HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 29-AUG-07 2R39
TITLE CRYSTAL STRUCTURE OF FIXG-RELATED PROTEIN FROM VIBRIO PARAHAEMOLYTICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIXG-RELATED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 373-487;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO PARAHAEMOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 223926;
SOURCE 4 STRAIN: RIMD 2210633;
SOURCE 5 GENE: VP3052;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) DERIVATIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS FIXG-RELATED PROTEIN, VIBRIO PARAHAEMOLYTICUS, STRUCTURAL GENOMICS,
KEYWDS 2 PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, IRON, IRON-SULFUR, METAL-BINDING, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,L.BIGELOW,J.ABDULLAH,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 3 13-JUL-11 2R39 1 VERSN
REVDAT 2 24-FEB-09 2R39 1 VERSN
REVDAT 1 11-SEP-07 2R39 0
JRNL AUTH C.CHANG,L.BIGELOW,J.ABDULLAH,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF FIXG-RELATED PROTEIN FROM VIBRIO
JRNL TITL 2 PARAHAEMOLYTICUS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.02 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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 9899
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 498
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) : 2.02
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 458
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.1880
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.2370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 862
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 40.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.99000
REMARK 3 B22 (A**2) : -0.99000
REMARK 3 B33 (A**2) : 1.48000
REMARK 3 B12 (A**2) : -0.49000
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): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.758
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 873 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1181 ; 1.326 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 107 ; 6.986 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 41 ;36.686 ;26.098
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 162 ;12.451 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;16.040 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 139 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 646 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 360 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 594 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 63 ; 0.159 ; 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): 36 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.181 ; 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): 560 ; 0.950 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 882 ; 1.368 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 353 ; 1.976 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 299 ; 3.013 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 378 A 389
REMARK 3 RESIDUE RANGE : A 398 A 413
REMARK 3 RESIDUE RANGE : A 441 A 447
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4418 28.8771 -13.3935
REMARK 3 T TENSOR
REMARK 3 T11: -0.0219 T22: 0.0210
REMARK 3 T33: -0.0723 T12: 0.1357
REMARK 3 T13: -0.0816 T23: -0.1451
REMARK 3 L TENSOR
REMARK 3 L11: 10.8218 L22: 1.3628
REMARK 3 L33: 5.4103 L12: -1.8774
REMARK 3 L13: -3.9118 L23: -0.9125
REMARK 3 S TENSOR
REMARK 3 S11: 0.4238 S12: 1.1145 S13: -0.8985
REMARK 3 S21: -0.6121 S22: -0.5193 S23: 0.3259
REMARK 3 S31: 0.4760 S32: 0.1656 S33: 0.0954
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 414 A 440
REMARK 3 RESIDUE RANGE : A 448 A 487
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3958 32.8278 -5.0235
REMARK 3 T TENSOR
REMARK 3 T11: -0.1872 T22: -0.1685
REMARK 3 T33: -0.1667 T12: 0.0337
REMARK 3 T13: -0.0117 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 5.9570 L22: 2.4233
REMARK 3 L33: 2.3969 L12: -2.6153
REMARK 3 L13: 0.1360 L23: -0.6834
REMARK 3 S TENSOR
REMARK 3 S11: 0.2377 S12: 0.0957 S13: -0.2813
REMARK 3 S21: -0.1821 S22: -0.1377 S23: 0.1003
REMARK 3 S31: 0.2441 S32: 0.1643 S33: -0.1000
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2R39 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-07.
REMARK 100 THE RCSB ID CODE IS RCSB044369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-07
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 : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97891
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10403
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 10.100
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 50.5300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.50
REMARK 200 R MERGE FOR SHELL (I) : 0.27300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES PH 7.5, 30% PEG 400, NACL, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 537 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 528 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 370
REMARK 465 ASN A 371
REMARK 465 ALA A 372
REMARK 465 GLN A 373
REMARK 465 ILE A 374
REMARK 465 ALA A 375
REMARK 465 ALA A 376
REMARK 465 ASN A 395
REMARK 465 SER A 396
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 ASN A 389 CG OD1
REMARK 470 VAL A 394 CG1 CG2
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 392 29.82 48.34
REMARK 500 ARG A 393 81.62 -52.13
REMARK 500 SER A 481 -159.23 -148.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC91026.1 RELATED DB: TARGETDB
DBREF 2R39 A 373 487 UNP Q87KC5 Q87KC5_VIBPA 373 487
SEQADV 2R39 SER A 370 UNP Q87KC5 EXPRESSION TAG
SEQADV 2R39 ASN A 371 UNP Q87KC5 EXPRESSION TAG
SEQADV 2R39 ALA A 372 UNP Q87KC5 EXPRESSION TAG
SEQRES 1 A 118 SER ASN ALA GLN ILE ALA ALA VAL ASP PRO ALA GLY MSE
SEQRES 2 A 118 SER VAL ILE ARG ASP ARG ASN GLN LEU PHE ARG VAL ASN
SEQRES 3 A 118 SER ALA GLY GLU VAL GLU ASN THR TYR THR LEU LYS VAL
SEQRES 4 A 118 ILE ASN LYS THR GLN GLN VAL GLN GLU TYR ASN LEU ASP
SEQRES 5 A 118 VAL LYS GLY LEU ASN ASP VAL SER TRP TYR GLY LYS GLN
SEQRES 6 A 118 THR ILE GLN VAL GLU PRO GLY GLU VAL LEU ASN LEU PRO
SEQRES 7 A 118 MSE SER LEU GLY ALA ASP PRO ASP LYS LEU ASN SER ALA
SEQRES 8 A 118 ILE THR THR ILE GLN PHE ILE LEU THR ASP LYS SER ASN
SEQRES 9 A 118 GLU PHE THR ILE GLU VAL GLU SER ARG PHE ILE LYS LYS
SEQRES 10 A 118 LEU
MODRES 2R39 MSE A 382 MET SELENOMETHIONINE
MODRES 2R39 MSE A 448 MET SELENOMETHIONINE
HET MSE A 382 8
HET MSE A 448 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 HOH *47(H2 O)
HELIX 1 1 ASP A 453 LEU A 457 5 5
HELIX 2 2 LYS A 471 GLU A 474 5 4
SHEET 1 A 4 ALA A 380 ARG A 386 0
SHEET 2 A 4 VAL A 400 ASN A 410 -1 O LYS A 407 N SER A 383
SHEET 3 A 4 VAL A 443 ALA A 452 -1 O LEU A 446 N LEU A 406
SHEET 4 A 4 SER A 429 TYR A 431 -1 N SER A 429 O GLY A 451
SHEET 1 B 4 THR A 435 VAL A 438 0
SHEET 2 B 4 GLN A 416 LYS A 423 -1 N GLN A 416 O VAL A 438
SHEET 3 B 4 ILE A 461 ASP A 470 -1 O THR A 469 N ASN A 419
SHEET 4 B 4 PHE A 475 ILE A 484 -1 O PHE A 483 N THR A 462
LINK C GLY A 381 N MSE A 382 1555 1555 1.33
LINK C MSE A 382 N SER A 383 1555 1555 1.32
LINK C PRO A 447 N MSE A 448 1555 1555 1.33
LINK C MSE A 448 N SER A 449 1555 1555 1.33
CRYST1 74.567 74.567 49.360 90.00 90.00 120.00 P 3 2 1 6
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 0.013411 0.007743 0.000000 0.00000
SCALE2 0.000000 0.015485 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020259 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
