8 100.1 86.1 101.8 80.1
REMARK 620 7 HOH A1678 O 102.7 72.9 124.3 81.6 144.7 92.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 186 OD1
REMARK 620 2 LEU A 187 O 83.9
REMARK 620 3 ASN A 190 O 161.0 79.9
REMARK 620 4 GLY A 196 O 87.6 87.6 101.4
REMARK 620 5 HOH A1227 O 87.1 84.2 81.5 170.7
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 CA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V7W RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH GLCNAC
REMARK 900 RELATED ID: 1V7X RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH GLCNAC AND SULFATE
DBREF 1V7V A 1 801 UNP Q76IQ9 Q76IQ9_VIBPR 1 801
SEQADV 1V7V HIS A 802 UNP Q76IQ9 EXPRESSION TAG
SEQADV 1V7V HIS A 803 UNP Q76IQ9 EXPRESSION TAG
SEQADV 1V7V HIS A 804 UNP Q76IQ9 EXPRESSION TAG
SEQADV 1V7V HIS A 805 UNP Q76IQ9 EXPRESSION TAG
SEQADV 1V7V HIS A 806 UNP Q76IQ9 EXPRESSION TAG
SEQADV 1V7V HIS A 807 UNP Q76IQ9 EXPRESSION TAG
SEQRES 1 A 807 MET LYS TYR GLY TYR PHE ASP ASN ASP ASN ARG GLU TYR
SEQRES 2 A 807 VAL ILE THR ARG PRO ASP VAL PRO ALA PRO TRP THR ASN
SEQRES 3 A 807 TYR LEU GLY THR GLU LYS PHE CYS THR VAL ILE SER HIS
SEQRES 4 A 807 ASN ALA GLY GLY TYR SER PHE TYR ASN SER PRO GLU TYR
SEQRES 5 A 807 ASN ARG VAL THR LYS PHE ARG PRO ASN ALA THR PHE ASP
SEQRES 6 A 807 ARG PRO GLY HIS TYR VAL TYR LEU ARG ASP ASP ASP SER
SEQRES 7 A 807 GLY ASP TYR TRP SER ILE SER TRP GLN PRO VAL ALA LYS
SEQRES 8 A 807 SER LEU ASP GLU ALA GLN TYR GLN ILE ARG HIS GLY LEU
SEQRES 9 A 807 SER TYR SER LYS PHE GLN CYS ASP TYR ASN GLY ILE HIS
SEQRES 10 A 807 ALA ARG LYS THR LEU PHE VAL PRO LYS GLY GLU ASP ALA
SEQRES 11 A 807 GLU ILE TRP ASP VAL VAL ILE LYS ASN THR SER ASP GLN
SEQRES 12 A 807 VAL ARG THR ILE SER ALA PHE SER PHE VAL GLU PHE SER
SEQRES 13 A 807 PHE SER HIS ILE GLN SER ASP ASN GLN ASN HIS GLN MET
SEQRES 14 A 807 SER LEU TYR SER ALA GLY THR ALA TYR ARG PRO GLY LEU
SEQRES 15 A 807 ILE GLU TYR ASP LEU TYR TYR ASN THR ASP ASP PHE GLU
SEQRES 16 A 807 GLY PHE TYR TYR LEU ALA SER THR PHE ASP PRO ASP SER
SEQRES 17 A 807 TYR ASP GLY GLN ARG ASP ARG PHE LEU GLY LEU TYR ARG
SEQRES 18 A 807 ASP GLU ALA ASN PRO LEU ALA VAL GLU GLN GLY ARG CYS
SEQRES 19 A 807 SER ASN SER ALA GLN THR CYS TYR ASN HIS CYS GLY SER
SEQRES 20 A 807 LEU HIS LYS GLN PHE THR LEU GLN PRO GLY GLU GLU ILE
SEQRES 21 A 807 ARG PHE ALA TYR ILE LEU GLY ILE GLY LYS GLY ASN GLY
SEQRES 22 A 807 GLU ARG LEU ARG GLU HIS TYR GLN ASP VAL ALA ASN ILE
SEQRES 23 A 807 ASP ALA ALA PHE ALA ALA ILE LYS ALA HIS TRP ASP GLU
SEQRES 24 A 807 ARG CYS ALA LYS PHE GLN VAL LYS SER PRO ASN GLN GLY
SEQRES 25 A 807 LEU ASP THR MET ILE ASN ALA TRP THR LEU TYR GLN ALA
SEQRES 26 A 807 GLU THR CYS VAL VAL TRP SER ARG PHE ALA SER PHE ILE
SEQRES 27 A 807 GLU VAL GLY GLY ARG THR GLY LEU GLY TYR ARG ASP THR
SEQRES 28 A 807 ALA GLN ASP ALA ILE SER VAL PRO HIS ALA ASN PRO GLU
SEQRES 29 A 807 MET THR ARG LYS ARG ILE VAL ASP LEU LEU ARG GLY GLN
SEQRES 30 A 807 VAL LYS ALA GLY TYR GLY LEU HIS LEU PHE ASP PRO ASP
SEQRES 31 A 807 TRP PHE ASP PRO GLU LYS GLU ASP VAL ALA PRO SER LYS
SEQRES 32 A 807 SER PRO THR VAL VAL PRO THR PRO SER ASP GLU ASP LYS
SEQRES 33 A 807 ILE HIS GLY ILE LYS ASP THR CYS SER ASP ASP HIS LEU
SEQRES 34 A 807 TRP LEU ILE PRO THR ILE CYS LYS TYR VAL MET GLU THR
SEQRES 35 A 807 GLY GLU THR SER PHE PHE ASP GLN MET ILE PRO TYR ALA
SEQRES 36 A 807 ASP GLY GLY GLU ALA SER VAL TYR GLU HIS MET LYS ALA
SEQRES 37 A 807 ALA LEU ASP PHE SER ALA GLU TYR VAL GLY GLN THR GLY
SEQRES 38 A 807 ILE CYS LYS GLY LEU ARG ALA ASP TRP ASN ASP CYS LEU
SEQRES 39 A 807 ASN LEU GLY GLY GLY GLU SER SER MET VAL SER PHE LEU
SEQRES 40 A 807 HIS PHE TRP ALA LEU GLN GLU PHE ILE ASP LEU ALA LYS
SEQRES 41 A 807 PHE LEU GLY LYS ASP GLN ASP VAL ASN THR TYR THR GLU
SEQRES 42 A 807 MET ALA ALA ASN VAL ARG GLU ALA CYS GLU THR HIS LEU
SEQRES 43 A 807 TRP ASP ASP GLU GLY GLY TRP TYR ILE ARG GLY LEU THR
SEQRES 44 A 807 LYS ASN GLY ASP LYS ILE GLY THR ALA GLN GLN GLN GLU
SEQRES 45 A 807 GLY ARG VAL HIS LEU GLU SER ASN THR LEU ALA VAL LEU
SEQRES 46 A 807 SER GLY LEU ALA SER GLN GLU ARG GLY GLU GLN ALA MET
SEQRES 47 A 807 ASP ALA VAL ASP GLU HIS LEU PHE SER PRO TYR GLY LEU
SEQRES 48 A 807 HIS LEU ASN ALA PRO SER PHE SER THR PRO ASN ASP ASP
SEQRES 49 A 807 ILE GLY PHE VAL THR ARG VAL TYR GLN GLY VAL LYS GLU
SEQRES 50 A 807 ASN GLY ALA ILE PHE SER HIS PRO ASN PRO TRP ALA TRP
SEQRES 51 A 807 VAL ALA GLU THR LYS LEU GLY ARG GLY ASP ARG ALA MET
SEQRES 52 A 807 LYS PHE TYR ASP ALA LEU ASN PRO TYR ASN GLN ASN ASP
SEQRES 53 A 807 ILE ILE GLU LYS ARG ILE ALA GLU PRO TYR SER TYR VAL
SEQRES 54 A 807 GLN PHE ILE MET GLY ARG ASP HIS GLN ASP HIS GLY ARG
SEQRES 55 A 807 ALA ASN HIS PRO TRP LEU THR GLY THR SER GLY TRP ALA
SEQRES 56 A 807 TYR PHE ALA VAL THR ASN TYR ILE LEU GLY VAL GLN SER
SEQRES 57 A 807 GLY PHE THR GLY LEU SER VAL ASP PRO CYS ILE PRO SER
SEQRES 58 A 807 ASP TRP PRO GLY PHE GLU VAL THR ARG GLN TRP ARG GLY
SEQRES 59 A 807 ALA THR TYR HIS ILE GLN VAL GLU ASN PRO ASP HIS VAL
SEQRES 60 A 807 SER LYS GLY VAL LYS SER ILE THR LEU ASN GLY ALA PRO
SEQRES 61 A 807 ILE GLN GLY ARG ILE PRO PRO GLN ALA GLN GLY SER ASP
SEQRES 62 A 807 ASN GLN VAL VAL VAL VAL LEU GLY HIS HIS HIS HIS HIS
SEQRES 63 A 807 HIS
HET CA A1001 1
HET CA A1002 1
HET CA A1003 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
FORMUL 5 HOH *676(H2 O)
HELIX 1 1 HIS A 159 GLN A 165 1 7
HELIX 2 2 ASN A 166 LEU A 171 1 6
HELIX 3 3 ARG A 213 GLY A 218 1 6
HELIX 4 4 PRO A 226 GLY A 232 1 7
HELIX 5 5 GLY A 271 TYR A 280 1 10
HELIX 6 6 ASP A 282 ALA A 302 1 21
HELIX 7 7 ASN A 310 ASN A 318 1 9
HELIX 8 8 ALA A 319 SER A 332 1 14
HELIX 9 9 TYR A 348 ALA A 355 1 8
HELIX 10 10 ASN A 362 GLY A 376 1 15
HELIX 11 11 ASP A 388 ASP A 393 5 6
HELIX 12 12 GLY A 419 THR A 423 5 5
HELIX 13 13 ASP A 426 GLY A 443 1 18
HELIX 14 14 GLU A 444 ASP A 449 5 6
HELIX 15 15 VAL A 462 TYR A 476 1 15
HELIX 16 16 SER A 502 GLY A 523 1 22
HELIX 17 17 LYS A 524 LEU A 546 1 23
HELIX 18 18 LEU A 577 SER A 586 1 10
HELIX 19 19 SER A 590 LEU A 605 1 16
HELIX 20 20 GLY A 626 VAL A 631 5 6
HELIX 21 21 PRO A 645 LEU A 656 1 12
HELIX 22 22 ARG A 658 ASN A 670 1 13
HELIX 23 23 PRO A 671 ASN A 675 5 5
HELIX 24 24 ILE A 677 ILE A 682 1 6
HELIX 25 25 GLY A 710 TYR A 722 1 13
SHEET 1 A10 GLY A 4 ASP A 7 0
SHEET 2 A10 GLU A 12 ILE A 15 -1 O GLU A 12 N ASP A 7
SHEET 3 A10 ALA A 96 GLY A 103 -1 O ILE A 100 N ILE A 15
SHEET 4 A10 TYR A 106 TYR A 113 -1 O TYR A 106 N GLY A 103
SHEET 5 A10 ILE A 116 PHE A 123 -1 O LYS A 120 N PHE A 109
SHEET 6 A10 ALA A 130 ASN A 139 -1 O LYS A 138 N HIS A 117
SHEET 7 A10 GLU A 259 ILE A 268 -1 O LEU A 266 N GLU A 131
SHEET 8 A10 PHE A 197 SER A 202 -1 N ALA A 201 O ILE A 265
SHEET 9 A10 LEU A 182 LEU A 187 -1 N ILE A 183 O LEU A 200
SHEET 10 A10 ALA A 174 ARG A 179 -1 N GLY A 175 O ASP A 186
SHEET 1 B 3 THR A 25 LEU A 28 0
SHEET 2 B 3 PHE A 33 SER A 38 -1 O THR A 35 N LEU A 28
SHEET 3 B 3 GLY A 43 TYR A 47 -1 O TYR A 44 N VAL A 36
SHEET 1 C 5 TYR A 81 SER A 83 0
SHEET 2 C 5 TYR A 70 ASP A 75 -1 N LEU A 73 O TRP A 82
SHEET 3 C 5 ARG A 145 PHE A 152 -1 O PHE A 150 N TYR A 72
SHEET 4 C 5 HIS A 244 LEU A 254 -1 O LEU A 254 N ARG A 145
SHEET 5 C 5 SER A 208 GLN A 212 -1 N SER A 208 O HIS A 249
SHEET 1 D 6 PHE A 304 LYS A 307 0
SHEET 2 D 6 GLY A 745 TRP A 752 -1 O GLU A 747 N LYS A 307
SHEET 3 D 6 ALA A 755 GLU A 762 -1 O VAL A 761 N PHE A 746
SHEET 4 D 6 ASP A 793 LEU A 800 1 O ASN A 794 N HIS A 758
SHEET 5 D 6 VAL A 771 LEU A 776 -1 N SER A 773 O VAL A 799
SHEET 6 D 6 ALA A 779 ILE A 781 -1 O ALA A 779 N LEU A 776
SHEET 1 E 2 LEU A 346 GLY A 347 0
SHEET 2 E 2 LEU A 386 PHE A 387 -1 O PHE A 387 N LEU A 346
SHEET 1 F 2 MET A 451 PRO A 453 0
SHEET 2 F 2 GLU A 459 SER A 461 -1 O ALA A 460 N ILE A 452
SHEET 1 G 4 LYS A 484 LEU A 486 0
SHEET 2 G 4 ASN A 495 SER A 501 -1 O ASN A 495 N LEU A 486
SHEET 3 G 4 GLY A 557 LEU A 558 -1 O LEU A 558 N GLU A 500
SHEET 4 G 4 LYS A 564 ILE A 565 -1 O ILE A 565 N GLY A 557
SHEET 1 H 2 TRP A 547 ASP A 548 0
SHEET 2 H 2 TRP A 553 TYR A 554 -1 O TRP A 553 N ASP A 548
SHEET 1 I 2 VAL A 575 HIS A 576 0
SHEET 2 I 2 ASN A 614 ALA A 615 -1 O ALA A 615 N VAL A 575
SHEET 1 J 2 PHE A 606 SER A 607 0
SHEET 2 J 2 GLY A 610 LEU A 611 -1 O GLY A 610 N SER A 607
SHEET 1 K 3 ILE A 641 PHE A 642 0
SHEET 2 K 3 VAL A 689 ILE A 692 -1 O ILE A 692 N ILE A 641
SHEET 3 K 3 ALA A 703 PRO A 706 -1 O ASN A 704 N PHE A 691
SHEET 1 L 2 VAL A 726 SER A 728 0
SHEET 2 L 2 LEU A 733 VAL A 735 -1 O SER A 734 N GLN A 727
SSBOND 1 CYS A 424 CYS A 493 1555 1555 2.03
LINK O GLY A 127 CA CA A1002 2655 1555 2.39
LINK O THR A 140 CA CA A1003 1565 1555 2.35
LINK OD1 ASP A 186 CA CA A1001 1555 1555 2.31
LINK O LEU A 187 CA CA A1001 1555 1555 2.42
LINK O ASN A 190 CA CA A1001 1555 1555 2.43
LINK O GLY A 196 CA CA A1001 1555 1555 2.70
LINK OE1 GLU A 459 CA CA A1003 1555 1555 2.36
LINK OE2 GLU A 459 CA CA A1003 1555 1555 2.56
LINK O GLY A 791 CA CA A1002 1555 1555 2.51
LINK OD2 ASP A 793 CA CA A1002 1555 1555 2.51
LINK CA CA A1001 O HOH A1227 1555 1555 2.30
LINK CA CA A1002 O HOH A1048 1555 1555 2.15
LINK CA CA A1002 O HOH A1088 1555 2655 2.25
LINK CA CA A1002 O HOH A1341 1555 1555 2.34
LINK CA CA A1003 O HOH A1279 1555 1565 2.59
LINK CA CA A1003 O HOH A1412 1555 1555 2.97
LINK CA CA A1003 O HOH A1435 1555 1555 2.41
LINK CA CA A1003 O HOH A1678 1555 1555 2.22
CISPEP 1 ARG A 66 PRO A 67 0 -1.60
CISPEP 2 GLN A 87 PRO A 88 0 1.35
CISPEP 3 ALA A 615 PRO A 616 0 -1.82
SITE 1 AC1 6 ASP A 186 LEU A 187 ASN A 190 GLY A 196
SITE 2 AC1 6 PHE A 197 HOH A1227
SITE 1 AC2 6 GLY A 127 GLY A 791 ASP A 793 HOH A1048
SITE 2 AC2 6 HOH A1088 HOH A1341
SITE 1 AC3 6 THR A 140 GLU A 459 HOH A1279 HOH A1412
SITE 2 AC3 6 HOH A1435 HOH A1678
CRYST1 140.946 70.580 80.045 90.00 98.40 90.00 C 1 2 1 4
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 0.007095 0.000000 0.001048 0.00000
SCALE2 0.000000 0.014168 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012629 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
