HEADER PHOTOSYNTHESIS 09-JUN-04 1TKW
TITLE THE TRANSIENT COMPLEX OF POPLAR PLASTOCYANIN WITH TURNIP CYTOCHROME F
TITLE 2 DETERMINED WITH PARAMAGNETIC NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASTOCYANIN A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CYTOCHROME F;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: POPULUS NIGRA;
SOURCE 3 ORGANISM_TAXID: 3691;
SOURCE 4 GENE: PETE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETPC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: BRASSICA RAPA SUBSP. RAPA;
SOURCE 12 ORGANISM_COMMON: TURNIP;
SOURCE 13 ORGANISM_TAXID: 51350;
SOURCE 14 STRAIN: SUBSP. RAPA;
SOURCE 15 GENE: PETA;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K12 SUBSTR. W3110;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 316407;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: W3110;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PTC1
KEYWDS ELECTRON TRANSFER, PHOTOSYNTHESIS, PARAMAGNETIC, RIGID BODY
KEYWDS 2 CALCULATIONS
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.LANGE,T.CORNVIK,I.DIAZ-MORENO,M.UBBINK
REVDAT 3 02-MAR-22 1TKW 1 REMARK LINK
REVDAT 2 24-FEB-09 1TKW 1 VERSN
REVDAT 1 24-MAY-05 1TKW 0
JRNL AUTH C.LANGE,T.CORNVIK,I.DIAZ-MORENO,M.UBBINK
JRNL TITL THE TRANSIENT COMPLEX OF POPLAR PLASTOCYANIN WITH CYTOCHROME
JRNL TITL 2 F: EFFECTS OF IONIC STRENGTH AND PH
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1707 179 2005
JRNL REFN ISSN 0006-3002
JRNL PMID 15863096
JRNL DOI 10.1016/J.BBABIO.2004.12.002
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AZARA 2.7, X-PLOR XPLOR-NIH 2.9.1
REMARK 3 AUTHORS : W. BOUCHER (AZARA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 38 CHEMICAL SHIFT PERTURBATION
REMARK 3 RESTRAINTS, 42 PSEUDOCONTACT SHIFTS RESTRAINTS, 42 PSEUDOCONTACT
REMARK 3 ANGLE RESTRAINTS, 120 MINIMAL DISTANCE RESTRAINTS AND 4
REMARK 3 ELECTROSTATIC RESTRAINTS.
REMARK 3 BACKBONE RMSD (IN ANGSTROM) WITH THE MEAN FOR EACH MODEL:
REMARK 3 1: 1.28,
REMARK 3 2: 2.26,
REMARK 3 3: 1.29,
REMARK 3 4: 3.12,
REMARK 3 5: 1.52,
REMARK 3 6: 1.49,
REMARK 3 7: 3.68,
REMARK 3 8: 2.68,
REMARK 3 9: 1.58,
REMARK 3 10: 3.43,
REMARK 3 AVERAGE=2.23+/-0.88
REMARK 4
REMARK 4 1TKW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022733.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 10 MM; 11 MM
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5 MM CD-SUBSTITUTED POPLAR
REMARK 210 PLASTOCYANIN + 0.35 MM SOLUBLE
REMARK 210 FRAGMENT OF TURNIP CYTOCHROME F
REMARK 210 IN OXIDIZED STATE IN 10 MM
REMARK 210 SODIUM PHOSPHATE PH 6.0; 0.5 MM
REMARK 210 CD-SUBSTITUTED POPLAR
REMARK 210 PLASTOCYANIN + 0.35 MM SOLUBLE
REMARK 210 FRAGMENT OF TURNIP CYTOCHROME F
REMARK 210 IN REDUCED STATE IN 10 MM SODIUM
REMARK 210 PHOSPHATE PH 6.0 + 1 MM SODIUM
REMARK 210 ASCORBATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG ANSIG-FOR-WINDOWS 1.02, X
REMARK 210 -PLOR XPLOR-NIH 2.9.1
REMARK 210 METHOD USED : RIGID BODY DOCKING USING
REMARK 210 INTERMOLECULAR PSEUDOCONTACT
REMARK 210 SHIFTS RESTRAINTS, CHEMICAL
REMARK 210 SHIFT PERTURBATION RESTRAINTS
REMARK 210 AND ELECTROSTATIC RESTRAINTS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 104
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING THE XRD STRUCTURES OF
REMARK 210 PLASTOCYANIN AND CYTOCHROME F, DOCKED ON THE BASIS OF
REMARK 210 INTERMOLECULAR PSEUDOCONTACT SHIFTS AND CHEMICAL SHIFT
REMARK 210 PERTURBATIONS DUE TO BINDING.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 VAL B 251
REMARK 465 GLN B 252
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HA3 GLY A 89 HBD2 HEC B 253 1.27
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 2 CYS B 21 CB CYS B 21 SG -0.117
REMARK 500 2 CYS B 24 CB CYS B 24 SG -0.096
REMARK 500 3 CYS B 21 CB CYS B 21 SG -0.097
REMARK 500 5 CYS B 21 CB CYS B 21 SG -0.106
REMARK 500 6 CYS B 21 CB CYS B 21 SG -0.112
REMARK 500 10 CYS B 21 CB CYS B 21 SG -0.115
REMARK 500 10 CYS B 24 CB CYS B 24 SG -0.101
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 1 VAL B 20 -9.23 -57.45
REMARK 500 1 ALA B 62 -8.80 -59.16
REMARK 500 1 ASN B 99 43.21 -146.86
REMARK 500 1 TYR B 123 56.83 -119.90
REMARK 500 1 LEU B 249 -129.80 -110.72
REMARK 500 2 ASN B 8 26.10 -141.23
REMARK 500 2 ALA B 62 -5.10 -58.33
REMARK 500 2 ASN B 99 43.84 -149.60
REMARK 500 2 TYR B 123 50.78 -117.61
REMARK 500 2 ASN B 138 108.26 -160.92
REMARK 500 2 LEU B 249 -128.97 -111.13
REMARK 500 3 ASN B 8 26.54 -140.99
REMARK 500 3 ALA B 62 -8.23 -56.66
REMARK 500 3 ASN B 99 44.01 -149.60
REMARK 500 3 TYR B 123 50.66 -117.49
REMARK 500 3 ASN B 138 108.20 -160.90
REMARK 500 3 LEU B 249 -128.84 -111.03
REMARK 500 4 ASN B 8 26.37 -140.86
REMARK 500 4 ASN B 99 44.11 -149.52
REMARK 500 4 TYR B 123 50.66 -117.62
REMARK 500 4 ASN B 138 108.09 -160.96
REMARK 500 4 LEU B 249 -128.83 -111.14
REMARK 500 5 ASN B 8 26.34 -141.09
REMARK 500 5 ALA B 62 -3.97 -55.05
REMARK 500 5 ASN B 99 44.04 -149.63
REMARK 500 5 TYR B 123 50.65 -117.49
REMARK 500 5 ASN B 138 108.24 -160.87
REMARK 500 5 LEU B 249 -128.90 -111.12
REMARK 500 6 ASN B 8 26.21 -141.07
REMARK 500 6 ALA B 62 -8.06 -58.00
REMARK 500 6 ASN B 99 43.92 -149.58
REMARK 500 6 TYR B 123 50.67 -117.47
REMARK 500 6 ASN B 138 108.20 -160.87
REMARK 500 6 LEU B 249 -128.96 -111.02
REMARK 500 7 VAL B 20 -9.69 -57.14
REMARK 500 7 ALA B 62 -8.70 -59.25
REMARK 500 7 ASN B 99 39.57 -145.06
REMARK 500 7 TYR B 123 57.13 -116.80
REMARK 500 7 ASN B 168 43.83 -109.33
REMARK 500 7 LEU B 249 -133.27 -110.48
REMARK 500 8 ASN B 8 26.44 -141.06
REMARK 500 8 ALA B 62 -7.19 -57.78
REMARK 500 8 ASN B 99 44.17 -149.51
REMARK 500 8 TYR B 123 51.02 -117.87
REMARK 500 8 ASN B 138 108.17 -160.91
REMARK 500 8 LEU B 249 -128.71 -111.27
REMARK 500 9 VAL B 20 -9.41 -57.27
REMARK 500 9 ALA B 62 -8.66 -57.37
REMARK 500 9 ASN B 99 43.35 -147.33
REMARK 500 9 TYR B 123 55.38 -119.43
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG B 13 0.32 SIDE CHAIN
REMARK 500 1 ARG B 18 0.31 SIDE CHAIN
REMARK 500 1 ARG B 88 0.31 SIDE CHAIN
REMARK 500 1 ARG B 106 0.21 SIDE CHAIN
REMARK 500 1 ARG B 154 0.28 SIDE CHAIN
REMARK 500 1 ARG B 156 0.26 SIDE CHAIN
REMARK 500 1 ARG B 184 0.30 SIDE CHAIN
REMARK 500 1 ARG B 201 0.32 SIDE CHAIN
REMARK 500 1 ARG B 209 0.31 SIDE CHAIN
REMARK 500 1 ARG B 250 0.32 SIDE CHAIN
REMARK 500 2 ARG B 13 0.26 SIDE CHAIN
REMARK 500 2 ARG B 18 0.26 SIDE CHAIN
REMARK 500 2 ARG B 88 0.23 SIDE CHAIN
REMARK 500 2 ARG B 106 0.10 SIDE CHAIN
REMARK 500 2 ARG B 154 0.25 SIDE CHAIN
REMARK 500 2 ARG B 156 0.22 SIDE CHAIN
REMARK 500 2 ARG B 184 0.25 SIDE CHAIN
REMARK 500 2 ARG B 201 0.26 SIDE CHAIN
REMARK 500 2 ARG B 209 0.30 SIDE CHAIN
REMARK 500 2 ARG B 250 0.28 SIDE CHAIN
REMARK 500 3 ARG B 13 0.31 SIDE CHAIN
REMARK 500 3 ARG B 18 0.28 SIDE CHAIN
REMARK 500 3 ARG B 88 0.27 SIDE CHAIN
REMARK 500 3 ARG B 106 0.13 SIDE CHAIN
REMARK 500 3 ARG B 154 0.26 SIDE CHAIN
REMARK 500 3 ARG B 156 0.23 SIDE CHAIN
REMARK 500 3 ARG B 184 0.26 SIDE CHAIN
REMARK 500 3 ARG B 201 0.28 SIDE CHAIN
REMARK 500 3 ARG B 209 0.31 SIDE CHAIN
REMARK 500 3 ARG B 250 0.30 SIDE CHAIN
REMARK 500 4 ARG B 13 0.30 SIDE CHAIN
REMARK 500 4 ARG B 18 0.30 SIDE CHAIN
REMARK 500 4 ARG B 88 0.29 SIDE CHAIN
REMARK 500 4 ARG B 106 0.16 SIDE CHAIN
REMARK 500 4 ARG B 154 0.27 SIDE CHAIN
REMARK 500 4 ARG B 156 0.23 SIDE CHAIN
REMARK 500 4 ARG B 184 0.28 SIDE CHAIN
REMARK 500 4 ARG B 201 0.30 SIDE CHAIN
REMARK 500 4 ARG B 209 0.27 SIDE CHAIN
REMARK 500 4 ARG B 250 0.32 SIDE CHAIN
REMARK 500 5 ARG B 13 0.29 SIDE CHAIN
REMARK 500 5 ARG B 18 0.27 SIDE CHAIN
REMARK 500 5 ARG B 88 0.26 SIDE CHAIN
REMARK 500 5 ARG B 106 0.12 SIDE CHAIN
REMARK 500 5 ARG B 154 0.25 SIDE CHAIN
REMARK 500 5 ARG B 156 0.22 SIDE CHAIN
REMARK 500 5 ARG B 184 0.25 SIDE CHAIN
REMARK 500 5 ARG B 201 0.27 SIDE CHAIN
REMARK 500 5 ARG B 209 0.27 SIDE CHAIN
REMARK 500 5 ARG B 250 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 97 PLANE DEVIATIONS.
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 CU A 100 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 37 ND1
REMARK 620 2 CYS A 84 SG 134.3
REMARK 620 3 HIS A 87 ND1 99.1 109.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 253 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 1 N
REMARK 620 2 HEC B 253 NA 91.3
REMARK 620 3 HEC B 253 NB 95.9 91.3
REMARK 620 4 HEC B 253 NC 88.6 179.5 88.2
REMARK 620 5 HEC B 253 ND 84.6 89.2 179.3 91.3
REMARK 620 6 HIS B 25 NE2 174.2 89.5 89.8 90.7 89.6
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 CU A 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 253
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HCZ RELATED DB: PDB
REMARK 900 CYTOCHROME F FROM BRASSICA RAPA (TURNIP)
REMARK 900 RELATED ID: 5PCY RELATED DB: PDB
REMARK 900 POPULUS SP. PLASTOCYANIN (CUI, PH 7)
REMARK 900 RELATED ID: 2PCF RELATED DB: PDB
REMARK 900 COMPLEX OF SPINACH PLASTOCYANIN AND TURNIP CYTOCHROME F DETERMINED
REMARK 900 WITH PARAMAGNETIC NMR
DBREF 1TKW A 1 99 UNP P00299 PLAS1_POPNI 70 168
DBREF 1TKW B 1 252 UNP P36438 CYF_BRARA 36 287
SEQRES 1 A 99 ILE ASP VAL LEU LEU GLY ALA ASP ASP GLY SER LEU ALA
SEQRES 2 A 99 PHE VAL PRO SER GLU PHE SER ILE SER PRO GLY GLU LYS
SEQRES 3 A 99 ILE VAL PHE LYS ASN ASN ALA GLY PHE PRO HIS ASN ILE
SEQRES 4 A 99 VAL PHE ASP GLU ASP SER ILE PRO SER GLY VAL ASP ALA
SEQRES 5 A 99 SER LYS ILE SER MET SER GLU GLU ASP LEU LEU ASN ALA
SEQRES 6 A 99 LYS GLY GLU THR PHE GLU VAL ALA LEU SER ASN LYS GLY
SEQRES 7 A 99 GLU TYR SER PHE TYR CYS SER PRO HIS GLN GLY ALA GLY
SEQRES 8 A 99 MET VAL GLY LYS VAL THR VAL ASN
SEQRES 1 B 252 TYR PRO ILE PHE ALA GLN GLN ASN TYR GLU ASN PRO ARG
SEQRES 2 B 252 GLU ALA THR GLY ARG ILE VAL CYS ALA ASN CYS HIS LEU
SEQRES 3 B 252 ALA SER LYS PRO VAL ASP ILE GLU VAL PRO GLN ALA VAL
SEQRES 4 B 252 LEU PRO ASP THR VAL PHE GLU ALA VAL VAL LYS ILE PRO
SEQRES 5 B 252 TYR ASP MET GLN LEU LYS GLN VAL LEU ALA ASN GLY LYS
SEQRES 6 B 252 LYS GLY ALA LEU ASN VAL GLY ALA VAL LEU ILE LEU PRO
SEQRES 7 B 252 GLU GLY PHE GLU LEU ALA PRO PRO ASP ARG ILE SER PRO
SEQRES 8 B 252 GLU MET LYS GLU LYS ILE GLY ASN LEU SER PHE GLN ASN
SEQRES 9 B 252 TYR ARG PRO ASN LYS LYS ASN ILE LEU VAL ILE GLY PRO
SEQRES 10 B 252 VAL PRO GLY GLN LYS TYR SER GLU ILE THR PHE PRO ILE
SEQRES 11 B 252 LEU ALA PRO ASP PRO ALA THR ASN LYS ASP VAL HIS PHE
SEQRES 12 B 252 LEU LYS TYR PRO ILE TYR VAL GLY GLY ASN ARG GLY ARG
SEQRES 13 B 252 GLY GLN ILE TYR PRO ASP GLY SER LYS SER ASN ASN THR
SEQRES 14 B 252 VAL TYR ASN ALA THR ALA GLY GLY ILE ILE SER LYS ILE
SEQRES 15 B 252 LEU ARG LYS GLU LYS GLY GLY TYR GLU ILE THR ILE VAL
SEQRES 16 B 252 ASP ALA SER ASN GLU ARG GLN VAL ILE ASP ILE ILE PRO
SEQRES 17 B 252 ARG GLY LEU GLU LEU LEU VAL SER GLU GLY GLU SER ILE
SEQRES 18 B 252 LYS LEU ASP GLN PRO LEU THR SER ASN PRO ASN VAL GLY
SEQRES 19 B 252 GLY PHE GLY GLN GLY ASP ALA GLU ILE VAL LEU GLN ASP
SEQRES 20 B 252 PRO LEU ARG VAL GLN
HET CU A 100 1
HET HEC B 253 75
HETNAM CU COPPER (II) ION
HETNAM HEC HEME C
FORMUL 3 CU CU 2+
FORMUL 4 HEC C34 H34 FE N4 O4
HELIX 1 1 ASP A 51 ILE A 55 5 5
HELIX 2 2 TYR B 1 TYR B 9 1 9
HELIX 3 3 ILE B 19 CYS B 24 5 6
HELIX 4 4 PRO B 85 ILE B 89 5 5
HELIX 5 5 SER B 90 ILE B 97 1 8
HELIX 6 6 GLY B 120 SER B 124 1 5
HELIX 7 7 ASP B 134 ASN B 138 5 5
SHEET 1 A 4 PHE A 14 VAL A 15 0
SHEET 2 A 4 ASP A 2 LEU A 5 -1 N LEU A 4 O VAL A 15
SHEET 3 A 4 LYS A 26 ASN A 31 1 O LYS A 30 N LEU A 5
SHEET 4 A 4 THR A 69 ALA A 73 -1 O PHE A 70 N PHE A 29
SHEET 1 B 4 GLU A 18 ILE A 21 0
SHEET 2 B 4 VAL A 93 VAL A 98 1 O THR A 97 N ILE A 21
SHEET 3 B 4 GLY A 78 TYR A 83 -1 N TYR A 80 O VAL A 96
SHEET 4 B 4 VAL A 40 PHE A 41 -1 N VAL A 40 O TYR A 83
SHEET 1 C 4 ASP B 32 GLU B 34 0
SHEET 2 C 4 VAL B 44 LYS B 50 -1 O LYS B 50 N ASP B 32
SHEET 3 C 4 GLU B 125 LEU B 131 -1 O PHE B 128 N ALA B 47
SHEET 4 C 4 GLU B 82 LEU B 83 -1 N GLU B 82 O LEU B 131
SHEET 1 D 6 ALA B 38 VAL B 39 0
SHEET 2 D 6 GLY B 235 LEU B 245 1 O VAL B 244 N VAL B 39
SHEET 3 D 6 LYS B 145 ARG B 154 -1 N VAL B 150 O GLY B 239
SHEET 4 D 6 ASN B 70 ILE B 76 -1 N ILE B 76 O TYR B 149
SHEET 5 D 6 LYS B 109 PRO B 119 -1 O VAL B 118 N VAL B 71
SHEET 6 D 6 GLN B 103 ARG B 106 -1 N GLN B 103 O VAL B 114
SHEET 1 E 2 GLN B 59 VAL B 60 0
SHEET 2 E 2 LYS B 66 GLY B 67 -1 O GLY B 67 N GLN B 59
SHEET 1 F 4 ARG B 201 ILE B 207 0
SHEET 2 F 4 TYR B 190 ASP B 196 -1 N ASP B 196 O ARG B 201
SHEET 3 F 4 GLY B 177 ARG B 184 -1 N LEU B 183 O GLU B 191
SHEET 4 F 4 SER B 220 ILE B 221 -1 O ILE B 221 N GLY B 177
LINK SG CYS B 21 CAB HEC B 253 1555 1555 1.77
LINK SG CYS B 24 CAC HEC B 253 1555 1555 1.74
LINK ND1 HIS A 37 CU CU A 100 1555 1555 2.13
LINK SG CYS A 84 CU CU A 100 1555 1555 2.15
LINK ND1 HIS A 87 CU CU A 100 1555 1555 2.40
LINK N TYR B 1 FE HEC B 253 1555 1555 2.00
LINK NE2 HIS B 25 FE HEC B 253 1555 1555 1.98
CISPEP 1 VAL A 15 PRO A 16 1 -1.50
CISPEP 2 PHE A 35 PRO A 36 1 3.05
CISPEP 3 GLY B 116 PRO B 117 1 0.64
CISPEP 4 VAL A 15 PRO A 16 2 0.80
CISPEP 5 PHE A 35 PRO A 36 2 2.77
CISPEP 6 GLY B 116 PRO B 117 2 -0.11
CISPEP 7 VAL A 15 PRO A 16 3 -1.26
CISPEP 8 PHE A 35 PRO A 36 3 2.47
CISPEP 9 GLY B 116 PRO B 117 3 -0.17
CISPEP 10 VAL A 15 PRO A 16 4 0.00
CISPEP 11 PHE A 35 PRO A 36 4 2.50
CISPEP 12 GLY B 116 PRO B 117 4 -0.07
CISPEP 13 VAL A 15 PRO A 16 5 -0.53
CISPEP 14 PHE A 35 PRO A 36 5 2.66
CISPEP 15 GLY B 116 PRO B 117 5 -0.27
CISPEP 16 VAL A 15 PRO A 16 6 0.00
CISPEP 17 PHE A 35 PRO A 36 6 2.80
CISPEP 18 GLY B 116 PRO B 117 6 -0.17
CISPEP 19 VAL A 15 PRO A 16 7 -1.37
CISPEP 20 PHE A 35 PRO A 36 7 3.68
CISPEP 21 GLY B 116 PRO B 117 7 0.37
CISPEP 22 VAL A 15 PRO A 16 8 -0.82
CISPEP 23 PHE A 35 PRO A 36 8 2.42
CISPEP 24 GLY B 116 PRO B 117 8 -0.38
CISPEP 25 VAL A 15 PRO A 16 9 -1.98
CISPEP 26 PHE A 35 PRO A 36 9 3.46
CISPEP 27 GLY B 116 PRO B 117 9 0.60
CISPEP 28 VAL A 15 PRO A 16 10 0.20
CISPEP 29 PHE A 35 PRO A 36 10 2.61
CISPEP 30 GLY B 116 PRO B 117 10 -0.36
SITE 1 AC1 4 HIS A 37 CYS A 84 HIS A 87 MET A 92
SITE 1 AC2 19 GLN A 88 GLY A 89 TYR B 1 PHE B 4
SITE 2 AC2 19 VAL B 20 CYS B 21 CYS B 24 HIS B 25
SITE 3 AC2 19 GLN B 59 LEU B 69 ASN B 70 VAL B 71
SITE 4 AC2 19 GLY B 72 ASN B 153 GLY B 155 ARG B 156
SITE 5 AC2 19 GLY B 157 ILE B 159 TYR B 160
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END