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HEADER HYDROLASE 16-FEB-09 3GA7
TITLE 1.55 ANGSTROM CRYSTAL STRUCTURE OF AN ACETYL ESTERASE FROM
TITLE 2 SALMONELLA TYPHIMURIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 99287;
SOURCE 4 STRAIN: LT2;
SOURCE 5 GENE: AES, STM0490;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ACETYL ESTERASE, PHOSPHOSERINE, IDP00896, CYTOPLASM,
KEYWDS 2 HYDROLASE, SERINE ESTERASE, STRUCTURAL GENOMICS, CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,Z.WAWRZAK,J.BRUNZELLE,O.ONOPRIYENKO,T.SKARINA,
AUTHOR 2 S.N.PETERSON,A.SAVCHENKO,W.F.ANDERSON,CENTER FOR STRUCTURAL
AUTHOR 3 GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 27-OCT-09 3GA7 1 AUTHOR JRNL
REVDAT 1 24-FEB-09 3GA7 0
JRNL AUTH G.MINASOV,Z.WAWRZAK,J.BRUNZELLE,O.ONOPRIYENKO,
JRNL AUTH 2 T.SKARINA,S.N.PETERSON,A.SAVCHENKO,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
JRNL AUTH 4 DISEASES (CSGID)
JRNL TITL 1.55 ANGSTROM CRYSTAL STRUCTURE OF AN ACETYL
JRNL TITL 2 ESTERASE FROM SALMONELLA TYPHIMURIUM.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0051
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 48985
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2628
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3532
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.1620
REMARK 3 BIN FREE R VALUE SET COUNT : 201
REMARK 3 BIN FREE R VALUE : 0.2050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2885
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 508
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : -0.30000
REMARK 3 B33 (A**2) : -0.13000
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): 0.068
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.276
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
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): 2985 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2043 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4101 ; 1.320 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4938 ; 0.801 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 388 ; 3.971 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 158 ;29.711 ;22.785
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 505 ;10.146 ;15.030
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;15.763 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 424 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3557 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 696 ; 0.002 ; 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): 1796 ; 1.240 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 709 ; 0.365 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2942 ; 2.146 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1189 ; 2.895 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1159 ; 4.436 ; 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 : 6
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 5 A 23
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4412 19.0076 -7.3348
REMARK 3 T TENSOR
REMARK 3 T11: 0.2005 T22: 0.2221
REMARK 3 T33: 0.1549 T12: -0.0210
REMARK 3 T13: -0.0384 T23: 0.0468
REMARK 3 L TENSOR
REMARK 3 L11: 0.4954 L22: 3.3447
REMARK 3 L33: 0.8023 L12: -0.2433
REMARK 3 L13: 0.4900 L23: 0.4442
REMARK 3 S TENSOR
REMARK 3 S11: 0.0242 S12: 0.1469 S13: 0.0540
REMARK 3 S21: -0.4070 S22: -0.0365 S23: 0.1006
REMARK 3 S31: 0.0067 S32: -0.0121 S33: 0.0123
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 36 A 49
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2196 29.3490 4.3315
REMARK 3 T TENSOR
REMARK 3 T11: 0.0491 T22: 0.1268
REMARK 3 T33: 0.0890 T12: 0.0073
REMARK 3 T13: 0.0181 T23: 0.0829
REMARK 3 L TENSOR
REMARK 3 L11: 3.3840 L22: 5.1439
REMARK 3 L33: 3.3885 L12: -2.2954
REMARK 3 L13: 0.9239 L23: -0.2617
REMARK 3 S TENSOR
REMARK 3 S11: 0.1928 S12: 0.5549 S13: 0.3136
REMARK 3 S21: -0.2192 S22: -0.2381 S23: -0.2595
REMARK 3 S31: -0.0206 S32: 0.2148 S33: 0.0452
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 50 A 183
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1955 21.0648 21.7646
REMARK 3 T TENSOR
REMARK 3 T11: 0.0151 T22: 0.0209
REMARK 3 T33: 0.0245 T12: -0.0030
REMARK 3 T13: -0.0011 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 1.0880 L22: 0.8138
REMARK 3 L33: 1.0105 L12: 0.2464
REMARK 3 L13: 0.0338 L23: 0.0623
REMARK 3 S TENSOR
REMARK 3 S11: 0.0180 S12: -0.1099 S13: 0.1431
REMARK 3 S21: 0.1030 S22: -0.0231 S23: -0.0042
REMARK 3 S31: -0.0287 S32: -0.0261 S33: 0.0052
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 184 A 212
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7788 8.7165 9.6667
REMARK 3 T TENSOR
REMARK 3 T11: 0.0323 T22: 0.0100
REMARK 3 T33: 0.0184 T12: 0.0048
REMARK 3 T13: 0.0035 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.5808 L22: 1.0036
REMARK 3 L33: 1.7264 L12: 0.0821
REMARK 3 L13: 0.2097 L23: 0.9935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: 0.0077 S13: -0.0084
REMARK 3 S21: -0.0288 S22: 0.0284 S23: -0.0344
REMARK 3 S31: 0.1221 S32: 0.0590 S33: -0.0363
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 213 A 246
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7109 7.7331 6.2007
REMARK 3 T TENSOR
REMARK 3 T11: 0.0689 T22: 0.0569
REMARK 3 T33: 0.0565 T12: -0.0076
REMARK 3 T13: 0.0274 T23: -0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 1.4129 L22: 1.6100
REMARK 3 L33: 1.0453 L12: 0.2467
REMARK 3 L13: 0.5119 L23: -0.1825
REMARK 3 S TENSOR
REMARK 3 S11: -0.0530 S12: 0.1541 S13: -0.0048
REMARK 3 S21: -0.2098 S22: 0.0797 S23: -0.1838
REMARK 3 S31: 0.0304 S32: 0.1317 S33: -0.0267
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 247 A 320
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9221 11.0580 11.9094
REMARK 3 T TENSOR
REMARK 3 T11: 0.0118 T22: 0.0312
REMARK 3 T33: 0.0275 T12: -0.0167
REMARK 3 T13: -0.0005 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 1.1153 L22: 0.9049
REMARK 3 L33: 1.1913 L12: -0.2660
REMARK 3 L13: 0.1122 L23: -0.0876
REMARK 3 S TENSOR
REMARK 3 S11: -0.0012 S12: -0.0366 S13: -0.0109
REMARK 3 S21: -0.0305 S22: -0.0072 S23: 0.1160
REMARK 3 S31: 0.1083 S32: -0.1638 S33: 0.0084
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3GA7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51647
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 14.800
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 58.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 14.90
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 V/V PROTEIN SOLUTION (10MG/ML
REMARK 280 PROTEIN, 0.3M NACL, 10MM NA HEPES PH 7.5) WITH THE SCREEN
REMARK 280 SOLUTION (0.2M SODIUM SULPHATE, PEG3350 20%), VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 32.06950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.06950
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 1.000000 0.000000 0.000000 41.37350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.60350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.37350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.60350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.06950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.37350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.60350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 32.06950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.37350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.60350
REMARK 290 SMTRY3 8 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 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 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 3
REMARK 465 PRO A 26
REMARK 465 GLY A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 PRO A 30
REMARK 465 TRP A 31
REMARK 465 PRO A 32
REMARK 465 ALA A 33
REMARK 465 ASP A 34
REMARK 465 GLY A 35
REMARK 465 PRO A 322
REMARK 465 ARG A 323
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 PHE A 95 -11.68 79.93
REMARK 500 ASN A 99 -165.71 -164.87
REMARK 500 PHE A 261 41.22 -104.50
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 CL A 324
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 325
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP00896 RELATED DB: TARGETDB
DBREF 3GA7 A 1 323 UNP Q8ZRA1 AES_SALTY 1 323
SEQADV 3GA7 SER A -2 UNP Q8ZRA1 EXPRESSION TAG
SEQADV 3GA7 ASN A -1 UNP Q8ZRA1 EXPRESSION TAG
SEQADV 3GA7 ALA A 0 UNP Q8ZRA1 EXPRESSION TAG
SEQRES 1 A 326 SER ASN ALA MSE LYS PRO GLU ASN LYS ILE PRO VAL LEU
SEQRES 2 A 326 THR ARG LEU SER ASP GLU MSE THR ALA VAL VAL ASN PHE
SEQRES 3 A 326 GLN GLN PRO GLY LEU PRO PRO TRP PRO ALA ASP GLY ASP
SEQRES 4 A 326 ILE GLU THR GLN ARG GLN TYR TYR LEU LEU GLU ARG ARG
SEQRES 5 A 326 PHE TRP ASN ALA ASP ALA PRO SER MSE THR THR ARG THR
SEQRES 6 A 326 CYS ALA VAL PRO THR PRO TYR GLY ASP VAL THR THR ARG
SEQRES 7 A 326 LEU TYR SER PRO GLN PRO THR SER GLN ALA THR LEU TYR
SEQRES 8 A 326 TYR LEU HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP
SEQRES 9 A 326 THR HIS ASP ARG ILE MSE ARG LEU LEU ALA ARG TYR THR
SEQRES 10 A 326 GLY CYS THR VAL ILE GLY ILE ASP TYR SER LEU SER PRO
SEQRES 11 A 326 GLN ALA ARG TYR PRO GLN ALA ILE GLU GLU THR VAL ALA
SEQRES 12 A 326 VAL CYS SER TYR PHE SER GLN HIS ALA ASP GLU TYR SER
SEQRES 13 A 326 LEU ASN VAL GLU LYS ILE GLY PHE ALA GLY ASP SEP ALA
SEQRES 14 A 326 GLY ALA MSE LEU ALA LEU ALA SER ALA LEU TRP LEU ARG
SEQRES 15 A 326 ASP LYS HIS ILE ARG CYS GLY ASN VAL ILE ALA ILE LEU
SEQRES 16 A 326 LEU TRP TYR GLY LEU TYR GLY LEU GLN ASP SER VAL SER
SEQRES 17 A 326 ARG ARG LEU PHE GLY GLY ALA TRP ASP GLY LEU THR ARG
SEQRES 18 A 326 GLU ASP LEU ASP MSE TYR GLU LYS ALA TYR LEU ARG ASN
SEQRES 19 A 326 ASP GLU ASP ARG GLU SER PRO TRP TYR CYS LEU PHE ASN
SEQRES 20 A 326 ASN ASP LEU THR ARG ASP VAL PRO PRO CYS PHE ILE ALA
SEQRES 21 A 326 SER ALA GLU PHE ASP PRO LEU ILE ASP ASP SER ARG LEU
SEQRES 22 A 326 LEU HIS GLN THR LEU GLN ALA HIS GLN GLN PRO CYS GLU
SEQRES 23 A 326 TYR LYS MSE TYR PRO GLY THR LEU HIS ALA PHE LEU HIS
SEQRES 24 A 326 TYR SER ARG MSE MSE THR ILE ALA ASP ASP ALA LEU GLN
SEQRES 25 A 326 ASP GLY ALA ARG PHE PHE MSE ALA ARG MSE LYS THR PRO
SEQRES 26 A 326 ARG
MODRES 3GA7 MSE A 17 MET SELENOMETHIONINE
MODRES 3GA7 MSE A 58 MET SELENOMETHIONINE
MODRES 3GA7 MSE A 107 MET SELENOMETHIONINE
MODRES 3GA7 SEP A 165 SER PHOSPHOSERINE
MODRES 3GA7 MSE A 169 MET SELENOMETHIONINE
MODRES 3GA7 MSE A 223 MET SELENOMETHIONINE
MODRES 3GA7 MSE A 286 MET SELENOMETHIONINE
MODRES 3GA7 MSE A 300 MET SELENOMETHIONINE
MODRES 3GA7 MSE A 301 MET SELENOMETHIONINE
MODRES 3GA7 MSE A 316 MET SELENOMETHIONINE
MODRES 3GA7 MSE A 319 MET SELENOMETHIONINE
HET MSE A 17 8
HET MSE A 58 8
HET MSE A 107 8
HET SEP A 165 10
HET MSE A 169 16
HET MSE A 223 8
HET MSE A 286 16
HET MSE A 300 16
HET MSE A 301 8
HET MSE A 316 16
HET MSE A 319 16
HET CL A 324 1
HET CL A 325 1
HETNAM MSE SELENOMETHIONINE
HETNAM SEP PHOSPHOSERINE
HETNAM CL CHLORIDE ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 CL 2(CL 1-)
FORMUL 4 HOH *472(H2 O)
HELIX 1 1 VAL A 9 LEU A 13 5 5
HELIX 2 2 SER A 14 GLN A 24 1 11
HELIX 3 3 ASP A 36 ASN A 52 1 17
HELIX 4 4 HIS A 103 GLY A 115 1 13
HELIX 5 5 PRO A 132 HIS A 148 1 17
HELIX 6 6 SEP A 165 HIS A 182 1 18
HELIX 7 7 SER A 203 PHE A 209 1 7
HELIX 8 8 THR A 217 LEU A 229 1 13
HELIX 9 9 ASN A 231 SER A 237 5 7
HELIX 10 10 CYS A 241 ASN A 245 5 5
HELIX 11 11 LEU A 264 HIS A 278 1 15
HELIX 12 12 ALA A 293 SER A 298 5 6
HELIX 13 13 MSE A 301 THR A 321 1 21
SHEET 1 A 8 THR A 59 VAL A 65 0
SHEET 2 A 8 VAL A 72 SER A 78 -1 O LEU A 76 N ARG A 61
SHEET 3 A 8 THR A 117 ILE A 121 -1 O VAL A 118 N TYR A 77
SHEET 4 A 8 THR A 86 LEU A 90 1 N LEU A 87 O ILE A 119
SHEET 5 A 8 LYS A 158 ASP A 164 1 O ALA A 162 N LEU A 90
SHEET 6 A 8 ASN A 187 TRP A 194 1 O ASN A 187 N ILE A 159
SHEET 7 A 8 CYS A 254 ALA A 259 1 O PHE A 255 N ILE A 191
SHEET 8 A 8 CYS A 282 TYR A 287 1 O GLU A 283 N ILE A 256
LINK C AGLU A 16 N MSE A 17 1555 1555 1.32
LINK C BGLU A 16 N MSE A 17 1555 1555 1.33
LINK C MSE A 17 N THR A 18 1555 1555 1.32
LINK C ASER A 57 N MSE A 58 1555 1555 1.33
LINK C BSER A 57 N MSE A 58 1555 1555 1.33
LINK C MSE A 58 N ATHR A 59 1555 1555 1.33
LINK C MSE A 58 N BTHR A 59 1555 1555 1.32
LINK C ILE A 106 N MSE A 107 1555 1555 1.32
LINK C MSE A 107 N ARG A 108 1555 1555 1.33
LINK C ASP A 164 N SEP A 165 1555 1555 1.34
LINK C SEP A 165 N ALA A 166 1555 1555 1.33
LINK C ALA A 168 N AMSE A 169 1555 1555 1.34
LINK C ALA A 168 N BMSE A 169 1555 1555 1.33
LINK C AMSE A 169 N ALEU A 170 1555 1555 1.33
LINK C BMSE A 169 N BLEU A 170 1555 1555 1.33
LINK C AASP A 222 N MSE A 223 1555 1555 1.33
LINK C BASP A 222 N MSE A 223 1555 1555 1.33
LINK C MSE A 223 N TYR A 224 1555 1555 1.33
LINK C LYS A 285 N AMSE A 286 1555 1555 1.33
LINK C LYS A 285 N BMSE A 286 1555 1555 1.33
LINK C AMSE A 286 N TYR A 287 1555 1555 1.32
LINK C BMSE A 286 N TYR A 287 1555 1555 1.33
LINK C AARG A 299 N AMSE A 300 1555 1555 1.33
LINK C BARG A 299 N BMSE A 300 1555 1555 1.33
LINK C AMSE A 300 N MSE A 301 1555 1555 1.33
LINK C BMSE A 300 N MSE A 301 1555 1555 1.33
LINK C MSE A 301 N ATHR A 302 1555 1555 1.33
LINK C MSE A 301 N BTHR A 302 1555 1555 1.33
LINK C PHE A 315 N AMSE A 316 1555 1555 1.32
LINK C PHE A 315 N BMSE A 316 1555 1555 1.33
LINK C AMSE A 316 N ALA A 317 1555 1555 1.33
LINK C BMSE A 316 N ALA A 317 1555 1555 1.33
LINK C AARG A 318 N AMSE A 319 1555 1555 1.32
LINK C BARG A 318 N BMSE A 319 1555 1555 1.33
LINK C AMSE A 319 N LYS A 320 1555 1555 1.33
LINK C BMSE A 319 N LYS A 320 1555 1555 1.33
CISPEP 1 GLN A 24 GLN A 25 0 -0.32
CISPEP 2 SER A 126 PRO A 127 0 5.59
CISPEP 3 TYR A 131 PRO A 132 0 0.35
SITE 1 AC1 3 HIS A 272 GLN A 273 HOH A 536
SITE 1 AC2 6 ARG A 41 SER A 126 PRO A 127 GLN A 128
SITE 2 AC2 6 HOH A 500 HOH A 529
CRYST1 82.747 133.207 64.139 90.00 90.00 90.00 C 2 2 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 0.012085 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015591 0.00000
TER 2886 THR A 321
MASTER 411 0 13 13 8 0 3 6 3395 1 158 26
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