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HEADER HYDROLASE 26-FEB-09 3GFF
TITLE CRYSTAL STRUCTURE OF IROE-LIKE SERINE HYDROLASE
TITLE 2 (NP_718593.1) FROM SHEWANELLA ONEIDENSIS AT 2.12 A
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IROE-LIKE SERINE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHEWANELLA ONEIDENSIS;
SOURCE 3 ORGANISM_TAXID: 70863;
SOURCE 4 GENE: NP_718593.1, SO_3025;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS NP_718593.1, IROE-LIKE SERINE HYDROLASE, STRUCTURAL
KEYWDS 2 GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,
KEYWDS 3 PROTEIN STRUCTURE INITIATIVE, PSI-2, PUTATIVE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 10-MAR-09 3GFF 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF IROE-LIKE SERINE HYDROLASE
JRNL TITL 2 (NP_718593.1) FROM SHEWANELLA ONEIDENSIS AT 2.12 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 33377
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1684
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) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2350
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE SET COUNT : 119
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5004
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 289
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.96000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : -1.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.14000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.294
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.221
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.376
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5138 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3474 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6956 ; 1.614 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8459 ; 0.990 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 634 ; 3.620 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 241 ;32.710 ;23.983
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 855 ;13.858 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;13.952 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 755 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5746 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1074 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1065 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3530 ; 0.200 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2487 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2511 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 313 ; 0.183 ; 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): 17 ; 0.189 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 42 ; 0.358 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.144 ; 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): 3246 ; 0.982 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1282 ; 0.276 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5042 ; 1.416 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2151 ; 1.007 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1912 ; 1.457 ; 3.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 10 A 328 4
REMARK 3 1 B 10 B 328 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 4151 ; 0.350 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4151 ; 0.630 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 10 A 328
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8403 62.0656 34.0691
REMARK 3 T TENSOR
REMARK 3 T11: -0.1124 T22: -0.1198
REMARK 3 T33: -0.0796 T12: 0.0063
REMARK 3 T13: -0.0091 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 1.0989 L22: 1.2772
REMARK 3 L33: 1.9076 L12: 0.0417
REMARK 3 L13: -0.4419 L23: -0.2524
REMARK 3 S TENSOR
REMARK 3 S11: -0.0250 S12: 0.0889 S13: -0.0111
REMARK 3 S21: -0.0668 S22: 0.0051 S23: -0.0211
REMARK 3 S31: 0.0598 S32: -0.0018 S33: 0.0198
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 : B 10 B 328
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6944 29.4571 34.4495
REMARK 3 T TENSOR
REMARK 3 T11: -0.0888 T22: -0.1018
REMARK 3 T33: -0.0667 T12: -0.0035
REMARK 3 T13: 0.0058 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 1.0730 L22: 1.2692
REMARK 3 L33: 1.5044 L12: -0.1103
REMARK 3 L13: 0.3422 L23: 0.4345
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: -0.0890 S13: 0.0082
REMARK 3 S21: 0.1360 S22: -0.0329 S23: 0.0254
REMARK 3 S31: -0.0146 S32: -0.0436 S33: 0.0501
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.A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 4.IMIDAZOLE (IMD) AND CHLORIDE (CL) FROM THE
REMARK 3 CRYSTALLIZATION CONDITION HAVE BEEN MODELED IN THE SOLVENT
REMARK 3 STRUCTURE. 5.RESIDUES A314 AND B314 ARE RAMACHANDRAN OUTLIERS
REMARK 3 IN A REGION OF POOR ELECTRON DENSITY. 6.THE NOMINAL RESOLUTION
REMARK 3 IS 2.25 A WITH 5447 OBSERVED REFLECTIONS BETWEEN 2.25-2.12
REMARK 3 (89.2% COMPLETE FOR THIS SHELL) INCLUDED IN THE REFINEMENT.
REMARK 4
REMARK 4 3GFF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 0.91162,0.97824,0.97864
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 : 33406
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 28.307
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15.0000% ETHANOL, 0.2000M MGCL2,
REMARK 280 0.1M IMIDAZOLE PH 8.0, NANODROP, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 62.78500
REMARK 290 SMTRY3 2 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: CRYSTAL PACKING ANALYSIS AND STATIC LIGHT SCATTERING
REMARK 300 SUPPORT THE ASSIGNMENT OF A DIMER AS THE
REMARK 300 STABLE OLIGOMERIC FORM IN SOLUTION.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 MSE A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 THR A 4
REMARK 465 SER A 5
REMARK 465 ILE A 6
REMARK 465 THR A 7
REMARK 465 ALA A 8
REMARK 465 VAL A 9
REMARK 465 SER A 271
REMARK 465 ASP A 272
REMARK 465 SER A 273
REMARK 465 LYS A 329
REMARK 465 ASP A 330
REMARK 465 GLY B 0
REMARK 465 MSE B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 THR B 4
REMARK 465 SER B 5
REMARK 465 ILE B 6
REMARK 465 THR B 7
REMARK 465 ALA B 8
REMARK 465 VAL B 9
REMARK 465 SER B 271
REMARK 465 ASP B 272
REMARK 465 SER B 273
REMARK 465 LYS B 329
REMARK 465 ASP B 330
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 ILE A 269 CG1 CG2 CD1
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 GLN A 278 CG CD OE1 NE2
REMARK 470 GLU A 302 CG CD OE1 OE2
REMARK 470 GLN A 306 CD OE1 NE2
REMARK 470 TYR A 307 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 309 CB CG OD1 OD2
REMARK 470 ARG A 310 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 GLN A 318 CG CD OE1 NE2
REMARK 470 GLU A 321 CG CD OE1 OE2
REMARK 470 ARG A 324 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 325 CG CD OE1 NE2
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 ILE B 269 CB CG1 CG2 CD1
REMARK 470 GLN B 298 CG CD OE1 NE2
REMARK 470 TYR B 307 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 309 CB CG OD1 OD2
REMARK 470 ARG B 310 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 315 CG CD OE1 OE2
REMARK 470 LYS B 317 CG CD CE NZ
REMARK 470 GLN B 318 CG CD OE1 NE2
REMARK 470 ARG B 324 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 325 CG CD OE1 NE2
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 NE2 GLN A 62 O HOH A 415 1.93
REMARK 500 O GLU B 10 O HOH B 620 2.16
REMARK 500 OG SER B 162 O HOH B 619 2.17
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 25 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 115 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 115 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 25 NE - CZ - NH2 ANGL. DEV. = -3.4 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 83 -81.65 -120.86
REMARK 500 GLU A 123 -61.37 -122.31
REMARK 500 SER A 144 -130.04 60.45
REMARK 500 SER A 212 139.71 -171.65
REMARK 500 ILE A 269 31.07 -81.45
REMARK 500 THR A 314 -146.52 35.41
REMARK 500 THR B 83 -78.55 -116.16
REMARK 500 GLU B 123 -59.53 -122.71
REMARK 500 SER B 144 -125.58 61.17
REMARK 500 ASN B 202 55.15 -112.55
REMARK 500 ALA B 230 63.82 35.69
REMARK 500 ILE B 269 2.29 -60.47
REMARK 500 GLN B 312 19.68 47.62
REMARK 500 LEU B 313 98.36 -63.76
REMARK 500 THR B 314 -166.50 40.03
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 331
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 331
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 332
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 332
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 379975 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS 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 3GFF A 1 330 UNP Q8ECU8 Q8ECU8_SHEON 1 330
DBREF 3GFF B 1 330 UNP Q8ECU8 Q8ECU8_SHEON 1 330
SEQADV 3GFF GLY A 0 UNP Q8ECU8 LEADER SEQUENCE
SEQADV 3GFF GLY B 0 UNP Q8ECU8 LEADER SEQUENCE
SEQRES 1 A 331 GLY MSE THR SER THR SER ILE THR ALA VAL GLU TYR GLN
SEQRES 2 A 331 SER LYS ARG LEU GLU SER ARG LEU LEU LYS GLU THR ARG
SEQRES 3 A 331 GLU TYR VAL ILE ALA LEU PRO GLU GLY TYR ALA GLN SER
SEQRES 4 A 331 LEU GLU ALA TYR PRO VAL VAL TYR LEU LEU ASP GLY GLU
SEQRES 5 A 331 ASP GLN PHE ASP HIS MSE ALA SER LEU LEU GLN PHE LEU
SEQRES 6 A 331 SER GLN GLY THR MSE PRO GLN ILE PRO LYS VAL ILE ILE
SEQRES 7 A 331 VAL GLY ILE HIS ASN THR ASN ARG MSE ARG ASP TYR THR
SEQRES 8 A 331 PRO THR HIS THR LEU VAL LEU PRO SER GLY ASN LYS GLY
SEQRES 9 A 331 ASN PRO GLN TYR GLN HIS THR GLY GLY ALA GLY ARG PHE
SEQRES 10 A 331 LEU ASP PHE ILE GLU LYS GLU LEU ALA PRO SER ILE GLU
SEQRES 11 A 331 SER GLN LEU ARG THR ASN GLY ILE ASN VAL LEU VAL GLY
SEQRES 12 A 331 HIS SER PHE GLY GLY LEU VAL ALA MSE GLU ALA LEU ARG
SEQRES 13 A 331 THR ASP ARG PRO LEU PHE SER ALA TYR LEU ALA LEU ASP
SEQRES 14 A 331 THR SER LEU TRP PHE ASP SER PRO HIS TYR LEU THR LEU
SEQRES 15 A 331 LEU GLU GLU ARG VAL VAL LYS GLY ASP PHE LYS GLN LYS
SEQRES 16 A 331 GLN LEU PHE MSE ALA ILE ALA ASN ASN PRO LEU SER PRO
SEQRES 17 A 331 GLY PHE GLY VAL SER SER TYR HIS LYS ASP LEU ASN LEU
SEQRES 18 A 331 ALA PHE ALA ASP LYS LEU THR LYS LEU ALA PRO LYS GLY
SEQRES 19 A 331 LEU GLY PHE MSE ALA LYS TYR TYR PRO GLU GLU THR HIS
SEQRES 20 A 331 GLN SER VAL SER HIS ILE GLY LEU TYR ASP GLY ILE ARG
SEQRES 21 A 331 HIS LEU PHE LYS ASP PHE ALA ILE ASP ILE TYR SER ASP
SEQRES 22 A 331 SER PHE SER LYS GLN GLN VAL ILE ASP GLN TYR GLY VAL
SEQRES 23 A 331 LEU SER GLU ARG PHE GLY HIS LYS VAL THR PRO SER GLN
SEQRES 24 A 331 GLN TYR LEU GLU GLN LEU ILE GLN TYR SER ASP ARG GLN
SEQRES 25 A 331 GLN LEU THR GLU ARG LYS GLN MSE LEU GLU GLY LEU ARG
SEQRES 26 A 331 GLN HIS PHE ALA LYS ASP
SEQRES 1 B 331 GLY MSE THR SER THR SER ILE THR ALA VAL GLU TYR GLN
SEQRES 2 B 331 SER LYS ARG LEU GLU SER ARG LEU LEU LYS GLU THR ARG
SEQRES 3 B 331 GLU TYR VAL ILE ALA LEU PRO GLU GLY TYR ALA GLN SER
SEQRES 4 B 331 LEU GLU ALA TYR PRO VAL VAL TYR LEU LEU ASP GLY GLU
SEQRES 5 B 331 ASP GLN PHE ASP HIS MSE ALA SER LEU LEU GLN PHE LEU
SEQRES 6 B 331 SER GLN GLY THR MSE PRO GLN ILE PRO LYS VAL ILE ILE
SEQRES 7 B 331 VAL GLY ILE HIS ASN THR ASN ARG MSE ARG ASP TYR THR
SEQRES 8 B 331 PRO THR HIS THR LEU VAL LEU PRO SER GLY ASN LYS GLY
SEQRES 9 B 331 ASN PRO GLN TYR GLN HIS THR GLY GLY ALA GLY ARG PHE
SEQRES 10 B 331 LEU ASP PHE ILE GLU LYS GLU LEU ALA PRO SER ILE GLU
SEQRES 11 B 331 SER GLN LEU ARG THR ASN GLY ILE ASN VAL LEU VAL GLY
SEQRES 12 B 331 HIS SER PHE GLY GLY LEU VAL ALA MSE GLU ALA LEU ARG
SEQRES 13 B 331 THR ASP ARG PRO LEU PHE SER ALA TYR LEU ALA LEU ASP
SEQRES 14 B 331 THR SER LEU TRP PHE ASP SER PRO HIS TYR LEU THR LEU
SEQRES 15 B 331 LEU GLU GLU ARG VAL VAL LYS GLY ASP PHE LYS GLN LYS
SEQRES 16 B 331 GLN LEU PHE MSE ALA ILE ALA ASN ASN PRO LEU SER PRO
SEQRES 17 B 331 GLY PHE GLY VAL SER SER TYR HIS LYS ASP LEU ASN LEU
SEQRES 18 B 331 ALA PHE ALA ASP LYS LEU THR LYS LEU ALA PRO LYS GLY
SEQRES 19 B 331 LEU GLY PHE MSE ALA LYS TYR TYR PRO GLU GLU THR HIS
SEQRES 20 B 331 GLN SER VAL SER HIS ILE GLY LEU TYR ASP GLY ILE ARG
SEQRES 21 B 331 HIS LEU PHE LYS ASP PHE ALA ILE ASP ILE TYR SER ASP
SEQRES 22 B 331 SER PHE SER LYS GLN GLN VAL ILE ASP GLN TYR GLY VAL
SEQRES 23 B 331 LEU SER GLU ARG PHE GLY HIS LYS VAL THR PRO SER GLN
SEQRES 24 B 331 GLN TYR LEU GLU GLN LEU ILE GLN TYR SER ASP ARG GLN
SEQRES 25 B 331 GLN LEU THR GLU ARG LYS GLN MSE LEU GLU GLY LEU ARG
SEQRES 26 B 331 GLN HIS PHE ALA LYS ASP
MODRES 3GFF MSE A 57 MET SELENOMETHIONINE
MODRES 3GFF MSE A 69 MET SELENOMETHIONINE
MODRES 3GFF MSE A 86 MET SELENOMETHIONINE
MODRES 3GFF MSE A 151 MET SELENOMETHIONINE
MODRES 3GFF MSE A 198 MET SELENOMETHIONINE
MODRES 3GFF MSE A 237 MET SELENOMETHIONINE
MODRES 3GFF MSE A 319 MET SELENOMETHIONINE
MODRES 3GFF MSE B 57 MET SELENOMETHIONINE
MODRES 3GFF MSE B 69 MET SELENOMETHIONINE
MODRES 3GFF MSE B 86 MET SELENOMETHIONINE
MODRES 3GFF MSE B 151 MET SELENOMETHIONINE
MODRES 3GFF MSE B 198 MET SELENOMETHIONINE
MODRES 3GFF MSE B 237 MET SELENOMETHIONINE
MODRES 3GFF MSE B 319 MET SELENOMETHIONINE
HET MSE A 57 8
HET MSE A 69 8
HET MSE A 86 8
HET MSE A 151 8
HET MSE A 198 8
HET MSE A 237 8
HET MSE A 319 8
HET MSE B 57 8
HET MSE B 69 8
HET MSE B 86 8
HET MSE B 151 8
HET MSE B 198 8
HET MSE B 237 8
HET MSE B 319 8
HET CL A 331 1
HET CL B 331 1
HET IMD A 332 5
HET IMD B 332 5
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM IMD IMIDAZOLE
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 3 CL 2(CL 1-)
FORMUL 5 IMD 2(C3 H5 N2 1+)
FORMUL 7 HOH *289(H2 O)
HELIX 1 1 GLY A 34 SER A 38 5 5
HELIX 2 2 ASP A 49 SER A 65 1 17
HELIX 3 3 ASN A 84 TYR A 89 1 6
HELIX 4 4 ASN A 104 THR A 110 5 7
HELIX 5 5 GLY A 112 GLU A 123 1 12
HELIX 6 6 GLU A 123 LEU A 132 1 10
HELIX 7 7 PHE A 145 THR A 156 1 12
HELIX 8 8 PRO A 176 GLY A 189 1 14
HELIX 9 9 SER A 213 ALA A 230 1 18
HELIX 10 10 SER A 248 LYS A 263 1 16
HELIX 11 11 ASP A 264 ALA A 266 5 3
HELIX 12 12 SER A 275 GLY A 291 1 17
HELIX 13 13 SER A 297 GLN A 311 1 15
HELIX 14 14 GLU A 315 PHE A 327 1 13
HELIX 15 15 GLY B 34 SER B 38 5 5
HELIX 16 16 ASP B 49 GLN B 66 1 18
HELIX 17 17 ASN B 84 TYR B 89 1 6
HELIX 18 18 ASN B 104 THR B 110 5 7
HELIX 19 19 GLY B 112 GLU B 123 1 12
HELIX 20 20 GLU B 123 LEU B 132 1 10
HELIX 21 21 PHE B 145 THR B 156 1 12
HELIX 22 22 PRO B 176 GLY B 189 1 14
HELIX 23 23 SER B 213 ALA B 230 1 18
HELIX 24 24 SER B 248 PHE B 262 1 15
HELIX 25 25 LYS B 263 ALA B 266 5 4
HELIX 26 26 SER B 275 GLY B 291 1 17
HELIX 27 27 SER B 297 GLN B 311 1 15
HELIX 28 28 LEU B 313 PHE B 327 1 15
SHEET 1 A 8 GLN A 12 SER A 18 0
SHEET 2 A 8 GLU A 23 ALA A 30 -1 O TYR A 27 N LYS A 14
SHEET 3 A 8 ILE A 76 ILE A 80 -1 O GLY A 79 N VAL A 28
SHEET 4 A 8 TYR A 42 LEU A 47 1 N LEU A 47 O VAL A 78
SHEET 5 A 8 THR A 134 HIS A 143 1 O VAL A 139 N TYR A 46
SHEET 6 A 8 ALA A 163 LEU A 167 1 O LEU A 167 N GLY A 142
SHEET 7 A 8 LYS A 194 ILE A 200 1 O PHE A 197 N ALA A 166
SHEET 8 A 8 LEU A 234 TYR A 240 1 O GLY A 235 N LYS A 194
SHEET 1 B 2 LEU A 205 SER A 206 0
SHEET 2 B 2 GLY A 210 VAL A 211 -1 O GLY A 210 N SER A 206
SHEET 1 C 8 TYR B 11 SER B 18 0
SHEET 2 C 8 GLU B 23 ALA B 30 -1 O TYR B 27 N LYS B 14
SHEET 3 C 8 ILE B 76 ILE B 80 -1 O GLY B 79 N VAL B 28
SHEET 4 C 8 TYR B 42 LEU B 47 1 N LEU B 47 O VAL B 78
SHEET 5 C 8 THR B 134 HIS B 143 1 O VAL B 139 N TYR B 46
SHEET 6 C 8 ALA B 163 LEU B 167 1 O LEU B 167 N GLY B 142
SHEET 7 C 8 LYS B 194 ALA B 201 1 O PHE B 197 N ALA B 166
SHEET 8 C 8 LEU B 234 TYR B 241 1 O GLY B 235 N LEU B 196
SHEET 1 D 2 LEU B 205 SER B 206 0
SHEET 2 D 2 GLY B 210 VAL B 211 -1 O GLY B 210 N SER B 206
LINK C HIS A 56 N MSE A 57 1555 1555 1.33
LINK C MSE A 57 N ALA A 58 1555 1555 1.34
LINK C THR A 68 N MSE A 69 1555 1555 1.34
LINK C MSE A 69 N PRO A 70 1555 1555 1.36
LINK C ARG A 85 N MSE A 86 1555 1555 1.33
LINK C MSE A 86 N ARG A 87 1555 1555 1.31
LINK C ALA A 150 N MSE A 151 1555 1555 1.34
LINK C MSE A 151 N GLU A 152 1555 1555 1.34
LINK C PHE A 197 N MSE A 198 1555 1555 1.33
LINK C MSE A 198 N ALA A 199 1555 1555 1.33
LINK C PHE A 236 N MSE A 237 1555 1555 1.31
LINK C MSE A 237 N ALA A 238 1555 1555 1.33
LINK C GLN A 318 N MSE A 319 1555 1555 1.34
LINK C MSE A 319 N LEU A 320 1555 1555 1.33
LINK C HIS B 56 N MSE B 57 1555 1555 1.33
LINK C MSE B 57 N ALA B 58 1555 1555 1.33
LINK C THR B 68 N MSE B 69 1555 1555 1.33
LINK C MSE B 69 N PRO B 70 1555 1555 1.34
LINK C ARG B 85 N MSE B 86 1555 1555 1.32
LINK C MSE B 86 N ARG B 87 1555 1555 1.33
LINK C ALA B 150 N MSE B 151 1555 1555 1.33
LINK C MSE B 151 N GLU B 152 1555 1555 1.32
LINK C PHE B 197 N MSE B 198 1555 1555 1.32
LINK C MSE B 198 N ALA B 199 1555 1555 1.32
LINK C PHE B 236 N MSE B 237 1555 1555 1.33
LINK C MSE B 237 N ALA B 238 1555 1555 1.33
LINK C GLN B 318 N MSE B 319 1555 1555 1.33
LINK C MSE B 319 N LEU B 320 1555 1555 1.33
CISPEP 1 SER A 175 PRO A 176 0 4.47
CISPEP 2 SER B 175 PRO B 176 0 2.58
SITE 1 AC1 3 ARG A 185 PHE A 191 LYS A 192
SITE 1 AC2 3 ASP B 157 LYS B 192 HOH B 349
SITE 1 AC3 5 SER A 144 SER A 170 TRP A 172 PRO A 207
SITE 2 AC3 5 HIS A 246
SITE 1 AC4 5 SER B 170 TRP B 172 PRO B 207 HIS B 215
SITE 2 AC4 5 HIS B 246
CRYST1 53.650 125.570 56.750 90.00 117.94 90.00 P 1 21 1 4
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 0.018639 0.000000 0.009884 0.00000
SCALE2 0.000000 0.007964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019946 0.00000
TER 2490 ALA A 328
TER 5006 ALA B 328
MASTER 444 0 18 28 20 0 6 6 5305 2 150 52
END |