Header list of 1pfd.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 05-MAY-98 1PFD
TITLE THE SOLUTION STRUCTURE OF HIGH PLANT PARSLEY [2FE-2S] FERREDOXIN, NMR,
TITLE 2 18 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.7.7.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PETROSELINUM CRISPUM;
SOURCE 3 ORGANISM_COMMON: PARSLEY;
SOURCE 4 ORGANISM_TAXID: 4043;
SOURCE 5 ORGAN: LEAVES
KEYWDS [2FE-2S] FERREDOXIN, SOLUTION STRUCTURE, PARAMAGNETISM, NUCLEAR
KEYWDS 2 RELAXATION, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR S.-C.IM,G.LIU,C.LUCHINAT,A.G.SYKES,I.BERTINI
REVDAT 3 23-FEB-22 1PFD 1 REMARK LINK
REVDAT 2 24-FEB-09 1PFD 1 VERSN
REVDAT 1 11-MAY-99 1PFD 0
JRNL AUTH S.C.IM,G.LIU,C.LUCHINAT,A.G.SYKES,I.BERTINI
JRNL TITL THE SOLUTION STRUCTURE OF PARSLEY [2FE-2S]FERREDOXIN.
JRNL REF EUR.J.BIOCHEM. V. 258 465 1998
JRNL REFN ISSN 0014-2956
JRNL PMID 9874213
JRNL DOI 10.1046/J.1432-1327.1998.2580465.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.BAUMANN,H.STICHT,M.SCHARPF,M.SUTTER,W.HAEHNEL,P.ROSCH
REMARK 1 TITL STRUCTURE OF SYNECHOCOCCUS ELONGATUS [FE2S2] FERREDOXIN IN
REMARK 1 TITL 2 SOLUTION
REMARK 1 REF BIOCHEMISTRY V. 35 12831 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.LELONG,P.SETIF,H.BOTTIN,F.ANDRE,J.M.NEUMANN
REMARK 1 TITL 1H AND 15N NMR SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE,
REMARK 1 TITL 2 AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS
REMARK 1 TITL 3 SP. PCC 6803
REMARK 1 REF BIOCHEMISTRY V. 34 14462 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.C.POCHAPSKY,X.M.YE,G.RATNASWAMY,T.A.LYONS
REMARK 1 TITL AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED
REMARK 1 TITL 2 PUTIDAREDOXIN, A 2-FE, 2-S FERREDOXIN FROM PSEUDOMONAS
REMARK 1 REF BIOCHEMISTRY V. 33 6424 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH B.H.OH,J.L.MARKLEY
REMARK 1 TITL MULTINUCLEAR MAGNETIC RESONANCE STUDIES OF THE
REMARK 1 TITL 2 2FE(DOT)2SFERREDOXIN FROM ANABAENA SPECIES STRAIN PCC 7120.
REMARK 1 TITL 3 1. SEQUENCE-SPECIFIC HYDROGEN-1 RESONANCE ASSIGNMENTS AND
REMARK 1 TITL 4 SECONDARY STRUCTURE IN SOLUTION OF THE OXIDIZED FORM
REMARK 1 REF BIOCHEMISTRY V. 29 3993 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PFD 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_1000175639.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0.10 M
REMARK 210 PRESSURE : NORMAL
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY;
REMARK 210 INVERSION-RECOVER NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE-800; AVANCE-600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, DYANAT1, AMBER
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: MODEL NUMBER 1 WAS DETERMINED USING 2D NMR SPECTROSCOPY
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: 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 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 2 CYS A 44 CB - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 2 CYS A 44 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 2 CYS A 47 CB - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 2 CYS A 47 CA - CB - SG ANGL. DEV. = 10.6 DEGREES
REMARK 500 3 CYS A 39 CA - CB - SG ANGL. DEV. = 9.5 DEGREES
REMARK 500 8 CYS A 39 CA - CB - SG ANGL. DEV. = 11.0 DEGREES
REMARK 500 8 CYS A 44 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 8 CYS A 47 CA - CB - SG ANGL. DEV. = 9.2 DEGREES
REMARK 500 10 CYS A 44 CB - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 10 CYS A 47 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 12 CYS A 39 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 12 VAL A 96 CA - C - O ANGL. DEV. = -38.6 DEGREES
REMARK 500 16 CYS A 39 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 16 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.0 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 1 THR A 2 78.25 58.78
REMARK 500 1 GLU A 13 142.72 71.95
REMARK 500 1 LEU A 25 -61.56 -169.11
REMARK 500 1 ALA A 41 -47.50 -132.51
REMARK 500 1 SER A 43 69.21 -154.14
REMARK 500 1 SER A 45 50.24 -144.73
REMARK 500 1 SER A 46 -152.56 -158.27
REMARK 500 1 CYS A 47 71.23 45.10
REMARK 500 1 ASP A 60 -42.37 -154.48
REMARK 500 1 PHE A 63 -73.16 -156.45
REMARK 500 1 GLU A 92 -70.08 -65.17
REMARK 500 1 GLU A 93 33.16 -72.92
REMARK 500 2 THR A 2 89.57 78.80
REMARK 500 2 GLU A 13 147.35 67.55
REMARK 500 2 SER A 38 -51.93 -168.75
REMARK 500 2 CYS A 39 -150.17 -94.11
REMARK 500 2 ARG A 40 176.29 168.52
REMARK 500 2 ALA A 41 -42.62 103.55
REMARK 500 2 SER A 43 59.13 -103.66
REMARK 500 2 CYS A 44 -137.83 -119.57
REMARK 500 2 SER A 45 -93.55 -72.01
REMARK 500 2 SER A 46 -57.26 -156.15
REMARK 500 2 CYS A 47 43.91 26.23
REMARK 500 2 SER A 62 53.30 -153.00
REMARK 500 2 PHE A 63 -65.97 -151.69
REMARK 500 2 THR A 76 -56.28 74.39
REMARK 500 2 GLU A 92 -71.60 -67.30
REMARK 500 3 THR A 2 123.38 80.80
REMARK 500 3 GLU A 13 153.79 68.57
REMARK 500 3 LEU A 25 -43.07 -163.34
REMARK 500 3 PRO A 36 91.25 -66.31
REMARK 500 3 SER A 38 -161.85 56.56
REMARK 500 3 CYS A 39 -136.03 34.55
REMARK 500 3 ARG A 40 137.89 179.08
REMARK 500 3 ALA A 41 83.32 70.90
REMARK 500 3 SER A 43 42.02 -171.14
REMARK 500 3 SER A 46 -157.03 -169.71
REMARK 500 3 CYS A 47 111.84 32.53
REMARK 500 3 GLN A 61 -65.64 -99.79
REMARK 500 3 PHE A 63 -72.42 -154.88
REMARK 500 3 THR A 76 -55.14 73.37
REMARK 500 3 GLU A 92 -70.56 -53.13
REMARK 500 3 GLU A 93 39.12 -79.77
REMARK 500 4 THR A 2 85.04 76.11
REMARK 500 4 GLU A 13 141.68 67.89
REMARK 500 4 ARG A 40 67.35 -154.63
REMARK 500 4 ALA A 41 -63.19 -166.99
REMARK 500 4 SER A 43 85.98 -167.61
REMARK 500 4 SER A 45 62.95 -151.93
REMARK 500 4 CYS A 47 176.86 74.89
REMARK 500
REMARK 500 THIS ENTRY HAS 290 RAMACHANDRAN OUTLIERS.
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 CYS A 39 ARG A 40 6 146.74
REMARK 500 ALA A 1 THR A 2 13 144.28
REMARK 500 ALA A 1 THR A 2 14 137.28
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 TYR A 3 0.13 SIDE CHAIN
REMARK 500 1 TYR A 23 0.07 SIDE CHAIN
REMARK 500 1 TYR A 73 0.07 SIDE CHAIN
REMARK 500 2 TYR A 37 0.11 SIDE CHAIN
REMARK 500 2 TYR A 73 0.09 SIDE CHAIN
REMARK 500 2 TYR A 80 0.09 SIDE CHAIN
REMARK 500 4 TYR A 23 0.09 SIDE CHAIN
REMARK 500 4 TYR A 73 0.11 SIDE CHAIN
REMARK 500 5 TYR A 3 0.14 SIDE CHAIN
REMARK 500 5 TYR A 37 0.13 SIDE CHAIN
REMARK 500 5 TYR A 73 0.10 SIDE CHAIN
REMARK 500 6 TYR A 37 0.11 SIDE CHAIN
REMARK 500 6 TYR A 73 0.11 SIDE CHAIN
REMARK 500 7 TYR A 37 0.08 SIDE CHAIN
REMARK 500 7 TYR A 73 0.12 SIDE CHAIN
REMARK 500 8 TYR A 37 0.08 SIDE CHAIN
REMARK 500 8 TYR A 73 0.10 SIDE CHAIN
REMARK 500 9 TYR A 3 0.12 SIDE CHAIN
REMARK 500 9 ASP A 20 0.07 SIDE CHAIN
REMARK 500 9 TYR A 37 0.14 SIDE CHAIN
REMARK 500 9 TYR A 73 0.12 SIDE CHAIN
REMARK 500 10 TYR A 3 0.14 SIDE CHAIN
REMARK 500 10 TYR A 23 0.06 SIDE CHAIN
REMARK 500 10 TYR A 73 0.10 SIDE CHAIN
REMARK 500 11 TYR A 3 0.10 SIDE CHAIN
REMARK 500 11 PHE A 16 0.08 SIDE CHAIN
REMARK 500 11 TYR A 23 0.10 SIDE CHAIN
REMARK 500 11 PHE A 63 0.09 SIDE CHAIN
REMARK 500 13 TYR A 3 0.10 SIDE CHAIN
REMARK 500 13 ASP A 20 0.09 SIDE CHAIN
REMARK 500 13 TYR A 37 0.09 SIDE CHAIN
REMARK 500 13 PHE A 63 0.09 SIDE CHAIN
REMARK 500 14 TYR A 3 0.15 SIDE CHAIN
REMARK 500 14 TYR A 23 0.07 SIDE CHAIN
REMARK 500 14 TYR A 37 0.09 SIDE CHAIN
REMARK 500 14 TYR A 73 0.10 SIDE CHAIN
REMARK 500 15 TYR A 3 0.12 SIDE CHAIN
REMARK 500 15 ASP A 20 0.08 SIDE CHAIN
REMARK 500 15 TYR A 37 0.12 SIDE CHAIN
REMARK 500 15 TYR A 73 0.10 SIDE CHAIN
REMARK 500 16 ASP A 20 0.08 SIDE CHAIN
REMARK 500 16 TYR A 23 0.10 SIDE CHAIN
REMARK 500 16 TYR A 37 0.20 SIDE CHAIN
REMARK 500 16 TYR A 73 0.09 SIDE CHAIN
REMARK 500 17 TYR A 23 0.07 SIDE CHAIN
REMARK 500 17 ARG A 40 0.09 SIDE CHAIN
REMARK 500 17 TYR A 73 0.12 SIDE CHAIN
REMARK 500 18 TYR A 3 0.13 SIDE CHAIN
REMARK 500 18 TYR A 37 0.08 SIDE CHAIN
REMARK 500 18 TYR A 73 0.10 SIDE CHAIN
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 FES A 97 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 39 SG
REMARK 620 2 FES A 97 S1 107.4
REMARK 620 3 FES A 97 S2 110.6 107.0
REMARK 620 4 CYS A 44 SG 106.5 110.6 114.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 97 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 47 SG
REMARK 620 2 FES A 97 S1 110.5
REMARK 620 3 FES A 97 S2 102.1 107.2
REMARK 620 4 CYS A 77 SG 111.4 112.1 113.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FES
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: IRON BIND SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 97
DBREF 1PFD A 1 96 UNP Q7M1S1 Q7M1S1_PETCR 1 96
SEQRES 1 A 96 ALA THR TYR ASN VAL LYS LEU ILE THR PRO ASP GLY GLU
SEQRES 2 A 96 VAL GLU PHE LYS CYS ASP ASP ASP VAL TYR VAL LEU ASP
SEQRES 3 A 96 GLN ALA GLU GLU GLU GLY ILE ASP ILE PRO TYR SER CYS
SEQRES 4 A 96 ARG ALA GLY SER CYS SER SER CYS ALA GLY LYS VAL VAL
SEQRES 5 A 96 SER GLY SER ILE ASP GLN SER ASP GLN SER PHE LEU ASP
SEQRES 6 A 96 ASP GLU GLN MET ASP ALA GLY TYR VAL LEU THR CYS HIS
SEQRES 7 A 96 ALA TYR PRO THR SER ASP VAL VAL ILE GLU THR HIS LYS
SEQRES 8 A 96 GLU GLU GLU ILE VAL
HET FES A 97 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 1 ASP A 26 GLU A 31 1 6
HELIX 2 2 ASP A 66 ALA A 71 1 6
SHEET 1 A 5 VAL A 14 CYS A 18 0
SHEET 2 A 5 TYR A 3 ILE A 8 -1 N LEU A 7 O VAL A 14
SHEET 3 A 5 VAL A 86 THR A 89 1 N ILE A 87 O LYS A 6
SHEET 4 A 5 ALA A 48 SER A 53 -1 N SER A 53 O VAL A 86
SHEET 5 A 5 TYR A 73 LEU A 75 -1 N VAL A 74 O GLY A 49
LINK SG CYS A 39 FE1 FES A 97 1555 1555 2.35
LINK SG CYS A 44 FE1 FES A 97 1555 1555 2.34
LINK SG CYS A 47 FE2 FES A 97 1555 1555 2.28
LINK SG CYS A 77 FE2 FES A 97 1555 1555 2.39
SITE 1 FES 4 CYS A 39 ALA A 41 CYS A 47 CYS A 77
SITE 1 AC1 7 SER A 38 CYS A 39 GLY A 42 CYS A 44
SITE 2 AC1 7 CYS A 47 CYS A 77 HIS A 78
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 - b 23 2 Bytes