| 3KSR-pdb | HEADER HYDROLASE 23-NOV-09 3KSR
TITLE CRYSTAL STRUCTURE OF PUTATIVE SERINE HYDROLASE (NP_639225.1)
TITLE 2 FROM XANTHOMONAS CAMPESTRIS AT 2.69 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SERINE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS
SOURCE 3 STR. ATCC 33913;
SOURCE 4 ORGANISM_TAXID: 190485;
SOURCE 5 GENE: XCC3885;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS SERINE HYDROLASE, CATALYTIC TRIAD, STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI-2
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 22-DEC-09 3KSR 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE SERINE HYDROLASE
JRNL TITL 2 (NP_639225.1) FROM XANTHOMONAS CAMPESTRIS AT 2.69 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0053
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 10275
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 497
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) : 2.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 677
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.3690
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1857
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 81.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.55000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : -1.10000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.498
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.271
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.192
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.998
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1905 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1242 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2595 ; 1.517 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3027 ; 0.975 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 242 ; 5.488 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;37.732 ;23.735
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 301 ;15.764 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;17.027 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 292 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2141 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 376 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1207 ; 1.405 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 492 ; 0.265 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1927 ; 2.617 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 698 ; 5.150 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 668 ; 7.151 ;11.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 243
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4660 12.2514 66.9184
REMARK 3 T TENSOR
REMARK 3 T11: 0.2135 T22: 0.0861
REMARK 3 T33: 0.1219 T12: -0.0927
REMARK 3 T13: -0.0868 T23: 0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 1.2317 L22: 1.4436
REMARK 3 L33: 1.6784 L12: 0.5999
REMARK 3 L13: 0.7020 L23: 1.3580
REMARK 3 S TENSOR
REMARK 3 S11: -0.1264 S12: 0.1757 S13: 0.0937
REMARK 3 S21: -0.1466 S22: 0.1428 S23: -0.1726
REMARK 3 S31: -0.2296 S32: 0.1408 S33: -0.0165
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORDS CONTAIN RESIDUAL B FACTORS
REMARK 3 ONLY. 3. PHOSPHATE (PO4) AND CHLORIDE (CL) MODELLED ARE
REMARK 3 PRESENT IN CRYSTALLIZATION CONDITION. 4. RAMACHANDRAN OUTLIER
REMARK 3 (G242) IS LIKELY DUE TO POOR QUALITY OF THE MAPS AT THIS
REMARK 3 LOCATION.
REMARK 4
REMARK 4 3KSR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-09.
REMARK 100 THE RCSB ID CODE IS RCSB056401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.64
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97849
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10299
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690
REMARK 200 RESOLUTION RANGE LOW (A) : 39.559
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.69300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.82M DI-AMMONIUM HYDROGEN
REMARK 280 PHOSPHATE, 0.2M SODIUM CHLORIDE, 0.1M IMIDAZOLE PH 7.64,
REMARK 280 NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 110.12500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.43250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.43250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 165.18750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.43250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.43250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 55.06250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.43250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.43250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 165.18750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.43250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.43250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.06250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 110.12500
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 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 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 110.12500
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 0
REMARK 465 ARG A 244
REMARK 465 ILE A 245
REMARK 465 ALA A 246
REMARK 465 LEU A 247
REMARK 465 ALA A 248
REMARK 465 LYS A 249
REMARK 465 GLU A 250
REMARK 465 VAL A 251
REMARK 465 VAL A 252
REMARK 465 ALA A 253
REMARK 465 ALA A 254
REMARK 465 ARG A 255
REMARK 465 LYS A 256
REMARK 465 GLN A 257
REMARK 465 LEU A 258
REMARK 465 LEU A 259
REMARK 465 LYS A 260
REMARK 465 GLU A 261
REMARK 465 GLN A 262
REMARK 465 GLN A 263
REMARK 465 GLY A 264
REMARK 465 ASP A 265
REMARK 465 ALA A 266
REMARK 465 VAL A 267
REMARK 465 SER A 268
REMARK 465 LEU A 269
REMARK 465 PRO A 270
REMARK 465 GLY A 271
REMARK 465 GLN A 272
REMARK 465 GLY A 273
REMARK 465 SER A 274
REMARK 465 ARG A 275
REMARK 465 GLU A 276
REMARK 465 PHE A 277
REMARK 465 ARG A 278
REMARK 465 GLY A 279
REMARK 465 ASP A 280
REMARK 465 ILE A 281
REMARK 465 ARG A 282
REMARK 465 ALA A 283
REMARK 465 VAL A 284
REMARK 465 GLU A 285
REMARK 465 LYS A 286
REMARK 465 THR A 287
REMARK 465 SER A 288
REMARK 465 ALA A 289
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 ARG A 119 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 210 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 230 CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 55 CB CYS A 55 SG -0.113
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 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.1 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 GLU A 66 -115.48 60.58
REMARK 500 SER A 108 -115.03 41.71
REMARK 500 THR A 202 24.26 -77.06
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 PO4 A 290
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 291
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 292
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 383078 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3KSR A 1 289 UNP Q8P431 Q8P431_XANCP 1 289
SEQADV 3KSR GLY A 0 UNP Q8P431 LEADER SEQUENCE
SEQRES 1 A 290 GLY MSE GLU ALA LYS LEU SER SER ILE GLU ILE PRO VAL
SEQRES 2 A 290 GLY GLN ASP GLU LEU SER GLY THR LEU LEU THR PRO THR
SEQRES 3 A 290 GLY MSE PRO GLY VAL LEU PHE VAL HIS GLY TRP GLY GLY
SEQRES 4 A 290 SER GLN HIS HIS SER LEU VAL ARG ALA ARG GLU ALA VAL
SEQRES 5 A 290 GLY LEU GLY CYS ILE CYS MSE THR PHE ASP LEU ARG GLY
SEQRES 6 A 290 HIS GLU GLY TYR ALA SER MSE ARG GLN SER VAL THR ARG
SEQRES 7 A 290 ALA GLN ASN LEU ASP ASP ILE LYS ALA ALA TYR ASP GLN
SEQRES 8 A 290 LEU ALA SER LEU PRO TYR VAL ASP ALA HIS SER ILE ALA
SEQRES 9 A 290 VAL VAL GLY LEU SER TYR GLY GLY TYR LEU SER ALA LEU
SEQRES 10 A 290 LEU THR ARG GLU ARG PRO VAL GLU TRP LEU ALA LEU ARG
SEQRES 11 A 290 SER PRO ALA LEU TYR LYS ASP ALA HIS TRP ASP GLN PRO
SEQRES 12 A 290 LYS VAL SER LEU ASN ALA ASP PRO ASP LEU MSE ASP TYR
SEQRES 13 A 290 ARG ARG ARG ALA LEU ALA PRO GLY ASP ASN LEU ALA LEU
SEQRES 14 A 290 ALA ALA CYS ALA GLN TYR LYS GLY ASP VAL LEU LEU VAL
SEQRES 15 A 290 GLU ALA GLU ASN ASP VAL ILE VAL PRO HIS PRO VAL MSE
SEQRES 16 A 290 ARG ASN TYR ALA ASP ALA PHE THR ASN ALA ARG SER LEU
SEQRES 17 A 290 THR SER ARG VAL ILE ALA GLY ALA ASP HIS ALA LEU SER
SEQRES 18 A 290 VAL LYS GLU HIS GLN GLN GLU TYR THR ARG ALA LEU ILE
SEQRES 19 A 290 ASP TRP LEU THR GLU MSE VAL VAL GLY ARG ARG ILE ALA
SEQRES 20 A 290 LEU ALA LYS GLU VAL VAL ALA ALA ARG LYS GLN LEU LEU
SEQRES 21 A 290 LYS GLU GLN GLN GLY ASP ALA VAL SER LEU PRO GLY GLN
SEQRES 22 A 290 GLY SER ARG GLU PHE ARG GLY ASP ILE ARG ALA VAL GLU
SEQRES 23 A 290 LYS THR SER ALA
MODRES 3KSR MSE A 1 MET SELENOMETHIONINE
MODRES 3KSR MSE A 27 MET SELENOMETHIONINE
MODRES 3KSR MSE A 58 MET SELENOMETHIONINE
MODRES 3KSR MSE A 71 MET SELENOMETHIONINE
MODRES 3KSR MSE A 153 MET SELENOMETHIONINE
MODRES 3KSR MSE A 194 MET SELENOMETHIONINE
MODRES 3KSR MSE A 239 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 27 8
HET MSE A 58 8
HET MSE A 71 8
HET MSE A 153 8
HET MSE A 194 8
HET MSE A 239 8
HET PO4 A 290 5
HET PO4 A 291 5
HET CL A 292 1
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 CL CL 1-
FORMUL 5 HOH *10(H2 O)
HELIX 1 1 SER A 43 LEU A 53 1 11
HELIX 2 2 HIS A 65 ARG A 72 5 8
HELIX 3 3 THR A 76 SER A 93 1 18
HELIX 4 4 SER A 108 THR A 118 1 11
HELIX 5 5 PRO A 142 ASP A 149 1 8
HELIX 6 6 ASP A 151 ARG A 156 1 6
HELIX 7 7 ALA A 161 ASP A 164 5 4
HELIX 8 8 ASN A 165 TYR A 174 1 10
HELIX 9 9 PRO A 190 PHE A 201 1 12
HELIX 10 10 VAL A 221 GLY A 242 1 22
SHEET 1 A 2 GLU A 2 VAL A 12 0
SHEET 2 A 2 ASP A 15 THR A 25 -1 O THR A 23 N LYS A 4
SHEET 1 B 6 ILE A 56 MSE A 58 0
SHEET 2 B 6 MSE A 27 VAL A 33 1 N VAL A 30 O ILE A 56
SHEET 3 B 6 VAL A 97 LEU A 107 1 O VAL A 105 N LEU A 31
SHEET 4 B 6 TRP A 125 ARG A 129 1 O ARG A 129 N GLY A 106
SHEET 5 B 6 ASP A 177 ALA A 183 1 O LEU A 179 N LEU A 128
SHEET 6 B 6 SER A 206 ILE A 212 1 O ILE A 212 N GLU A 182
LINK C MSE A 1 N GLU A 2 1555 1555 1.35
LINK C MSE A 27 N PRO A 28 1555 1555 1.33
LINK C MSE A 58 N THR A 59 1555 1555 1.33
LINK C MSE A 71 N ARG A 72 1555 1555 1.33
LINK C MSE A 153 N ASP A 154 1555 1555 1.32
LINK C MSE A 194 N ARG A 195 1555 1555 1.34
LINK C MSE A 239 N VAL A 240 1555 1555 1.32
SITE 1 AC1 7 TRP A 36 TYR A 134 LYS A 143 ASN A 147
SITE 2 AC1 7 ARG A 156 ILE A 188 HOH A 300
SITE 1 AC2 2 LYS A 85 ARG A 121
SITE 1 AC3 4 ASP A 186 VAL A 187 ASP A 216 HIS A 217
CRYST1 56.865 56.865 220.250 90.00 90.00 90.00 P 43 21 2 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 0.017585 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017585 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004540 0.00000
TER 1858 ARG A 243
MASTER 418 0 10 10 8 0 4 6 1878 1 73 23
END
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