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HEADER HYDROLASE 01-AUG-09 3III
TITLE 1.95 ANGSTROM CRYSTAL STRUCTURE OF COCE/NOND FAMILY
TITLE 2 HYDROLASE (SACOL2612) FROM STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COCE/NOND FAMILY HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS
SOURCE 3 COL;
SOURCE 4 ORGANISM_TAXID: 93062;
SOURCE 5 STRAIN: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS COL;
SOURCE 6 GENE: SACOL2612;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG19C
KEYWDS STRUCTURAL GENOMICS, HYDROLASE, CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS OF INFECTIOUS DISEASES, CSGID
EXPDTA X-RAY DIFFRACTION
AUTHOR T.OSINSKI,M.CHRUSZCZ,M.J.DOMAGALSKI,M.CYMBOROWSKI,
AUTHOR 2 I.A.SHUMILIN,T.SKARINA,O.ONOPRIYENKO,M.D.ZIMMERMAN,
AUTHOR 3 A.SAVCHENKO,A.EDWARDS,W.F.ANDERSON,W.MINOR,CENTER FOR
AUTHOR 4 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 1 18-AUG-09 3III 0
JRNL AUTH T.OSINSKI,M.CHRUSZCZ,M.J.DOMAGALSKI,M.CYMBOROWSKI,
JRNL AUTH 2 I.A.SHUMILIN,T.SKARINA,O.ONOPRIYENKO,M.D.ZIMMERMAN,
JRNL AUTH 3 A.SAVCHENKO,A.EDWARDS,W.F.ANDERSON,W.MINOR,
JRNL AUTH 4 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
JRNL AUTH 5 DISEASES (CSGID)
JRNL TITL 1.95 ANGSTROM CRYSTAL STRUCTURE OF COCE/NOND FAMILY
JRNL TITL 2 HYDROLASE (SACOL2612) FROM STAPHYLOCOCCUS AUREUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 42010
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2232
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3024
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.1690
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 556
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.32000
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): 0.141
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.237
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4719 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3188 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6416 ; 1.605 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7777 ; 2.217 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 570 ; 6.854 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;35.283 ;24.958
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 789 ;12.630 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;17.327 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 662 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5313 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 952 ; 0.006 ; 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): 2816 ; 0.899 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1136 ; 0.150 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4572 ; 1.466 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1903 ; 2.770 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1844 ; 3.978 ; 4.500
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 : 5
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 4 A 37
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7910 36.1020 -9.5020
REMARK 3 T TENSOR
REMARK 3 T11: 0.1692 T22: 0.2037
REMARK 3 T33: 0.2069 T12: -0.0603
REMARK 3 T13: -0.0555 T23: 0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 1.4354 L22: 3.2252
REMARK 3 L33: 2.0665 L12: -0.8830
REMARK 3 L13: -0.7292 L23: 0.5802
REMARK 3 S TENSOR
REMARK 3 S11: -0.0307 S12: 0.1581 S13: 0.4769
REMARK 3 S21: -0.0796 S22: 0.0044 S23: -0.3712
REMARK 3 S31: -0.3024 S32: 0.2305 S33: 0.0263
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 38 A 78
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6740 42.3290 0.7650
REMARK 3 T TENSOR
REMARK 3 T11: 0.2620 T22: 0.1167
REMARK 3 T33: 0.1410 T12: -0.0004
REMARK 3 T13: -0.0980 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 1.0394 L22: 0.5918
REMARK 3 L33: 1.5021 L12: 0.0680
REMARK 3 L13: -0.1829 L23: -0.0523
REMARK 3 S TENSOR
REMARK 3 S11: -0.1103 S12: 0.0726 S13: 0.2765
REMARK 3 S21: 0.0993 S22: 0.0365 S23: -0.0838
REMARK 3 S31: -0.4131 S32: -0.0643 S33: 0.0738
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 79 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7170 31.4100 7.5460
REMARK 3 T TENSOR
REMARK 3 T11: 0.4978 T22: 0.4116
REMARK 3 T33: 0.4763 T12: 0.0263
REMARK 3 T13: -0.0611 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 9.1127 L22: 21.9846
REMARK 3 L33: 1.1435 L12: -8.9940
REMARK 3 L13: 2.6190 L23: -4.8465
REMARK 3 S TENSOR
REMARK 3 S11: -0.1684 S12: 0.1796 S13: 0.6717
REMARK 3 S21: -0.4611 S22: -0.1290 S23: -1.2904
REMARK 3 S31: 0.0482 S32: 0.0527 S33: 0.2975
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 88 A 355
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2310 26.6290 10.4270
REMARK 3 T TENSOR
REMARK 3 T11: 0.1310 T22: 0.0880
REMARK 3 T33: 0.0300 T12: 0.0018
REMARK 3 T13: -0.0379 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.4585 L22: 0.3955
REMARK 3 L33: 0.7207 L12: -0.1126
REMARK 3 L13: -0.0097 L23: -0.1180
REMARK 3 S TENSOR
REMARK 3 S11: -0.0780 S12: 0.0028 S13: 0.0613
REMARK 3 S21: 0.0760 S22: -0.0104 S23: 0.0163
REMARK 3 S31: -0.1119 S32: -0.0786 S33: 0.0885
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 356 A 560
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9610 6.5950 30.2040
REMARK 3 T TENSOR
REMARK 3 T11: 0.2411 T22: 0.1177
REMARK 3 T33: 0.0438 T12: 0.0205
REMARK 3 T13: 0.0311 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.6190 L22: 1.0931
REMARK 3 L33: 1.0590 L12: -0.2305
REMARK 3 L13: -0.1698 L23: 0.2262
REMARK 3 S TENSOR
REMARK 3 S11: -0.1618 S12: -0.1281 S13: -0.0754
REMARK 3 S21: 0.3099 S22: 0.0358 S23: 0.0863
REMARK 3 S31: 0.1266 S32: -0.0549 S33: 0.1261
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3III COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-09.
REMARK 100 THE RCSB ID CODE IS RCSB054453.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44452
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 42.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 16.200
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : 0.11200
REMARK 200 FOR THE DATA SET : 29.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.30
REMARK 200 R MERGE FOR SHELL (I) : 0.63700
REMARK 200 R SYM FOR SHELL (I) : 0.63700
REMARK 200 FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000: SOLVE/RESOLVE, SHELXD, SHELXE,
REMARK 200 MLPHARE, DM, ARP/WARP, CCP4, O, COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SUBERIC ACID, SEBACIC ACID,
REMARK 280 HEXADECANEDIOIC ACID, DODECANEDIOIC ACID 12MM EACH, PEG3350
REMARK 280 20%, HEPES 0.1M PH 7.5, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 105.34050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.24900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.24900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.67025
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.24900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.24900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 158.01075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.24900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.24900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.67025
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.24900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.24900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 158.01075
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 105.34050
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 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 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 MSE A 1
REMARK 465 ASN A 2
REMARK 465 ILE A 84
REMARK 465 THR A 85
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 GLU A 106 CB CG CD OE1 OE2
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 37 N CA C O CB CG CD
REMARK 480 GLU A 37 OE1 OE2
REMARK 480 HIS A 373 N CA C O CB CG ND1
REMARK 480 HIS A 373 CD2 CE1 NE2
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 106 -5.98 88.65
REMARK 500 ASP A 129 -132.49 61.30
REMARK 500 SER A 169 -119.36 63.30
REMARK 500 GLU A 193 87.83 69.66
REMARK 500 ASN A 196 13.56 -152.60
REMARK 500 VAL A 202 -43.98 -137.25
REMARK 500 ASP A 245 -166.04 -106.71
REMARK 500 LEU A 273 -92.77 -133.55
REMARK 500 ARG A 297 -164.15 -118.06
REMARK 500 GLU A 299 -70.06 -66.99
REMARK 500 GLN A 451 -168.75 -125.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1015 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH A1018 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A1024 DISTANCE = 5.29 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PLM A 566
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 NI A 561 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 15 NE2
REMARK 620 2 HOH A1009 O 172.1
REMARK 620 3 HOH A1011 O 83.1 89.8
REMARK 620 4 HOH A1122 O 94.1 81.1 78.6
REMARK 620 5 HOH A1010 O 92.0 94.9 173.4 97.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 561
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 562
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 563
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 564
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 565
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 566
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP00832 RELATED DB: TARGETDB
DBREF 3III A 1 560 UNP Q5HCV6 Q5HCV6_STAAC 1 560
SEQRES 1 A 560 MSE ASN GLN HIS LEU LEU GLY ASN PRO LYS LEU THR VAL
SEQRES 2 A 560 THR HIS VAL ASN GLU VAL LYS ALA GLY ILE ASN HIS ILE
SEQRES 3 A 560 VAL VAL ASP SER VAL GLN TYR GLY ASN GLN GLU MSE ILE
SEQRES 4 A 560 MSE GLU LYS ASP GLY THR VAL GLU MSE ARG ASP GLY GLU
SEQRES 5 A 560 LYS LEU TYR ILE ASN ILE PHE ARG PRO ASN LYS ASP GLY
SEQRES 6 A 560 LYS PHE PRO VAL VAL MSE SER ALA ASP THR TYR GLY LYS
SEQRES 7 A 560 ASP ASN LYS PRO LYS ILE THR ASN MSE GLY ALA LEU TRP
SEQRES 8 A 560 PRO THR LEU GLY THR ILE PRO THR SER SER PHE THR PRO
SEQRES 9 A 560 GLU GLU SER PRO ASP PRO GLY PHE TRP VAL PRO ASN ASP
SEQRES 10 A 560 TYR VAL VAL VAL LYS VAL ALA LEU ARG GLY SER ASP LYS
SEQRES 11 A 560 SER LYS GLY VAL LEU SER PRO TRP SER LYS ARG GLU ALA
SEQRES 12 A 560 GLU ASP TYR TYR GLU VAL ILE GLU TRP ALA ALA ASN GLN
SEQRES 13 A 560 SER TRP SER ASN GLY ASN ILE GLY THR ASN GLY VAL SER
SEQRES 14 A 560 TYR LEU ALA VAL THR GLN TRP TRP VAL ALA SER LEU ASN
SEQRES 15 A 560 PRO PRO HIS LEU LYS ALA MSE ILE PRO TRP GLU GLY LEU
SEQRES 16 A 560 ASN ASP MSE TYR ARG GLU VAL ALA PHE HIS GLY GLY ILE
SEQRES 17 A 560 PRO ASP THR GLY PHE TYR ARG PHE TRP THR GLN GLY ILE
SEQRES 18 A 560 PHE ALA ARG TRP THR ASP ASN PRO ASN ILE GLU ASP LEU
SEQRES 19 A 560 ILE GLN ALA GLN GLN GLU HIS PRO LEU PHE ASP ASP PHE
SEQRES 20 A 560 TRP LYS GLN ARG GLN VAL PRO LEU SER GLN ILE LYS THR
SEQRES 21 A 560 PRO LEU LEU THR CYS ALA SER TRP SER THR GLN GLY LEU
SEQRES 22 A 560 HIS ASN ARG GLY SER PHE GLU GLY PHE LYS GLN ALA ALA
SEQRES 23 A 560 SER GLU GLU LYS TRP LEU TYR VAL HIS GLY ARG LYS GLU
SEQRES 24 A 560 TRP GLU SER TYR TYR ALA ARG GLU ASN LEU GLU ARG GLN
SEQRES 25 A 560 LYS SER PHE PHE ASP PHE TYR LEU LYS GLU GLU ASN ASN
SEQRES 26 A 560 ASP TRP LYS ASP THR PRO HIS VAL ILE TYR GLU VAL ARG
SEQRES 27 A 560 ASP GLN PHE TYR LYS GLY GLU PHE LYS SER ALA SER ALA
SEQRES 28 A 560 PHE PRO LEU PRO ASN ALA GLU TYR THR PRO LEU TYR LEU
SEQRES 29 A 560 ASN ALA GLU ASN HIS THR LEU ASN HIS ALA LYS ILE SER
SEQRES 30 A 560 SER ALA HIS VAL ALA GLN TYR ASP SER GLU ASP LYS GLN
SEQRES 31 A 560 GLN ASP VAL SER PHE LYS TYR THR PHE ASP LYS ASP THR
SEQRES 32 A 560 GLU LEU VAL GLY ASN MSE ASN LEU LYS LEU TRP VAL SER
SEQRES 33 A 560 THR LYS ASP SER ASP ASP MSE ASP LEU PHE ALA GLY ILE
SEQRES 34 A 560 LYS LYS LEU ASP ARG ARG GLY ASN GLU VAL ASN PHE PRO
SEQRES 35 A 560 ASP PHE ASN HIS ILE GLU ASN GLY GLN VAL ALA THR GLY
SEQRES 36 A 560 TRP LEU ARG VAL SER HIS ARG GLU LEU ASP GLN GLU LYS
SEQRES 37 A 560 SER SER ILE ALA GLN PRO TRP HIS LYS HIS GLU THR GLU
SEQRES 38 A 560 LEU LYS LEU SER GLN ASP GLU ILE VAL PRO VAL GLU ILE
SEQRES 39 A 560 GLU LEU LEU PRO SER GLY THR LEU PHE LYS GLN GLY GLU
SEQRES 40 A 560 THR LEU GLU VAL VAL VAL LYS GLY SER GLU ILE VAL ILE
SEQRES 41 A 560 GLY ASN SER THR PRO GLY MSE LYS THR ARG TYR GLU HIS
SEQRES 42 A 560 GLU GLU THR VAL ASN LYS GLY MSE HIS MSE ILE TYR THR
SEQRES 43 A 560 GLY GLY LYS TYR ASP SER GLN LEU ILE ILE PRO ILE VAL
SEQRES 44 A 560 ASN
MODRES 3III MSE A 38 MET SELENOMETHIONINE
MODRES 3III MSE A 40 MET SELENOMETHIONINE
MODRES 3III MSE A 48 MET SELENOMETHIONINE
MODRES 3III MSE A 71 MET SELENOMETHIONINE
MODRES 3III MSE A 87 MET SELENOMETHIONINE
MODRES 3III MSE A 189 MET SELENOMETHIONINE
MODRES 3III MSE A 198 MET SELENOMETHIONINE
MODRES 3III MSE A 409 MET SELENOMETHIONINE
MODRES 3III MSE A 423 MET SELENOMETHIONINE
MODRES 3III MSE A 527 MET SELENOMETHIONINE
MODRES 3III MSE A 541 MET SELENOMETHIONINE
MODRES 3III MSE A 543 MET SELENOMETHIONINE
HET MSE A 38 8
HET MSE A 40 8
HET MSE A 48 8
HET MSE A 71 8
HET MSE A 87 8
HET MSE A 189 8
HET MSE A 198 8
HET MSE A 409 8
HET MSE A 423 8
HET MSE A 527 16
HET MSE A 541 8
HET MSE A 543 16
HET NI A 561 1
HET CL A 562 1
HET CL A 563 1
HET CL A 564 1
HET CL A 565 1
HET PLM A 566 10
HETNAM MSE SELENOMETHIONINE
HETNAM NI NICKEL (II) ION
HETNAM CL CHLORIDE ION
HETNAM PLM PALMITIC ACID
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 2 NI NI 2+
FORMUL 3 CL 4(CL 1-)
FORMUL 7 PLM C16 H32 O2
FORMUL 8 HOH *556(H2 O)
HELIX 1 1 GLN A 3 GLY A 7 5 5
HELIX 2 2 HIS A 15 VAL A 19 5 5
HELIX 3 3 ASN A 86 TRP A 91 1 6
HELIX 4 4 PRO A 92 GLY A 95 5 4
HELIX 5 5 ASP A 109 VAL A 114 1 6
HELIX 6 6 PRO A 115 ASP A 117 5 3
HELIX 7 7 SER A 139 ASN A 155 1 17
HELIX 8 8 SER A 169 SER A 180 1 12
HELIX 9 9 ASP A 197 VAL A 202 1 6
HELIX 10 10 GLY A 212 TRP A 225 1 14
HELIX 11 11 ASP A 233 HIS A 241 1 9
HELIX 12 12 ASP A 245 GLN A 250 1 6
HELIX 13 13 PRO A 254 ILE A 258 5 5
HELIX 14 14 SER A 269 GLN A 271 5 3
HELIX 15 15 HIS A 274 ALA A 285 1 12
HELIX 16 16 LYS A 298 ALA A 305 1 8
HELIX 17 17 ALA A 305 LEU A 320 1 16
HELIX 18 18 ASP A 326 THR A 330 5 5
HELIX 19 19 SER A 460 ARG A 462 5 3
SHEET 1 A 7 GLY A 22 SER A 30 0
SHEET 2 A 7 GLY A 34 GLU A 47 -1 O LYS A 42 N GLY A 22
SHEET 3 A 7 LYS A 53 ARG A 60 -1 O ARG A 60 N ILE A 39
SHEET 4 A 7 VAL A 119 ALA A 124 -1 O VAL A 120 N PHE A 59
SHEET 5 A 7 PHE A 67 ASP A 74 1 N PRO A 68 O VAL A 119
SHEET 6 A 7 SER A 159 VAL A 168 1 O GLY A 164 N VAL A 69
SHEET 7 A 7 LEU A 186 TRP A 192 1 O LYS A 187 N ILE A 163
SHEET 1 B 2 PHE A 204 HIS A 205 0
SHEET 2 B 2 ILE A 208 PRO A 209 -1 O ILE A 208 N HIS A 205
SHEET 1 C 4 LEU A 262 SER A 267 0
SHEET 2 C 4 LYS A 290 HIS A 295 1 O TRP A 291 N THR A 264
SHEET 3 C 4 VAL A 333 GLN A 340 1 O ILE A 334 N VAL A 294
SHEET 4 C 4 LYS A 343 ALA A 349 -1 O GLU A 345 N VAL A 337
SHEET 1 D 6 THR A 370 ASN A 372 0
SHEET 2 D 6 GLU A 358 ASN A 365 -1 N TYR A 363 O ASN A 372
SHEET 3 D 6 GLN A 553 VAL A 559 -1 O ILE A 558 N GLU A 358
SHEET 4 D 6 THR A 403 THR A 417 -1 N LYS A 412 O GLN A 553
SHEET 5 D 6 MSE A 541 THR A 546 -1 O TYR A 545 N TRP A 414
SHEET 6 D 6 HIS A 380 ASP A 385 -1 N ALA A 382 O ILE A 544
SHEET 1 E 5 THR A 370 ASN A 372 0
SHEET 2 E 5 GLU A 358 ASN A 365 -1 N TYR A 363 O ASN A 372
SHEET 3 E 5 GLN A 553 VAL A 559 -1 O ILE A 558 N GLU A 358
SHEET 4 E 5 THR A 403 THR A 417 -1 N LYS A 412 O GLN A 553
SHEET 5 E 5 VAL A 490 PHE A 503 -1 O VAL A 490 N VAL A 415
SHEET 1 F 4 VAL A 393 THR A 398 0
SHEET 2 F 4 THR A 508 LYS A 514 -1 O VAL A 511 N PHE A 395
SHEET 3 F 4 ASP A 424 LEU A 432 -1 N LYS A 430 O GLU A 510
SHEET 4 F 4 ALA A 453 ARG A 458 -1 O ALA A 453 N ILE A 429
SHEET 1 G 2 PHE A 441 ASP A 443 0
SHEET 2 G 2 ILE A 447 GLY A 450 -1 O ILE A 447 N ASP A 443
LINK C AGLU A 37 N MSE A 38 1555 1555 1.32
LINK C BGLU A 37 N MSE A 38 1555 1555 1.31
LINK C MSE A 38 N ILE A 39 1555 1555 1.33
LINK C ILE A 39 N MSE A 40 1555 1555 1.33
LINK C MSE A 40 N GLU A 41 1555 1555 1.32
LINK C GLU A 47 N MSE A 48 1555 1555 1.34
LINK C MSE A 48 N ARG A 49 1555 1555 1.33
LINK C VAL A 70 N MSE A 71 1555 1555 1.33
LINK C MSE A 71 N SER A 72 1555 1555 1.34
LINK C ASN A 86 N MSE A 87 1555 1555 1.34
LINK C MSE A 87 N GLY A 88 1555 1555 1.33
LINK C ALA A 188 N MSE A 189 1555 1555 1.33
LINK C MSE A 189 N ILE A 190 1555 1555 1.34
LINK C ASP A 197 N MSE A 198 1555 1555 1.32
LINK C MSE A 198 N TYR A 199 1555 1555 1.33
LINK C ASN A 408 N MSE A 409 1555 1555 1.34
LINK C MSE A 409 N ASN A 410 1555 1555 1.32
LINK C ASP A 422 N MSE A 423 1555 1555 1.33
LINK C MSE A 423 N ASP A 424 1555 1555 1.32
LINK C GLY A 526 N AMSE A 527 1555 1555 1.34
LINK C GLY A 526 N BMSE A 527 1555 1555 1.34
LINK C AMSE A 527 N LYS A 528 1555 1555 1.33
LINK C BMSE A 527 N LYS A 528 1555 1555 1.33
LINK C GLY A 540 N MSE A 541 1555 1555 1.33
LINK C MSE A 541 N HIS A 542 1555 1555 1.32
LINK C HIS A 542 N AMSE A 543 1555 1555 1.33
LINK C HIS A 542 N BMSE A 543 1555 1555 1.33
LINK C AMSE A 543 N ILE A 544 1555 1555 1.33
LINK C BMSE A 543 N ILE A 544 1555 1555 1.34
LINK NE2 HIS A 15 NI NI A 561 1555 1555 1.81
LINK NI NI A 561 O HOH A1009 1555 1555 1.93
LINK NI NI A 561 O HOH A1011 1555 1555 1.90
LINK NI NI A 561 O HOH A1122 1555 1555 1.95
LINK NI NI A 561 O HOH A1010 1555 1555 1.96
CISPEP 1 PHE A 352 PRO A 353 0 -2.38
CISPEP 2 PHE A 444 ASN A 445 0 -7.09
SITE 1 AC1 6 HIS A 15 HIS A 380 HOH A1009 HOH A1010
SITE 2 AC1 6 HOH A1011 HOH A1122
SITE 1 AC2 4 ARG A 200 GLN A 252 LYS A 468 TRP A 475
SITE 1 AC3 2 TYR A 397 ASP A 400
SITE 1 AC4 4 PRO A 331 HIS A 332 SER A 350 HOH A1100
SITE 1 AC5 4 PRO A 353 TYR A 359 GLY A 407 ASN A 408
SITE 1 AC6 6 TYR A 76 SER A 169 PHE A 216 TRP A 300
SITE 2 AC6 6 HOH A 593 HOH A 965
CRYST1 74.498 74.498 210.681 90.00 90.00 90.00 P 41 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 0.013423 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013423 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004747 0.00000
TER 4594 ASN A 560
MASTER 455 0 18 19 30 0 8 6 5164 1 154 44
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