HEADER METAL TRANSPORT 05-SEP-05 2D2A
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI SUFA INVOLVED IN BIOSYNTHESIS OF
TITLE 2 IRON-SULFUR CLUSTERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUFA PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-19B
KEYWDS IRON-SULFUR CLUSTER, IRON, SUF, SUFA, ISCA, YADR, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR K.WADA,Y.HASEGAWA,Z.GONG,Y.MINAMI,K.FUKUYAMA,Y.TAKAHASHI
REVDAT 4 25-OCT-23 2D2A 1 SEQADV
REVDAT 3 11-OCT-17 2D2A 1 REMARK
REVDAT 2 24-FEB-09 2D2A 1 VERSN
REVDAT 1 13-DEC-05 2D2A 0
JRNL AUTH K.WADA,Y.HASEGAWA,Z.GONG,Y.MINAMI,K.FUKUYAMA,Y.TAKAHASHI
JRNL TITL CRYSTAL STRUCTURE OF ESCHERICHIA COLI SUFA INVOLVED IN
JRNL TITL 2 BIOSYNTHESIS OF IRON-SULFUR CLUSTERS: IMPLICATIONS FOR A
JRNL TITL 3 FUNCTIONAL DIMER
JRNL REF FEBS LETT. V. 579 6543 2005
JRNL REFN ISSN 0014-5793
JRNL PMID 16298366
JRNL DOI 10.1016/J.FEBSLET.2005.10.046
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 421277.640
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 7692
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) : 0.232
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.600
REMARK 3 FREE R VALUE TEST SET COUNT : 817
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1021
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 125
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1640
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.42000
REMARK 3 B22 (A**2) : 5.78000
REMARK 3 B33 (A**2) : -2.37000
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) : 0.32
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.047
REMARK 3 BOND ANGLES (DEGREES) : 3.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 3.050
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 43.83
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.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D2A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000024898.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8136
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
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) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.34900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1S98
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG2000MME, PH 4.8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 12.58100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.00650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.00650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 12.58100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER IN THE ASYMMETRIC UNIT.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
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: 1930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 50.32400
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -44.25000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 61.00650
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 -22
REMARK 465 GLY A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 HIS A -7
REMARK 465 ILE A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 LEU A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 MET A 3
REMARK 465 HIS A 4
REMARK 465 SER A 5
REMARK 465 GLY A 6
REMARK 465 THR A 7
REMARK 465 PHE A 8
REMARK 465 MET B -22
REMARK 465 GLY B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 HIS B -7
REMARK 465 ILE B -6
REMARK 465 ASP B -5
REMARK 465 ASP B -4
REMARK 465 ASP B -3
REMARK 465 ASP B -2
REMARK 465 LEU B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 MET B 3
REMARK 465 HIS B 4
REMARK 465 THR B 48
REMARK 465 GLY B 49
REMARK 465 CYS B 50
REMARK 465 ALA B 51
REMARK 465 GLN B 111
REMARK 465 ASN B 112
REMARK 465 GLU B 113
REMARK 465 CYS B 114
REMARK 465 GLY B 115
REMARK 465 CYS B 116
REMARK 465 GLY B 117
REMARK 465 GLU B 118
REMARK 465 SER B 119
REMARK 465 PHE B 120
REMARK 465 GLY B 121
REMARK 465 VAL B 122
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 9 CG OD1 ND2
REMARK 470 LYS A 46 CG CD CE NZ
REMARK 470 LYS A 65 CG CD CE NZ
REMARK 470 GLN A 111 CG CD OE1 NE2
REMARK 470 GLU A 113 CG CD OE1 OE2
REMARK 470 SER B 5 OG
REMARK 470 GLN B 11 CG CD OE1 NE2
REMARK 470 LYS B 65 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 10 CA PRO A 10 C 0.130
REMARK 500 GLN A 11 CB GLN A 11 CG 0.266
REMARK 500 GLN A 11 CG GLN A 11 CD 0.261
REMARK 500 ASP A 12 CB ASP A 12 CG 0.166
REMARK 500 THR A 19 C THR A 19 O -0.134
REMARK 500 ARG A 29 CZ ARG A 29 NH2 0.125
REMARK 500 VAL A 32 CA VAL A 32 CB -0.158
REMARK 500 PRO A 36 CD PRO A 36 N 0.105
REMARK 500 PRO A 36 C PRO A 36 O 0.124
REMARK 500 LYS A 46 CA LYS A 46 CB 0.178
REMARK 500 GLN A 47 CB GLN A 47 CG 0.190
REMARK 500 GLN A 47 CG GLN A 47 CD 0.311
REMARK 500 GLY A 49 CA GLY A 49 C 0.148
REMARK 500 CYS A 50 CB CYS A 50 SG 0.125
REMARK 500 PHE A 53 CB PHE A 53 CG 0.133
REMARK 500 PHE A 53 CG PHE A 53 CD2 0.113
REMARK 500 PHE A 53 CE1 PHE A 53 CZ 0.139
REMARK 500 TYR A 55 CG TYR A 55 CD1 -0.092
REMARK 500 TYR A 55 CE2 TYR A 55 CD2 0.106
REMARK 500 VAL A 56 CB VAL A 56 CG1 0.131
REMARK 500 ASP A 58 CG ASP A 58 OD1 0.216
REMARK 500 SER A 59 CA SER A 59 CB -0.095
REMARK 500 SER A 59 CB SER A 59 OG -0.125
REMARK 500 VAL A 60 CB VAL A 60 CG2 -0.134
REMARK 500 SER A 61 CB SER A 61 OG -0.084
REMARK 500 GLU A 62 CG GLU A 62 CD 0.122
REMARK 500 GLU A 62 CD GLU A 62 OE2 0.131
REMARK 500 ASP A 66 CB ASP A 66 CG 0.291
REMARK 500 PHE A 70 CE1 PHE A 70 CZ 0.132
REMARK 500 GLU A 71 CD GLU A 71 OE2 0.089
REMARK 500 ASP A 73 CB ASP A 73 CG 0.317
REMARK 500 ASP A 73 C ASP A 73 O -0.128
REMARK 500 PHE A 86 CB PHE A 86 CG 0.137
REMARK 500 PHE A 86 CD1 PHE A 86 CE1 0.174
REMARK 500 PHE A 86 CE1 PHE A 86 CZ 0.131
REMARK 500 PHE A 86 CZ PHE A 86 CE2 0.115
REMARK 500 PHE A 86 CE2 PHE A 86 CD2 0.120
REMARK 500 GLU A 91 CD GLU A 91 OE1 0.103
REMARK 500 VAL A 95 CB VAL A 95 CG1 -0.151
REMARK 500 PHE A 103 CG PHE A 103 CD1 0.090
REMARK 500 PHE A 103 CZ PHE A 103 CE2 0.127
REMARK 500 GLU A 118 C GLU A 118 O -0.152
REMARK 500 GLY A 121 C GLY A 121 O 0.101
REMARK 500 PHE B 103 CB PHE B 103 CG 0.117
REMARK 500 LYS B 104 CD LYS B 104 CE 0.199
REMARK 500 LYS B 104 CE LYS B 104 NZ 0.193
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 ASP A 12 CB - CG - OD2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLN A 16 CB - CA - C ANGL. DEV. = -12.8 DEGREES
REMARK 500 LEU A 18 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG A 29 NE - CZ - NH2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO A 36 CB - CA - C ANGL. DEV. = -12.8 DEGREES
REMARK 500 ARG A 42 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 CYS A 50 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 GLY A 54 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 LEU A 57 CB - CG - CD2 ANGL. DEV. = 14.7 DEGREES
REMARK 500 VAL A 60 CG1 - CB - CG2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ASP A 66 OD1 - CG - OD2 ANGL. DEV. = -14.2 DEGREES
REMARK 500 ASP A 66 CB - CG - OD2 ANGL. DEV. = 14.1 DEGREES
REMARK 500 ASP A 67 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 73 OD1 - CG - OD2 ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASP A 73 CB - CG - OD1 ANGL. DEV. = 12.5 DEGREES
REMARK 500 PRO A 85 N - CD - CG ANGL. DEV. = -11.3 DEGREES
REMARK 500 ASP A 88 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 93 CB - CG - OD1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP A 93 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 LEU A 99 CA - CB - CG ANGL. DEV. = 21.2 DEGREES
REMARK 500 ALA A 110 CA - C - N ANGL. DEV. = 17.9 DEGREES
REMARK 500 GLN A 111 CA - C - N ANGL. DEV. = 15.5 DEGREES
REMARK 500 GLN A 111 O - C - N ANGL. DEV. = -11.9 DEGREES
REMARK 500 CYS A 114 CA - CB - SG ANGL. DEV. = -15.0 DEGREES
REMARK 500 SER A 119 N - CA - CB ANGL. DEV. = -14.7 DEGREES
REMARK 500 VAL A 122 CB - CA - C ANGL. DEV. = -12.6 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 PRO A 10 -65.38 -127.87
REMARK 500 GLN A 11 -147.23 -178.33
REMARK 500 ASP A 12 91.23 60.13
REMARK 500 PHE A 13 3.00 -160.79
REMARK 500 ALA A 14 94.36 37.37
REMARK 500 CYS A 50 -99.06 -77.98
REMARK 500 ALA A 51 32.72 -98.91
REMARK 500 PHE A 53 122.85 -177.34
REMARK 500 GLN A 82 4.30 -60.96
REMARK 500 ILE A 87 16.73 -141.31
REMARK 500 GLN A 111 172.69 43.46
REMARK 500 HIS B 72 117.74 -170.56
REMARK 500 LYS B 109 41.47 -87.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 32 ALA A 33 -148.59
REMARK 500 GLY A 49 CYS A 50 149.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2D2A A 1 122 UNP P77667 SUFA_ECOLI 1 122
DBREF 2D2A B 1 122 UNP P77667 SUFA_ECOLI 1 122
SEQADV 2D2A MET A -22 UNP P77667 EXPRESSION TAG
SEQADV 2D2A GLY A -21 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -20 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -19 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -18 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -17 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -16 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -15 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -14 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -13 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -12 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -11 UNP P77667 EXPRESSION TAG
SEQADV 2D2A SER A -10 UNP P77667 EXPRESSION TAG
SEQADV 2D2A SER A -9 UNP P77667 EXPRESSION TAG
SEQADV 2D2A GLY A -8 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A -7 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ILE A -6 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ASP A -5 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ASP A -4 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ASP A -3 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ASP A -2 UNP P77667 EXPRESSION TAG
SEQADV 2D2A LEU A -1 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS A 0 UNP P77667 EXPRESSION TAG
SEQADV 2D2A MET B -22 UNP P77667 EXPRESSION TAG
SEQADV 2D2A GLY B -21 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -20 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -19 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -18 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -17 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -16 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -15 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -14 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -13 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -12 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -11 UNP P77667 EXPRESSION TAG
SEQADV 2D2A SER B -10 UNP P77667 EXPRESSION TAG
SEQADV 2D2A SER B -9 UNP P77667 EXPRESSION TAG
SEQADV 2D2A GLY B -8 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B -7 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ILE B -6 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ASP B -5 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ASP B -4 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ASP B -3 UNP P77667 EXPRESSION TAG
SEQADV 2D2A ASP B -2 UNP P77667 EXPRESSION TAG
SEQADV 2D2A LEU B -1 UNP P77667 EXPRESSION TAG
SEQADV 2D2A HIS B 0 UNP P77667 EXPRESSION TAG
SEQRES 1 A 145 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 145 SER GLY HIS ILE ASP ASP ASP ASP LEU HIS MET ASP MET
SEQRES 3 A 145 HIS SER GLY THR PHE ASN PRO GLN ASP PHE ALA TRP GLN
SEQRES 4 A 145 GLY LEU THR LEU THR PRO ALA ALA ALA ILE HIS ILE ARG
SEQRES 5 A 145 GLU LEU VAL ALA LYS GLN PRO GLY MET VAL GLY VAL ARG
SEQRES 6 A 145 LEU GLY VAL LYS GLN THR GLY CYS ALA GLY PHE GLY TYR
SEQRES 7 A 145 VAL LEU ASP SER VAL SER GLU PRO ASP LYS ASP ASP LEU
SEQRES 8 A 145 LEU PHE GLU HIS ASP GLY ALA LYS LEU PHE VAL PRO LEU
SEQRES 9 A 145 GLN ALA MET PRO PHE ILE ASP GLY THR GLU VAL ASP PHE
SEQRES 10 A 145 VAL ARG GLU GLY LEU ASN GLN ILE PHE LYS PHE HIS ASN
SEQRES 11 A 145 PRO LYS ALA GLN ASN GLU CYS GLY CYS GLY GLU SER PHE
SEQRES 12 A 145 GLY VAL
SEQRES 1 B 145 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 B 145 SER GLY HIS ILE ASP ASP ASP ASP LEU HIS MET ASP MET
SEQRES 3 B 145 HIS SER GLY THR PHE ASN PRO GLN ASP PHE ALA TRP GLN
SEQRES 4 B 145 GLY LEU THR LEU THR PRO ALA ALA ALA ILE HIS ILE ARG
SEQRES 5 B 145 GLU LEU VAL ALA LYS GLN PRO GLY MET VAL GLY VAL ARG
SEQRES 6 B 145 LEU GLY VAL LYS GLN THR GLY CYS ALA GLY PHE GLY TYR
SEQRES 7 B 145 VAL LEU ASP SER VAL SER GLU PRO ASP LYS ASP ASP LEU
SEQRES 8 B 145 LEU PHE GLU HIS ASP GLY ALA LYS LEU PHE VAL PRO LEU
SEQRES 9 B 145 GLN ALA MET PRO PHE ILE ASP GLY THR GLU VAL ASP PHE
SEQRES 10 B 145 VAL ARG GLU GLY LEU ASN GLN ILE PHE LYS PHE HIS ASN
SEQRES 11 B 145 PRO LYS ALA GLN ASN GLU CYS GLY CYS GLY GLU SER PHE
SEQRES 12 B 145 GLY VAL
FORMUL 3 HOH *37(H2 O)
HELIX 1 1 THR A 21 GLN A 35 1 15
HELIX 2 2 ALA A 83 ASP A 88 1 6
HELIX 3 3 THR B 21 GLN B 35 1 15
HELIX 4 4 ALA B 83 ASP B 88 1 6
SHEET 1 A 3 THR A 19 LEU A 20 0
SHEET 2 A 3 GLU A 91 GLU A 97 1 O VAL A 92 N THR A 19
SHEET 3 A 3 ASN A 100 HIS A 106 -1 O ILE A 102 N VAL A 95
SHEET 1 B 4 GLY A 52 VAL A 60 0
SHEET 2 B 4 GLY A 40 THR A 48 -1 N ARG A 42 O ASP A 58
SHEET 3 B 4 ALA A 75 PRO A 80 1 O PHE A 78 N VAL A 41
SHEET 4 B 4 ASP A 67 HIS A 72 -1 N LEU A 68 O VAL A 79
SHEET 1 C 4 SER A 119 GLY A 121 0
SHEET 2 C 4 ASN B 100 HIS B 106 -1 O PHE B 103 N PHE A 120
SHEET 3 C 4 GLU B 91 GLU B 97 -1 N GLU B 97 O ASN B 100
SHEET 4 C 4 THR B 19 LEU B 20 1 N THR B 19 O VAL B 92
SHEET 1 D 4 GLY B 54 VAL B 60 0
SHEET 2 D 4 GLY B 40 LYS B 46 -1 N GLY B 44 O VAL B 56
SHEET 3 D 4 ALA B 75 PRO B 80 1 O PHE B 78 N VAL B 41
SHEET 4 D 4 ASP B 67 HIS B 72 -1 N LEU B 68 O VAL B 79
CRYST1 25.162 88.500 122.013 90.00 90.00 90.00 P 21 21 21 8
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 0.039742 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011299 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008196 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
