HEADER TRANSFERASE 31-AUG-04 1XC3
TITLE STRUCTURE OF A PUTATIVE FRUCTOKINASE FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE FRUCTOKINASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.1.4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: YDHR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS REDUCTIVELY METHYLATED, FRUCTOKINASE, ZN-COORDIATION, STRUCTURAL
KEYWDS 2 GENOMICS, PROTEIN STRUCTURE INITIATIVE, MCSG, PSI, MIDWEST CENTER
KEYWDS 3 FOR STRUCTURAL GENOMICS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.CUFF,P.QUARTEY,L.LEZONDRA,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 8 14-FEB-24 1XC3 1 REMARK SEQADV LINK
REVDAT 7 11-OCT-17 1XC3 1 REMARK
REVDAT 6 10-OCT-12 1XC3 1 JRNL
REVDAT 5 13-JUL-11 1XC3 1 VERSN
REVDAT 4 27-OCT-10 1XC3 1 KEYWDS
REVDAT 3 24-FEB-09 1XC3 1 VERSN
REVDAT 2 18-JAN-05 1XC3 1 AUTHOR KEYWDS REMARK
REVDAT 1 12-OCT-04 1XC3 0
JRNL AUTH B.NOCEK,A.J.STEIN,R.JEDRZEJCZAK,M.E.CUFF,H.LI,L.VOLKART,
JRNL AUTH 2 A.JOACHIMIAK
JRNL TITL STRUCTURAL STUDIES OF ROK FRUCTOKINASE YDHR FROM BACILLUS
JRNL TITL 2 SUBTILIS: INSIGHTS INTO SUBSTRATE BINDING AND FRUCTOSE
JRNL TITL 3 SPECIFICITY.
JRNL REF J.MOL.BIOL. V. 406 325 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21185308
JRNL DOI 10.1016/J.JMB.2010.12.021
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 29850
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1603
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2236
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 103
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 221
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 0.17000
REMARK 3 B12 (A**2) : -0.06000
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): 0.139
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.160
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2350 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3186 ; 1.172 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 300 ; 5.851 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;36.020 ;24.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 382 ;13.824 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;12.346 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 345 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1793 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1128 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1630 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 210 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.031 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 59 ; 0.166 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.145 ; 0.200
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): 1515 ; 0.738 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2360 ; 1.279 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 959 ; 1.764 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 826 ; 2.884 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 1XC3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030189.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 150
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : SBC2
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SBCCOLLECT
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29850
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 95.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
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: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS, GLYCEROL, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.02900
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 50.05800
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 50.05800
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 25.02900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). THE BIOLOGICAL UNIT FOR
REMARK 300 THE PROTEIN IS UNKNOWN.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 499 LIES ON A SPECIAL POSITION.
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 GLY A 295
REMARK 465 GLU A 296
REMARK 465 VAL A 297
REMARK 465 ARG A 298
REMARK 465 SER A 299
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 392 O HOH A 479 2.01
REMARK 500 O ARG A 157 O HOH A 524 2.16
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 LYS A 32 -141.28 -115.08
REMARK 500 HIS A 83 -0.04 73.98
REMARK 500 ASP A 173 43.97 -104.79
REMARK 500 ALA A 193 -39.32 -158.56
REMARK 500 SER A 259 -93.64 -134.27
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 PT A 303 PT
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 94 SD
REMARK 620 2 HOH A 401 O 164.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 153 ND1
REMARK 620 2 CYS A 168 SG 102.3
REMARK 620 3 HIS A 171 ND1 101.8 104.9
REMARK 620 4 CYS A 174 SG 118.3 105.8 121.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PT A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC1098 RELATED DB: TARGETDB
DBREF 1XC3 A 1 299 UNP O05510 SCRK_BACSU 1 299
SEQADV 1XC3 SER A -2 UNP O05510 CLONING ARTIFACT
SEQADV 1XC3 ASN A -1 UNP O05510 CLONING ARTIFACT
SEQADV 1XC3 ALA A 0 UNP O05510 CLONING ARTIFACT
SEQRES 1 A 302 SER ASN ALA MET LEU GLY GLY ILE GLU ALA GLY GLY THR
SEQRES 2 A 302 LYS PHE VAL CYS ALA VAL GLY ARG GLU ASP GLY THR ILE
SEQRES 3 A 302 ILE ASP ARG ILE GLU PHE PRO THR LYS MET PRO ASP GLU
SEQRES 4 A 302 THR ILE GLU LYS VAL ILE GLN TYR PHE SER GLN PHE SER
SEQRES 5 A 302 LEU GLN ALA ILE GLY ILE GLY SER PHE GLY PRO VAL ASP
SEQRES 6 A 302 ASN ASP LYS THR SER GLN THR TYR GLY THR ILE THR ALA
SEQRES 7 A 302 THR PRO LYS ALA GLY TRP ARG HIS TYR PRO PHE LEU GLN
SEQRES 8 A 302 THR VAL LYS ASN GLU MET LYS ILE PRO VAL GLY PHE SER
SEQRES 9 A 302 THR ASP VAL ASN ALA ALA ALA LEU GLY GLU PHE LEU PHE
SEQRES 10 A 302 GLY GLU ALA LYS GLY LEU ASP SER CYS LEU TYR ILE THR
SEQRES 11 A 302 ILE GLY THR GLY ILE GLY ALA GLY ALA ILE VAL GLU GLY
SEQRES 12 A 302 ARG LEU LEU GLN GLY LEU SER HIS PRO GLU MET GLY HIS
SEQRES 13 A 302 ILE TYR ILE ARG ARG HIS PRO ASP ASP VAL TYR GLN GLY
SEQRES 14 A 302 LYS CYS PRO TYR HIS GLY ASP CYS PHE GLU GLY LEU ALA
SEQRES 15 A 302 SER GLY PRO ALA ILE GLU ALA ARG TRP GLY LYS LYS ALA
SEQRES 16 A 302 ALA ASP LEU SER ASP ILE ALA GLN VAL TRP GLU LEU GLU
SEQRES 17 A 302 GLY TYR TYR ILE ALA GLN ALA LEU ALA GLN TYR ILE LEU
SEQRES 18 A 302 ILE LEU ALA PRO LYS LYS ILE ILE LEU GLY GLY GLY VAL
SEQRES 19 A 302 MET GLN GLN LYS GLN VAL PHE SER TYR ILE TYR GLN TYR
SEQRES 20 A 302 VAL PRO LYS ILE MET ASN SER TYR LEU ASP PHE SER GLU
SEQRES 21 A 302 LEU SER ASP ASP ILE SER ASP TYR ILE VAL PRO PRO ARG
SEQRES 22 A 302 LEU GLY SER ASN ALA GLY ILE ILE GLY THR LEU VAL LEU
SEQRES 23 A 302 ALA HIS GLN ALA LEU GLN ALA GLU ALA ALA SER GLY GLU
SEQRES 24 A 302 VAL ARG SER
HET PT A 301 1
HET ZN A 302 1
HET PT A 303 1
HET GOL A 305 6
HET GOL A 306 6
HETNAM PT PLATINUM (II) ION
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 PT 2(PT 2+)
FORMUL 3 ZN ZN 2+
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 HOH *221(H2 O)
HELIX 1 1 MET A 33 SER A 46 1 14
HELIX 2 2 PRO A 85 LYS A 95 1 11
HELIX 3 3 ASP A 103 GLY A 115 1 13
HELIX 4 4 GLU A 150 ILE A 154 5 5
HELIX 5 5 CYS A 174 SER A 180 1 7
HELIX 6 6 SER A 180 GLY A 189 1 10
HELIX 7 7 ILE A 198 LEU A 220 1 23
HELIX 8 8 GLY A 229 GLN A 234 5 6
HELIX 9 9 LYS A 235 ASN A 250 1 16
HELIX 10 10 PHE A 255 SER A 259 5 5
HELIX 11 11 ASP A 261 ASP A 264 5 4
HELIX 12 12 LEU A 271 SER A 273 5 3
HELIX 13 13 ASN A 274 ALA A 292 1 19
SHEET 1 A 5 ILE A 23 PRO A 30 0
SHEET 2 A 5 LYS A 11 GLY A 17 -1 N CYS A 14 O ILE A 27
SHEET 3 A 5 LEU A 2 ALA A 7 -1 N GLU A 6 O VAL A 13
SHEET 4 A 5 ALA A 52 SER A 57 1 O GLY A 56 N ILE A 5
SHEET 5 A 5 VAL A 98 THR A 102 1 O GLY A 99 N ILE A 53
SHEET 1 B 5 ARG A 141 LEU A 142 0
SHEET 2 B 5 ILE A 132 VAL A 138 -1 N VAL A 138 O ARG A 141
SHEET 3 B 5 CYS A 123 ILE A 128 -1 N TYR A 125 O GLY A 135
SHEET 4 B 5 ILE A 225 GLY A 228 1 O ILE A 226 N LEU A 124
SHEET 5 B 5 ILE A 266 VAL A 267 1 O VAL A 267 N LEU A 227
LINK SD MET A 33 PT PT A 301 1555 1555 1.88
LINK SD MET A 94 PT PT A 303 1555 1555 2.11
LINK ND1 HIS A 153 ZN ZN A 302 1555 1555 2.04
LINK SG CYS A 168 ZN ZN A 302 1555 1555 2.37
LINK ND1 HIS A 171 ZN ZN A 302 1555 1555 2.02
LINK SG CYS A 174 ZN ZN A 302 1555 1555 2.18
LINK PT PT A 303 O HOH A 401 1555 1555 3.58
CISPEP 1 GLY A 59 PRO A 60 0 3.34
SITE 1 AC1 1 MET A 33
SITE 1 AC2 4 HIS A 153 CYS A 168 HIS A 171 CYS A 174
SITE 1 AC3 1 MET A 94
SITE 1 AC4 10 GLY A 59 PRO A 60 ASP A 103 HIS A 148
SITE 2 AC4 10 PRO A 149 GLU A 150 GOL A 306 HOH A 310
SITE 3 AC4 10 HOH A 315 HOH A 333
SITE 1 AC5 7 ASP A 103 GLY A 131 ILE A 132 GLY A 133
SITE 2 AC5 7 GOL A 305 HOH A 333 HOH A 373
CRYST1 112.660 112.660 75.087 90.00 90.00 120.00 P 31 2 1 6
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 0.008876 0.005125 0.000000 0.00000
SCALE2 0.000000 0.010249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013318 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
