Header list of 2pcf.pdb file
Complete list - r 16 2 Bytes
HEADER COMPLEX (ELECTRON TRANSPORT PROTEINS) 22-DEC-97 2PCF
TITLE THE COMPLEX OF CYTOCHROME F AND PLASTOCYANIN DETERMINED WITH
TITLE 2 PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND
TITLE 3 PLASTOCYANIN, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASTOCYANIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CYTOCHROME F;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: SOLUBLE DOMAIN;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE 3 ORGANISM_COMMON: SPINACH;
SOURCE 4 ORGANISM_TAXID: 3562;
SOURCE 5 ORGANELLE: CHLOROPLAST;
SOURCE 6 CELLULAR_LOCATION: THYLAKOID LUMEN;
SOURCE 7 GENE: PETE;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PSY2;
SOURCE 13 EXPRESSION_SYSTEM_GENE: PETE;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: BRASSICA RAPA;
SOURCE 16 ORGANISM_TAXID: 3711;
SOURCE 17 ORGANELLE: CHLOROPLAST;
SOURCE 18 CELLULAR_LOCATION: THYLAKOID MEMBRANE;
SOURCE 19 GENE: PETE;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PSY2;
SOURCE 24 EXPRESSION_SYSTEM_GENE: PETE
KEYWDS ELECTRON TRANSPORT, PARAMAGNETIC, CHEMICAL SHIFT, COMPLEX FORMATION,
KEYWDS 2 DYNAMIC COMPLEX, PHOTOSYNTHESIS, PSEUDOCONTACT SHIFT, COMPLEX
KEYWDS 3 (ELECTRON TRANSPORT PROTEINS)
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.UBBINK,M.EJDEBACK,B.G.KARLSSON,D.S.BENDALL
REVDAT 3 16-MAR-22 2PCF 1 REMARK LINK
REVDAT 2 24-FEB-09 2PCF 1 VERSN
REVDAT 1 08-APR-98 2PCF 0
JRNL AUTH M.UBBINK,M.EJDEBACK,B.G.KARLSSON,D.S.BENDALL
JRNL TITL THE STRUCTURE OF THE COMPLEX OF PLASTOCYANIN AND CYTOCHROME
JRNL TITL 2 F, DETERMINED BY PARAMAGNETIC NMR AND RESTRAINED RIGID-BODY
JRNL TITL 3 MOLECULAR DYNAMICS.
JRNL REF STRUCTURE V. 6 323 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9551554
JRNL DOI 10.1016/S0969-2126(98)00035-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.EJDEBACK,S.YOUNG,A.SAMUELSSON,B.G.KARLSSON
REMARK 1 TITL EFFECTS OF CODON USAGE AND VECTOR-HOST COMBINATIONS ON THE
REMARK 1 TITL 2 EXPRESSION OF SPINACH PLASTOCYANIN IN ESCHERICHIA COLI
REMARK 1 REF PROTEIN EXPR.PURIF. V. 11 17 1997
REMARK 1 REFN ISSN 1046-5928
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.E.MARTINEZ,D.HUANG,A.SZCZEPANIAK,W.A.CRAMER,J.L.SMITH
REMARK 1 TITL CRYSTAL STRUCTURE OF CHLOROPLAST CYTOCHROME F REVEALS A
REMARK 1 TITL 2 NOVEL CYTOCHROME FOLD AND UNEXPECTED HEME LIGATION
REMARK 1 REF STRUCTURE V. 2 95 1994
REMARK 1 REFN ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND BELOW
REMARK 3 AND IN THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2PCF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178448.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM; UNITY; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 9999
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : REFER TO PUBLICATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 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 HA ASP A 51 HZ2 LYS B 187 1.29
REMARK 500 O PHE B 4 OD1 ASN B 8 2.13
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 ASP A 9 -41.83 -145.69
REMARK 500 1 ASP A 18 111.14 -167.11
REMARK 500 1 ASN A 32 -67.90 -104.51
REMARK 500 1 GLU A 43 44.84 -100.39
REMARK 500 1 VAL A 50 157.56 61.67
REMARK 500 1 PRO A 86 21.93 -74.98
REMARK 500 1 HIS A 87 49.18 -173.33
REMARK 500 1 ALA B 62 7.87 -60.79
REMARK 500 1 ASN B 99 39.37 -149.94
REMARK 500 1 TYR B 123 57.47 -109.25
REMARK 500 1 ALA B 136 1.00 -67.99
REMARK 500 1 ASN B 168 41.35 -104.40
REMARK 500 1 ASP B 224 -3.93 79.13
REMARK 500 1 LEU B 249 -132.70 -109.14
REMARK 500 2 ASP A 9 -41.38 -143.21
REMARK 500 2 ASP A 18 113.26 -164.88
REMARK 500 2 ASN A 32 -70.46 -112.64
REMARK 500 2 VAL A 50 152.42 62.61
REMARK 500 2 PRO A 86 34.68 -74.04
REMARK 500 2 HIS A 87 34.61 174.12
REMARK 500 2 ALA A 90 -72.57 -67.65
REMARK 500 2 ALA B 62 7.87 -60.79
REMARK 500 2 ASN B 99 39.37 -149.94
REMARK 500 2 TYR B 123 57.47 -109.25
REMARK 500 2 ALA B 136 1.00 -67.99
REMARK 500 2 ASN B 168 41.35 -104.40
REMARK 500 2 ASP B 224 -3.93 79.13
REMARK 500 2 LEU B 249 -132.70 -109.14
REMARK 500 3 ASP A 9 -41.34 -145.60
REMARK 500 3 ASP A 18 105.63 -166.98
REMARK 500 3 ASN A 32 -65.74 -104.65
REMARK 500 3 VAL A 50 156.06 62.50
REMARK 500 3 ALA B 62 7.87 -60.79
REMARK 500 3 ASN B 99 39.37 -149.94
REMARK 500 3 TYR B 123 57.47 -109.25
REMARK 500 3 ALA B 136 1.00 -67.99
REMARK 500 3 ASN B 168 41.35 -104.40
REMARK 500 3 ASP B 224 -3.93 79.13
REMARK 500 3 LEU B 249 -132.70 -109.14
REMARK 500 4 ASP A 9 -41.11 -145.38
REMARK 500 4 ASP A 18 110.08 -166.90
REMARK 500 4 ASN A 32 -65.46 -101.21
REMARK 500 4 VAL A 50 156.68 62.24
REMARK 500 4 PRO A 86 31.67 -76.25
REMARK 500 4 HIS A 87 49.79 175.77
REMARK 500 4 ALA B 62 7.87 -60.79
REMARK 500 4 ASN B 99 39.37 -149.94
REMARK 500 4 TYR B 123 57.47 -109.25
REMARK 500 4 ALA B 136 1.00 -67.99
REMARK 500 4 ASN B 168 41.35 -104.40
REMARK 500
REMARK 500 THIS ENTRY HAS 132 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 0.26 SIDE CHAIN
REMARK 500 1 ARG B 18 0.27 SIDE CHAIN
REMARK 500 1 ARG B 88 0.31 SIDE CHAIN
REMARK 500 1 ARG B 106 0.12 SIDE CHAIN
REMARK 500 1 ARG B 154 0.23 SIDE CHAIN
REMARK 500 1 ARG B 156 0.28 SIDE CHAIN
REMARK 500 1 ARG B 184 0.29 SIDE CHAIN
REMARK 500 1 ARG B 201 0.29 SIDE CHAIN
REMARK 500 1 ARG B 209 0.26 SIDE CHAIN
REMARK 500 1 ARG B 250 0.30 SIDE CHAIN
REMARK 500 2 ARG B 13 0.26 SIDE CHAIN
REMARK 500 2 ARG B 18 0.27 SIDE CHAIN
REMARK 500 2 ARG B 88 0.31 SIDE CHAIN
REMARK 500 2 ARG B 106 0.12 SIDE CHAIN
REMARK 500 2 ARG B 154 0.23 SIDE CHAIN
REMARK 500 2 ARG B 156 0.28 SIDE CHAIN
REMARK 500 2 ARG B 184 0.29 SIDE CHAIN
REMARK 500 2 ARG B 201 0.29 SIDE CHAIN
REMARK 500 2 ARG B 209 0.26 SIDE CHAIN
REMARK 500 2 ARG B 250 0.30 SIDE CHAIN
REMARK 500 3 ARG B 13 0.26 SIDE CHAIN
REMARK 500 3 ARG B 18 0.27 SIDE CHAIN
REMARK 500 3 ARG B 88 0.31 SIDE CHAIN
REMARK 500 3 ARG B 106 0.12 SIDE CHAIN
REMARK 500 3 ARG B 154 0.23 SIDE CHAIN
REMARK 500 3 ARG B 156 0.28 SIDE CHAIN
REMARK 500 3 ARG B 184 0.29 SIDE CHAIN
REMARK 500 3 ARG B 201 0.29 SIDE CHAIN
REMARK 500 3 ARG B 209 0.26 SIDE CHAIN
REMARK 500 3 ARG B 250 0.30 SIDE CHAIN
REMARK 500 4 ARG B 13 0.26 SIDE CHAIN
REMARK 500 4 ARG B 18 0.27 SIDE CHAIN
REMARK 500 4 ARG B 88 0.31 SIDE CHAIN
REMARK 500 4 ARG B 106 0.12 SIDE CHAIN
REMARK 500 4 ARG B 154 0.23 SIDE CHAIN
REMARK 500 4 ARG B 156 0.28 SIDE CHAIN
REMARK 500 4 ARG B 184 0.29 SIDE CHAIN
REMARK 500 4 ARG B 201 0.29 SIDE CHAIN
REMARK 500 4 ARG B 209 0.26 SIDE CHAIN
REMARK 500 4 ARG B 250 0.30 SIDE CHAIN
REMARK 500 5 ARG B 13 0.26 SIDE CHAIN
REMARK 500 5 ARG B 18 0.27 SIDE CHAIN
REMARK 500 5 ARG B 88 0.31 SIDE CHAIN
REMARK 500 5 ARG B 106 0.12 SIDE CHAIN
REMARK 500 5 ARG B 154 0.23 SIDE CHAIN
REMARK 500 5 ARG B 156 0.28 SIDE CHAIN
REMARK 500 5 ARG B 184 0.29 SIDE CHAIN
REMARK 500 5 ARG B 201 0.29 SIDE CHAIN
REMARK 500 5 ARG B 209 0.26 SIDE CHAIN
REMARK 500 5 ARG B 250 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 100 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 79.6
REMARK 620 3 HIS A 87 ND1 136.3 127.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 251 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 1 N
REMARK 620 2 HEC B 251 NA 88.7
REMARK 620 3 HEC B 251 NB 96.3 91.3
REMARK 620 4 HEC B 251 NC 90.3 178.8 88.3
REMARK 620 5 HEC B 251 ND 86.1 90.0 177.4 90.5
REMARK 620 6 HIS B 25 NE2 174.3 91.3 89.4 89.8 88.3
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 251
DBREF 2PCF A 1 99 UNP P00289 PLAS_SPIOL 70 168
DBREF 2PCF B 1 250 UNP P36438 CYF_BRARA 36 285
SEQRES 1 A 99 VAL GLU VAL LEU LEU GLY GLY GLY ASP GLY SER LEU ALA
SEQRES 2 A 99 PHE LEU PRO GLY ASP PHE SER VAL ALA SER GLY GLU GLU
SEQRES 3 A 99 ILE VAL PHE LYS ASN ASN ALA GLY PHE PRO HIS ASN VAL
SEQRES 4 A 99 VAL PHE ASP GLU ASP GLU ILE PRO SER GLY VAL ASP ALA
SEQRES 5 A 99 ALA LYS ILE SER MET SER GLU GLU ASP LEU LEU ASN ALA
SEQRES 6 A 99 PRO GLY GLU THR TYR LYS VAL THR LEU THR GLU LYS GLY
SEQRES 7 A 99 THR TYR LYS 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 250 TYR PRO ILE PHE ALA GLN GLN ASN TYR GLU ASN PRO ARG
SEQRES 2 B 250 GLU ALA THR GLY ARG ILE VAL CYS ALA ASN CYS HIS LEU
SEQRES 3 B 250 ALA SER LYS PRO VAL ASP ILE GLU VAL PRO GLN ALA VAL
SEQRES 4 B 250 LEU PRO ASP THR VAL PHE GLU ALA VAL VAL LYS ILE PRO
SEQRES 5 B 250 TYR ASP MET GLN LEU LYS GLN VAL LEU ALA ASN GLY LYS
SEQRES 6 B 250 LYS GLY ALA LEU ASN VAL GLY ALA VAL LEU ILE LEU PRO
SEQRES 7 B 250 GLU GLY PHE GLU LEU ALA PRO PRO ASP ARG ILE SER PRO
SEQRES 8 B 250 GLU MET LYS GLU LYS ILE GLY ASN LEU SER PHE GLN ASN
SEQRES 9 B 250 TYR ARG PRO ASN LYS LYS ASN ILE LEU VAL ILE GLY PRO
SEQRES 10 B 250 VAL PRO GLY GLN LYS TYR SER GLU ILE THR PHE PRO ILE
SEQRES 11 B 250 LEU ALA PRO ASP PRO ALA THR ASN LYS ASP VAL HIS PHE
SEQRES 12 B 250 LEU LYS TYR PRO ILE TYR VAL GLY GLY ASN ARG GLY ARG
SEQRES 13 B 250 GLY GLN ILE TYR PRO ASP GLY SER LYS SER ASN ASN THR
SEQRES 14 B 250 VAL TYR ASN ALA THR ALA GLY GLY ILE ILE SER LYS ILE
SEQRES 15 B 250 LEU ARG LYS GLU LYS GLY GLY TYR GLU ILE THR ILE VAL
SEQRES 16 B 250 ASP ALA SER ASN GLU ARG GLN VAL ILE ASP ILE ILE PRO
SEQRES 17 B 250 ARG GLY LEU GLU LEU LEU VAL SER GLU GLY GLU SER ILE
SEQRES 18 B 250 LYS LEU ASP GLN PRO LEU THR SER ASN PRO ASN VAL GLY
SEQRES 19 B 250 GLY PHE GLY GLN GLY ASP ALA GLU ILE VAL LEU GLN ASP
SEQRES 20 B 250 PRO LEU ARG
HET CU A 100 1
HET HEC B 251 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 ALA A 52 ILE A 55 1 4
HELIX 2 3 TYR B 1 TYR B 9 1 9
HELIX 3 4 ILE B 19 HIS B 25 5 7
HELIX 4 6 SER B 90 ILE B 97 1 8
SHEET 1 A 2 GLU A 2 LEU A 5 0
SHEET 2 A 2 VAL A 28 ASN A 31 1 N VAL A 28 O VAL A 3
SHEET 1 B 2 PHE A 19 VAL A 21 0
SHEET 2 B 2 VAL A 96 VAL A 98 1 N THR A 97 O PHE A 19
SHEET 1 C 2 VAL A 39 PHE A 41 0
SHEET 2 C 2 PHE A 82 CYS A 84 -1 N TYR A 83 O VAL A 40
SHEET 1 LDA 4 PRO B 30 PRO B 36 0
SHEET 2 LDA 4 THR B 43 ILE B 51 -1 O VAL B 48 N GLU B 34
SHEET 3 LDA 4 SER B 124 ALA B 132 -1 O PHE B 128 N ALA B 47
SHEET 4 LDA 4 GLU B 82 ALA B 84 -1 O GLU B 82 N LEU B 131
SHEET 1 LDB 6 GLN B 37 VAL B 39 0
SHEET 2 LDB 6 GLY B 234 GLN B 246 1 O VAL B 244 N VAL B 39
SHEET 3 LDB 6 LEU B 144 GLY B 155 -1 O VAL B 150 N GLY B 239
SHEET 4 LDB 6 ASN B 70 LEU B 77 -1 O VAL B 74 N GLY B 151
SHEET 5 LDB 6 ASN B 111 VAL B 118 -1 O ILE B 115 N ALA B 73
SHEET 6 LDB 6 GLN B 103 TYR B 105 -1 O GLN B 103 N VAL B 114
SHEET 1 LDC 2 GLN B 59 LEU B 61 0
SHEET 2 LDC 2 LYS B 65 GLY B 67 -1 N GLY B 67 O GLN B 59
SHEET 1 LDD 2 GLN B 158 TYR B 160 0
SHEET 2 LDD 2 SER B 164 SER B 166 -1 O SER B 164 N TYR B 160
SHEET 1 SDA 4 ARG B 201 PRO B 208 0
SHEET 2 SDA 4 GLY B 189 ASP B 196 -1 O ILE B 192 N ASP B 205
SHEET 3 SDA 4 GLY B 176 ILE B 179 -1 O ILE B 178 N VAL B 195
SHEET 4 SDA 4 GLU B 219 LYS B 222 -1 N ILE B 221 O GLY B 177
SHEET 1 SDB 4 ARG B 201 PRO B 208 0
SHEET 2 SDB 4 GLY B 189 ASP B 196 -1 O ILE B 192 N ASP B 205
SHEET 3 SDB 4 LYS B 181 LYS B 185 -1 N LEU B 183 O GLU B 191
SHEET 4 SDB 4 GLU B 219 LYS B 222 -1
LINK SG CYS B 21 CAB HEC B 251 1555 1555 1.77
LINK SG CYS B 24 CAC HEC B 251 1555 1555 1.77
LINK ND1 HIS A 37 CU CU A 100 1555 1555 2.45
LINK SG CYS A 84 CU CU A 100 1555 1555 2.61
LINK ND1 HIS A 87 CU CU A 100 1555 1555 2.43
LINK N TYR B 1 FE HEC B 251 1555 1555 1.99
LINK NE2 HIS B 25 FE HEC B 251 1555 1555 1.97
CISPEP 1 LEU A 15 PRO A 16 1 -0.27
CISPEP 2 PHE A 35 PRO A 36 1 -0.04
CISPEP 3 GLY B 116 PRO B 117 1 2.79
CISPEP 4 LEU A 15 PRO A 16 2 -0.23
CISPEP 5 PHE A 35 PRO A 36 2 0.05
CISPEP 6 GLY B 116 PRO B 117 2 2.79
CISPEP 7 LEU A 15 PRO A 16 3 -0.22
CISPEP 8 PHE A 35 PRO A 36 3 -0.06
CISPEP 9 GLY B 116 PRO B 117 3 2.79
CISPEP 10 LEU A 15 PRO A 16 4 -0.27
CISPEP 11 PHE A 35 PRO A 36 4 -0.16
CISPEP 12 GLY B 116 PRO B 117 4 2.79
CISPEP 13 LEU A 15 PRO A 16 5 -0.27
CISPEP 14 PHE A 35 PRO A 36 5 0.12
CISPEP 15 GLY B 116 PRO B 117 5 2.79
CISPEP 16 LEU A 15 PRO A 16 6 -0.35
CISPEP 17 PHE A 35 PRO A 36 6 -0.25
CISPEP 18 GLY B 116 PRO B 117 6 2.79
CISPEP 19 LEU A 15 PRO A 16 7 -0.27
CISPEP 20 PHE A 35 PRO A 36 7 -0.02
CISPEP 21 GLY B 116 PRO B 117 7 2.79
CISPEP 22 LEU A 15 PRO A 16 8 -0.27
CISPEP 23 PHE A 35 PRO A 36 8 -0.14
CISPEP 24 GLY B 116 PRO B 117 8 2.79
CISPEP 25 LEU A 15 PRO A 16 9 -0.25
CISPEP 26 PHE A 35 PRO A 36 9 0.25
CISPEP 27 GLY B 116 PRO B 117 9 2.79
CISPEP 28 LEU A 15 PRO A 16 10 -0.24
CISPEP 29 PHE A 35 PRO A 36 10 -0.09
CISPEP 30 GLY B 116 PRO B 117 10 2.79
SITE 1 AC1 5 PRO A 36 HIS A 37 CYS A 84 HIS A 87
SITE 2 AC1 5 MET A 92
SITE 1 AC2 19 SER A 85 PRO A 86 HIS A 87 GLN A 88
SITE 2 AC2 19 TYR B 1 ALA B 5 CYS B 21 CYS B 24
SITE 3 AC2 19 HIS B 25 GLN B 59 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
Complete list - r 16 2 Bytes