HEADER CELL ADHESION 14-MAR-06 2DGJ
TITLE CRYSTAL STRUCTURE OF EBHA (756-1003 DOMAIN) FROM STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN EBHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2-249;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 STRAIN: MU50;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS HELIX-BUNDLE, ROD-LIKE STRUCTURE, ADHESIN, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.TANAKA,M.YAO,M.KURODA,N.WATANABE,T.OHTA,I.TANAKA
REVDAT 3 13-JUL-11 2DGJ 1 VERSN
REVDAT 2 13-MAY-08 2DGJ 1 JRNL REMARK VERSN
REVDAT 1 20-MAR-07 2DGJ 0
JRNL AUTH Y.TANAKA,S.SAKAMOTO,M.KURODA,S.GODA,Y.-G.GAO,K.TSUMOTO,
JRNL AUTH 2 Y.HIRAGI,M.YAO,N.WATANABE,T.OHTA,I.TANAKA
JRNL TITL A HELICAL STRING OF ALTERNATELY CONNECTED THREE-HELIX
JRNL TITL 2 BUNDLES FOR THE CELL WALL-ASSOCIATED ADHESION PROTEIN EBH
JRNL TITL 3 FROM STAPHYLOCOCCUS AUREUS
JRNL REF STRUCTURE V. 16 488 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18334223
JRNL DOI 10.1016/J.STR.2007.12.018
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2600153.160
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 20173
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 SET) : 0.241
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1975
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2785
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 311
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3629
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.89000
REMARK 3 B22 (A**2) : -11.11000
REMARK 3 B33 (A**2) : 15.00000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.59
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.290 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.540 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.260 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.440 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 32.57
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DGJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB025391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97904
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20244
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.13100
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, OASIS V. 2004, DM, SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE, 2.3M AMMONIUM SULFATE,
REMARK 280 PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.68300
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 66.68300
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 22.63250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 80.92400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 22.63250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 80.92400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.68300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.63250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 80.92400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 66.68300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 22.63250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 80.92400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 22.63250
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 80.92400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -66.68300
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -66.68300
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 -22.63250
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 80.92400
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 22.63250
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 80.92400
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -66.68300
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 MSE A 1
REMARK 465 THR A 48
REMARK 465 GLY A 49
REMARK 465 SER A 50
REMARK 465 ASN A 51
REMARK 465 SER A 52
REMARK 465 HIS A 253
REMARK 465 HIS A 254
REMARK 465 HIS A 255
REMARK 465 HIS A 256
REMARK 465 HIS A 257
REMARK 465 MSE B 1
REMARK 465 ALA B 2
REMARK 465 MSE B 3
REMARK 465 GLY B 49
REMARK 465 SER B 50
REMARK 465 ASN B 51
REMARK 465 SER B 52
REMARK 465 LEU B 250
REMARK 465 GLU B 251
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 HIS B 254
REMARK 465 HIS B 255
REMARK 465 HIS B 256
REMARK 465 HIS B 257
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2075 O HOH A 2075 3654 2.19
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 LYS A 54 N - CA - C ANGL. DEV. = -19.4 DEGREES
REMARK 500 PRO B 218 C - N - CA ANGL. DEV. = 12.0 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 LYS A 54 -28.52 -147.67
REMARK 500 ASP B 138 30.93 -95.89
REMARK 500 PRO B 218 -16.88 -48.51
REMARK 500 LEU B 220 -154.25 -145.55
REMARK 500 LYS B 247 35.13 -75.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LYS A 54 45.6 L L OUTSIDE RANGE
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 SO4 A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XVH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN BUT THE OTHER REGION
DBREF 2DGJ A 2 249 UNP Q931R6 Q931R6_STAAM 756 1003
DBREF 2DGJ B 2 249 UNP Q931R6 Q931R6_STAAM 756 1003
SEQADV 2DGJ MSE A 1 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ LEU A 250 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ GLU A 251 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS A 252 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS A 253 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS A 254 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS A 255 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS A 256 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS A 257 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ MSE B 1 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ LEU B 250 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ GLU B 251 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS B 252 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS B 253 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS B 254 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS B 255 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS B 256 UNP Q931R6 EXPRESSION TAG
SEQADV 2DGJ HIS B 257 UNP Q931R6 EXPRESSION TAG
SEQRES 1 A 257 MSE ALA MSE GLY GLN LEU GLN HIS GLY ILE ASP ASP GLU
SEQRES 2 A 257 ASN ALA THR LYS GLN THR GLN LYS TYR ARG ASP ALA GLU
SEQRES 3 A 257 GLN SER LYS LYS THR ALA TYR ASP GLN ALA VAL ALA ALA
SEQRES 4 A 257 ALA LYS ALA ILE LEU ASN LYS GLN THR GLY SER ASN SER
SEQRES 5 A 257 ASP LYS ALA ALA VAL ASP ARG ALA LEU GLN GLN VAL THR
SEQRES 6 A 257 SER THR LYS ASP ALA LEU ASN GLY ASP ALA LYS LEU ALA
SEQRES 7 A 257 GLU ALA LYS ALA ALA ALA ARG GLN ASN LEU GLY THR LEU
SEQRES 8 A 257 ASN HIS ILE THR ASN ALA GLN ARG THR ALA LEU GLU GLY
SEQRES 9 A 257 GLN ILE ASN GLN ALA THR THR VAL ASP GLY VAL ASN THR
SEQRES 10 A 257 VAL LYS THR ASN ALA ASN THR LEU ASP GLY ALA MSE ASN
SEQRES 11 A 257 SER LEU GLN GLY ALA ILE ASN ASP LYS ASP ALA THR LEU
SEQRES 12 A 257 ARG ASN GLN ASN TYR LEU ASP ALA ASP GLU SER LYS ARG
SEQRES 13 A 257 ASN ALA TYR THR GLN ALA VAL THR ALA ALA GLU GLY ILE
SEQRES 14 A 257 LEU ASN LYS GLN THR GLY GLY ASN THR SER LYS ALA ASP
SEQRES 15 A 257 VAL ASP ASN ALA LEU ASN ALA VAL THR ARG ALA LYS ALA
SEQRES 16 A 257 ALA LEU ASN GLY ALA GLU ASN LEU ARG ASN ALA LYS THR
SEQRES 17 A 257 SER ALA THR ASN THR ILE ASN GLY LEU PRO ASN LEU THR
SEQRES 18 A 257 GLN LEU GLN LYS ASP ASN LEU LYS HIS GLN VAL GLU GLN
SEQRES 19 A 257 ALA GLN ASN VAL VAL GLY VAL ASN GLY VAL LYS ASP LYS
SEQRES 20 A 257 GLY ASN LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 257 MSE ALA MSE GLY GLN LEU GLN HIS GLY ILE ASP ASP GLU
SEQRES 2 B 257 ASN ALA THR LYS GLN THR GLN LYS TYR ARG ASP ALA GLU
SEQRES 3 B 257 GLN SER LYS LYS THR ALA TYR ASP GLN ALA VAL ALA ALA
SEQRES 4 B 257 ALA LYS ALA ILE LEU ASN LYS GLN THR GLY SER ASN SER
SEQRES 5 B 257 ASP LYS ALA ALA VAL ASP ARG ALA LEU GLN GLN VAL THR
SEQRES 6 B 257 SER THR LYS ASP ALA LEU ASN GLY ASP ALA LYS LEU ALA
SEQRES 7 B 257 GLU ALA LYS ALA ALA ALA ARG GLN ASN LEU GLY THR LEU
SEQRES 8 B 257 ASN HIS ILE THR ASN ALA GLN ARG THR ALA LEU GLU GLY
SEQRES 9 B 257 GLN ILE ASN GLN ALA THR THR VAL ASP GLY VAL ASN THR
SEQRES 10 B 257 VAL LYS THR ASN ALA ASN THR LEU ASP GLY ALA MSE ASN
SEQRES 11 B 257 SER LEU GLN GLY ALA ILE ASN ASP LYS ASP ALA THR LEU
SEQRES 12 B 257 ARG ASN GLN ASN TYR LEU ASP ALA ASP GLU SER LYS ARG
SEQRES 13 B 257 ASN ALA TYR THR GLN ALA VAL THR ALA ALA GLU GLY ILE
SEQRES 14 B 257 LEU ASN LYS GLN THR GLY GLY ASN THR SER LYS ALA ASP
SEQRES 15 B 257 VAL ASP ASN ALA LEU ASN ALA VAL THR ARG ALA LYS ALA
SEQRES 16 B 257 ALA LEU ASN GLY ALA GLU ASN LEU ARG ASN ALA LYS THR
SEQRES 17 B 257 SER ALA THR ASN THR ILE ASN GLY LEU PRO ASN LEU THR
SEQRES 18 B 257 GLN LEU GLN LYS ASP ASN LEU LYS HIS GLN VAL GLU GLN
SEQRES 19 B 257 ALA GLN ASN VAL VAL GLY VAL ASN GLY VAL LYS ASP LYS
SEQRES 20 B 257 GLY ASN LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 2DGJ MSE A 3 MET SELENOMETHIONINE
MODRES 2DGJ MSE A 129 MET SELENOMETHIONINE
MODRES 2DGJ MSE B 129 MET SELENOMETHIONINE
HET MSE A 3 8
HET MSE A 129 8
HET MSE B 129 8
HET SO4 A2002 5
HET SO4 B2001 5
HET ACY A1501 4
HET GOL B1001 6
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM ACY ACETIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 ACY C2 H4 O2
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *280(H2 O)
HELIX 1 1 ALA A 2 ASP A 12 1 11
HELIX 2 2 ASP A 12 THR A 19 1 8
HELIX 3 3 THR A 19 ASP A 24 1 6
HELIX 4 4 GLU A 26 GLN A 47 1 22
HELIX 5 5 LYS A 54 LEU A 71 1 18
HELIX 6 6 ASN A 72 GLY A 89 1 18
HELIX 7 7 THR A 95 ALA A 109 1 15
HELIX 8 8 THR A 111 ILE A 136 1 26
HELIX 9 9 ASP A 138 ASN A 145 1 8
HELIX 10 10 ASN A 145 ASP A 150 1 6
HELIX 11 11 ASP A 152 ASN A 171 1 20
HELIX 12 12 SER A 179 ALA A 195 1 17
HELIX 13 13 ASN A 198 GLY A 216 1 19
HELIX 14 14 THR A 221 ALA A 235 1 15
HELIX 15 15 ASN A 237 GLU A 251 1 15
HELIX 16 16 GLY B 4 ASP B 11 1 8
HELIX 17 17 GLU B 13 GLN B 18 1 6
HELIX 18 18 THR B 19 ASP B 24 1 6
HELIX 19 19 GLU B 26 LYS B 46 1 21
HELIX 20 20 ASP B 53 LEU B 71 1 19
HELIX 21 21 ASN B 72 GLY B 89 1 18
HELIX 22 22 THR B 95 ALA B 109 1 15
HELIX 23 23 THR B 111 ILE B 136 1 26
HELIX 24 24 ASP B 138 ARG B 144 1 7
HELIX 25 25 ASN B 145 ASP B 150 1 6
HELIX 26 26 ASP B 152 ASN B 171 1 20
HELIX 27 27 SER B 179 LEU B 197 1 19
HELIX 28 28 ASN B 198 LEU B 217 1 20
HELIX 29 29 LYS B 225 ALA B 235 1 11
HELIX 30 30 ASN B 237 ASP B 246 1 10
LINK C ALA A 2 N MSE A 3 1555 1555 1.33
LINK C MSE A 3 N GLY A 4 1555 1555 1.33
LINK C ALA A 128 N MSE A 129 1555 1555 1.33
LINK C MSE A 129 N ASN A 130 1555 1555 1.33
LINK C ALA B 128 N MSE B 129 1555 1555 1.33
LINK C MSE B 129 N ASN B 130 1555 1555 1.33
SITE 1 AC1 4 ALA A 109 THR A 110 THR A 111 HOH A2096
SITE 1 AC2 6 ASN A 219 HIS A 252 THR B 110 THR B 111
SITE 2 AC2 6 GLY B 114 HOH B2030
SITE 1 AC3 3 LYS A 81 ARG A 85 HOH A2138
SITE 1 AC4 3 ALA B 78 LYS B 81 ARG B 85
CRYST1 45.265 161.848 133.366 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 0.022092 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006179 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007498 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
