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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 08-APR-09 3H04
TITLE THE CRYSTAL STRUCTURE OF THE PROTEIN WITH UNKNOWN FUNCTION
TITLE 2 FROM STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MU50
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS
SOURCE 3 MU50;
SOURCE 4 ORGANISM_TAXID: 158878;
SOURCE 5 STRAIN: MU50;
SOURCE 6 GENE: GI:14246089, SAV0321;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS PROTEIN WITH UNKNOWN FUNCTION, STRUCTURAL GENOMICS, MCSG,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ZHANG,C.TESAR,A.SATHER,S.CLANCY,A.JOACHIMIAK,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 07-JUL-09 3H04 0
JRNL AUTH R.ZHANG,C.TESAR,A.SATHER,S.CLANCY,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF THE PROTEIN WITH UNKNOWN
JRNL TITL 2 FUNCTION FROM STAPHYLOCOCCUS AUREUS SUBSP. AUREUS
JRNL TITL 3 MU50
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0054
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 20087
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1086
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1006
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.1810
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2199
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : -0.10000
REMARK 3 B33 (A**2) : 0.15000
REMARK 3 B12 (A**2) : -0.05000
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): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.153
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2253 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1497 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3066 ; 1.618 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3658 ; 0.975 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 5.799 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 109 ;34.839 ;24.404
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 376 ;13.605 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;13.430 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 342 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2504 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 458 ; 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): 1367 ; 0.912 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 543 ; 0.294 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2236 ; 1.594 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 886 ; 2.656 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 830 ; 3.896 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 50
REMARK 3 RESIDUE RANGE : A 51 A 100
REMARK 3 RESIDUE RANGE : A 101 A 150
REMARK 3 RESIDUE RANGE : A 151 A 200
REMARK 3 RESIDUE RANGE : A 201 A 240
REMARK 3 RESIDUE RANGE : A 241 A 274
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0680 4.8960 16.3720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0609 T22: 0.0680
REMARK 3 T33: 0.0285 T12: 0.0045
REMARK 3 T13: 0.0038 T23: 0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 0.7368 L22: 1.1154
REMARK 3 L33: 2.0459 L12: -0.2520
REMARK 3 L13: -0.0821 L23: -0.2941
REMARK 3 S TENSOR
REMARK 3 S11: 0.0283 S12: -0.0027 S13: 0.0180
REMARK 3 S21: 0.0394 S22: 0.0889 S23: 0.0705
REMARK 3 S31: -0.0394 S32: -0.0816 S33: -0.1172
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
REMARK 4
REMARK 4 3H04 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052523.
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 : 5.1
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) : 0.9794, 0.9796
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20087
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 67.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.8
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.50300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: HIKL3000_SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CALCIUM CHLORIDE DIHYDRATE,
REMARK 280 20% PEG3350, PH 5.1, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 134.82867
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 269.65733
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 202.24300
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 337.07167
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 67.41433
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 134.82867
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 269.65733
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 337.07167
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 202.24300
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 67.41433
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 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 MET A 1
REMARK 465 THR A 2
REMARK 465 VAL A 275
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 172 NE - CZ - NH2 ANGL. DEV. = -3.0 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 ASN A 46 53.69 -92.87
REMARK 500 SER A 104 -126.80 61.14
REMARK 500 HIS A 234 -34.98 -137.17
REMARK 500 HIS A 248 -74.88 -106.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC61011 RELATED DB: TARGETDB
DBREF 3H04 A 1 275 UNP Q99WQ5 Q99WQ5_STAAM 1 275
SEQRES 1 A 275 MET THR GLU ILE LYS TYR LYS VAL ILE THR LYS ASP ALA
SEQRES 2 A 275 PHE ALA LEU PRO TYR THR ILE ILE LYS ALA LYS ASN GLN
SEQRES 3 A 275 PRO THR LYS GLY VAL ILE VAL TYR ILE HIS GLY GLY GLY
SEQRES 4 A 275 LEU MET PHE GLY LYS ALA ASN ASP LEU SER PRO GLN TYR
SEQRES 5 A 275 ILE ASP ILE LEU THR GLU HIS TYR ASP LEU ILE GLN LEU
SEQRES 6 A 275 SER TYR ARG LEU LEU PRO GLU VAL SER LEU ASP CYS ILE
SEQRES 7 A 275 ILE GLU ASP VAL TYR ALA SER PHE ASP ALA ILE GLN SER
SEQRES 8 A 275 GLN TYR SER ASN CYS PRO ILE PHE THR PHE GLY ARG SER
SEQRES 9 A 275 SER GLY ALA TYR LEU SER LEU LEU ILE ALA ARG ASP ARG
SEQRES 10 A 275 ASP ILE ASP GLY VAL ILE ASP PHE TYR GLY TYR SER ARG
SEQRES 11 A 275 ILE ASN THR GLU PRO PHE LYS THR THR ASN SER TYR TYR
SEQRES 12 A 275 ALA LYS ILE ALA GLN SER ILE ASN GLU THR MET ILE ALA
SEQRES 13 A 275 GLN LEU THR SER PRO THR PRO VAL VAL GLN ASP GLN ILE
SEQRES 14 A 275 ALA GLN ARG PHE LEU ILE TYR VAL TYR ALA ARG GLY THR
SEQRES 15 A 275 GLY LYS TRP ILE ASN MET ILE ASN ILE ALA ASP TYR THR
SEQRES 16 A 275 ASP SER LYS TYR ASN ILE ALA PRO ASP GLU LEU LYS THR
SEQRES 17 A 275 LEU PRO PRO VAL PHE ILE ALA HIS CYS ASN GLY ASP TYR
SEQRES 18 A 275 ASP VAL PRO VAL GLU GLU SER GLU HIS ILE MET ASN HIS
SEQRES 19 A 275 VAL PRO HIS SER THR PHE GLU ARG VAL ASN LYS ASN GLU
SEQRES 20 A 275 HIS ASP PHE ASP ARG ARG PRO ASN ASP GLU ALA ILE THR
SEQRES 21 A 275 ILE TYR ARG LYS VAL VAL ASP PHE LEU ASN ALA ILE THR
SEQRES 22 A 275 MET VAL
FORMUL 2 HOH *98(H2 O)
HELIX 1 1 SER A 49 THR A 57 1 9
HELIX 2 2 SER A 74 GLN A 92 1 19
HELIX 3 3 SER A 104 ARG A 117 1 14
HELIX 4 4 THR A 133 THR A 138 1 6
HELIX 5 5 ASN A 140 GLN A 148 1 9
HELIX 6 6 ASN A 151 GLN A 157 1 7
HELIX 7 7 ILE A 169 GLN A 171 5 3
HELIX 8 8 ARG A 172 THR A 182 1 11
HELIX 9 9 LYS A 184 ASN A 190 1 7
HELIX 10 10 ASP A 196 ASN A 200 5 5
HELIX 11 11 ALA A 202 LYS A 207 1 6
HELIX 12 12 VAL A 225 ASN A 233 1 9
HELIX 13 13 ASN A 255 MET A 274 1 20
SHEET 1 A 8 ILE A 4 ILE A 9 0
SHEET 2 A 8 ALA A 15 ILE A 21 -1 O LEU A 16 N VAL A 8
SHEET 3 A 8 TYR A 60 LEU A 65 -1 O LEU A 62 N ILE A 21
SHEET 4 A 8 GLY A 30 ILE A 35 1 N ILE A 32 O ASP A 61
SHEET 5 A 8 ILE A 98 ARG A 103 1 O PHE A 99 N VAL A 33
SHEET 6 A 8 GLY A 121 PHE A 125 1 O ILE A 123 N THR A 100
SHEET 7 A 8 VAL A 212 CYS A 217 1 O PHE A 213 N ASP A 124
SHEET 8 A 8 SER A 238 VAL A 243 1 O THR A 239 N ILE A 214
CISPEP 1 GLN A 26 PRO A 27 0 5.36
CISPEP 2 LEU A 70 PRO A 71 0 3.96
CRYST1 47.033 47.033 404.486 90.00 90.00 120.00 P 61 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 0.021262 0.012275 0.000000 0.00000
SCALE2 0.000000 0.024551 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002472 0.00000
TER 2200 MET A 274
MASTER 340 0 0 13 8 0 0 6 2297 1 0 22
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