HEADER OXYGEN STORAGE/TRANSPORT 24-JAN-00 1DW0
TITLE STRUCTURE OF OXIDIZED SHP, AN OXYGEN BINDING CYTOCHROME C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A, B, C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 3 ORGANISM_TAXID: 1063
KEYWDS CYTOCHROME C, ASPARAGINE LIGATION, OXYGEN BINDING, DISULFIDE BRIDGE,
KEYWDS 2 OXYGEN STORAGE-TRANSPORT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.LEYS,K.BACKERS,T.E.MEYER,W.R.HAGEN,M.A.CUSANOVICH,J.J.VAN BEEUMEN
REVDAT 4 03-MAR-21 1DW0 1 COMPND REMARK HET HETNAM
REVDAT 4 2 1 HETSYN FORMUL LINK SITE
REVDAT 4 3 1 ATOM
REVDAT 3 24-FEB-09 1DW0 1 VERSN
REVDAT 2 27-DEC-00 1DW0 1 REMARK
REVDAT 1 28-JUN-00 1DW0 0
JRNL AUTH D.LEYS,K.BACKERS,T.E.MEYER,W.R.HAGEN,M.A.CUSANOVICH,
JRNL AUTH 2 J.J.VAN BEEUMEN
JRNL TITL CRYSTAL STRUCTURES OF AN OXYGEN-BINDING CYTOCHROME C FROM
JRNL TITL 2 RHODOBACTER SPHAEROIDES.
JRNL REF J.BIOL.CHEM. V. 275 16050 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10821858
JRNL DOI 10.1074/JBC.275.21.16050
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 45463
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2273
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2390
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 139
REMARK 3 SOLVENT ATOMS : 424
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DW0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010424.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-98
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : DW32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45463
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
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: NULL
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+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 -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 0.00000
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 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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.67250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.74900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.83000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.67250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.74900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.83000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.67250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.74900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.83000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.67250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.74900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.83000
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: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 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 GLU A 23 CG CD OE1 OE2
REMARK 470 THR A 34 OG1 CG2
REMARK 470 LYS A 37 CE NZ
REMARK 470 ARG A 53 NE CZ NH1 NH2
REMARK 470 GLY B 1 N
REMARK 470 LYS B 37 CD CE NZ
REMARK 470 ARG B 58 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 61 CG CD CE NZ
REMARK 470 LYS B 83 CE NZ
REMARK 470 LYS C 37 CD CE NZ
REMARK 470 LYS C 61 CG CD CE NZ
REMARK 470 GLU C 62 CD OE1 OE2
REMARK 470 LYS C 83 CE NZ
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 PRO C 72 O HOH C 262 2.08
REMARK 500
REMARK 500 REMARK: NULL
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 OE1 GLU B 62 O HOH A 569 4556 2.16
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 GLN A 56 CB - CG - CD ANGL. DEV. = 21.6 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 80 CD - NE - CZ ANGL. DEV. = 23.9 DEGREES
REMARK 500 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 80 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 GLY B 1 O - C - N ANGL. DEV. = -10.0 DEGREES
REMARK 500 ASP B 2 C - N - CA ANGL. DEV. = 20.4 DEGREES
REMARK 500 ARG B 26 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 53 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 74 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP B 96 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 THR C 44 N - CA - CB ANGL. DEV. = -14.9 DEGREES
REMARK 500 ASP C 77 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG C 80 CD - NE - CZ ANGL. DEV. = 17.2 DEGREES
REMARK 500 ARG C 80 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP C 96 CB - CG - OD1 ANGL. DEV. = 7.6 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 ASP B 2 -20.97 122.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 602 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH B 654 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 658 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH C 117 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH C 194 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH C 205 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH C 214 DISTANCE = 6.18 ANGSTROMS
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 HEC A 113 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 47 NE2
REMARK 620 2 HEC A 113 NA 97.0
REMARK 620 3 HEC A 113 NB 91.0 88.7
REMARK 620 4 HEC A 113 NC 86.4 176.4 90.2
REMARK 620 5 HEC A 113 ND 90.6 91.3 178.4 89.7
REMARK 620 6 ASN A 88 ND2 173.1 89.3 86.3 87.3 92.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 113 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 47 NE2
REMARK 620 2 HEC B 113 NA 95.2
REMARK 620 3 HEC B 113 NB 91.0 89.0
REMARK 620 4 HEC B 113 NC 87.1 177.6 90.2
REMARK 620 5 HEC B 113 ND 91.1 90.4 177.9 90.3
REMARK 620 6 ASN B 88 ND2 174.5 89.7 86.3 88.0 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC C 113 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 47 NE2
REMARK 620 2 HEC C 113 NA 98.1
REMARK 620 3 HEC C 113 NB 91.1 90.2
REMARK 620 4 HEC C 113 NC 84.1 177.8 89.5
REMARK 620 5 HEC C 113 ND 91.4 89.5 177.5 90.8
REMARK 620 6 ASN C 88 ND2 170.0 91.4 85.6 86.5 91.9
REMARK 620 N 1 2 3 4 5
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 113
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 113
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC C 113
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DW1 RELATED DB: PDB
REMARK 900 STRUCTURE OF CYANIDE COMPLEX OF SHP
REMARK 900 RELATED ID: 1DW2 RELATED DB: PDB
REMARK 900 STRUCTURE OF NITRIC OXIDE COMPLEX OF REDUCED SHP
REMARK 900 RELATED ID: 1DW3 RELATED DB: PDB
REMARK 900 STRUCTURE OF REDUCED SHP
DBREF 1DW0 A 1 112 UNP P81238 SHP_RHOS4 1 112
DBREF 1DW0 B 1 112 UNP P81238 SHP_RHOS4 1 112
DBREF 1DW0 C 1 112 UNP P81238 SHP_RHOS4 1 112
SEQRES 1 A 112 GLY ASP THR SER PRO ALA GLN LEU ILE ALA GLY TYR GLU
SEQRES 2 A 112 ALA ALA ALA GLY ALA PRO ALA ASP ALA GLU ARG GLY ARG
SEQRES 3 A 112 ALA LEU PHE LEU SER THR GLN THR GLY GLY LYS PRO ASP
SEQRES 4 A 112 THR PRO SER CYS THR THR CYS HIS GLY ALA ASP VAL THR
SEQRES 5 A 112 ARG ALA GLY GLN THR ARG THR GLY LYS GLU ILE ALA PRO
SEQRES 6 A 112 LEU ALA PRO SER ALA THR PRO ASP ARG PHE THR ASP SER
SEQRES 7 A 112 ALA ARG VAL GLU LYS TRP LEU GLY ARG ASN CYS ASN SER
SEQRES 8 A 112 VAL ILE GLY ARG ASP CYS THR PRO GLY GLU LYS ALA ASP
SEQRES 9 A 112 LEU LEU ALA TRP LEU ALA ALA GLN
SEQRES 1 B 112 GLY ASP THR SER PRO ALA GLN LEU ILE ALA GLY TYR GLU
SEQRES 2 B 112 ALA ALA ALA GLY ALA PRO ALA ASP ALA GLU ARG GLY ARG
SEQRES 3 B 112 ALA LEU PHE LEU SER THR GLN THR GLY GLY LYS PRO ASP
SEQRES 4 B 112 THR PRO SER CYS THR THR CYS HIS GLY ALA ASP VAL THR
SEQRES 5 B 112 ARG ALA GLY GLN THR ARG THR GLY LYS GLU ILE ALA PRO
SEQRES 6 B 112 LEU ALA PRO SER ALA THR PRO ASP ARG PHE THR ASP SER
SEQRES 7 B 112 ALA ARG VAL GLU LYS TRP LEU GLY ARG ASN CYS ASN SER
SEQRES 8 B 112 VAL ILE GLY ARG ASP CYS THR PRO GLY GLU LYS ALA ASP
SEQRES 9 B 112 LEU LEU ALA TRP LEU ALA ALA GLN
SEQRES 1 C 112 GLY ASP THR SER PRO ALA GLN LEU ILE ALA GLY TYR GLU
SEQRES 2 C 112 ALA ALA ALA GLY ALA PRO ALA ASP ALA GLU ARG GLY ARG
SEQRES 3 C 112 ALA LEU PHE LEU SER THR GLN THR GLY GLY LYS PRO ASP
SEQRES 4 C 112 THR PRO SER CYS THR THR CYS HIS GLY ALA ASP VAL THR
SEQRES 5 C 112 ARG ALA GLY GLN THR ARG THR GLY LYS GLU ILE ALA PRO
SEQRES 6 C 112 LEU ALA PRO SER ALA THR PRO ASP ARG PHE THR ASP SER
SEQRES 7 C 112 ALA ARG VAL GLU LYS TRP LEU GLY ARG ASN CYS ASN SER
SEQRES 8 C 112 VAL ILE GLY ARG ASP CYS THR PRO GLY GLU LYS ALA ASP
SEQRES 9 C 112 LEU LEU ALA TRP LEU ALA ALA GLN
HET SO4 A 500 5
HET HEC A 113 45
HET SO4 B 600 5
HET HEC B 113 43
HET HEC C 113 43
HETNAM SO4 SULFATE ION
HETNAM HEC HEME C
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 HEC 3(C34 H34 FE N4 O4)
FORMUL 9 HOH *424(H2 O)
HELIX 1 1 SER A 4 GLY A 17 1 14
HELIX 2 2 ASP A 21 SER A 31 1 11
HELIX 3 3 CYS A 43 GLY A 48 1 6
HELIX 4 4 ASP A 77 GLY A 94 1 18
HELIX 5 5 THR A 98 ALA A 111 1 14
HELIX 6 6 SER B 4 GLY B 17 1 14
HELIX 7 7 ASP B 21 SER B 31 1 11
HELIX 8 8 CYS B 43 GLY B 48 1 6
HELIX 9 9 ASP B 77 GLY B 94 1 18
HELIX 10 10 THR B 98 ALA B 111 1 14
HELIX 11 11 SER C 4 GLY C 17 1 14
HELIX 12 12 ASP C 21 SER C 31 1 11
HELIX 13 13 CYS C 43 GLY C 48 1 6
HELIX 14 14 ASP C 77 GLY C 94 1 18
HELIX 15 15 THR C 98 ALA C 111 1 14
SHEET 1 A 2 GLY A 55 GLN A 56 0
SHEET 2 A 2 GLU A 62 ILE A 63 -1 O ILE A 63 N GLY A 55
SHEET 1 B 2 GLY B 55 GLN B 56 0
SHEET 2 B 2 GLU B 62 ILE B 63 -1 O ILE B 63 N GLY B 55
SHEET 1 C 2 GLY C 55 GLN C 56 0
SHEET 2 C 2 GLU C 62 ILE C 63 -1 O ILE C 63 N GLY C 55
SSBOND 1 CYS A 89 CYS A 97 1555 1555 1.98
SSBOND 2 CYS B 89 CYS B 97 1555 1555 1.98
SSBOND 3 CYS C 89 CYS C 97 1555 1555 1.99
LINK SG CYS A 43 CAB HEC A 113 1555 1555 1.95
LINK SG CYS A 46 CAC HEC A 113 1555 1555 2.07
LINK SG CYS B 43 CAB HEC B 113 1555 1555 1.95
LINK SG CYS B 46 CAC HEC B 113 1555 1555 2.05
LINK SG CYS C 43 CAB HEC C 113 1555 1555 1.89
LINK SG CYS C 46 CAC HEC C 113 1555 1555 2.06
LINK NE2 HIS A 47 FE HEC A 113 1555 1555 2.14
LINK ND2 ASN A 88 FE HEC A 113 1555 1555 2.20
LINK NE2 HIS B 47 FE HEC B 113 1555 1555 2.15
LINK ND2 ASN B 88 FE HEC B 113 1555 1555 2.15
LINK NE2 HIS C 47 FE HEC C 113 1555 1555 2.10
LINK ND2 ASN C 88 FE HEC C 113 1555 1555 2.09
SITE 1 AC1 6 ARG A 87 SER A 91 HOH A 544 HOH A 564
SITE 2 AC1 6 HOH A 592 HOH A 593
SITE 1 AC2 6 ARG B 87 ASN B 88 SER B 91 HEC B 113
SITE 2 AC2 6 HOH B 614 HOH B 692
SITE 1 AC3 15 CYS A 43 CYS A 46 HIS A 47 ARG A 74
SITE 2 AC3 15 PHE A 75 ARG A 80 VAL A 81 TRP A 84
SITE 3 AC3 15 ASN A 88 VAL A 92 HOH A 510 HOH A 527
SITE 4 AC3 15 HOH A 552 HOH A 561 HOH A 612
SITE 1 AC4 15 CYS B 43 CYS B 46 HIS B 47 ARG B 74
SITE 2 AC4 15 PHE B 75 ARG B 80 VAL B 81 TRP B 84
SITE 3 AC4 15 ASN B 88 VAL B 92 LEU B 105 SO4 B 600
SITE 4 AC4 15 HOH B 609 HOH B 622 HOH B 668
SITE 1 AC5 15 CYS C 43 CYS C 46 HIS C 47 ARG C 58
SITE 2 AC5 15 ILE C 63 ARG C 74 PHE C 75 ARG C 80
SITE 3 AC5 15 VAL C 81 TRP C 84 ASN C 88 HOH C 135
SITE 4 AC5 15 HOH C 150 HOH C 182 HOH C 242
CRYST1 83.345 103.498 113.660 90.00 90.00 90.00 I 2 2 2 24
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 0.012000 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009660 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008800 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
