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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 13-JUL-07 2QM0
TITLE CRYSTAL STRUCTURE OF IROE PROTEIN FROM BACILLUS CEREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IROE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS ATCC 14579;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: DSM 31;
SOURCE 5 GENE: BC_3734;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ALPHA-BETA STRUCTURE, STRUCTURAL GENOMICS, PSI-2, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,N.MALTSEVA,A.ZAWADZKA,D.HOLZLE,A.JOACHIMIAK,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 31-JUL-07 2QM0 0
JRNL AUTH Y.KIM,N.MALTSEVA,A.ZAWADZKA,D.HOLZLE,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF IROE FROM BACILLUS CEREUS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.84 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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 49733
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5567
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2334
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 245
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4991
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54000
REMARK 3 B22 (A**2) : -1.59000
REMARK 3 B33 (A**2) : 2.12000
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): 0.146
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.882
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4576 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6211 ; 1.788 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 559 ; 6.113 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 213 ;42.806 ;25.070
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 799 ;16.100 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;13.521 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 658 ; 0.268 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3472 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2330 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3095 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 461 ; 0.172 ; 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): 53 ; 0.308 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.185 ; 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): 2838 ; 0.936 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4445 ; 1.478 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2009 ; 2.358 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1766 ; 3.602 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: NULL
REMARK 4
REMARK 4 2QM0 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB043766.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930, 0.97950
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55348
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 45.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09900
REMARK 200 FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49900
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: HKL-3000, SHELXD, SHELXE, MLPHARE, DM, SOLVE/
REMARK 200 RESOLVE, CCP4, 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 (%): 53.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 0.1 M
REMARK 280 SODIUM CACODYLATE PH 6.5, 0.2 M NACL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 289K
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,1/2+Z
REMARK 290 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 1/2+X,1/2-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 -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 100.43650
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 100.43650
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 24.42450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 67.52900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.42450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 67.52900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 100.43650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.42450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 67.52900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 100.43650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.42450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 67.52900
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 AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS PROTEIN
REMARK 300 IS UNKNOWN. SEE REMARK 350 FOR THE PROGRAM GENERATED
REMARK 300 ASSEMBLY INFORMATION FOR THE STRUCTURE IN THIS ENTRY.
REMARK 300 THE REMARK MAY ALSO PROVIDE INFORMATION ON BURIED
REMARK 300 SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 5570/22760 ANGSTROM**2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 13210/43450 ANGSTROM**2
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 48.84900
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 100.43650
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 831 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 840 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 ASP A 109
REMARK 465 ALA A 110
REMARK 465 PRO A 111
REMARK 465 LEU A 112
REMARK 465 LYS A 113
REMARK 465 PRO A 114
REMARK 465 ASP A 115
REMARK 465 GLY A 116
REMARK 465 LYS A 117
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 THR B 4
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
REMARK 500 CB MSE B 223 O3 SO4 B 605 2.11
REMARK 500 O HOH A 831 O HOH A 838 2.11
REMARK 500 O HOH A 835 O HOH A 870 2.14
REMARK 500 O HOH B 643 O HOH B 853 2.14
REMARK 500 OE1 GLU A 232 O HOH A 866 2.17
REMARK 500 O HOH B 757 O HOH B 862 2.19
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 M RES CSSEQI PSI PHI
REMARK 500 ARG A 70 61.99 -111.80
REMARK 500 SER A 107 171.03 -48.31
REMARK 500 GLU A 135 -57.58 -123.54
REMARK 500 SVY A 157 -135.63 84.69
REMARK 500 SER A 181 56.81 32.62
REMARK 500 SVY B 157 -133.90 80.11
REMARK 500 ASN B 170 45.62 -148.49
REMARK 500 SER B 181 53.67 39.94
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 A 819 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH A 826 DISTANCE = 7.55 ANGSTROMS
REMARK 525 HOH A 831 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A 832 DISTANCE = 8.05 ANGSTROMS
REMARK 525 HOH A 838 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 7.79 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 DIISOPROPYLPHOSPHONO GROUP IS COVALENTLY BOUND
REMARK 600 TO SERINE 157
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC26071 RELATED DB: TARGETDB
DBREF 2QM0 A 1 272 UNP Q81A57 Q81A57_BACCR 1 272
DBREF 2QM0 B 1 272 UNP Q81A57 Q81A57_BACCR 1 272
SEQADV 2QM0 SER A -2 UNP Q81A57 CLONING ARTIFACT
SEQADV 2QM0 ASN A -1 UNP Q81A57 CLONING ARTIFACT
SEQADV 2QM0 ALA A 0 UNP Q81A57 CLONING ARTIFACT
SEQADV 2QM0 MSE A 1 UNP Q81A57 MET 1 MODIFIED RESIDUE
SEQADV 2QM0 MSE A 20 UNP Q81A57 MET 20 MODIFIED RESIDUE
SEQADV 2QM0 SVY A 157 UNP Q81A57 SER 157 MODIFIED RESIDUE
SEQADV 2QM0 MSE A 223 UNP Q81A57 MET 223 MODIFIED RESIDUE
SEQADV 2QM0 SER B -2 UNP Q81A57 CLONING ARTIFACT
SEQADV 2QM0 ASN B -1 UNP Q81A57 CLONING ARTIFACT
SEQADV 2QM0 ALA B 0 UNP Q81A57 CLONING ARTIFACT
SEQADV 2QM0 MSE B 1 UNP Q81A57 MET 1 MODIFIED RESIDUE
SEQADV 2QM0 MSE B 20 UNP Q81A57 MET 20 MODIFIED RESIDUE
SEQADV 2QM0 SVY B 157 UNP Q81A57 SER 157 MODIFIED RESIDUE
SEQADV 2QM0 MSE B 223 UNP Q81A57 MET 223 MODIFIED RESIDUE
SEQRES 1 A 275 SER ASN ALA MSE ASN THR THR VAL GLU LYS GLN GLN ILE
SEQRES 2 A 275 ILE THR SER ASN THR GLU GLN TRP LYS MSE TYR SER LYS
SEQRES 3 A 275 LEU GLU GLY LYS GLU TYR GLN ILE HIS ILE SER LYS PRO
SEQRES 4 A 275 LYS GLN PRO ALA PRO ASP SER GLY TYR PRO VAL ILE TYR
SEQRES 5 A 275 VAL LEU ASP GLY ASN ALA PHE PHE GLN THR PHE HIS GLU
SEQRES 6 A 275 ALA VAL LYS ILE GLN SER VAL ARG ALA GLU LYS THR GLY
SEQRES 7 A 275 VAL SER PRO ALA ILE ILE VAL GLY VAL GLY TYR PRO ILE
SEQRES 8 A 275 GLU GLY ALA PHE SER GLY GLU GLU ARG CYS TYR ASP PHE
SEQRES 9 A 275 THR PRO SER VAL ILE SER LYS ASP ALA PRO LEU LYS PRO
SEQRES 10 A 275 ASP GLY LYS PRO TRP PRO LYS THR GLY GLY ALA HIS ASN
SEQRES 11 A 275 PHE PHE THR PHE ILE GLU GLU GLU LEU LYS PRO GLN ILE
SEQRES 12 A 275 GLU LYS ASN PHE GLU ILE ASP LYS GLY LYS GLN THR LEU
SEQRES 13 A 275 PHE GLY HIS SVY LEU GLY GLY LEU PHE ALA LEU HIS ILE
SEQRES 14 A 275 LEU PHE THR ASN LEU ASN ALA PHE GLN ASN TYR PHE ILE
SEQRES 15 A 275 SER SER PRO SER ILE TRP TRP ASN ASN LYS SER VAL LEU
SEQRES 16 A 275 GLU LYS GLU GLU ASN LEU ILE ILE GLU LEU ASN ASN ALA
SEQRES 17 A 275 LYS PHE GLU THR GLY VAL PHE LEU THR VAL GLY SER LEU
SEQRES 18 A 275 GLU ARG GLU HIS MSE VAL VAL GLY ALA ASN GLU LEU SER
SEQRES 19 A 275 GLU ARG LEU LEU GLN VAL ASN HIS ASP LYS LEU LYS PHE
SEQRES 20 A 275 LYS PHE TYR GLU ALA GLU GLY GLU ASN HIS ALA SER VAL
SEQRES 21 A 275 VAL PRO THR SER LEU SER LYS GLY LEU ARG PHE ILE SER
SEQRES 22 A 275 TYR VAL
SEQRES 1 B 275 SER ASN ALA MSE ASN THR THR VAL GLU LYS GLN GLN ILE
SEQRES 2 B 275 ILE THR SER ASN THR GLU GLN TRP LYS MSE TYR SER LYS
SEQRES 3 B 275 LEU GLU GLY LYS GLU TYR GLN ILE HIS ILE SER LYS PRO
SEQRES 4 B 275 LYS GLN PRO ALA PRO ASP SER GLY TYR PRO VAL ILE TYR
SEQRES 5 B 275 VAL LEU ASP GLY ASN ALA PHE PHE GLN THR PHE HIS GLU
SEQRES 6 B 275 ALA VAL LYS ILE GLN SER VAL ARG ALA GLU LYS THR GLY
SEQRES 7 B 275 VAL SER PRO ALA ILE ILE VAL GLY VAL GLY TYR PRO ILE
SEQRES 8 B 275 GLU GLY ALA PHE SER GLY GLU GLU ARG CYS TYR ASP PHE
SEQRES 9 B 275 THR PRO SER VAL ILE SER LYS ASP ALA PRO LEU LYS PRO
SEQRES 10 B 275 ASP GLY LYS PRO TRP PRO LYS THR GLY GLY ALA HIS ASN
SEQRES 11 B 275 PHE PHE THR PHE ILE GLU GLU GLU LEU LYS PRO GLN ILE
SEQRES 12 B 275 GLU LYS ASN PHE GLU ILE ASP LYS GLY LYS GLN THR LEU
SEQRES 13 B 275 PHE GLY HIS SVY LEU GLY GLY LEU PHE ALA LEU HIS ILE
SEQRES 14 B 275 LEU PHE THR ASN LEU ASN ALA PHE GLN ASN TYR PHE ILE
SEQRES 15 B 275 SER SER PRO SER ILE TRP TRP ASN ASN LYS SER VAL LEU
SEQRES 16 B 275 GLU LYS GLU GLU ASN LEU ILE ILE GLU LEU ASN ASN ALA
SEQRES 17 B 275 LYS PHE GLU THR GLY VAL PHE LEU THR VAL GLY SER LEU
SEQRES 18 B 275 GLU ARG GLU HIS MSE VAL VAL GLY ALA ASN GLU LEU SER
SEQRES 19 B 275 GLU ARG LEU LEU GLN VAL ASN HIS ASP LYS LEU LYS PHE
SEQRES 20 B 275 LYS PHE TYR GLU ALA GLU GLY GLU ASN HIS ALA SER VAL
SEQRES 21 B 275 VAL PRO THR SER LEU SER LYS GLY LEU ARG PHE ILE SER
SEQRES 22 B 275 TYR VAL
MODRES 2QM0 MSE A 20 MET SELENOMETHIONINE
MODRES 2QM0 MSE A 223 MET SELENOMETHIONINE
MODRES 2QM0 MSE B 20 MET SELENOMETHIONINE
MODRES 2QM0 MSE B 223 MET SELENOMETHIONINE
HET MSE A 20 8
HET SVY A 157 16
HET MSE A 223 8
HET MSE B 20 8
HET SVY B 157 32
HET MSE B 223 8
HET SO4 B 601 5
HET SO4 A 602 5
HET SO4 B 603 5
HET SO4 A 604 5
HET SO4 B 605 5
HETNAM MSE SELENOMETHIONINE
HETNAM SVY O-[BIS(1-METHYLETHOXY)PHOSPHORYL]-L-SERINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 1 SVY 2(C9 H20 N O6 P)
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 8 HOH *538(H2 O)
HELIX 1 1 ASP A 52 SER A 68 1 17
HELIX 2 2 ARG A 70 GLY A 75 1 6
HELIX 3 3 SER A 93 THR A 102 1 10
HELIX 4 4 GLY A 124 GLU A 135 1 12
HELIX 5 5 GLU A 135 PHE A 144 1 10
HELIX 6 6 SVY A 157 ASN A 170 1 14
HELIX 7 7 LEU A 171 PHE A 174 5 4
HELIX 8 8 TRP A 185 SER A 190 1 6
HELIX 9 9 VAL A 191 GLU A 195 5 5
HELIX 10 10 GLU A 196 ASN A 204 1 9
HELIX 11 11 ARG A 220 VAL A 237 1 18
HELIX 12 12 SER A 256 SER A 270 1 15
HELIX 13 13 ASP B 52 SER B 68 1 17
HELIX 14 14 ARG B 70 GLY B 75 1 6
HELIX 15 15 GLY B 94 THR B 102 1 9
HELIX 16 16 GLY B 124 GLU B 135 1 12
HELIX 17 17 GLU B 135 PHE B 144 1 10
HELIX 18 18 SVY B 157 ASN B 170 1 14
HELIX 19 19 LEU B 171 PHE B 174 5 4
HELIX 20 20 TRP B 185 SER B 190 1 6
HELIX 21 21 VAL B 191 GLU B 195 5 5
HELIX 22 22 GLU B 196 ALA B 205 1 10
HELIX 23 23 ARG B 220 VAL B 237 1 18
HELIX 24 24 SER B 256 SER B 270 1 15
SHEET 1 A 9 GLU A 6 GLN A 8 0
SHEET 2 A 9 THR B 15 TYR B 21 -1 O GLN B 17 N GLN A 8
SHEET 3 A 9 GLU B 28 SER B 34 -1 O ILE B 33 N GLU B 16
SHEET 4 A 9 ILE B 80 GLY B 85 -1 O GLY B 83 N HIS B 32
SHEET 5 A 9 TYR B 45 LEU B 51 1 N VAL B 50 O VAL B 82
SHEET 6 A 9 ILE B 146 HIS B 156 1 O PHE B 154 N TYR B 49
SHEET 7 A 9 ASN B 176 SER B 180 1 O SER B 180 N GLY B 155
SHEET 8 A 9 THR B 209 GLY B 216 1 O PHE B 212 N ILE B 179
SHEET 9 A 9 LEU B 242 ALA B 249 1 O LYS B 243 N THR B 209
SHEET 1 B 9 LEU A 242 ALA A 249 0
SHEET 2 B 9 THR A 209 GLY A 216 1 N THR A 209 O LYS A 243
SHEET 3 B 9 ASN A 176 SER A 180 1 N TYR A 177 O PHE A 212
SHEET 4 B 9 ILE A 146 HIS A 156 1 N LEU A 153 O PHE A 178
SHEET 5 B 9 TYR A 45 LEU A 51 1 N TYR A 49 O THR A 152
SHEET 6 B 9 ILE A 80 GLY A 85 1 O VAL A 82 N ILE A 48
SHEET 7 B 9 GLU A 28 SER A 34 -1 N HIS A 32 O GLY A 83
SHEET 8 B 9 THR A 15 TYR A 21 -1 N TRP A 18 O ILE A 31
SHEET 9 B 9 GLU B 6 GLN B 8 -1 O GLN B 8 N GLN A 17
CRYST1 48.849 135.058 200.873 90.00 90.00 90.00 C 2 2 21 16
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 0.020471 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007404 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004978 0.00000
TER 2197 VAL A 272
TER 4430 VAL B 272
MASTER 356 0 11 24 18 0 0 6 4991 2 105 44
END |