HEADER PENICILLIN BINDING 29-JUN-04 1TVF
TITLE CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 4 (PBP4) FROM
TITLE 2 STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENICILLIN BINDING PROTEIN 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PBP4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: PBP4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET T7
KEYWDS STRUCTURAL GENOMICS, NYSGXRC TARGET, T72, PBP4, SAV0642, SA0598, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, PENICILLIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.RAJASHANKAR,S.S.RAY,J.B.BONANNO,M.PINHO,A.TOMASZ,S.K.BURLEY,NEW
AUTHOR 2 YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 6 23-AUG-23 1TVF 1 REMARK
REVDAT 5 03-FEB-21 1TVF 1 AUTHOR JRNL REMARK SEQADV
REVDAT 4 24-FEB-09 1TVF 1 VERSN
REVDAT 3 05-APR-05 1TVF 1 AUTHOR JRNL
REVDAT 2 25-JAN-05 1TVF 1 AUTHOR KEYWDS REMARK
REVDAT 1 06-JUL-04 1TVF 0
JRNL AUTH K.R.RAJASHANKAR,S.S.RAY,J.B.BONANNO,M.PINHO,A.TOMASZ,
JRNL AUTH 2 S.K.BURLEY
JRNL TITL CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 4 (PBP4)
JRNL TITL 2 FROM STAPHYLOCOCCUS AUREUS
JRNL REF TO BE PUBLISHED
JRNL REFN
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 425919.560
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 67366
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) : 0.166
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3423
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10502
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE : 0.2280
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 548
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5796
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 781
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.66000
REMARK 3 B22 (A**2) : 2.23000
REMARK 3 B33 (A**2) : 1.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.024
REMARK 3 BOND ANGLES (DEGREES) : 2.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.370
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) : 1.280 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.250 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.090 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 54.87
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: UNIDENTIFIED ELECTRON DENSITY IS
REMARK 3 OBSERVED NEAR THE ACTIVE SITE.
REMARK 4
REMARK 4 1TVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022939.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-01; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X9A; X9A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98; 1.25
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111);
REMARK 200 SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67865
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.19600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS, MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: ARP/WARP AUTOBUILT MODEL USING PHASES FROM TWO
REMARK 200 TA6BR12 CLUSTERS AND A POOR MOLECULAR REPLACEMENT SOLUTION. MR
REMARK 200 WAS CARRIED OUT USING A MODEL DERIVED FROM PDB ENTRY 1HD8, WHICH
REMARK 200 IS A MUTANT OF PBP5, SHARING ~26% IDENTITY WITH PBP4 OVER A 245
REMARK 200 RESIDUE RANGE. PHASE COMBINATION WITH MR SOLUTION WAS NECESSARY,
REMARK 200 AS TA6BR12 CLUSTERS OCCUPIED POSITIONS ON THE SYMMETRY PLANES
REMARK 200 RESULTING IN CENTROSYMMETRIC PHASES AND HENCE UNINTERPRETABLE
REMARK 200 MAPS.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 4000, 100MM CITRATE BUFFER,
REMARK 280 200MM AMMONIUM SULFATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 24.35650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.88750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.09450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.88750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.35650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.09450
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: EACH MONOMER SEEM TO FORM A 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: 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 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 984 O HOH A 1106 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP B 130 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 197 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
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 THR A 25 42.36 -71.38
REMARK 500 TYR A 38 46.52 -107.20
REMARK 500 TYR A 40 43.30 -61.07
REMARK 500 ALA A 74 -132.06 49.99
REMARK 500 ASN A 117 167.45 177.79
REMARK 500 ARG A 188 -127.20 54.60
REMARK 500 ALA A 230 59.88 -155.29
REMARK 500 SER A 251 120.60 -37.70
REMARK 500 LEU A 258 -60.84 -131.13
REMARK 500 ASN A 267 -141.75 55.27
REMARK 500 LEU A 294 -49.94 -178.23
REMARK 500 ASP A 358 65.45 31.71
REMARK 500 ASN A 371 -179.31 -171.77
REMARK 500 THR B 25 41.84 -75.86
REMARK 500 ALA B 74 -135.80 53.10
REMARK 500 GLU B 114 -1.59 69.47
REMARK 500 ASN B 117 169.83 177.09
REMARK 500 ARG B 188 -119.03 50.00
REMARK 500 ALA B 230 62.86 -163.00
REMARK 500 SER B 251 124.06 -38.22
REMARK 500 LEU B 258 -56.55 -129.50
REMARK 500 ASN B 267 -142.71 54.99
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 A 208 0.08 SIDE CHAIN
REMARK 500 TYR B 208 0.07 SIDE CHAIN
REMARK 500 TYR B 291 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL B 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T72 RELATED DB: TARGETDB
DBREF 1TVF A 21 383 UNP Q53613 Q53613_STAAU 21 383
DBREF 1TVF B 21 383 UNP Q53613 Q53613_STAAU 21 383
SEQADV 1TVF GLY A 15 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF PRO A 16 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF HIS A 17 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF THR A 18 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF SER A 19 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF SER A 20 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF GLY B 15 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF PRO B 16 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF HIS B 17 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF THR B 18 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF SER B 19 UNP Q53613 CLONING ARTIFACT
SEQADV 1TVF SER B 20 UNP Q53613 CLONING ARTIFACT
SEQRES 1 A 369 GLY PRO HIS THR SER SER TYR ALA GLN ALA THR ASN SER
SEQRES 2 A 369 ASP VAL THR PRO VAL GLN ALA ALA ASN GLN TYR GLY TYR
SEQRES 3 A 369 ALA GLY LEU SER ALA ALA TYR GLU PRO THR SER ALA VAL
SEQRES 4 A 369 ASN VAL SER GLN THR GLY GLN LEU LEU TYR GLN TYR ASN
SEQRES 5 A 369 ILE ASP THR LYS TRP ASN PRO ALA SER MET THR LYS LEU
SEQRES 6 A 369 MET THR MET TYR LEU THR LEU GLU ALA VAL ASN LYS GLY
SEQRES 7 A 369 GLN LEU SER LEU ASP ASP THR VAL THR MET THR ASN LYS
SEQRES 8 A 369 GLU TYR ILE MET SER THR LEU PRO GLU LEU SER ASN THR
SEQRES 9 A 369 LYS LEU TYR PRO GLY GLN VAL TRP THR ILE ALA ASP LEU
SEQRES 10 A 369 LEU GLN ILE THR VAL SER ASN SER SER ASN ALA ALA ALA
SEQRES 11 A 369 LEU ILE LEU ALA LYS LYS VAL SER LYS ASN THR SER ASP
SEQRES 12 A 369 PHE VAL ASP LEU MET ASN ASN LYS ALA LYS ALA ILE GLY
SEQRES 13 A 369 MET LYS ASN THR HIS PHE VAL ASN PRO THR GLY ALA GLU
SEQRES 14 A 369 ASN SER ARG LEU ARG SER PHE ALA PRO THR LYS TYR LYS
SEQRES 15 A 369 ASP GLN GLU ARG THR VAL THR THR ALA ARG ASP TYR ALA
SEQRES 16 A 369 ILE LEU ASP LEU HIS VAL ILE LYS GLU THR PRO LYS ILE
SEQRES 17 A 369 LEU ASP PHE THR LYS GLN LEU ALA PRO THR THR HIS ALA
SEQRES 18 A 369 VAL THR TYR TYR THR PHE ASN PHE SER LEU GLU GLY ALA
SEQRES 19 A 369 LYS MET SER LEU PRO GLY THR ASP GLY LEU LYS THR GLY
SEQRES 20 A 369 SER SER ASP THR ALA ASN TYR ASN HIS THR ILE THR THR
SEQRES 21 A 369 LYS ARG GLY LYS PHE ARG ILE ASN GLN VAL ILE MET GLY
SEQRES 22 A 369 ALA GLY ASP TYR LYS ASN LEU GLY GLY GLU LYS GLN ARG
SEQRES 23 A 369 ASN MET MET GLY ASN ALA LEU MET GLU ARG SER PHE ASP
SEQRES 24 A 369 GLN TYR LYS TYR VAL LYS ILE LEU SER LYS GLY GLU GLN
SEQRES 25 A 369 ARG ILE ASN GLY LYS LYS TYR TYR VAL GLU ASN ASP LEU
SEQRES 26 A 369 TYR ASP VAL LEU PRO SER ASP PHE SER LYS LYS ASP TYR
SEQRES 27 A 369 LYS LEU VAL VAL GLU ASP GLY LYS VAL HIS ALA ASP TYR
SEQRES 28 A 369 PRO ARG GLU PHE ILE ASN LYS ASP TYR GLY PRO PRO THR
SEQRES 29 A 369 VAL GLU VAL HIS GLN
SEQRES 1 B 369 GLY PRO HIS THR SER SER TYR ALA GLN ALA THR ASN SER
SEQRES 2 B 369 ASP VAL THR PRO VAL GLN ALA ALA ASN GLN TYR GLY TYR
SEQRES 3 B 369 ALA GLY LEU SER ALA ALA TYR GLU PRO THR SER ALA VAL
SEQRES 4 B 369 ASN VAL SER GLN THR GLY GLN LEU LEU TYR GLN TYR ASN
SEQRES 5 B 369 ILE ASP THR LYS TRP ASN PRO ALA SER MET THR LYS LEU
SEQRES 6 B 369 MET THR MET TYR LEU THR LEU GLU ALA VAL ASN LYS GLY
SEQRES 7 B 369 GLN LEU SER LEU ASP ASP THR VAL THR MET THR ASN LYS
SEQRES 8 B 369 GLU TYR ILE MET SER THR LEU PRO GLU LEU SER ASN THR
SEQRES 9 B 369 LYS LEU TYR PRO GLY GLN VAL TRP THR ILE ALA ASP LEU
SEQRES 10 B 369 LEU GLN ILE THR VAL SER ASN SER SER ASN ALA ALA ALA
SEQRES 11 B 369 LEU ILE LEU ALA LYS LYS VAL SER LYS ASN THR SER ASP
SEQRES 12 B 369 PHE VAL ASP LEU MET ASN ASN LYS ALA LYS ALA ILE GLY
SEQRES 13 B 369 MET LYS ASN THR HIS PHE VAL ASN PRO THR GLY ALA GLU
SEQRES 14 B 369 ASN SER ARG LEU ARG SER PHE ALA PRO THR LYS TYR LYS
SEQRES 15 B 369 ASP GLN GLU ARG THR VAL THR THR ALA ARG ASP TYR ALA
SEQRES 16 B 369 ILE LEU ASP LEU HIS VAL ILE LYS GLU THR PRO LYS ILE
SEQRES 17 B 369 LEU ASP PHE THR LYS GLN LEU ALA PRO THR THR HIS ALA
SEQRES 18 B 369 VAL THR TYR TYR THR PHE ASN PHE SER LEU GLU GLY ALA
SEQRES 19 B 369 LYS MET SER LEU PRO GLY THR ASP GLY LEU LYS THR GLY
SEQRES 20 B 369 SER SER ASP THR ALA ASN TYR ASN HIS THR ILE THR THR
SEQRES 21 B 369 LYS ARG GLY LYS PHE ARG ILE ASN GLN VAL ILE MET GLY
SEQRES 22 B 369 ALA GLY ASP TYR LYS ASN LEU GLY GLY GLU LYS GLN ARG
SEQRES 23 B 369 ASN MET MET GLY ASN ALA LEU MET GLU ARG SER PHE ASP
SEQRES 24 B 369 GLN TYR LYS TYR VAL LYS ILE LEU SER LYS GLY GLU GLN
SEQRES 25 B 369 ARG ILE ASN GLY LYS LYS TYR TYR VAL GLU ASN ASP LEU
SEQRES 26 B 369 TYR ASP VAL LEU PRO SER ASP PHE SER LYS LYS ASP TYR
SEQRES 27 B 369 LYS LEU VAL VAL GLU ASP GLY LYS VAL HIS ALA ASP TYR
SEQRES 28 B 369 PRO ARG GLU PHE ILE ASN LYS ASP TYR GLY PRO PRO THR
SEQRES 29 B 369 VAL GLU VAL HIS GLN
HET SO4 A 801 5
HET SO4 A 802 5
HET SO4 A 803 5
HET UNL A 900 9
HET SO4 B 804 5
HET SO4 B 805 5
HET UNL B 901 9
HETNAM SO4 SULFATE ION
HETNAM UNL UNKNOWN LIGAND
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 10 HOH *781(H2 O)
HELIX 1 1 GLY A 15 ALA A 22 1 8
HELIX 2 2 THR A 30 TYR A 38 1 9
HELIX 3 3 SER A 44 GLU A 48 5 5
HELIX 4 4 PRO A 73 SER A 75 5 3
HELIX 5 5 MET A 76 LYS A 91 1 16
HELIX 6 6 THR A 103 SER A 110 1 8
HELIX 7 7 ILE A 128 ASN A 138 1 11
HELIX 8 8 SER A 140 SER A 152 1 13
HELIX 9 9 ASN A 154 ILE A 169 1 16
HELIX 10 10 GLU A 183 ARG A 188 1 6
HELIX 11 11 SER A 189 ALA A 191 5 3
HELIX 12 12 PRO A 192 LYS A 196 5 5
HELIX 13 13 THR A 204 THR A 219 1 16
HELIX 14 14 LYS A 221 LYS A 227 1 7
HELIX 15 15 GLY A 296 GLN A 314 1 19
HELIX 16 16 SER A 348 TYR A 352 5 5
HELIX 17 17 GLY B 15 TYR B 21 1 7
HELIX 18 18 THR B 30 GLY B 39 1 10
HELIX 19 19 SER B 44 GLU B 48 5 5
HELIX 20 20 PRO B 73 SER B 75 5 3
HELIX 21 21 MET B 76 LYS B 91 1 16
HELIX 22 22 THR B 103 SER B 110 1 8
HELIX 23 23 ILE B 128 ASN B 138 1 11
HELIX 24 24 SER B 140 SER B 152 1 13
HELIX 25 25 ASN B 154 GLY B 170 1 17
HELIX 26 26 GLU B 183 ARG B 188 1 6
HELIX 27 27 SER B 189 ALA B 191 5 3
HELIX 28 28 PRO B 192 LYS B 196 5 5
HELIX 29 29 THR B 204 THR B 219 1 16
HELIX 30 30 LYS B 221 LYS B 227 1 7
HELIX 31 31 GLY B 296 GLN B 314 1 19
HELIX 32 32 SER B 348 TYR B 352 5 5
SHEET 1 A 5 LEU A 61 TYR A 65 0
SHEET 2 A 5 SER A 51 SER A 56 -1 N ASN A 54 O LEU A 62
SHEET 3 A 5 PHE A 279 ALA A 288 -1 O ASN A 282 N VAL A 55
SHEET 4 A 5 ASN A 267 ARG A 276 -1 N ILE A 272 O GLN A 283
SHEET 5 A 5 THR A 255 SER A 263 -1 N GLY A 261 O ASN A 269
SHEET 1 B 2 THR A 99 THR A 101 0
SHEET 2 B 2 VAL A 125 THR A 127 -1 O TRP A 126 N VAL A 100
SHEET 1 C 2 THR A 232 THR A 233 0
SHEET 2 C 2 VAL A 236 THR A 237 -1 O VAL A 236 N THR A 233
SHEET 1 D 2 TYR A 315 LEU A 321 0
SHEET 2 D 2 LEU A 339 PRO A 344 -1 O LEU A 339 N ILE A 320
SHEET 1 E 5 GLY A 324 ILE A 328 0
SHEET 2 E 5 LYS A 331 VAL A 335 -1 O VAL A 335 N GLY A 324
SHEET 3 E 5 VAL A 379 HIS A 382 -1 O HIS A 382 N TYR A 334
SHEET 4 E 5 LYS A 360 ASP A 364 -1 N VAL A 361 O VAL A 379
SHEET 5 E 5 LYS A 353 GLU A 357 -1 N VAL A 355 O HIS A 362
SHEET 1 F 5 LEU B 61 TYR B 65 0
SHEET 2 F 5 SER B 51 SER B 56 -1 N ASN B 54 O LEU B 62
SHEET 3 F 5 PHE B 279 ALA B 288 -1 O ASN B 282 N VAL B 55
SHEET 4 F 5 ASN B 267 ARG B 276 -1 N TYR B 268 O ALA B 288
SHEET 5 F 5 THR B 255 SER B 263 -1 N GLY B 261 O ASN B 269
SHEET 1 G 2 THR B 99 THR B 101 0
SHEET 2 G 2 VAL B 125 THR B 127 -1 O TRP B 126 N VAL B 100
SHEET 1 H 2 THR B 232 THR B 233 0
SHEET 2 H 2 VAL B 236 THR B 237 -1 O VAL B 236 N THR B 233
SHEET 1 I 2 TYR B 315 LEU B 321 0
SHEET 2 I 2 LEU B 339 PRO B 344 -1 O LEU B 339 N ILE B 320
SHEET 1 J 5 GLY B 324 ILE B 328 0
SHEET 2 J 5 LYS B 331 VAL B 335 -1 O LYS B 331 N ILE B 328
SHEET 3 J 5 VAL B 379 HIS B 382 -1 O HIS B 382 N TYR B 334
SHEET 4 J 5 LYS B 360 ASP B 364 -1 N VAL B 361 O VAL B 379
SHEET 5 J 5 LYS B 353 GLU B 357 -1 N VAL B 355 O HIS B 362
CISPEP 1 GLY A 257 LEU A 258 0 2.31
CISPEP 2 GLY B 257 LEU B 258 0 0.51
SITE 1 AC1 7 ASN A 154 THR A 155 SER A 156 PRO A 192
SITE 2 AC1 7 THR A 193 HOH A1031 HOH A1196
SITE 1 AC2 8 GLN A 124 VAL A 125 LYS A 172 HIS A 234
SITE 2 AC2 8 HOH A1023 HOH A1129 HOH A1224 HOH A1227
SITE 1 AC3 6 ASP A 197 GLN A 198 GLU A 199 ARG A 200
SITE 2 AC3 6 HOH A1061 HOH A1230
SITE 1 AC4 3 GLN B 198 GLU B 199 ARG B 200
SITE 1 AC5 8 GLN B 124 VAL B 125 LYS B 172 HIS B 234
SITE 2 AC5 8 HOH B1111 HOH B1262 HOH B1272 HOH B1285
SITE 1 AC6 14 GLY A 15 PRO A 16 HIS A 17 THR A 18
SITE 2 AC6 14 SER A 75 SER A 116 SER A 139 PHE A 241
SITE 3 AC6 14 THR A 260 GLY A 261 SER A 262 HOH A 941
SITE 4 AC6 14 HOH A 996 HOH A1048
SITE 1 AC7 14 GLY B 15 PRO B 16 HIS B 17 THR B 18
SITE 2 AC7 14 SER B 75 SER B 116 SER B 139 PHE B 241
SITE 3 AC7 14 THR B 260 GLY B 261 SER B 262 HOH B 910
SITE 4 AC7 14 HOH B 963 HOH B1042
CRYST1 48.713 140.189 145.775 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 0.020528 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007133 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006860 0.00000
(ATOM LINES ARE NOT SHOWN.)
END