HEADER TOXIN 17-OCT-06 2ISG
TITLE BOTULINUM NEUROTOXIN A LIGHT CHAIN WT CRYSTAL FORM B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROTOXIN BONT/A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGHT CHAIN;
COMPND 5 SYNONYM: BONT/A; BOTULINUM NEUROTOXIN TYPE A;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM;
SOURCE 3 ORGANISM_TAXID: 1491;
SOURCE 4 VARIANT: SEROTYPE A;
SOURCE 5 GENE: BONT/A, BONT/A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBN3
KEYWDS BOTULINUM NEUROTOXIN, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.T.BRUNGER,C.M.STEGMANN
REVDAT 5 30-AUG-23 2ISG 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 2ISG 1 VERSN
REVDAT 3 13-MAR-07 2ISG 1 JRNL
REVDAT 2 21-NOV-06 2ISG 1 JRNL
REVDAT 1 07-NOV-06 2ISG 0
JRNL AUTH J.C.BURNETT,G.RUTHEL,C.M.STEGMANN,R.G.PANCHAL,T.L.NGUYEN,
JRNL AUTH 2 A.R.HERMONE,R.G.STAFFORD,D.J.LANE,T.A.KENNY,C.F.MCGRATH,
JRNL AUTH 3 P.WIPF,A.M.STAHL,J.J.SCHMIDT,R.GUSSIO,A.T.BRUNGER,S.BAVARI
JRNL TITL INHIBITION OF METALLOPROTEASE BOTULINUM SEROTYPE A FROM A
JRNL TITL 2 PSEUDO-PEPTIDE BINDING MODE TO A SMALL MOLECULE THAT IS
JRNL TITL 3 ACTIVE IN PRIMARY NEURONS.
JRNL REF J.BIOL.CHEM. V. 282 5004 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17092934
JRNL DOI 10.1074/JBC.M608166200
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1088331.850
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 53667
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) : 0.240
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2714
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4766
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 254
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6732
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 262
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : -4.09000
REMARK 3 B33 (A**2) : 4.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.76000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 46.86
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ISG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000039958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.20
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53858
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 42.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> 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: NULL
REMARK 200 STARTING MODEL: 1XTF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 2000 MME, 100 MM HEPES PH 7.8,
REMARK 280 10 MM NICL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 95.47750
REMARK 290 SMTRY3 2 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 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 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 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 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 ASN A 418
REMARK 465 PHE A 419
REMARK 465 THR A 420
REMARK 465 PRO A 421
REMARK 465 GLY A 422
REMARK 465 ASN B 418
REMARK 465 PHE B 419
REMARK 465 THR B 420
REMARK 465 PRO B 421
REMARK 465 GLY B 422
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ALA A 27 CB
REMARK 480 GLN A 29 CB CG CD OE1 NE2
REMARK 480 VAL A 202 CB CG1 CG2
REMARK 480 ASP A 203 CB CG OD1 OD2
REMARK 480 THR A 204 CB OG1 CG2
REMARK 480 ASN A 205 CB CG OD1 ND2
REMARK 480 THR A 247 CB OG1 CG2
REMARK 480 ASN A 248 CB CG OD1 ND2
REMARK 480 ALA A 249 CB
REMARK 480 TYR A 250 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR A 250 OH
REMARK 480 TYR A 251 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR A 251 OH
REMARK 480 GLU A 252 CB CG CD OE1 OE2
REMARK 480 MET A 253 CB CG SD CE
REMARK 480 SER A 254 CB OG
REMARK 480 ALA B 27 CB
REMARK 480 GLN B 29 CB CG CD OE1 NE2
REMARK 480 VAL B 202 CB CG1 CG2
REMARK 480 ASP B 203 CB CG OD1 OD2
REMARK 480 THR B 204 CB OG1 CG2
REMARK 480 ASN B 205 CB CG OD1 ND2
REMARK 480 THR B 247 CB OG1 CG2
REMARK 480 ASN B 248 CB CG OD1 ND2
REMARK 480 ALA B 249 C
REMARK 480 TYR B 250 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR B 250 OH
REMARK 480 TYR B 251 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR B 251 OH
REMARK 480 GLU B 252 CB CG CD OE1 OE2
REMARK 480 MET B 253 CB CG SD CE
REMARK 480 SER B 254 CB OG
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 VAL A 17 -72.73 -116.94
REMARK 500 ASN A 26 -90.45 -1.59
REMARK 500 ALA A 27 178.71 176.08
REMARK 500 GLU A 64 9.73 89.10
REMARK 500 VAL A 68 -81.08 -8.29
REMARK 500 ASP A 74 95.20 -174.57
REMARK 500 SER A 121 150.59 -42.69
REMARK 500 ASP A 124 -9.41 -51.75
REMARK 500 SER A 157 -147.50 -86.79
REMARK 500 SER A 199 57.67 -95.85
REMARK 500 GLU A 201 77.59 -113.01
REMARK 500 VAL A 202 -1.04 73.83
REMARK 500 ASP A 203 -24.51 68.28
REMARK 500 LEU A 207 72.15 46.17
REMARK 500 ASN A 246 -108.08 -62.44
REMARK 500 THR A 247 -81.41 -150.93
REMARK 500 TYR A 251 133.93 -37.08
REMARK 500 GLU A 252 38.53 70.69
REMARK 500 SER A 254 41.28 -76.85
REMARK 500 LYS A 301 -51.66 -128.41
REMARK 500 THR A 306 -85.16 -146.83
REMARK 500 THR A 307 21.26 -72.61
REMARK 500 ASN A 409 53.04 -112.20
REMARK 500 VAL B 17 -71.97 -117.10
REMARK 500 ASN B 26 -88.34 -4.50
REMARK 500 ALA B 27 178.77 175.78
REMARK 500 GLU B 64 9.71 88.02
REMARK 500 VAL B 68 -75.22 -14.44
REMARK 500 ASP B 74 94.83 -175.29
REMARK 500 SER B 121 150.38 -42.04
REMARK 500 ASP B 124 -9.46 -51.66
REMARK 500 SER B 157 -146.86 -86.77
REMARK 500 SER B 199 57.94 -96.27
REMARK 500 GLU B 201 78.68 -111.55
REMARK 500 VAL B 202 -3.06 73.13
REMARK 500 ASP B 203 -28.71 70.52
REMARK 500 LEU B 207 71.85 46.45
REMARK 500 ASN B 246 -113.33 -61.37
REMARK 500 THR B 247 -83.55 -166.54
REMARK 500 ALA B 249 -95.73 -176.94
REMARK 500 TYR B 250 -67.53 -148.08
REMARK 500 MET B 253 34.06 71.80
REMARK 500 LYS B 301 -51.50 -127.90
REMARK 500 THR B 306 -85.36 -146.66
REMARK 500 THR B 307 21.11 -72.52
REMARK 500 ASN B 409 53.15 -113.15
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 NI B 503 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 64 OE1
REMARK 620 2 HOH A 567 O 90.7
REMARK 620 3 HOH A 628 O 85.8 84.5
REMARK 620 4 HOH A 629 O 83.9 170.3 87.1
REMARK 620 5 LYS B 272 NZ 88.1 94.3 173.7 93.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 223 NE2
REMARK 620 2 HIS A 227 NE2 95.0
REMARK 620 3 GLU A 262 OE1 95.8 91.2
REMARK 620 4 GLU A 262 OE2 155.5 87.4 59.8
REMARK 620 5 HOH A 541 O 90.2 174.7 87.5 87.5
REMARK 620 6 HOH A 624 O 106.1 102.8 152.6 97.1 76.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 502 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 272 NZ
REMARK 620 2 HOH A 585 O 88.6
REMARK 620 3 GLU B 64 OE1 87.3 88.8
REMARK 620 4 HOH B 636 O 173.5 89.6 86.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 223 NE2
REMARK 620 2 HIS B 227 NE2 94.5
REMARK 620 3 GLU B 262 OE2 158.1 88.7
REMARK 620 4 GLU B 262 OE1 98.2 89.8 60.2
REMARK 620 5 HOH B 527 O 87.1 177.9 89.3 88.6
REMARK 620 6 HOH B 632 O 102.9 101.1 97.7 155.4 79.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ISE RELATED DB: PDB
REMARK 900 RELATED ID: 2ISH RELATED DB: PDB
DBREF 2ISG A 2 420 UNP Q7B8V4 Q7B8V4_CLOBO 2 420
DBREF 2ISG B 2 420 UNP Q7B8V4 Q7B8V4_CLOBO 2 420
SEQADV 2ISG PRO A 421 UNP Q7B8V4 CLONING ARTIFACT
SEQADV 2ISG GLY A 422 UNP Q7B8V4 CLONING ARTIFACT
SEQADV 2ISG PRO B 421 UNP Q7B8V4 CLONING ARTIFACT
SEQADV 2ISG GLY B 422 UNP Q7B8V4 CLONING ARTIFACT
SEQRES 1 A 421 PRO PHE VAL ASN LYS GLN PHE ASN TYR LYS ASP PRO VAL
SEQRES 2 A 421 ASN GLY VAL ASP ILE ALA TYR ILE LYS ILE PRO ASN ALA
SEQRES 3 A 421 GLY GLN MET GLN PRO VAL LYS ALA PHE LYS ILE HIS ASN
SEQRES 4 A 421 LYS ILE TRP VAL ILE PRO GLU ARG ASP THR PHE THR ASN
SEQRES 5 A 421 PRO GLU GLU GLY ASP LEU ASN PRO PRO PRO GLU ALA LYS
SEQRES 6 A 421 GLN VAL PRO VAL SER TYR TYR ASP SER THR TYR LEU SER
SEQRES 7 A 421 THR ASP ASN GLU LYS ASP ASN TYR LEU LYS GLY VAL THR
SEQRES 8 A 421 LYS LEU PHE GLU ARG ILE TYR SER THR ASP LEU GLY ARG
SEQRES 9 A 421 MET LEU LEU THR SER ILE VAL ARG GLY ILE PRO PHE TRP
SEQRES 10 A 421 GLY GLY SER THR ILE ASP THR GLU LEU LYS VAL ILE ASP
SEQRES 11 A 421 THR ASN CYS ILE ASN VAL ILE GLN PRO ASP GLY SER TYR
SEQRES 12 A 421 ARG SER GLU GLU LEU ASN LEU VAL ILE ILE GLY PRO SER
SEQRES 13 A 421 ALA ASP ILE ILE GLN PHE GLU CYS LYS SER PHE GLY HIS
SEQRES 14 A 421 GLU VAL LEU ASN LEU THR ARG ASN GLY TYR GLY SER THR
SEQRES 15 A 421 GLN TYR ILE ARG PHE SER PRO ASP PHE THR PHE GLY PHE
SEQRES 16 A 421 GLU GLU SER LEU GLU VAL ASP THR ASN PRO LEU LEU GLY
SEQRES 17 A 421 ALA GLY LYS PHE ALA THR ASP PRO ALA VAL THR LEU ALA
SEQRES 18 A 421 HIS GLU LEU ILE HIS ALA GLY HIS ARG LEU TYR GLY ILE
SEQRES 19 A 421 ALA ILE ASN PRO ASN ARG VAL PHE LYS VAL ASN THR ASN
SEQRES 20 A 421 ALA TYR TYR GLU MET SER GLY LEU GLU VAL SER PHE GLU
SEQRES 21 A 421 GLU LEU ARG THR PHE GLY GLY HIS ASP ALA LYS PHE ILE
SEQRES 22 A 421 ASP SER LEU GLN GLU ASN GLU PHE ARG LEU TYR TYR TYR
SEQRES 23 A 421 ASN LYS PHE LYS ASP ILE ALA SER THR LEU ASN LYS ALA
SEQRES 24 A 421 LYS SER ILE VAL GLY THR THR ALA SER LEU GLN TYR MET
SEQRES 25 A 421 LYS ASN VAL PHE LYS GLU LYS TYR LEU LEU SER GLU ASP
SEQRES 26 A 421 THR SER GLY LYS PHE SER VAL ASP LYS LEU LYS PHE ASP
SEQRES 27 A 421 LYS LEU TYR LYS MET LEU THR GLU ILE TYR THR GLU ASP
SEQRES 28 A 421 ASN PHE VAL LYS PHE PHE LYS VAL LEU ASN ARG LYS THR
SEQRES 29 A 421 TYR LEU ASN PHE ASP LYS ALA VAL PHE LYS ILE ASN ILE
SEQRES 30 A 421 VAL PRO LYS VAL ASN TYR THR ILE TYR ASP GLY PHE ASN
SEQRES 31 A 421 LEU ARG ASN THR ASN LEU ALA ALA ASN PHE ASN GLY GLN
SEQRES 32 A 421 ASN THR GLU ILE ASN ASN MET ASN PHE THR LYS LEU LYS
SEQRES 33 A 421 ASN PHE THR PRO GLY
SEQRES 1 B 421 PRO PHE VAL ASN LYS GLN PHE ASN TYR LYS ASP PRO VAL
SEQRES 2 B 421 ASN GLY VAL ASP ILE ALA TYR ILE LYS ILE PRO ASN ALA
SEQRES 3 B 421 GLY GLN MET GLN PRO VAL LYS ALA PHE LYS ILE HIS ASN
SEQRES 4 B 421 LYS ILE TRP VAL ILE PRO GLU ARG ASP THR PHE THR ASN
SEQRES 5 B 421 PRO GLU GLU GLY ASP LEU ASN PRO PRO PRO GLU ALA LYS
SEQRES 6 B 421 GLN VAL PRO VAL SER TYR TYR ASP SER THR TYR LEU SER
SEQRES 7 B 421 THR ASP ASN GLU LYS ASP ASN TYR LEU LYS GLY VAL THR
SEQRES 8 B 421 LYS LEU PHE GLU ARG ILE TYR SER THR ASP LEU GLY ARG
SEQRES 9 B 421 MET LEU LEU THR SER ILE VAL ARG GLY ILE PRO PHE TRP
SEQRES 10 B 421 GLY GLY SER THR ILE ASP THR GLU LEU LYS VAL ILE ASP
SEQRES 11 B 421 THR ASN CYS ILE ASN VAL ILE GLN PRO ASP GLY SER TYR
SEQRES 12 B 421 ARG SER GLU GLU LEU ASN LEU VAL ILE ILE GLY PRO SER
SEQRES 13 B 421 ALA ASP ILE ILE GLN PHE GLU CYS LYS SER PHE GLY HIS
SEQRES 14 B 421 GLU VAL LEU ASN LEU THR ARG ASN GLY TYR GLY SER THR
SEQRES 15 B 421 GLN TYR ILE ARG PHE SER PRO ASP PHE THR PHE GLY PHE
SEQRES 16 B 421 GLU GLU SER LEU GLU VAL ASP THR ASN PRO LEU LEU GLY
SEQRES 17 B 421 ALA GLY LYS PHE ALA THR ASP PRO ALA VAL THR LEU ALA
SEQRES 18 B 421 HIS GLU LEU ILE HIS ALA GLY HIS ARG LEU TYR GLY ILE
SEQRES 19 B 421 ALA ILE ASN PRO ASN ARG VAL PHE LYS VAL ASN THR ASN
SEQRES 20 B 421 ALA TYR TYR GLU MET SER GLY LEU GLU VAL SER PHE GLU
SEQRES 21 B 421 GLU LEU ARG THR PHE GLY GLY HIS ASP ALA LYS PHE ILE
SEQRES 22 B 421 ASP SER LEU GLN GLU ASN GLU PHE ARG LEU TYR TYR TYR
SEQRES 23 B 421 ASN LYS PHE LYS ASP ILE ALA SER THR LEU ASN LYS ALA
SEQRES 24 B 421 LYS SER ILE VAL GLY THR THR ALA SER LEU GLN TYR MET
SEQRES 25 B 421 LYS ASN VAL PHE LYS GLU LYS TYR LEU LEU SER GLU ASP
SEQRES 26 B 421 THR SER GLY LYS PHE SER VAL ASP LYS LEU LYS PHE ASP
SEQRES 27 B 421 LYS LEU TYR LYS MET LEU THR GLU ILE TYR THR GLU ASP
SEQRES 28 B 421 ASN PHE VAL LYS PHE PHE LYS VAL LEU ASN ARG LYS THR
SEQRES 29 B 421 TYR LEU ASN PHE ASP LYS ALA VAL PHE LYS ILE ASN ILE
SEQRES 30 B 421 VAL PRO LYS VAL ASN TYR THR ILE TYR ASP GLY PHE ASN
SEQRES 31 B 421 LEU ARG ASN THR ASN LEU ALA ALA ASN PHE ASN GLY GLN
SEQRES 32 B 421 ASN THR GLU ILE ASN ASN MET ASN PHE THR LYS LEU LYS
SEQRES 33 B 421 ASN PHE THR PRO GLY
HET ZN A 500 1
HET ZN B 501 1
HET NI B 502 1
HET NI B 503 1
HETNAM ZN ZINC ION
HETNAM NI NICKEL (II) ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 NI 2(NI 2+)
FORMUL 7 HOH *262(H2 O)
HELIX 1 1 THR A 80 SER A 100 1 21
HELIX 2 2 THR A 101 GLY A 114 1 14
HELIX 3 3 ILE A 130 THR A 132 5 3
HELIX 4 4 ASP A 216 TYR A 233 1 18
HELIX 5 5 PHE A 260 GLY A 267 1 8
HELIX 6 6 GLY A 268 ILE A 274 5 7
HELIX 7 7 ASP A 275 LYS A 299 1 25
HELIX 8 8 SER A 309 TYR A 321 1 13
HELIX 9 9 ASP A 334 GLU A 347 1 14
HELIX 10 10 THR A 350 LYS A 359 1 10
HELIX 11 11 PHE A 401 ASN A 405 5 5
HELIX 12 12 ASN A 409 PHE A 413 5 5
HELIX 13 13 THR B 80 SER B 100 1 21
HELIX 14 14 THR B 101 GLY B 114 1 14
HELIX 15 15 ILE B 130 THR B 132 5 3
HELIX 16 16 ASP B 216 TYR B 233 1 18
HELIX 17 17 PHE B 260 GLY B 267 1 8
HELIX 18 18 GLY B 268 ILE B 274 5 7
HELIX 19 19 ASP B 275 LYS B 299 1 25
HELIX 20 20 SER B 309 TYR B 321 1 13
HELIX 21 21 ASP B 334 GLU B 347 1 14
HELIX 22 22 THR B 350 LYS B 359 1 10
HELIX 23 23 PHE B 401 ASN B 405 5 5
HELIX 24 24 ASN B 409 PHE B 413 5 5
SHEET 1 A 8 TYR A 144 GLU A 148 0
SHEET 2 A 8 CYS A 134 ILE A 138 -1 N VAL A 137 O ARG A 145
SHEET 3 A 8 ILE A 19 LYS A 23 -1 N LYS A 23 O ASN A 136
SHEET 4 A 8 VAL A 33 HIS A 39 -1 O ALA A 35 N ALA A 20
SHEET 5 A 8 ILE A 42 ARG A 48 -1 O VAL A 44 N PHE A 36
SHEET 6 A 8 LEU A 151 GLY A 155 1 O ILE A 153 N ILE A 45
SHEET 7 A 8 GLN A 184 ARG A 187 1 O ILE A 186 N VAL A 152
SHEET 8 A 8 GLU A 164 LYS A 166 -1 N LYS A 166 O TYR A 185
SHEET 1 B 2 GLU A 126 LEU A 127 0
SHEET 2 B 2 SER A 302 ILE A 303 1 O SER A 302 N LEU A 127
SHEET 1 C 4 GLY A 211 ALA A 214 0
SHEET 2 C 4 PHE A 192 GLU A 198 -1 N PHE A 196 O PHE A 213
SHEET 3 C 4 ALA A 372 LYS A 375 -1 O PHE A 374 N THR A 193
SHEET 4 C 4 THR A 414 LYS A 415 -1 O THR A 414 N LYS A 375
SHEET 1 D 2 VAL A 242 LYS A 244 0
SHEET 2 D 2 GLU A 257 SER A 259 -1 O VAL A 258 N PHE A 243
SHEET 1 E 2 SER A 324 GLU A 325 0
SHEET 2 E 2 PHE A 331 SER A 332 -1 O SER A 332 N SER A 324
SHEET 1 F 8 TYR B 144 GLU B 148 0
SHEET 2 F 8 CYS B 134 ILE B 138 -1 N VAL B 137 O ARG B 145
SHEET 3 F 8 ILE B 19 LYS B 23 -1 N LYS B 23 O ASN B 136
SHEET 4 F 8 VAL B 33 HIS B 39 -1 O ALA B 35 N ALA B 20
SHEET 5 F 8 ILE B 42 ARG B 48 -1 O ILE B 42 N HIS B 39
SHEET 6 F 8 LEU B 151 GLY B 155 1 O ILE B 153 N ILE B 45
SHEET 7 F 8 GLN B 184 ARG B 187 1 O ILE B 186 N VAL B 152
SHEET 8 F 8 GLU B 164 LYS B 166 -1 N LYS B 166 O TYR B 185
SHEET 1 G 2 GLU B 126 LEU B 127 0
SHEET 2 G 2 SER B 302 ILE B 303 1 O SER B 302 N LEU B 127
SHEET 1 H 4 GLY B 211 ALA B 214 0
SHEET 2 H 4 PHE B 192 GLU B 198 -1 N PHE B 196 O PHE B 213
SHEET 3 H 4 ALA B 372 LYS B 375 -1 O PHE B 374 N THR B 193
SHEET 4 H 4 THR B 414 LYS B 415 -1 O THR B 414 N LYS B 375
SHEET 1 I 2 VAL B 242 LYS B 244 0
SHEET 2 I 2 GLU B 257 SER B 259 -1 O VAL B 258 N PHE B 243
SHEET 1 J 2 SER B 324 GLU B 325 0
SHEET 2 J 2 PHE B 331 SER B 332 -1 O SER B 332 N SER B 324
LINK OE1 GLU A 64 NI NI B 503 1555 1555 2.16
LINK NE2 HIS A 223 ZN ZN A 500 1555 1555 2.14
LINK NE2 HIS A 227 ZN ZN A 500 1555 1555 2.15
LINK OE1 GLU A 262 ZN ZN A 500 1555 1555 2.12
LINK OE2 GLU A 262 ZN ZN A 500 1555 1555 2.31
LINK NZ LYS A 272 NI NI B 502 1554 1555 1.93
LINK ZN ZN A 500 O HOH A 541 1555 1555 1.98
LINK ZN ZN A 500 O HOH A 624 1555 1555 2.15
LINK O HOH A 567 NI NI B 503 1455 1555 2.23
LINK O HOH A 585 NI NI B 502 1554 1555 2.21
LINK O HOH A 628 NI NI B 503 1555 1555 1.75
LINK O HOH A 629 NI NI B 503 1555 1555 2.09
LINK OE1 GLU B 64 NI NI B 502 1555 1555 2.14
LINK NE2 HIS B 223 ZN ZN B 501 1555 1555 2.12
LINK NE2 HIS B 227 ZN ZN B 501 1555 1555 2.21
LINK OE2 GLU B 262 ZN ZN B 501 1555 1555 2.31
LINK OE1 GLU B 262 ZN ZN B 501 1555 1555 2.07
LINK NZ LYS B 272 NI NI B 503 1555 1555 1.89
LINK ZN ZN B 501 O HOH B 527 1555 1555 1.93
LINK ZN ZN B 501 O HOH B 632 1555 1555 2.13
LINK NI NI B 502 O HOH B 636 1555 1555 1.77
SITE 1 AC1 5 HIS A 223 HIS A 227 GLU A 262 HOH A 541
SITE 2 AC1 5 HOH A 624
SITE 1 AC2 5 HIS B 223 HIS B 227 GLU B 262 HOH B 527
SITE 2 AC2 5 HOH B 632
SITE 1 AC3 5 HIS A 269 LYS A 272 HOH A 585 GLU B 64
SITE 2 AC3 5 HOH B 636
SITE 1 AC4 6 GLU A 64 HOH A 567 HOH A 628 HOH A 629
SITE 2 AC4 6 HIS B 269 LYS B 272
CRYST1 41.991 190.955 56.949 90.00 90.09 90.00 P 1 21 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 0.023815 0.000000 0.000037 0.00000
SCALE2 0.000000 0.005237 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
