HEADER TRANSPORT PROTEIN 04-MAR-08 3CFX
TITLE CRYSTAL STRUCTURE OF M. ACETIVORANS PERIPLASMIC BINDING PROTEIN
TITLE 2 MODA/WTPA WITH BOUND TUNGSTATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UPF0100 PROTEIN MA_0280;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MOLYBDATE ABC TRANSPORTER, SOLUTE-BINDING PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: MOLYBDATE ABC TRANSPORTER, SOLUTE-BINDING PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOSARCINA ACETIVORANS;
SOURCE 3 ORGANISM_TAXID: 2214;
SOURCE 4 GENE: MODA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODON PLUS(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-19B
KEYWDS ABC TRANSPORTER, BINDING PROTEIN, MOLYBDATE, TUNGSTATE, LIGAND,
KEYWDS 2 UNKNOWN FUNCTION, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.COMELLAS-BIGLER,K.HOLLENSTEIN,K.P.LOCHER
REVDAT 6 21-FEB-24 3CFX 1 REMARK
REVDAT 5 28-JUL-21 3CFX 1 REMARK LINK
REVDAT 4 13-JUL-11 3CFX 1 VERSN
REVDAT 3 25-AUG-09 3CFX 1 REMARK
REVDAT 2 21-JUL-09 3CFX 1
REVDAT 1 10-MAR-09 3CFX 0
JRNL AUTH K.HOLLENSTEIN,M.COMELLAS-BIGLER,L.E.BEVERS,M.C.FEITERS,
JRNL AUTH 2 W.MEYER-KLAUCKE,P.L.HAGEDOORN,K.P.LOCHER
JRNL TITL DISTORTED OCTAHEDRAL COORDINATION OF TUNGSTATE IN A
JRNL TITL 2 SUBFAMILY OF SPECIFIC BINDING PROTEINS.
JRNL REF J.BIOL.INORG.CHEM. V. 14 663 2009
JRNL REFN ISSN 0949-8257
JRNL PMID 19234723
JRNL DOI 10.1007/S00775-009-0479-7
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 165102
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 8211
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 4566
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 423
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 3CFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046727.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.21440
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XDX
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 165102
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
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) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
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: SAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, MAGNESIUM ACETATE, PEG 8000, PH
REMARK 280 6.5, VAPOR DIFFUSION, TEMPERATURE 293K
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 57.75000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.93000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.75000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.93000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 GLY A 37
REMARK 465 HIS A 38
REMARK 465 MET A 39
REMARK 465 GLY B 37
REMARK 465 HIS B 38
REMARK 465 MET B 39
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 GLU A 200 CD OE1 OE2
REMARK 480 GLU A 318 CD OE1 OE2
REMARK 480 GLU A 326 CD OE1 OE2
REMARK 480 GLU B 41 CD OE1 OE2
REMARK 480 GLU B 56 CD OE1 OE2
REMARK 480 GLU B 110 CD OE1 OE2
REMARK 480 GLU B 200 CG CD OE1 OE2
REMARK 480 GLU B 269 CD OE1 OE2
REMARK 480 GLU B 306 CD OE1 OE2
REMARK 480 GLU B 318 CD OE1 OE2
REMARK 480 GLN B 321 CD OE1 NE2
REMARK 480 GLN B 322 CD OE1 NE2
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 OE1 GLU B 227 W WO4 B 702 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 SER A 215 68.17 33.06
REMARK 500 SER B 215 63.32 39.14
REMARK 500 ASN B 327 42.14 -106.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 165 0.06 SIDE CHAIN
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 MG A 704 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 59 OE1
REMARK 620 2 GLU A 63 OE2 87.0
REMARK 620 3 ASP A 70 OD1 177.0 95.2
REMARK 620 4 VAL A 71 O 83.1 96.3 98.6
REMARK 620 5 HOH A1025 O 84.3 83.1 94.0 167.4
REMARK 620 6 HOH A1036 O 79.7 166.6 97.9 84.1 93.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 175 OE1
REMARK 620 2 GLU A 175 OE2 60.3
REMARK 620 3 ASP A 181 O 92.5 92.7
REMARK 620 4 ASP A 185 OD1 152.8 92.5 88.4
REMARK 620 5 HOH A 902 O 100.4 160.6 85.3 106.7
REMARK 620 6 HOH A1046 O 91.4 94.3 173.0 90.9 88.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 706 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 59 OE1
REMARK 620 2 GLU B 63 OE2 93.5
REMARK 620 3 ASP B 70 OD2 172.6 89.7
REMARK 620 4 VAL B 71 O 73.5 105.8 99.2
REMARK 620 5 HOH B 944 O 82.6 174.9 94.6 76.3
REMARK 620 6 HOH B 982 O 89.8 73.4 97.5 163.3 103.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 705 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 175 OE1
REMARK 620 2 GLU B 175 OE2 61.4
REMARK 620 3 ASP B 181 O 92.3 89.6
REMARK 620 4 ASP B 185 OD1 153.1 91.8 90.1
REMARK 620 5 HOH B 905 O 100.4 161.1 85.7 106.5
REMARK 620 6 HOH B 910 O 84.7 94.8 172.6 95.7 88.2
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 MG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 904
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ONR RELATED DB: PDB
REMARK 900 RELATED ID: 3CFZ RELATED DB: PDB
REMARK 900 RELATED ID: 3CG1 RELATED DB: PDB
REMARK 900 RELATED ID: 3CG3 RELATED DB: PDB
DBREF 3CFX A 40 332 UNP Q8TTZ5 Y280_METAC 40 332
DBREF 3CFX B 40 332 UNP Q8TTZ5 Y280_METAC 40 332
SEQADV 3CFX GLY A 37 UNP Q8TTZ5 EXPRESSION TAG
SEQADV 3CFX HIS A 38 UNP Q8TTZ5 EXPRESSION TAG
SEQADV 3CFX MET A 39 UNP Q8TTZ5 EXPRESSION TAG
SEQADV 3CFX GLY B 37 UNP Q8TTZ5 EXPRESSION TAG
SEQADV 3CFX HIS B 38 UNP Q8TTZ5 EXPRESSION TAG
SEQADV 3CFX MET B 39 UNP Q8TTZ5 EXPRESSION TAG
SEQRES 1 A 296 GLY HIS MET GLY GLU VAL LEU THR VAL PHE HIS ALA GLY
SEQRES 2 A 296 SER LEU SER VAL PRO PHE GLU GLU LEU GLU ALA GLU PHE
SEQRES 3 A 296 GLU ALA GLN HIS PRO GLY VAL ASP VAL GLN ARG GLU ALA
SEQRES 4 A 296 ALA GLY SER ALA GLN SER VAL ARG LYS ILE THR GLU LEU
SEQRES 5 A 296 GLY LYS LYS ALA ASP VAL LEU ALA SER ALA ASP TYR ALA
SEQRES 6 A 296 LEU ILE PRO SER LEU MET VAL PRO GLU TYR ALA ASP TRP
SEQRES 7 A 296 TYR ALA ALA PHE ALA ARG ASN GLN MET ILE LEU ALA TYR
SEQRES 8 A 296 THR ASN GLU SER LYS TYR GLY ASP GLU ILE ASN THR ASP
SEQRES 9 A 296 ASN TRP TYR GLU ILE LEU ARG ARG PRO ASP VAL ARG TYR
SEQRES 10 A 296 GLY PHE SER ASN PRO ASN ASP ASP PRO ALA GLY TYR ARG
SEQRES 11 A 296 SER GLN MET VAL THR GLN LEU ALA GLU SER TYR TYR ASN
SEQRES 12 A 296 ASP ASP MET ILE TYR ASP ASP LEU MET LEU ALA ASN THR
SEQRES 13 A 296 GLY MET THR LEU THR THR GLU GLU ASN GLY THR ALA LEU
SEQRES 14 A 296 ILE HIS VAL PRO ALA SER GLU GLU ILE SER PRO ASN THR
SEQRES 15 A 296 SER LYS ILE MET LEU ARG SER MET GLU VAL GLU LEU SER
SEQRES 16 A 296 SER ALA LEU GLU THR GLY GLU ILE ASP TYR LEU TYR ILE
SEQRES 17 A 296 TYR ARG SER VAL ALA GLU GLN HIS GLY PHE GLU TYR VAL
SEQRES 18 A 296 ALA LEU PRO PRO ALA ILE ASP LEU SER SER LEU GLU TYR
SEQRES 19 A 296 ALA ASP ASN TYR SER LYS VAL GLN VAL GLU MET VAL ASN
SEQRES 20 A 296 GLY GLU VAL VAL THR GLY SER PRO ILE VAL TYR GLY VAL
SEQRES 21 A 296 THR ILE PRO ASN ASN ALA GLU ASN SER GLU LEU ALA THR
SEQRES 22 A 296 GLU PHE VAL ALA LEU LEU LEU GLY GLU THR GLY GLN GLN
SEQRES 23 A 296 ILE PHE ILE GLU ASN GLY GLN PRO PRO ILE
SEQRES 1 B 296 GLY HIS MET GLY GLU VAL LEU THR VAL PHE HIS ALA GLY
SEQRES 2 B 296 SER LEU SER VAL PRO PHE GLU GLU LEU GLU ALA GLU PHE
SEQRES 3 B 296 GLU ALA GLN HIS PRO GLY VAL ASP VAL GLN ARG GLU ALA
SEQRES 4 B 296 ALA GLY SER ALA GLN SER VAL ARG LYS ILE THR GLU LEU
SEQRES 5 B 296 GLY LYS LYS ALA ASP VAL LEU ALA SER ALA ASP TYR ALA
SEQRES 6 B 296 LEU ILE PRO SER LEU MET VAL PRO GLU TYR ALA ASP TRP
SEQRES 7 B 296 TYR ALA ALA PHE ALA ARG ASN GLN MET ILE LEU ALA TYR
SEQRES 8 B 296 THR ASN GLU SER LYS TYR GLY ASP GLU ILE ASN THR ASP
SEQRES 9 B 296 ASN TRP TYR GLU ILE LEU ARG ARG PRO ASP VAL ARG TYR
SEQRES 10 B 296 GLY PHE SER ASN PRO ASN ASP ASP PRO ALA GLY TYR ARG
SEQRES 11 B 296 SER GLN MET VAL THR GLN LEU ALA GLU SER TYR TYR ASN
SEQRES 12 B 296 ASP ASP MET ILE TYR ASP ASP LEU MET LEU ALA ASN THR
SEQRES 13 B 296 GLY MET THR LEU THR THR GLU GLU ASN GLY THR ALA LEU
SEQRES 14 B 296 ILE HIS VAL PRO ALA SER GLU GLU ILE SER PRO ASN THR
SEQRES 15 B 296 SER LYS ILE MET LEU ARG SER MET GLU VAL GLU LEU SER
SEQRES 16 B 296 SER ALA LEU GLU THR GLY GLU ILE ASP TYR LEU TYR ILE
SEQRES 17 B 296 TYR ARG SER VAL ALA GLU GLN HIS GLY PHE GLU TYR VAL
SEQRES 18 B 296 ALA LEU PRO PRO ALA ILE ASP LEU SER SER LEU GLU TYR
SEQRES 19 B 296 ALA ASP ASN TYR SER LYS VAL GLN VAL GLU MET VAL ASN
SEQRES 20 B 296 GLY GLU VAL VAL THR GLY SER PRO ILE VAL TYR GLY VAL
SEQRES 21 B 296 THR ILE PRO ASN ASN ALA GLU ASN SER GLU LEU ALA THR
SEQRES 22 B 296 GLU PHE VAL ALA LEU LEU LEU GLY GLU THR GLY GLN GLN
SEQRES 23 B 296 ILE PHE ILE GLU ASN GLY GLN PRO PRO ILE
HET MG A 703 1
HET MG A 704 1
HET WO4 A 701 5
HET GOL A 901 6
HET MG B 705 1
HET MG B 706 1
HET WO4 B 702 5
HET GOL B 902 6
HET GOL B 903 6
HET GOL B 904 6
HETNAM MG MAGNESIUM ION
HETNAM WO4 TUNGSTATE(VI)ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MG 4(MG 2+)
FORMUL 5 WO4 2(O4 W 2-)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 13 HOH *423(H2 O)
HELIX 1 1 LEU A 51 HIS A 66 1 16
HELIX 2 2 GLY A 77 GLU A 87 1 11
HELIX 3 3 ALA A 101 MET A 107 1 7
HELIX 4 4 ASN A 141 ARG A 148 1 8
HELIX 5 5 ASP A 161 TYR A 178 1 18
HELIX 6 6 MET A 182 MET A 188 1 7
HELIX 7 7 LEU A 189 THR A 192 5 4
HELIX 8 8 ALA A 210 ILE A 214 5 5
HELIX 9 9 MET A 226 GLU A 229 5 4
HELIX 10 10 LEU A 230 THR A 236 1 7
HELIX 11 11 ARG A 246 GLY A 253 1 8
HELIX 12 12 SER A 267 GLU A 269 5 3
HELIX 13 13 TYR A 270 SER A 275 1 6
HELIX 14 14 ASN A 304 GLY A 317 1 14
HELIX 15 15 GLY A 317 ASN A 327 1 11
HELIX 16 16 LEU B 51 HIS B 66 1 16
HELIX 17 17 GLY B 77 GLU B 87 1 11
HELIX 18 18 ALA B 101 MET B 107 1 7
HELIX 19 19 ASN B 141 ARG B 148 1 8
HELIX 20 20 ASP B 161 ASN B 179 1 19
HELIX 21 21 MET B 182 MET B 188 1 7
HELIX 22 22 ALA B 210 ILE B 214 5 5
HELIX 23 23 MET B 226 GLU B 229 5 4
HELIX 24 24 LEU B 230 THR B 236 1 7
HELIX 25 25 ARG B 246 GLY B 253 1 8
HELIX 26 26 SER B 267 GLU B 269 5 3
HELIX 27 27 TYR B 270 SER B 275 1 6
HELIX 28 28 ASN B 304 GLY B 317 1 14
HELIX 29 29 GLY B 317 ASN B 327 1 11
SHEET 1 A10 ASP A 70 ALA A 75 0
SHEET 2 A10 VAL A 42 HIS A 47 1 N LEU A 43 O GLN A 72
SHEET 3 A10 VAL A 94 SER A 97 1 O VAL A 94 N PHE A 46
SHEET 4 A10 VAL A 293 THR A 297 -1 O GLY A 295 N SER A 97
SHEET 5 A10 TYR A 115 ARG A 120 -1 N ALA A 119 O TYR A 294
SHEET 6 A10 TYR B 115 ARG B 120 -1 O ALA B 117 N TYR A 115
SHEET 7 A10 VAL B 293 THR B 297 -1 O TYR B 294 N ALA B 119
SHEET 8 A10 VAL B 94 SER B 97 -1 N SER B 97 O GLY B 295
SHEET 9 A10 GLU B 41 HIS B 47 1 N PHE B 46 O VAL B 94
SHEET 10 A10 VAL B 69 ALA B 75 1 O GLN B 72 N VAL B 45
SHEET 1 B 5 ILE A 221 ARG A 224 0
SHEET 2 B 5 TYR A 153 SER A 156 1 N TYR A 153 O MET A 222
SHEET 3 B 5 TYR A 241 TYR A 245 1 O TYR A 243 N GLY A 154
SHEET 4 B 5 MET A 123 TYR A 127 -1 N ALA A 126 O LEU A 242
SHEET 5 B 5 GLU A 255 VAL A 257 -1 O VAL A 257 N LEU A 125
SHEET 1 C 4 THR A 195 THR A 198 0
SHEET 2 C 4 ALA A 204 HIS A 207 -1 O HIS A 207 N THR A 195
SHEET 3 C 4 VAL A 277 GLU A 280 1 O GLU A 280 N ILE A 206
SHEET 4 C 4 VAL A 286 THR A 288 -1 O VAL A 287 N VAL A 279
SHEET 1 D 5 ILE B 221 ARG B 224 0
SHEET 2 D 5 TYR B 153 SER B 156 1 N TYR B 153 O MET B 222
SHEET 3 D 5 TYR B 241 TYR B 245 1 O TYR B 243 N GLY B 154
SHEET 4 D 5 MET B 123 TYR B 127 -1 N ALA B 126 O LEU B 242
SHEET 5 D 5 GLU B 255 ALA B 258 -1 O GLU B 255 N TYR B 127
SHEET 1 E 4 THR B 195 THR B 198 0
SHEET 2 E 4 ALA B 204 HIS B 207 -1 O HIS B 207 N THR B 195
SHEET 3 E 4 VAL B 277 GLU B 280 1 O GLU B 280 N ILE B 206
SHEET 4 E 4 VAL B 286 THR B 288 -1 O VAL B 287 N VAL B 279
LINK OE1 GLU A 59 MG MG A 704 1555 1555 2.26
LINK OE2 GLU A 63 MG MG A 704 1555 1555 2.20
LINK OD1 ASP A 70 MG MG A 704 1555 1555 2.22
LINK O VAL A 71 MG MG A 704 1555 1555 2.10
LINK OE1 GLU A 175 MG MG A 703 1555 1555 2.22
LINK OE2 GLU A 175 MG MG A 703 1555 1555 2.16
LINK O ASP A 181 MG MG A 703 1555 1555 2.10
LINK OD1 ASP A 185 MG MG A 703 1555 1555 1.99
LINK MG MG A 703 O HOH A 902 1555 1555 2.15
LINK MG MG A 703 O HOH A1046 1555 1555 2.11
LINK MG MG A 704 O HOH A1025 1555 1555 2.14
LINK MG MG A 704 O HOH A1036 1555 1555 2.09
LINK OE1 GLU B 59 MG MG B 706 1555 1555 2.19
LINK OE2 GLU B 63 MG MG B 706 1555 1555 2.33
LINK OD2 ASP B 70 MG MG B 706 1555 1555 2.04
LINK O VAL B 71 MG MG B 706 1555 1555 2.19
LINK OE1 GLU B 175 MG MG B 705 1555 1555 2.15
LINK OE2 GLU B 175 MG MG B 705 1555 1555 2.16
LINK O ASP B 181 MG MG B 705 1555 1555 2.11
LINK OD1 ASP B 185 MG MG B 705 1555 1555 1.99
LINK MG MG B 705 O HOH B 905 1555 1555 2.05
LINK MG MG B 705 O HOH B 910 1555 1555 2.17
LINK MG MG B 706 O HOH B 944 1555 1555 2.31
LINK MG MG B 706 O HOH B 982 1555 1555 2.29
CISPEP 1 VAL A 108 PRO A 109 0 0.25
CISPEP 2 VAL B 108 PRO B 109 0 0.07
SITE 1 AC1 5 GLU A 175 ASP A 181 ASP A 185 HOH A 902
SITE 2 AC1 5 HOH A1046
SITE 1 AC2 6 GLU A 59 GLU A 63 ASP A 70 VAL A 71
SITE 2 AC2 6 HOH A1025 HOH A1036
SITE 1 AC3 12 ALA A 48 GLY A 49 SER A 50 GLY A 77
SITE 2 AC3 12 SER A 78 ALA A 98 ASP A 161 PRO A 162
SITE 3 AC3 12 ALA A 163 MET A 226 GLU A 227 TYR A 245
SITE 1 AC4 5 GLU B 175 ASP B 181 ASP B 185 HOH B 905
SITE 2 AC4 5 HOH B 910
SITE 1 AC5 6 GLU B 59 GLU B 63 ASP B 70 VAL B 71
SITE 2 AC5 6 HOH B 944 HOH B 982
SITE 1 AC6 11 ALA B 48 GLY B 49 SER B 50 GLY B 77
SITE 2 AC6 11 SER B 78 ALA B 98 ASP B 161 PRO B 162
SITE 3 AC6 11 ALA B 163 GLU B 227 TYR B 245
SITE 1 AC7 6 ASN A 157 LEU A 223 SER A 225 ALA B 190
SITE 2 AC7 6 HOH B 974 HOH B 983
SITE 1 AC8 5 LYS B 132 ASP B 150 ASP B 240 HOH B 954
SITE 2 AC8 5 HOH B 994
SITE 1 AC9 1 HIS B 252
SITE 1 BC1 3 GLY A 40 HIS B 66 GLU B 310
CRYST1 115.500 51.860 124.048 90.00 116.93 90.00 C 1 2 1 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 0.008658 0.000000 0.004398 0.00000
SCALE2 0.000000 0.019283 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009042 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
