HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 30-DEC-05 2FIY
TITLE THE CRYSTAL STRUCTURE OF THE FDHE PROTEIN FROM PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN FDHE HOMOLOG;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: FDHE GI:9951077;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS FDHE PROTEIN, PSEUDOMONAS AERUGINOSA, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ZHANG,E.EVDOKIMOVA,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 3 13-JUL-11 2FIY 1 VERSN
REVDAT 2 24-FEB-09 2FIY 1 VERSN
REVDAT 1 14-FEB-06 2FIY 0
JRNL AUTH R.ZHANG,E.EVDOKIMOVA,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF THE FDHE PROTEIN FROM PSEUDOMONAS
JRNL TITL 2 AERUGINOSA PAO1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 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 WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 35601
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1890
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2497
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4364
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 369
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 35.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : -0.32000
REMARK 3 B33 (A**2) : 0.77000
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): 0.225
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.189
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.140
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.745
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4470 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4170 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6072 ; 1.407 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9643 ; 0.880 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 558 ; 6.604 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 195 ;36.561 ;22.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 710 ;16.758 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;16.219 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 660 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4977 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 905 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1025 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4176 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2073 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2634 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 306 ; 0.188 ; 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): 36 ; 0.235 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 118 ; 0.240 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.183 ; 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): 3620 ; 0.931 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1135 ; 0.125 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4452 ; 1.051 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1912 ; 1.467 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1620 ; 2.128 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 19 A 78
REMARK 3 RESIDUE RANGE : A 79 A 180
REMARK 3 RESIDUE RANGE : A 181 A 250
REMARK 3 RESIDUE RANGE : A 251 A 307
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2050 96.4260 51.6310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0624 T22: -0.1297
REMARK 3 T33: -0.1193 T12: 0.0152
REMARK 3 T13: 0.0489 T23: 0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 1.5549 L22: 2.4971
REMARK 3 L33: 1.7231 L12: -0.0422
REMARK 3 L13: -0.1417 L23: 0.1655
REMARK 3 S TENSOR
REMARK 3 S11: 0.0961 S12: 0.0538 S13: 0.1357
REMARK 3 S21: -0.0150 S22: -0.0233 S23: -0.2280
REMARK 3 S31: -0.2212 S32: -0.0217 S33: -0.0728
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 18 B 78
REMARK 3 RESIDUE RANGE : B 79 B 182
REMARK 3 RESIDUE RANGE : B 183 B 250
REMARK 3 RESIDUE RANGE : B 251 B 308
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6720 47.4860 52.9300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0785 T22: -0.1808
REMARK 3 T33: -0.1913 T12: 0.0408
REMARK 3 T13: -0.0357 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 2.3079 L22: 3.1053
REMARK 3 L33: 2.8972 L12: 0.4225
REMARK 3 L13: -0.2393 L23: 0.4154
REMARK 3 S TENSOR
REMARK 3 S11: -0.0353 S12: 0.0295 S13: -0.2351
REMARK 3 S21: 0.1703 S22: 0.0320 S23: 0.1140
REMARK 3 S31: 0.0657 S32: 0.0681 S33: 0.0033
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2FIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-06.
REMARK 100 THE RCSB ID CODE IS RCSB035930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SBCCOLLECT
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35601
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 97.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M (NH4)2SO4, 0.1M TRIS PH8.5, 25%
REMARK 280 P 5K MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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 70.31000
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 70.31000
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
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 SER A 2
REMARK 465 ARG A 3
REMARK 465 THR A 4
REMARK 465 ILE A 5
REMARK 465 LEU A 6
REMARK 465 GLN A 7
REMARK 465 PRO A 8
REMARK 465 GLY A 9
REMARK 465 GLN A 10
REMARK 465 ILE A 11
REMARK 465 GLU A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ASN A 16
REMARK 465 ILE A 17
REMARK 465 PRO A 18
REMARK 465 GLY A 200
REMARK 465 GLY A 201
REMARK 465 LYS A 202
REMARK 465 GLU A 203
REMARK 465 ASP A 242
REMARK 465 GLU A 309
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 THR B 4
REMARK 465 ILE B 5
REMARK 465 LEU B 6
REMARK 465 GLN B 7
REMARK 465 PRO B 8
REMARK 465 GLY B 9
REMARK 465 GLN B 10
REMARK 465 ILE B 11
REMARK 465 GLU B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 ASN B 16
REMARK 465 ILE B 17
REMARK 465 GLU B 172
REMARK 465 GLU B 180
REMARK 465 SER B 181
REMARK 465 GLY B 200
REMARK 465 GLY B 201
REMARK 465 LYS B 202
REMARK 465 GLU B 203
REMARK 465 GLU B 240
REMARK 465 HIS B 241
REMARK 465 ASP B 242
REMARK 465 GLU B 309
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 SER A 231 OG
REMARK 470 GLU B 230 CG CD OE1 OE2
REMARK 470 SER B 231 OG
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 DISTANCE
REMARK 500 O GLU A 180 O HOH A 422 1.93
REMARK 500 O HIS A 233 O HOH A 602 2.09
REMARK 500
REMARK 500 REMARK: NULL
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 THR A 255 C THR A 255 O -0.140
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 ARG A 133 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 LEU A 148 CA - CB - CG ANGL. DEV. = 15.3 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 ALA A 89 114.06 -37.84
REMARK 500 GLU A 172 52.62 70.36
REMARK 500 SER A 181 59.44 -142.10
REMARK 500 ILE A 223 47.80 -108.99
REMARK 500 HIS A 227 -77.69 -108.69
REMARK 500 HIS A 233 97.80 -41.74
REMARK 500 ASP A 271 105.16 -161.17
REMARK 500 ALA B 89 112.09 -35.69
REMARK 500 ALA B 114 -87.53 -72.84
REMARK 500 ILE B 223 57.10 -109.95
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 LEU A 171 GLU A 172 48.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR A 255 10.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 185 SG
REMARK 620 2 CYS A 211 SG 109.1
REMARK 620 3 CYS A 214 SG 104.5 111.7
REMARK 620 4 CYS A 188 SG 114.1 94.9 122.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 402 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 185 SG
REMARK 620 2 CYS B 188 SG 115.7
REMARK 620 3 CYS B 211 SG 107.8 93.6
REMARK 620 4 CYS B 214 SG 106.5 121.8 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 403 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 259 SG
REMARK 620 2 CYS A 225 SG 102.7
REMARK 620 3 CYS A 256 SG 112.2 104.8
REMARK 620 4 CYS A 228 SG 123.9 104.2 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 404 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 228 SG
REMARK 620 2 CYS B 259 SG 64.1
REMARK 620 3 CYS B 256 SG 118.2 116.9
REMARK 620 4 CYS B 225 SG 127.8 100.9 113.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 405 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 20 NE2
REMARK 620 2 HIS B 22 NE2 105.6
REMARK 620 3 HIS B 219 NE2 118.1 113.0
REMARK 620 4 GLU B 173 OE1 100.1 130.9 89.4
REMARK 620 5 GLU B 173 OE2 129.8 82.1 102.6 49.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC5764 RELATED DB: TARGETDB
DBREF 2FIY A 1 309 UNP Q9HV00 FDHE_PSEAE 1 309
DBREF 2FIY B 1 309 UNP Q9HV00 FDHE_PSEAE 1 309
SEQRES 1 A 309 MET SER ARG THR ILE LEU GLN PRO GLY GLN ILE GLU ALA
SEQRES 2 A 309 ALA ALA ASN ILE PRO PRO HIS LEU HIS GLN PRO SER ARG
SEQRES 3 A 309 ASP LEU PHE ALA ARG ARG GLY GLU ARG LEU LEU GLN LEU
SEQRES 4 A 309 ALA GLU GLY HIS PRO MET GLY ASP TYR LEU ARG LEU VAL
SEQRES 5 A 309 ALA GLY LEU CYS ARG LEU GLN GLN ALA LEU LEU ASP ASN
SEQRES 6 A 309 PRO PRO ALA LEU ALA PRO LEU ASP PRO GLU ARG LEU ARG
SEQRES 7 A 309 LYS SER ARG GLU HIS GLY MET PRO PRO LEU ALA TYR ASP
SEQRES 8 A 309 LEU LEU VAL ARG GLU GLY ALA TRP LEU PRO TRP LEU ASP
SEQRES 9 A 309 ALA LEU LEU ALA GLY TYR PRO ALA PRO ALA ASN ALA ALA
SEQRES 10 A 309 VAL GLY ALA ALA LEU GLU GLN LEU ARG GLU ALA GLU GLU
SEQRES 11 A 309 GLY GLN ARG LYS ALA TRP ALA ILE ALA LEU LEU SER GLY
SEQRES 12 A 309 GLN PHE ASP LEU LEU PRO ALA ALA LEU VAL PRO PHE LEU
SEQRES 13 A 309 GLY ALA ALA LEU GLN VAL ALA TRP SER HIS TRP LEU LEU
SEQRES 14 A 309 GLY LEU GLU GLU GLY ALA VAL VAL GLU THR GLU SER ARG
SEQRES 15 A 309 THR LEU CYS PRO ALA CYS GLY SER PRO PRO MET ALA GLY
SEQRES 16 A 309 MET ILE ARG GLN GLY GLY LYS GLU THR GLY LEU ARG TYR
SEQRES 17 A 309 LEU SER CYS SER LEU CYS ALA CYS GLU TRP HIS TYR VAL
SEQRES 18 A 309 ARG ILE LYS CYS SER HIS CYS GLU GLU SER LYS HIS LEU
SEQRES 19 A 309 ALA TYR LEU SER LEU GLU HIS ASP GLY GLN PRO ALA GLU
SEQRES 20 A 309 LYS ALA VAL LEU ARG ALA GLU THR CYS PRO SER CYS GLN
SEQRES 21 A 309 GLY TYR LEU LYS GLN PHE TYR LEU GLU PHE ASP ARG HIS
SEQRES 22 A 309 ALA ASP ALA LEU ALA ASP ASP LEU ALA SER LEU ALA LEU
SEQRES 23 A 309 ASP MET ARG LEU ALA GLU ASP GLY TYR LEU ARG ARG SER
SEQRES 24 A 309 PRO ASN LEU LEU LEU ALA PRO GLY GLY GLU
SEQRES 1 B 309 MET SER ARG THR ILE LEU GLN PRO GLY GLN ILE GLU ALA
SEQRES 2 B 309 ALA ALA ASN ILE PRO PRO HIS LEU HIS GLN PRO SER ARG
SEQRES 3 B 309 ASP LEU PHE ALA ARG ARG GLY GLU ARG LEU LEU GLN LEU
SEQRES 4 B 309 ALA GLU GLY HIS PRO MET GLY ASP TYR LEU ARG LEU VAL
SEQRES 5 B 309 ALA GLY LEU CYS ARG LEU GLN GLN ALA LEU LEU ASP ASN
SEQRES 6 B 309 PRO PRO ALA LEU ALA PRO LEU ASP PRO GLU ARG LEU ARG
SEQRES 7 B 309 LYS SER ARG GLU HIS GLY MET PRO PRO LEU ALA TYR ASP
SEQRES 8 B 309 LEU LEU VAL ARG GLU GLY ALA TRP LEU PRO TRP LEU ASP
SEQRES 9 B 309 ALA LEU LEU ALA GLY TYR PRO ALA PRO ALA ASN ALA ALA
SEQRES 10 B 309 VAL GLY ALA ALA LEU GLU GLN LEU ARG GLU ALA GLU GLU
SEQRES 11 B 309 GLY GLN ARG LYS ALA TRP ALA ILE ALA LEU LEU SER GLY
SEQRES 12 B 309 GLN PHE ASP LEU LEU PRO ALA ALA LEU VAL PRO PHE LEU
SEQRES 13 B 309 GLY ALA ALA LEU GLN VAL ALA TRP SER HIS TRP LEU LEU
SEQRES 14 B 309 GLY LEU GLU GLU GLY ALA VAL VAL GLU THR GLU SER ARG
SEQRES 15 B 309 THR LEU CYS PRO ALA CYS GLY SER PRO PRO MET ALA GLY
SEQRES 16 B 309 MET ILE ARG GLN GLY GLY LYS GLU THR GLY LEU ARG TYR
SEQRES 17 B 309 LEU SER CYS SER LEU CYS ALA CYS GLU TRP HIS TYR VAL
SEQRES 18 B 309 ARG ILE LYS CYS SER HIS CYS GLU GLU SER LYS HIS LEU
SEQRES 19 B 309 ALA TYR LEU SER LEU GLU HIS ASP GLY GLN PRO ALA GLU
SEQRES 20 B 309 LYS ALA VAL LEU ARG ALA GLU THR CYS PRO SER CYS GLN
SEQRES 21 B 309 GLY TYR LEU LYS GLN PHE TYR LEU GLU PHE ASP ARG HIS
SEQRES 22 B 309 ALA ASP ALA LEU ALA ASP ASP LEU ALA SER LEU ALA LEU
SEQRES 23 B 309 ASP MET ARG LEU ALA GLU ASP GLY TYR LEU ARG ARG SER
SEQRES 24 B 309 PRO ASN LEU LEU LEU ALA PRO GLY GLY GLU
HET FE A 401 1
HET FE B 402 1
HET FE A 403 1
HET FE B 404 1
HET FE B 405 1
HETNAM FE FE (III) ION
FORMUL 3 FE 5(FE 3+)
FORMUL 8 HOH *369(H2 O)
HELIX 1 1 ASP A 27 GLU A 41 1 15
HELIX 2 2 MET A 45 ASP A 64 1 20
HELIX 3 3 ASP A 73 HIS A 83 1 11
HELIX 4 4 ALA A 89 GLY A 97 1 9
HELIX 5 5 TRP A 99 GLY A 109 1 11
HELIX 6 6 ASN A 115 ALA A 128 1 14
HELIX 7 7 GLU A 129 SER A 142 1 14
HELIX 8 8 GLN A 144 LEU A 148 5 5
HELIX 9 9 PRO A 149 ALA A 151 5 3
HELIX 10 10 LEU A 152 GLY A 170 1 19
HELIX 11 11 ASP A 275 ALA A 282 1 8
HELIX 12 12 SER A 283 ASP A 293 1 11
HELIX 13 13 ASP B 27 GLU B 41 1 15
HELIX 14 14 MET B 45 ASN B 65 1 21
HELIX 15 15 ASP B 73 HIS B 83 1 11
HELIX 16 16 ALA B 89 GLY B 97 1 9
HELIX 17 17 TRP B 99 GLY B 109 1 11
HELIX 18 18 ASN B 115 ALA B 128 1 14
HELIX 19 19 GLU B 129 SER B 142 1 14
HELIX 20 20 GLY B 143 LEU B 148 5 6
HELIX 21 21 PRO B 149 ALA B 151 5 3
HELIX 22 22 LEU B 152 GLY B 170 1 19
HELIX 23 23 PRO B 245 ALA B 249 5 5
HELIX 24 24 ASP B 275 ALA B 282 1 8
HELIX 25 25 SER B 283 ASP B 293 1 11
SHEET 1 A 7 LEU A 21 HIS A 22 0
SHEET 2 A 7 GLU A 217 HIS A 219 -1 O GLU A 217 N HIS A 22
SHEET 3 A 7 LEU A 206 CYS A 211 -1 N LEU A 209 O TRP A 218
SHEET 4 A 7 PRO A 192 ARG A 198 -1 N MET A 193 O SER A 210
SHEET 5 A 7 GLY A 261 TYR A 267 1 O PHE A 266 N ILE A 197
SHEET 6 A 7 LEU A 251 GLU A 254 -1 N GLU A 254 O LEU A 263
SHEET 7 A 7 TYR A 236 LEU A 237 -1 N LEU A 237 O ALA A 253
SHEET 1 B 6 LEU A 21 HIS A 22 0
SHEET 2 B 6 GLU A 217 HIS A 219 -1 O GLU A 217 N HIS A 22
SHEET 3 B 6 LEU A 206 CYS A 211 -1 N LEU A 209 O TRP A 218
SHEET 4 B 6 PRO A 192 ARG A 198 -1 N MET A 193 O SER A 210
SHEET 5 B 6 GLY A 261 TYR A 267 1 O PHE A 266 N ILE A 197
SHEET 6 B 6 LEU A 296 ARG A 297 1 O LEU A 296 N TYR A 262
SHEET 1 C 6 GLU B 217 HIS B 219 0
SHEET 2 C 6 LEU B 206 CYS B 211 -1 N LEU B 209 O TRP B 218
SHEET 3 C 6 PRO B 192 ARG B 198 -1 N MET B 196 O TYR B 208
SHEET 4 C 6 GLY B 261 TYR B 267 1 O PHE B 266 N ILE B 197
SHEET 5 C 6 LEU B 251 CYS B 256 -1 N GLU B 254 O LEU B 263
SHEET 6 C 6 ALA B 235 LEU B 237 -1 N LEU B 237 O ALA B 253
SHEET 1 D 5 GLU B 217 HIS B 219 0
SHEET 2 D 5 LEU B 206 CYS B 211 -1 N LEU B 209 O TRP B 218
SHEET 3 D 5 PRO B 192 ARG B 198 -1 N MET B 196 O TYR B 208
SHEET 4 D 5 GLY B 261 TYR B 267 1 O PHE B 266 N ILE B 197
SHEET 5 D 5 LEU B 296 ARG B 297 1 O LEU B 296 N TYR B 262
SSBOND 1 CYS B 228 CYS B 259 1555 1555 2.08
LINK FE FE A 401 SG CYS A 185 1555 1555 2.28
LINK FE FE B 402 SG CYS B 185 1555 1555 2.30
LINK FE FE A 403 SG CYS A 259 1555 1555 1.89
LINK FE FE B 404 SG CYS B 228 1555 1555 2.13
LINK FE FE B 404 SG CYS B 259 1555 1555 1.74
LINK FE FE B 405 NE2 HIS B 20 1555 1555 2.10
LINK FE FE B 405 NE2 HIS B 22 1555 1555 2.06
LINK FE FE B 405 NE2 HIS B 219 1555 1555 2.09
LINK FE FE A 401 SG CYS A 211 1555 1555 2.38
LINK FE FE A 401 SG CYS A 214 1555 1555 2.32
LINK FE FE A 401 SG CYS A 188 1555 1555 2.35
LINK FE FE A 403 SG CYS A 225 1555 1555 2.63
LINK FE FE A 403 SG CYS A 256 1555 1555 2.41
LINK FE FE A 403 SG CYS A 228 1555 1555 2.45
LINK FE FE B 402 SG CYS B 188 1555 1555 2.39
LINK FE FE B 402 SG CYS B 211 1555 1555 2.40
LINK FE FE B 402 SG CYS B 214 1555 1555 2.35
LINK FE FE B 404 SG CYS B 256 1555 1555 2.41
LINK FE FE B 404 SG CYS B 225 1555 1555 2.41
LINK FE FE B 405 OE1 GLU B 173 1555 4566 2.73
LINK FE FE B 405 OE2 GLU B 173 1555 4566 2.40
CISPEP 1 PRO A 306 GLY A 307 0 9.66
CISPEP 2 GLY A 307 GLY A 308 0 -1.04
CISPEP 3 PRO B 306 GLY B 307 0 -4.08
CISPEP 4 GLY B 307 GLY B 308 0 19.03
SITE 1 AC1 4 CYS A 185 CYS A 188 CYS A 211 CYS A 214
SITE 1 AC2 4 CYS B 185 CYS B 188 CYS B 211 CYS B 214
SITE 1 AC3 4 CYS A 225 CYS A 228 CYS A 256 CYS A 259
SITE 1 AC4 4 CYS B 225 CYS B 228 CYS B 256 CYS B 259
SITE 1 AC5 4 HIS B 20 HIS B 22 GLU B 173 HIS B 219
CRYST1 46.261 96.617 140.620 90.00 90.00 90.00 P 2 2 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 0.021616 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010350 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007111 0.00000
(ATOM LINES ARE NOT SHOWN.)
END