HEADER HYDROLASE 19-APR-06 2GPZ
TITLE TRANSTHYRETIN-LIKE PROTEIN FROM SALMONELLA DUBLIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN-LIKE PROTEIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 3 DUBLIN;
SOURCE 4 ORGANISM_TAXID: 98360;
SOURCE 5 STRAIN: SUBSP. ENTERICA SEROVAR DUBLIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS SALMONELLA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.BUCKLE,R.H.LAW,J.C.WHISSTOCK
REVDAT 4 30-AUG-23 2GPZ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GPZ 1 VERSN
REVDAT 2 04-JUL-06 2GPZ 1 JRNL
REVDAT 1 16-MAY-06 2GPZ 0
JRNL AUTH S.C.HENNEBRY,R.H.LAW,S.J.RICHARDSON,A.M.BUCKLE,J.C.WHISSTOCK
JRNL TITL THE CRYSTAL STRUCTURE OF THE TRANSTHYRETIN-LIKE PROTEIN FROM
JRNL TITL 2 SALMONELLA DUBLIN, A PROKARYOTE 5-HYDROXYISOURATE HYDROLASE.
JRNL REF J.MOL.BIOL. V. 359 1389 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16787778
JRNL DOI 10.1016/J.JMB.2006.04.057
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 10306
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 496
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 700
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 30
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1732
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.69000
REMARK 3 B22 (A**2) : -0.69000
REMARK 3 B33 (A**2) : 1.04000
REMARK 3 B12 (A**2) : -0.35000
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): 0.465
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.282
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.236
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.260
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1786 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2426 ; 1.193 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 216 ; 6.014 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 78 ;31.307 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 278 ;16.602 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ; 9.216 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 258 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1360 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 750 ; 0.162 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1144 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 95 ; 0.123 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 83 ; 0.159 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.098 ; 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): 1130 ; 0.529 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1758 ; 0.969 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 770 ; 1.424 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 668 ; 2.084 ;10.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 115 1
REMARK 3 1 C 5 C 115 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 866 ; NULL ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 866 ; 0.01 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2GPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037411.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-13
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10308
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.497
REMARK 200 RESOLUTION RANGE LOW (A) : 82.017
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : 0.11100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.45700
REMARK 200 R SYM FOR SHELL (I) : 0.45700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1SN0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M MAGNESIUM CHLORIDE,
REMARK 280 0.1M SODIUM CACODYLATE, PH 6.0, EVAPORATION, RECRYSTALLIZATION,
REMARK 280 TEMPERATURE 295K, PH 6.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 X-Y,X,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 -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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
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 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: BIOLOGICAL TETRAMER GENERATED FROM THE DIMER IN THE
REMARK 300 ASYMMETRIC UNIT, BY -X, -Y-1, Z
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 47.35250
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -82.01694
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 128 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 123 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 ASN A 33
REMARK 465 ASN C 33
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 7 CD1 CD2
REMARK 470 LYS A 30 CE NZ
REMARK 470 LYS A 31 CB CG CD CE NZ
REMARK 470 ASP A 32 CG OD1 OD2
REMARK 470 LYS A 56 CE NZ
REMARK 470 GLN A 71 CG CD NE2
REMARK 470 GLU A 74 CD OE2
REMARK 470 ASP A 79 OD1 OD2
REMARK 470 LYS A 93 NZ
REMARK 470 LEU C 7 CD1 CD2
REMARK 470 LYS C 30 CE NZ
REMARK 470 LYS C 31 CB CG CD CE NZ
REMARK 470 ASP C 32 CG OD1 OD2
REMARK 470 LYS C 56 CE NZ
REMARK 470 GLN C 71 CG CD NE2
REMARK 470 GLU C 74 CD OE2
REMARK 470 ASP C 79 OD1 OD2
REMARK 470 LYS C 93 NZ
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 TRP A 53 73.51 53.58
REMARK 500 GLU A 55 99.64 -56.90
REMARK 500 TRP C 53 74.52 53.18
REMARK 500 GLU C 55 99.67 -57.22
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 C 116
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 116
DBREF 2GPZ A 6 115 GB 66947663 CAI99863 27 136
DBREF 2GPZ C 6 115 GB 66947663 CAI99863 27 136
SEQADV 2GPZ MET A 5 GB 66947663 INITIATING METHIONINE
SEQADV 2GPZ MET C 5 GB 66947663 INITIATING METHIONINE
SEQRES 1 A 111 MET ILE LEU SER VAL HIS ILE LEU ASP GLN GLN THR GLY
SEQRES 2 A 111 LYS PRO ALA PRO GLY VAL GLU VAL VAL LEU GLU GLN LYS
SEQRES 3 A 111 LYS ASP ASN GLY TRP THR GLN LEU ASN THR GLY HIS THR
SEQRES 4 A 111 ASP GLN ASP GLY ARG ILE LYS ALA LEU TRP PRO GLU LYS
SEQRES 5 A 111 ALA ALA ALA PRO GLY ASP TYR ARG VAL ILE PHE LYS THR
SEQRES 6 A 111 GLY GLN TYR PHE GLU SER LYS LYS LEU ASP THR PHE PHE
SEQRES 7 A 111 PRO GLU ILE PRO VAL GLU PHE HIS ILE SER LYS THR ASN
SEQRES 8 A 111 GLU HIS TYR HIS VAL PRO LEU LEU LEU SER GLN TYR GLY
SEQRES 9 A 111 TYR SER THR TYR ARG GLY SER
SEQRES 1 C 111 MET ILE LEU SER VAL HIS ILE LEU ASP GLN GLN THR GLY
SEQRES 2 C 111 LYS PRO ALA PRO GLY VAL GLU VAL VAL LEU GLU GLN LYS
SEQRES 3 C 111 LYS ASP ASN GLY TRP THR GLN LEU ASN THR GLY HIS THR
SEQRES 4 C 111 ASP GLN ASP GLY ARG ILE LYS ALA LEU TRP PRO GLU LYS
SEQRES 5 C 111 ALA ALA ALA PRO GLY ASP TYR ARG VAL ILE PHE LYS THR
SEQRES 6 C 111 GLY GLN TYR PHE GLU SER LYS LYS LEU ASP THR PHE PHE
SEQRES 7 C 111 PRO GLU ILE PRO VAL GLU PHE HIS ILE SER LYS THR ASN
SEQRES 8 C 111 GLU HIS TYR HIS VAL PRO LEU LEU LEU SER GLN TYR GLY
SEQRES 9 C 111 TYR SER THR TYR ARG GLY SER
HET SO4 A 116 5
HET SO4 C 116 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *32(H2 O)
HELIX 1 1 LYS A 68 LYS A 76 1 9
HELIX 2 2 LYS C 68 LYS C 76 1 9
SHEET 1 A 3 LYS A 18 PRO A 19 0
SHEET 2 A 3 ILE A 6 ASP A 13 -1 N ASP A 13 O LYS A 18
SHEET 3 A 3 HIS A 97 HIS A 99 1 O TYR A 98 N ILE A 6
SHEET 1 B 4 ARG A 48 ILE A 49 0
SHEET 2 B 4 ILE A 6 ASP A 13 -1 N VAL A 9 O ILE A 49
SHEET 3 B 4 LEU A 102 SER A 105 1 O LEU A 102 N LEU A 12
SHEET 4 B 4 GLY A 108 THR A 111 -1 O SER A 110 N LEU A 103
SHEET 1 C 4 TRP A 35 HIS A 42 0
SHEET 2 C 4 GLU A 24 LYS A 30 -1 N VAL A 25 O GLY A 41
SHEET 3 C 4 GLY A 61 PHE A 67 -1 O ARG A 64 N GLU A 28
SHEET 4 C 4 ILE A 85 ILE A 91 -1 O PHE A 89 N TYR A 63
SHEET 1 D 3 LYS C 18 PRO C 19 0
SHEET 2 D 3 ILE C 6 ASP C 13 -1 N ASP C 13 O LYS C 18
SHEET 3 D 3 HIS C 97 HIS C 99 1 O TYR C 98 N ILE C 6
SHEET 1 E 4 ARG C 48 ILE C 49 0
SHEET 2 E 4 ILE C 6 ASP C 13 -1 N VAL C 9 O ILE C 49
SHEET 3 E 4 LEU C 102 SER C 105 1 O LEU C 102 N LEU C 12
SHEET 4 E 4 GLY C 108 THR C 111 -1 O SER C 110 N LEU C 103
SHEET 1 F 4 TRP C 35 HIS C 42 0
SHEET 2 F 4 GLU C 24 LYS C 30 -1 N VAL C 25 O GLY C 41
SHEET 3 F 4 GLY C 61 PHE C 67 -1 O ARG C 64 N GLU C 28
SHEET 4 F 4 ILE C 85 ILE C 91 -1 O PHE C 89 N TYR C 63
CISPEP 1 LEU A 52 TRP A 53 0 6.79
CISPEP 2 GLY A 114 SER A 115 0 4.90
CISPEP 3 LEU C 52 TRP C 53 0 7.07
CISPEP 4 GLY C 114 SER C 115 0 4.60
SITE 1 AC1 5 ASP C 44 GLN C 45 ASP C 46 LYS C 50
SITE 2 AC1 5 HIS C 97
SITE 1 AC2 5 ASP A 44 GLN A 45 ASP A 46 LYS A 50
SITE 2 AC2 5 HIS A 97
CRYST1 94.705 94.705 57.381 90.00 90.00 120.00 P 6 12
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 0.010559 0.006096 0.000000 0.00000
SCALE2 0.000000 0.012193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017427 0.00000
(ATOM LINES ARE NOT SHOWN.)
END