HEADER TOXIN 25-OCT-05 2ERP
TITLE CRYSTAL STRUCTURE OF VASCULAR APOPTOSIS-INDUCING PROTEIN-1(INHIBITOR-
TITLE 2 BOUND FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VASCULAR APOPTOSIS-INDUCING PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 184-610;
COMPND 5 SYNONYM: VAP-1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CROTALUS ATROX;
SOURCE 3 ORGANISM_COMMON: WESTERN DIAMONDBACK RATTLESNAKE;
SOURCE 4 ORGANISM_TAXID: 8730;
SOURCE 5 SECRETION: VENOM
KEYWDS METALLOPROTEASE, DISINTEGRIN, CALCIUM-BINDING, ADAM, SVMP, MDC
KEYWDS 2 PROTEIN, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.TAKEDA,T.IGARASHI,S.ARAKI
REVDAT 5 25-OCT-23 2ERP 1 HETSYN
REVDAT 4 29-JUL-20 2ERP 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-11 2ERP 1 VERSN
REVDAT 2 24-FEB-09 2ERP 1 VERSN
REVDAT 1 20-JUN-06 2ERP 0
JRNL AUTH S.TAKEDA,T.IGARASHI,H.MORI,S.ARAKI
JRNL TITL CRYSTAL STRUCTURES OF VAP1 REVEAL ADAMS' MDC DOMAIN
JRNL TITL 2 ARCHITECTURE AND ITS UNIQUE C-SHAPED SCAFFOLD
JRNL REF EMBO J. V. 25 2388 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16688218
JRNL DOI 10.1038/SJ.EMBOJ.7601131
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.IGARASHI,Y.OISHI,S.ARAKI,H.MORI,S.TAKEDA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC
REMARK 1 TITL 2 ANALYSIS OF TWO VASCULAR APOPTOSIS-INDUCING PROTEINS (VAPS)
REMARK 1 TITL 3 FROM CROTALUS ATROX VENOM
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 23295
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) : 0.208
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1195
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.06
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3430
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 129
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6558
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 119
REMARK 3 SOLVENT ATOMS : 35
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 0.920
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.570
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ERP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035011.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23345
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.950
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
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: 2ERO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG8000, 100MM SODIUM/CACODYLATE,
REMARK 280 20MM COBALTOUS CHLORIDE, PH 6.5, 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 43.17250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.01950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.68950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.01950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.17250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.68950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: ASYMMETRIC UNIT CONTAINS ONE DISULFIDE-LINKED HOMODIMER
REMARK 300 MOLECULE THAT IS THE BIOLOGICAL UNIT.
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: 4450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -91.37900
REMARK 350 BIOMT3 2 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 GLN A 184
REMARK 465 GLN B 184
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 THR A 277 -60.46 -104.03
REMARK 500 CYS A 310 -19.26 75.53
REMARK 500 ASP A 321 47.31 -77.27
REMARK 500 ASP A 348 -8.55 -59.98
REMARK 500 CYS A 352 26.77 -151.29
REMARK 500 CYS A 365 6.67 -69.90
REMARK 500 ASN A 386 -51.17 -136.36
REMARK 500 TYR A 409 20.95 48.69
REMARK 500 CYS A 425 129.55 -39.94
REMARK 500 ARG A 462 129.97 -177.91
REMARK 500 ASP A 466 -162.80 -119.97
REMARK 500 CYS A 504 75.72 -118.39
REMARK 500 ASP A 524 -55.53 -22.59
REMARK 500 PHE A 527 -17.38 -49.63
REMARK 500 HIS A 535 -43.00 -27.33
REMARK 500 GLN A 543 -70.35 -158.12
REMARK 500 PRO A 551 -32.45 -39.63
REMARK 500 LYS A 591 105.40 -58.02
REMARK 500 CYS A 592 -83.33 -87.34
REMARK 500 ALA A 593 -163.20 -77.66
REMARK 500 ASP A 594 -88.59 -58.64
REMARK 500 ARG A 595 49.67 -96.23
REMARK 500 SER A 599 -69.50 -99.52
REMARK 500 PRO A 609 98.69 -58.79
REMARK 500 TYR B 215 43.96 -109.12
REMARK 500 ARG B 239 4.94 -67.98
REMARK 500 THR B 255 151.11 162.50
REMARK 500 ASP B 278 -70.03 -93.68
REMARK 500 CYS B 310 -28.01 69.95
REMARK 500 TYR B 314 -10.76 -146.64
REMARK 500 SER B 364 144.52 163.03
REMARK 500 ALA B 432 -14.76 -48.40
REMARK 500 GLN B 439 128.24 -24.03
REMARK 500 ALA B 444 -64.94 -122.11
REMARK 500 THR B 482 150.60 -45.38
REMARK 500 LYS B 493 71.53 48.60
REMARK 500 PRO B 505 107.79 -59.71
REMARK 500 ALA B 525 -35.73 -39.17
REMARK 500 ASN B 534 -156.45 -72.76
REMARK 500 GLN B 543 -70.50 -109.90
REMARK 500 ASN B 544 -5.10 -151.78
REMARK 500 LYS B 555 27.07 -71.25
REMARK 500 ASN B 564 77.61 -58.93
REMARK 500 PRO B 566 3.63 -64.37
REMARK 500 GLU B 567 -63.73 -103.22
REMARK 500 ASN B 568 124.09 -37.61
REMARK 500 ALA B 593 -173.09 175.88
REMARK 500 SER B 599 -65.85 -97.42
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 3CO A 703 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 238 NE2
REMARK 620 2 HIS A 243 NE2 90.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 700 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 335 NE2
REMARK 620 2 HIS A 339 NE2 94.6
REMARK 620 3 HIS A 345 NE2 99.9 100.4
REMARK 620 4 GM6 A1002 OAG 109.5 97.6 143.9
REMARK 620 5 GM6 A1002 OAE 104.7 160.5 79.9 72.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 405 O
REMARK 620 2 ASN A 408 OD1 58.6
REMARK 620 3 PHE A 410 O 147.7 90.7
REMARK 620 4 GLU A 412 OE1 79.6 70.4 80.6
REMARK 620 5 GLU A 415 OE1 124.8 149.8 76.1 80.6
REMARK 620 6 GLU A 415 OE2 80.5 138.1 126.4 94.9 50.7
REMARK 620 7 ASP A 418 OD1 86.6 73.2 94.3 143.1 133.9 116.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 469 OD2
REMARK 620 2 MET A 470 O 81.1
REMARK 620 3 ASP A 472 OD1 162.5 84.9
REMARK 620 4 ASP A 472 OD2 142.1 109.0 53.3
REMARK 620 5 ASP A 483 OD1 97.5 167.3 98.4 64.5
REMARK 620 6 ARG A 484 O 80.7 89.0 88.7 134.2 103.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 700 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 335 NE2
REMARK 620 2 HIS B 339 NE2 89.1
REMARK 620 3 HIS B 345 NE2 99.4 102.4
REMARK 620 4 GM6 B1001 OAG 113.5 103.8 137.9
REMARK 620 5 GM6 B1001 OAE 91.9 177.7 79.5 74.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 405 O
REMARK 620 2 ASN B 408 OD1 65.3
REMARK 620 3 PHE B 410 O 149.4 86.6
REMARK 620 4 GLU B 412 OE1 76.5 83.1 89.0
REMARK 620 5 GLU B 415 OE1 127.3 159.1 76.6 84.2
REMARK 620 6 GLU B 415 OE2 80.1 144.9 128.5 94.6 52.9
REMARK 620 7 ASP B 418 OD2 86.1 78.5 100.4 158.8 116.4 94.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 469 OD2
REMARK 620 2 MET B 470 O 81.9
REMARK 620 3 ASP B 472 OD2 146.6 116.7
REMARK 620 4 ASP B 472 OD1 163.9 92.6 49.0
REMARK 620 5 ASP B 483 OD1 87.2 140.4 92.8 87.6
REMARK 620 6 ARG B 484 O 71.5 72.4 138.7 92.4 68.0
REMARK 620 7 ARG B 484 N 118.2 102.4 86.3 48.1 51.0 52.9
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ERO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(ORTHORHOMBIC CRYSTAL FORM)
REMARK 900 RELATED ID: 2ERQ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(TETRAGONAL CRYSTAL FORM)
DBREF 2ERP A 184 610 GB 11320556 BAB18307 184 610
DBREF 2ERP B 184 610 GB 11320556 BAB18307 184 610
SEQRES 1 A 427 GLN SER ASN LEU THR PRO GLU GLN GLN ARG TYR LEU ASN
SEQRES 2 A 427 ALA LYS LYS TYR VAL LYS LEU PHE LEU VAL ALA ASP TYR
SEQRES 3 A 427 ILE MET TYR LEU LYS TYR GLY ARG ASN LEU THR ALA VAL
SEQRES 4 A 427 ARG THR ARG MET TYR ASP ILE VAL ASN VAL ILE THR PRO
SEQRES 5 A 427 ILE TYR HIS ARG MET ASN ILE HIS VAL ALA LEU VAL GLY
SEQRES 6 A 427 LEU GLU ILE TRP SER ASN THR ASP LYS ILE ILE VAL GLN
SEQRES 7 A 427 SER SER ALA ASP VAL THR LEU ASP LEU PHE ALA LYS TRP
SEQRES 8 A 427 ARG ALA THR ASP LEU LEU SER ARG LYS SER HIS ASP ASN
SEQRES 9 A 427 ALA GLN LEU LEU THR GLY ILE ASN PHE ASN GLY PRO THR
SEQRES 10 A 427 ALA GLY LEU GLY TYR LEU GLY GLY ILE CYS ASN THR MET
SEQRES 11 A 427 TYR SER ALA GLY ILE VAL GLN ASP HIS SER LYS ILE HIS
SEQRES 12 A 427 HIS LEU VAL ALA ILE ALA MET ALA HIS GLU MET GLY HIS
SEQRES 13 A 427 ASN LEU GLY MET ASP HIS ASP LYS ASP THR CYS THR CYS
SEQRES 14 A 427 GLY THR ARG PRO CYS VAL MET ALA GLY ALA LEU SER CYS
SEQRES 15 A 427 GLU ALA SER PHE LEU PHE SER ASP CYS SER GLN LYS ASP
SEQRES 16 A 427 HIS ARG GLU PHE LEU ILE LYS ASN MET PRO GLN CYS ILE
SEQRES 17 A 427 LEU LYS LYS PRO LEU LYS THR ASP VAL VAL SER PRO ALA
SEQRES 18 A 427 VAL CYS GLY ASN TYR PHE VAL GLU VAL GLY GLU GLU CYS
SEQRES 19 A 427 ASP CYS GLY SER PRO ARG THR CYS ARG ASP PRO CYS CYS
SEQRES 20 A 427 ASP ALA THR THR CYS LYS LEU ARG GLN GLY ALA GLN CYS
SEQRES 21 A 427 ALA GLU GLY LEU CYS CYS ASP GLN CYS ARG PHE LYS GLY
SEQRES 22 A 427 ALA GLY THR GLU CYS ARG ALA ALA LYS ASP GLU CYS ASP
SEQRES 23 A 427 MET ALA ASP VAL CYS THR GLY ARG SER ALA GLU CYS THR
SEQRES 24 A 427 ASP ARG PHE GLN ARG ASN GLY GLN PRO CYS LYS ASN ASN
SEQRES 25 A 427 ASN GLY TYR CYS TYR ASN GLY LYS CYS PRO ILE MET ALA
SEQRES 26 A 427 ASP GLN CYS ILE ALA LEU PHE GLY PRO GLY ALA THR VAL
SEQRES 27 A 427 SER GLN ASP ALA CYS PHE GLN PHE ASN ARG GLU GLY ASN
SEQRES 28 A 427 HIS TYR GLY TYR CYS ARG LYS GLU GLN ASN THR LYS ILE
SEQRES 29 A 427 ALA CYS GLU PRO GLN ASP VAL LYS CYS GLY ARG LEU TYR
SEQRES 30 A 427 CYS PHE PRO ASN SER PRO GLU ASN LYS ASN PRO CYS ASN
SEQRES 31 A 427 ILE TYR TYR SER PRO ASN ASP GLU ASP LYS GLY MET VAL
SEQRES 32 A 427 LEU PRO GLY THR LYS CYS ALA ASP ARG LYS ALA CYS SER
SEQRES 33 A 427 ASN GLY GLN CYS VAL ASP VAL THR THR PRO TYR
SEQRES 1 B 427 GLN SER ASN LEU THR PRO GLU GLN GLN ARG TYR LEU ASN
SEQRES 2 B 427 ALA LYS LYS TYR VAL LYS LEU PHE LEU VAL ALA ASP TYR
SEQRES 3 B 427 ILE MET TYR LEU LYS TYR GLY ARG ASN LEU THR ALA VAL
SEQRES 4 B 427 ARG THR ARG MET TYR ASP ILE VAL ASN VAL ILE THR PRO
SEQRES 5 B 427 ILE TYR HIS ARG MET ASN ILE HIS VAL ALA LEU VAL GLY
SEQRES 6 B 427 LEU GLU ILE TRP SER ASN THR ASP LYS ILE ILE VAL GLN
SEQRES 7 B 427 SER SER ALA ASP VAL THR LEU ASP LEU PHE ALA LYS TRP
SEQRES 8 B 427 ARG ALA THR ASP LEU LEU SER ARG LYS SER HIS ASP ASN
SEQRES 9 B 427 ALA GLN LEU LEU THR GLY ILE ASN PHE ASN GLY PRO THR
SEQRES 10 B 427 ALA GLY LEU GLY TYR LEU GLY GLY ILE CYS ASN THR MET
SEQRES 11 B 427 TYR SER ALA GLY ILE VAL GLN ASP HIS SER LYS ILE HIS
SEQRES 12 B 427 HIS LEU VAL ALA ILE ALA MET ALA HIS GLU MET GLY HIS
SEQRES 13 B 427 ASN LEU GLY MET ASP HIS ASP LYS ASP THR CYS THR CYS
SEQRES 14 B 427 GLY THR ARG PRO CYS VAL MET ALA GLY ALA LEU SER CYS
SEQRES 15 B 427 GLU ALA SER PHE LEU PHE SER ASP CYS SER GLN LYS ASP
SEQRES 16 B 427 HIS ARG GLU PHE LEU ILE LYS ASN MET PRO GLN CYS ILE
SEQRES 17 B 427 LEU LYS LYS PRO LEU LYS THR ASP VAL VAL SER PRO ALA
SEQRES 18 B 427 VAL CYS GLY ASN TYR PHE VAL GLU VAL GLY GLU GLU CYS
SEQRES 19 B 427 ASP CYS GLY SER PRO ARG THR CYS ARG ASP PRO CYS CYS
SEQRES 20 B 427 ASP ALA THR THR CYS LYS LEU ARG GLN GLY ALA GLN CYS
SEQRES 21 B 427 ALA GLU GLY LEU CYS CYS ASP GLN CYS ARG PHE LYS GLY
SEQRES 22 B 427 ALA GLY THR GLU CYS ARG ALA ALA LYS ASP GLU CYS ASP
SEQRES 23 B 427 MET ALA ASP VAL CYS THR GLY ARG SER ALA GLU CYS THR
SEQRES 24 B 427 ASP ARG PHE GLN ARG ASN GLY GLN PRO CYS LYS ASN ASN
SEQRES 25 B 427 ASN GLY TYR CYS TYR ASN GLY LYS CYS PRO ILE MET ALA
SEQRES 26 B 427 ASP GLN CYS ILE ALA LEU PHE GLY PRO GLY ALA THR VAL
SEQRES 27 B 427 SER GLN ASP ALA CYS PHE GLN PHE ASN ARG GLU GLY ASN
SEQRES 28 B 427 HIS TYR GLY TYR CYS ARG LYS GLU GLN ASN THR LYS ILE
SEQRES 29 B 427 ALA CYS GLU PRO GLN ASP VAL LYS CYS GLY ARG LEU TYR
SEQRES 30 B 427 CYS PHE PRO ASN SER PRO GLU ASN LYS ASN PRO CYS ASN
SEQRES 31 B 427 ILE TYR TYR SER PRO ASN ASP GLU ASP LYS GLY MET VAL
SEQRES 32 B 427 LEU PRO GLY THR LYS CYS ALA ASP ARG LYS ALA CYS SER
SEQRES 33 B 427 ASN GLY GLN CYS VAL ASP VAL THR THR PRO TYR
MODRES 2ERP ASN A 218 ASN GLYCOSYLATION SITE
MODRES 2ERP ASN B 218 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET ZN A 700 1
HET CA A 701 1
HET CA A 702 1
HET 3CO A 703 1
HET GM6 A1002 28
HET ZN B 700 1
HET CA B 701 1
HET CA B 702 1
HET GM6 B1001 28
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM 3CO COBALT (III) ION
HETNAM GM6 3-(N-HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-
HETNAM 2 GM6 METHYLAMIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GM6 GM6001
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 CA 4(CA 2+)
FORMUL 8 3CO CO 3+
FORMUL 9 GM6 2(C20 H28 N4 O4)
FORMUL 14 HOH *35(H2 O)
HELIX 1 1 THR A 188 ALA A 197 1 10
HELIX 2 2 ASP A 208 TYR A 215 1 8
HELIX 3 3 ASN A 218 ARG A 239 1 22
HELIX 4 4 SER A 263 ASP A 278 1 16
HELIX 5 5 ILE A 325 LEU A 341 1 17
HELIX 6 6 SER A 372 MET A 387 1 16
HELIX 7 7 PRO A 388 LYS A 393 5 6
HELIX 8 8 ILE A 506 GLY A 516 1 11
HELIX 9 9 GLN A 523 ARG A 531 5 9
HELIX 10 10 GLN A 552 GLY A 557 5 6
HELIX 11 11 THR B 188 ALA B 197 1 10
HELIX 12 12 ASP B 208 TYR B 215 1 8
HELIX 13 13 ASN B 218 ARG B 239 1 22
HELIX 14 14 SER B 263 ASP B 278 1 16
HELIX 15 15 LEU B 279 ARG B 282 5 4
HELIX 16 16 ILE B 325 LEU B 341 1 17
HELIX 17 17 SER B 372 MET B 387 1 16
HELIX 18 18 GLN B 389 LYS B 393 5 5
HELIX 19 19 ILE B 506 PHE B 515 1 10
HELIX 20 20 GLN B 523 GLN B 528 1 6
HELIX 21 21 PHE B 529 GLY B 533 5 5
HELIX 22 22 ASP B 553 GLY B 557 5 5
SHEET 1 A 5 ILE A 242 ILE A 251 0
SHEET 2 A 5 LYS A 199 ALA A 207 1 N VAL A 201 O ALA A 245
SHEET 3 A 5 ASN A 287 THR A 292 1 O LEU A 291 N VAL A 206
SHEET 4 A 5 ALA A 316 GLN A 320 1 O GLY A 317 N LEU A 290
SHEET 5 A 5 GLY A 302 GLY A 304 -1 N LEU A 303 O ILE A 318
SHEET 1 B 2 CYS A 449 ASP A 450 0
SHEET 2 B 2 ARG A 453 PHE A 454 -1 O ARG A 453 N ASP A 450
SHEET 1 C 2 GLU A 460 ARG A 462 0
SHEET 2 C 2 ASP A 472 VAL A 473 -1 O ASP A 472 N ARG A 462
SHEET 1 D 2 PRO A 491 CYS A 492 0
SHEET 2 D 2 GLY A 497 TYR A 498 -1 O GLY A 497 N CYS A 492
SHEET 1 E 2 THR A 520 VAL A 521 0
SHEET 2 E 2 CYS A 561 PHE A 562 -1 O PHE A 562 N THR A 520
SHEET 1 F 2 ARG A 540 LYS A 541 0
SHEET 2 F 2 LYS A 546 ILE A 547 -1 O ILE A 547 N ARG A 540
SHEET 1 G 2 LYS A 596 CYS A 598 0
SHEET 2 G 2 CYS A 603 ASP A 605 -1 O VAL A 604 N ALA A 597
SHEET 1 H 5 ILE B 242 ILE B 251 0
SHEET 2 H 5 LYS B 199 ALA B 207 1 N ALA B 207 O GLU B 250
SHEET 3 H 5 ASN B 287 THR B 292 1 O LEU B 291 N VAL B 206
SHEET 4 H 5 ALA B 316 GLN B 320 1 O VAL B 319 N LEU B 290
SHEET 5 H 5 GLY B 302 GLY B 304 -1 N LEU B 303 O ILE B 318
SHEET 1 I 2 CYS B 449 ASP B 450 0
SHEET 2 I 2 ARG B 453 PHE B 454 -1 O ARG B 453 N ASP B 450
SHEET 1 J 2 GLU B 460 ARG B 462 0
SHEET 2 J 2 ASP B 472 VAL B 473 -1 O ASP B 472 N ARG B 462
SHEET 1 K 2 ASP B 469 MET B 470 0
SHEET 2 K 2 ARG B 484 PHE B 485 -1 O ARG B 484 N MET B 470
SHEET 1 L 2 PRO B 491 CYS B 492 0
SHEET 2 L 2 GLY B 497 TYR B 498 -1 O GLY B 497 N CYS B 492
SHEET 1 M 3 ALA B 519 VAL B 521 0
SHEET 2 M 3 TYR B 560 PRO B 563 -1 O PHE B 562 N THR B 520
SHEET 3 M 3 ASN B 573 ILE B 574 -1 O ASN B 573 N CYS B 561
SHEET 1 N 3 LYS B 591 ALA B 593 0
SHEET 2 N 3 LYS B 596 CYS B 598 -1 O LYS B 596 N ALA B 593
SHEET 3 N 3 CYS B 603 ASP B 605 -1 O VAL B 604 N ALA B 597
SSBOND 1 CYS A 310 CYS A 390 1555 1555 2.03
SSBOND 2 CYS A 350 CYS A 374 1555 1555 2.03
SSBOND 3 CYS A 352 CYS A 357 1555 1555 2.03
SSBOND 4 CYS A 365 CYS B 365 1555 1555 2.03
SSBOND 5 CYS A 406 CYS A 435 1555 1555 2.03
SSBOND 6 CYS A 417 CYS A 430 1555 1555 2.03
SSBOND 7 CYS A 419 CYS A 425 1555 1555 2.03
SSBOND 8 CYS A 429 CYS A 452 1555 1555 2.03
SSBOND 9 CYS A 443 CYS A 449 1555 1555 2.03
SSBOND 10 CYS A 448 CYS A 474 1555 1555 2.03
SSBOND 11 CYS A 461 CYS A 481 1555 1555 2.03
SSBOND 12 CYS A 468 CYS A 499 1555 1555 2.03
SSBOND 13 CYS A 492 CYS A 504 1555 1555 2.03
SSBOND 14 CYS A 511 CYS A 561 1555 1555 2.03
SSBOND 15 CYS A 526 CYS A 572 1555 1555 2.03
SSBOND 16 CYS A 539 CYS A 549 1555 1555 2.03
SSBOND 17 CYS A 556 CYS A 598 1555 1555 2.03
SSBOND 18 CYS A 592 CYS A 603 1555 1555 2.03
SSBOND 19 CYS B 310 CYS B 390 1555 1555 2.03
SSBOND 20 CYS B 350 CYS B 374 1555 1555 2.03
SSBOND 21 CYS B 352 CYS B 357 1555 1555 2.03
SSBOND 22 CYS B 406 CYS B 435 1555 1555 2.03
SSBOND 23 CYS B 417 CYS B 430 1555 1555 2.03
SSBOND 24 CYS B 419 CYS B 425 1555 1555 2.03
SSBOND 25 CYS B 429 CYS B 452 1555 1555 2.03
SSBOND 26 CYS B 443 CYS B 449 1555 1555 2.03
SSBOND 27 CYS B 448 CYS B 474 1555 1555 2.03
SSBOND 28 CYS B 461 CYS B 481 1555 1555 2.03
SSBOND 29 CYS B 468 CYS B 499 1555 1555 2.03
SSBOND 30 CYS B 492 CYS B 504 1555 1555 2.03
SSBOND 31 CYS B 511 CYS B 561 1555 1555 2.03
SSBOND 32 CYS B 526 CYS B 572 1555 1555 2.03
SSBOND 33 CYS B 539 CYS B 549 1555 1555 2.03
SSBOND 34 CYS B 556 CYS B 598 1555 1555 2.03
SSBOND 35 CYS B 592 CYS B 603 1555 1555 2.03
LINK ND2 ASN A 218 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN B 218 C1 NAG D 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.39
LINK NE2 HIS A 238 CO 3CO A 703 1555 1555 2.57
LINK NE2 HIS A 243 CO 3CO A 703 1555 1555 2.25
LINK NE2 HIS A 335 ZN ZN A 700 1555 1555 2.19
LINK NE2 HIS A 339 ZN ZN A 700 1555 1555 2.08
LINK NE2 HIS A 345 ZN ZN A 700 1555 1555 2.09
LINK O VAL A 405 CA CA A 701 1555 1555 2.65
LINK OD1 ASN A 408 CA CA A 701 1555 1555 2.04
LINK O PHE A 410 CA CA A 701 1555 1555 2.49
LINK OE1 GLU A 412 CA CA A 701 1555 1555 2.56
LINK OE1 GLU A 415 CA CA A 701 1555 1555 2.33
LINK OE2 GLU A 415 CA CA A 701 1555 1555 2.74
LINK OD1 ASP A 418 CA CA A 701 1555 1555 2.36
LINK OD2 ASP A 469 CA CA A 702 1555 1555 2.41
LINK O MET A 470 CA CA A 702 1555 1555 2.33
LINK OD1 ASP A 472 CA CA A 702 1555 1555 2.39
LINK OD2 ASP A 472 CA CA A 702 1555 1555 2.50
LINK OD1 ASP A 483 CA CA A 702 1555 1555 2.40
LINK O ARG A 484 CA CA A 702 1555 1555 2.36
LINK ZN ZN A 700 OAG GM6 A1002 1555 1555 2.33
LINK ZN ZN A 700 OAE GM6 A1002 1555 1555 2.26
LINK NE2 HIS B 335 ZN ZN B 700 1555 1555 2.21
LINK NE2 HIS B 339 ZN ZN B 700 1555 1555 2.06
LINK NE2 HIS B 345 ZN ZN B 700 1555 1555 1.99
LINK O VAL B 405 CA CA B 701 1555 1555 2.52
LINK OD1 ASN B 408 CA CA B 701 1555 1555 2.12
LINK O PHE B 410 CA CA B 701 1555 1555 2.39
LINK OE1 GLU B 412 CA CA B 701 1555 1555 2.64
LINK OE1 GLU B 415 CA CA B 701 1555 1555 2.27
LINK OE2 GLU B 415 CA CA B 701 1555 1555 2.61
LINK OD2 ASP B 418 CA CA B 701 1555 1555 2.32
LINK OD2 ASP B 469 CA CA B 702 1555 1555 2.68
LINK O MET B 470 CA CA B 702 1555 1555 2.34
LINK OD2 ASP B 472 CA CA B 702 1555 1555 2.44
LINK OD1 ASP B 472 CA CA B 702 1555 1555 2.79
LINK OD1 ASP B 483 CA CA B 702 1555 1555 3.01
LINK O ARG B 484 CA CA B 702 1555 1555 2.60
LINK N ARG B 484 CA CA B 702 1555 1555 3.32
LINK ZN ZN B 700 OAG GM6 B1001 1555 1555 2.21
LINK ZN ZN B 700 OAE GM6 B1001 1555 1555 2.32
CRYST1 86.345 91.379 136.039 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 0.011581 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010943 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
