HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 15-FEB-06 2G2C
TITLE PUTATIVE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN FROM
TITLE 2 CORYNEBACTERIUM DIPHTHERIAE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE MOLYBDENUM COFACTOR BIOSYNTHESIS
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM DIPHTHERIAE;
SOURCE 3 ORGANISM_TAXID: 1717;
SOURCE 4 GENE: DIP0503;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PUTATIVE MOLYBDENUM COFACTOR
KEYWDS 2 BIOSYNTHESIS PROTEIN, PSI, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN
KEYWDS 4 FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,H.LI,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 2 24-FEB-09 2G2C 1 VERSN
REVDAT 1 28-MAR-06 2G2C 0
JRNL AUTH J.OSIPIUK,H.LI,S.CLANCY,A.JOACHIMIAK
JRNL TITL X-RAY CRYSTAL STRUCTURE OF PUTATIVE MOLYBDENUM
JRNL TITL 2 COFACTOR BIOSYNTHESIS PROTEIN FROM CORYNEBACTERIUM
JRNL TITL 3 DIPHTHERIAE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 23317
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1801
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 925
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1189
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.65000
REMARK 3 B22 (A**2) : 0.65000
REMARK 3 B33 (A**2) : -0.98000
REMARK 3 B12 (A**2) : 0.33000
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): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.149
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1216 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1667 ; 1.535 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 171 ; 5.755 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 49 ;31.438 ;23.673
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 211 ;12.447 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;24.326 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 203 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 909 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 561 ; 0.218 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 858 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 121 ; 0.155 ; 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): 52 ; 0.278 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.147 ; 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): 784 ; 1.407 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1279 ; 2.166 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 440 ; 4.789 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 376 ; 5.501 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1224 ; 4.334 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 212 ; 5.934 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1189 ; 3.544 ; 3.000
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 : NULL
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. R-FACTOR-ALL CORRESPONDS TO DEPOSITED FILE.
REMARK 3 R-WORK AND R-FREE FACTORS ARE TAKEN FROM SECOND TO LAST ROUND
REMARK 3 OF REFINEMENT WHICH USED TEST DATA SET.
REMARK 4
REMARK 4 2G2C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-06.
REMARK 100 THE RCSB ID CODE IS RCSB036600.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-05
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) : 0.97894
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SBCCOLLECT
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23460
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 32.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 29.000
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 49.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 49.5
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 0.66400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, SHELXD, MLPHARE, DM, SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES BUFFER, 3 M NACL, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-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 -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 -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 57.13800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 57.13800
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 57.13800
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 57.13800
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 57.13800
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 57.13800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). THE AUTHORS STATE THAT THE
REMARK 300 BIOLOGICAL UNIT IS UNKNOWN.
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 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 381 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 -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 GLU A 34
REMARK 465 LEU A 35
REMARK 465 GLN A 36
REMARK 465 ASP A 37
REMARK 465 SER A 108
REMARK 465 THR A 109
REMARK 465 HIS A 110
REMARK 465 THR A 111
REMARK 465 HIS A 112
REMARK 465 LEU A 113
REMARK 465 ALA A 114
REMARK 465 SER A 164
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 SER A 11 123.21 -171.02
REMARK 500 CYS A 96 70.72 -113.59
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 NA A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC82505 RELATED DB: TARGETDB
DBREF 2G2C A 1 164 UNP Q6NJA6 Q6NJA6_CORDI 1 164
SEQADV 2G2C SER A -2 UNP Q6NJA6 CLONING ARTIFACT
SEQADV 2G2C ASN A -1 UNP Q6NJA6 CLONING ARTIFACT
SEQADV 2G2C ALA A 0 UNP Q6NJA6 CLONING ARTIFACT
SEQADV 2G2C MSE A 1 UNP Q6NJA6 MET 1 MODIFIED RESIDUE
SEQADV 2G2C MSE A 31 UNP Q6NJA6 MET 31 MODIFIED RESIDUE
SEQRES 1 A 167 SER ASN ALA MSE HIS ILE LYS SER ALA ILE ILE VAL VAL
SEQRES 2 A 167 SER ASP ARG ILE SER THR GLY THR ARG GLU ASN LYS ALA
SEQRES 3 A 167 LEU PRO LEU LEU GLN ARG LEU MSE SER ASP GLU LEU GLN
SEQRES 4 A 167 ASP TYR SER TYR GLU LEU ILE SER GLU VAL VAL VAL PRO
SEQRES 5 A 167 GLU GLY TYR ASP THR VAL VAL GLU ALA ILE ALA THR ALA
SEQRES 6 A 167 LEU LYS GLN GLY ALA ARG PHE ILE ILE THR ALA GLY GLY
SEQRES 7 A 167 THR GLY ILE ARG ALA LYS ASN GLN THR PRO GLU ALA THR
SEQRES 8 A 167 ALA SER PHE ILE HIS THR ARG CYS GLU GLY LEU GLU GLN
SEQRES 9 A 167 GLN ILE LEU ILE HIS GLY SER THR HIS THR HIS LEU ALA
SEQRES 10 A 167 GLY LEU SER ARG GLY ILE VAL GLY VAL THR GLY ARG ASP
SEQRES 11 A 167 ASP HIS ALA ALA LEU ILE VAL ASN ALA PRO SER SER SER
SEQRES 12 A 167 GLY GLY ILE THR ASP THR TRP ALA VAL ILE SER PRO VAL
SEQRES 13 A 167 ILE PRO ASN ILE PHE GLU GLY LEU ASP ALA SER
MODRES 2G2C MSE A 1 MET SELENOMETHIONINE
MODRES 2G2C MSE A 31 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 31 8
HET NA A 301 1
HETNAM MSE SELENOMETHIONINE
HETNAM NA SODIUM ION
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 NA NA 1+
FORMUL 3 HOH *211(H2 O)
HELIX 1 1 SER A 11 GLY A 17 1 7
HELIX 2 2 LYS A 22 SER A 32 1 11
HELIX 3 3 GLY A 51 GLN A 65 1 15
HELIX 4 4 GLN A 83 SER A 90 1 8
HELIX 5 5 CYS A 96 GLY A 107 1 12
HELIX 6 6 SER A 139 SER A 151 1 13
HELIX 7 7 VAL A 153 ALA A 163 1 11
SHEET 1 A 6 SER A 39 VAL A 48 0
SHEET 2 A 6 HIS A 2 VAL A 10 1 N SER A 5 O GLU A 41
SHEET 3 A 6 PHE A 69 ALA A 73 1 O ALA A 73 N VAL A 10
SHEET 4 A 6 LEU A 132 ALA A 136 1 O ALA A 136 N THR A 72
SHEET 5 A 6 VAL A 121 VAL A 123 -1 N GLY A 122 O ILE A 133
SHEET 6 A 6 THR A 94 ARG A 95 -1 N THR A 94 O VAL A 123
LINK C MSE A 1 N HIS A 2 1555 1555 1.34
LINK C LEU A 30 N MSE A 31 1555 1555 1.34
LINK C MSE A 31 N SER A 32 1555 1555 1.33
LINK OG1 THR A 76 NA NA A 301 1555 1555 2.84
SITE 1 AC1 5 GLY A 74 GLY A 75 THR A 76 PRO A 137
SITE 2 AC1 5 SER A 138
CRYST1 67.822 67.822 114.276 90.00 90.00 120.00 P 63 2 2 12
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 0.014744 0.008513 0.000000 0.00000
SCALE2 0.000000 0.017025 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008751 0.00000
HETATM 1 N MSE A 1 25.164 59.259 10.142 1.00 34.19 N
ANISOU 1 N MSE A 1 4503 4201 4284 36 58 25 N
HETATM 2 CA MSE A 1 24.464 58.423 11.170 1.00 34.54 C
ANISOU 2 CA MSE A 1 4431 4255 4435 -43 38 39 C
HETATM 3 C MSE A 1 25.086 57.027 11.204 1.00 33.29 C
ANISOU 3 C MSE A 1 4278 4139 4232 -52 21 43 C
HETATM 4 O MSE A 1 24.812 56.224 10.329 1.00 33.67 O
ANISOU 4 O MSE A 1 4384 4117 4289 -52 0 23 O
HETATM 5 CB MSE A 1 22.935 58.363 10.900 1.00 35.57 C
ANISOU 5 CB MSE A 1 4520 4416 4576 -39 42 22 C
HETATM 6 CG MSE A 1 22.248 57.053 11.372 1.00 39.47 C
ANISOU 6 CG MSE A 1 5161 4793 5041 -125 78 91 C
HETATM 7 SE MSE A 1 20.319 57.057 11.803 0.50 45.18 SE
ANISOU 7 SE MSE A 1 5542 5548 6075 -300 275 193 SE
HETATM 8 CE MSE A 1 19.462 57.085 10.009 1.00 43.62 C
ANISOU 8 CE MSE A 1 5417 5266 5889 -226 198 83 C
(ATOM LINES ARE NOT SHOWN.)
END
