Header list of 1l3o.pdb file
Complete list - t 27 2 Bytes
HEADER OXYGEN STORAGE/TRANSPORT 28-FEB-02 1L3O
TITLE SOLUTION STRUCTURE DETERMINATION OF THE FULLY OXIDIZED DOUBLE MUTANT
TITLE 2 K9-10A CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS, ENSEMBLE OF 35
TITLE 3 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C7;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME C3, CYTOCHROME C551.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFUROMONAS ACETOXIDANS;
SOURCE 3 ORGANISM_TAXID: 891;
SOURCE 4 EXPRESSION_SYSTEM: DESULFOVIBRIO DESULFURICANS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 876;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: G201
KEYWDS AUTOMATIC ASSIGNMENT, CYTOCHROME C7, ELECTRON TRANSFER, MULTIHEME
KEYWDS 2 CYTOCHROMES, NMR SOLUTION STRUCTURES, OXYGEN STORAGE-TRANSPORT
KEYWDS 3 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR M.ASSFALG,I.BERTINI,P.TURANO,M.BRUSCHI,M.C.DURAND,M.T.GIUDICI-
AUTHOR 2 ORTICONI,A.DOLLA
REVDAT 3 27-OCT-21 1L3O 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1L3O 1 VERSN
REVDAT 1 13-MAR-02 1L3O 0
JRNL AUTH M.ASSFALG,I.BERTINI,P.TURANO,M.BRUSCHI,M.C.DURAND,
JRNL AUTH 2 M.T.GIUDICI-ORTICONI,A.DOLLA
JRNL TITL A QUICK SOLUTION STRUCTURE DETERMINATION OF THE FULLY
JRNL TITL 2 OXIDIZED DOUBLE MUTANT K9-10A CYTOCHROME C7 FROM
JRNL TITL 3 DESULFUROMONAS ACETOXIDANS AND MECHANISTIC IMPLICATIONS.
JRNL REF J.BIOMOL.NMR V. 22 107 2002
JRNL REFN ISSN 0925-2738
JRNL PMID 11883773
JRNL DOI 10.1023/A:1014202405862
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PSEUDYANA 1.5, AMBER 5.0
REMARK 3 AUTHORS : GUENTERT, P., WUETHRICH, K. (PSEUDYANA), KOLMAN,
REMARK 3 CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L3O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015614.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM CYTOCHROME C7
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION
REMARK 210 ANGLE SPACE AND RESTRAINED
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 35 STRUCTURES WITH THE
REMARK 210 LOWEST TARGET FUNCTION VALUES
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: 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 21 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.7 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 5 103.75 63.89
REMARK 500 1 THR A 14 78.92 55.04
REMARK 500 1 CYS A 26 -56.24 66.13
REMARK 500 1 GLU A 31 79.95 -66.51
REMARK 500 1 LYS A 41 24.20 -76.54
REMARK 500 1 LYS A 42 -54.39 -122.83
REMARK 500 1 ASP A 47 -52.31 -143.52
REMARK 500 1 CYS A 49 -58.74 70.20
REMARK 500 1 THR A 60 -35.45 -140.33
REMARK 500 2 ASP A 2 99.27 -18.97
REMARK 500 2 VAL A 3 85.40 47.96
REMARK 500 2 THR A 5 133.11 65.83
REMARK 500 2 ALA A 10 41.18 -94.64
REMARK 500 2 PHE A 15 90.37 -68.05
REMARK 500 2 LEU A 24 -89.33 -103.25
REMARK 500 2 ASP A 27 -63.25 -20.02
REMARK 500 2 ALA A 28 -31.75 -38.79
REMARK 500 2 THR A 33 76.44 50.81
REMARK 500 2 SER A 43 -59.98 -126.40
REMARK 500 2 ASP A 47 -50.46 -152.68
REMARK 500 3 ASP A 2 -154.17 -125.58
REMARK 500 3 VAL A 3 91.79 -61.59
REMARK 500 3 THR A 14 104.13 65.67
REMARK 500 3 LYS A 18 -70.08 -59.78
REMARK 500 3 LEU A 24 -65.70 -101.52
REMARK 500 3 ALA A 28 -33.64 -35.89
REMARK 500 3 THR A 33 79.02 8.23
REMARK 500 3 LYS A 36 175.62 173.28
REMARK 500 3 ASP A 47 -62.43 -148.02
REMARK 500 3 CYS A 49 -68.57 64.85
REMARK 500 3 HIS A 53 35.12 -63.98
REMARK 500 3 LYS A 61 152.87 -49.35
REMARK 500 3 CYS A 65 -66.79 -107.04
REMARK 500 4 ASP A 2 99.74 -36.53
REMARK 500 4 VAL A 3 115.69 62.33
REMARK 500 4 ASN A 8 -75.98 -71.12
REMARK 500 4 ALA A 9 -44.95 -173.89
REMARK 500 4 THR A 14 87.62 55.74
REMARK 500 4 LYS A 18 -70.57 -59.35
REMARK 500 4 CYS A 26 -54.69 65.18
REMARK 500 4 GLU A 31 81.62 -62.21
REMARK 500 4 LYS A 46 -61.96 -101.47
REMARK 500 4 ASP A 47 -59.65 -137.75
REMARK 500 4 CYS A 49 -61.32 70.74
REMARK 500 4 SER A 55 43.90 -77.87
REMARK 500 4 CYS A 65 -62.04 -108.74
REMARK 500 5 THR A 14 88.90 63.51
REMARK 500 5 LEU A 24 -94.79 -94.26
REMARK 500 5 ASP A 27 -66.22 -17.96
REMARK 500 5 ALA A 28 -29.55 -37.03
REMARK 500
REMARK 500 THIS ENTRY HAS 451 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 PHE A 15 ASP A 16 3 149.74
REMARK 500 ASP A 16 HIS A 17 3 147.39
REMARK 500 ALA A 1 ASP A 2 9 -148.34
REMARK 500 PHE A 15 ASP A 16 16 149.66
REMARK 500 ASP A 16 HIS A 17 16 147.82
REMARK 500 ALA A 1 ASP A 2 24 -146.35
REMARK 500 ALA A 1 ASP A 2 27 137.86
REMARK 500 ALA A 1 ASP A 2 29 142.32
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 6 0.10 SIDE CHAIN
REMARK 500 2 TYR A 6 0.11 SIDE CHAIN
REMARK 500 2 PHE A 15 0.09 SIDE CHAIN
REMARK 500 3 HIS A 30 0.08 SIDE CHAIN
REMARK 500 4 PHE A 15 0.20 SIDE CHAIN
REMARK 500 5 PHE A 15 0.10 SIDE CHAIN
REMARK 500 6 TYR A 6 0.07 SIDE CHAIN
REMARK 500 6 PHE A 15 0.09 SIDE CHAIN
REMARK 500 7 PHE A 15 0.10 SIDE CHAIN
REMARK 500 7 HIS A 17 0.09 SIDE CHAIN
REMARK 500 8 PHE A 15 0.10 SIDE CHAIN
REMARK 500 8 HIS A 17 0.09 SIDE CHAIN
REMARK 500 9 PHE A 15 0.09 SIDE CHAIN
REMARK 500 9 HIS A 17 0.12 SIDE CHAIN
REMARK 500 10 PHE A 15 0.11 SIDE CHAIN
REMARK 500 10 HIS A 17 0.17 SIDE CHAIN
REMARK 500 11 TYR A 6 0.22 SIDE CHAIN
REMARK 500 11 PHE A 15 0.10 SIDE CHAIN
REMARK 500 11 HIS A 17 0.10 SIDE CHAIN
REMARK 500 12 TYR A 6 0.10 SIDE CHAIN
REMARK 500 13 PHE A 15 0.07 SIDE CHAIN
REMARK 500 16 TYR A 6 0.15 SIDE CHAIN
REMARK 500 16 PHE A 15 0.08 SIDE CHAIN
REMARK 500 16 HIS A 17 0.14 SIDE CHAIN
REMARK 500 17 TYR A 6 0.14 SIDE CHAIN
REMARK 500 17 PHE A 15 0.10 SIDE CHAIN
REMARK 500 18 TYR A 6 0.07 SIDE CHAIN
REMARK 500 19 TYR A 6 0.07 SIDE CHAIN
REMARK 500 19 PHE A 15 0.11 SIDE CHAIN
REMARK 500 20 TYR A 6 0.10 SIDE CHAIN
REMARK 500 20 PHE A 15 0.07 SIDE CHAIN
REMARK 500 21 PHE A 15 0.12 SIDE CHAIN
REMARK 500 21 HIS A 17 0.12 SIDE CHAIN
REMARK 500 22 PHE A 15 0.14 SIDE CHAIN
REMARK 500 22 HIS A 17 0.13 SIDE CHAIN
REMARK 500 25 HIS A 30 0.10 SIDE CHAIN
REMARK 500 26 TYR A 6 0.08 SIDE CHAIN
REMARK 500 26 HIS A 17 0.09 SIDE CHAIN
REMARK 500 28 TYR A 6 0.13 SIDE CHAIN
REMARK 500 28 PHE A 15 0.10 SIDE CHAIN
REMARK 500 29 PHE A 15 0.12 SIDE CHAIN
REMARK 500 30 TYR A 6 0.15 SIDE CHAIN
REMARK 500 30 PHE A 15 0.09 SIDE CHAIN
REMARK 500 30 HIS A 30 0.09 SIDE CHAIN
REMARK 500 31 PHE A 15 0.13 SIDE CHAIN
REMARK 500 32 TYR A 6 0.08 SIDE CHAIN
REMARK 500 32 PHE A 15 0.07 SIDE CHAIN
REMARK 500 33 PHE A 15 0.10 SIDE CHAIN
REMARK 500 35 TYR A 6 0.06 SIDE CHAIN
REMARK 500 35 PHE A 15 0.15 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 HEC A 130 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 17 NE2
REMARK 620 2 HEC A 130 NA 91.3
REMARK 620 3 HEC A 130 NB 92.2 93.0
REMARK 620 4 HEC A 130 NC 88.8 178.0 89.0
REMARK 620 5 HEC A 130 ND 89.0 88.7 177.9 89.3
REMARK 620 6 HIS A 30 NE2 176.1 92.1 89.4 87.7 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 153 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 20 NE2
REMARK 620 2 HEC A 153 NA 90.3
REMARK 620 3 HEC A 153 NB 93.9 89.9
REMARK 620 4 HEC A 153 NC 90.7 178.9 89.5
REMARK 620 5 HEC A 153 ND 85.2 90.8 178.8 89.9
REMARK 620 6 HIS A 53 NE2 172.8 91.1 93.2 88.1 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 166 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 45 NE2
REMARK 620 2 HEC A 166 NA 93.3
REMARK 620 3 HEC A 166 NB 91.4 90.7
REMARK 620 4 HEC A 166 NC 87.3 179.3 89.7
REMARK 620 5 HEC A 166 ND 88.1 89.3 179.5 90.3
REMARK 620 6 HIS A 66 NE2 175.6 89.4 92.1 90.0 88.4
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 HEC A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 166
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KWJ RELATED DB: PDB
REMARK 900 CONTAINS THE ENERGY MINIMIZED AVERAGE NMR STRUCTURE FROM THE
REMARK 900 PRESENT FAMILY OF STRUCTURES
REMARK 900 RELATED ID: 1NEW RELATED DB: PDB
REMARK 900 CONTAINS 18 NMR STRUCTURES OF THE FULLY OXIDIZED NATIVE CYTOCHROME
REMARK 900 C7
REMARK 900 RELATED ID: 2NEW RELATED DB: PDB
REMARK 900 CONTAINS 17 NMR STRUCTURES OF THE FULLY OXIDIZED NATIVE CYTOCHROME
REMARK 900 C7
REMARK 900 RELATED ID: 1HH5 RELATED DB: PDB
REMARK 900 CONTAINS THE X-RAY STRUCTURE OF THE NATIVE PROTEIN
REMARK 900 RELATED ID: 1EHJ RELATED DB: PDB
REMARK 900 CONTAINS 35 NMR STRUCTURES OF THE FULLY REDUCED NATIVE PROTEIN
REMARK 900 RELATED ID: 5279 RELATED DB: BMRB
REMARK 900 CONTAINS THE PROTON SHIFTS FOR THE PRESENT STRUCTURE
DBREF 1L3O A 1 68 UNP P00137 CYC3_DESAC 1 68
SEQADV 1L3O ALA A 9 UNP P00137 LYS 9 ENGINEERED MUTATION
SEQADV 1L3O ALA A 10 UNP P00137 LYS 10 ENGINEERED MUTATION
SEQRES 1 A 68 ALA ASP VAL VAL THR TYR GLU ASN ALA ALA GLY ASN VAL
SEQRES 2 A 68 THR PHE ASP HIS LYS ALA HIS ALA GLU LYS LEU GLY CYS
SEQRES 3 A 68 ASP ALA CYS HIS GLU GLY THR PRO ALA LYS ILE ALA ILE
SEQRES 4 A 68 ASP LYS LYS SER ALA HIS LYS ASP ALA CYS LYS THR CYS
SEQRES 5 A 68 HIS LYS SER ASN ASN GLY PRO THR LYS CYS GLY GLY CYS
SEQRES 6 A 68 HIS ILE LYS
HET HEC A 130 75
HET HEC A 153 75
HET HEC A 166 75
HETNAM HEC HEME C
FORMUL 2 HEC 3(C34 H34 FE N4 O4)
HELIX 1 1 HIS A 20 GLY A 25 1 6
HELIX 2 2 CYS A 26 HIS A 30 5 5
HELIX 3 3 LYS A 42 ASP A 47 1 6
HELIX 4 4 CYS A 49 SER A 55 1 7
HELIX 5 5 LYS A 61 CYS A 65 5 5
LINK SG CYS A 26 CAB HEC A 130 1555 1555 1.81
LINK SG CYS A 29 CAC HEC A 130 1555 1555 1.82
LINK SG CYS A 49 CAB HEC A 153 1555 1555 1.82
LINK SG CYS A 52 CAC HEC A 153 1555 1555 1.81
LINK SG CYS A 62 CAB HEC A 166 1555 1555 1.81
LINK SG CYS A 65 CAC HEC A 166 1555 1555 1.82
LINK NE2 HIS A 17 FE HEC A 130 1555 1555 1.98
LINK NE2 HIS A 20 FE HEC A 153 1555 1555 2.00
LINK NE2 HIS A 30 FE HEC A 130 1555 1555 1.99
LINK NE2 HIS A 45 FE HEC A 166 1555 1555 1.97
LINK NE2 HIS A 53 FE HEC A 153 1555 1555 2.02
LINK NE2 HIS A 66 FE HEC A 166 1555 1555 1.99
SITE 1 AC1 12 TYR A 6 HIS A 17 ALA A 21 CYS A 26
SITE 2 AC1 12 CYS A 29 HIS A 30 PRO A 34 ALA A 35
SITE 3 AC1 12 LYS A 36 ILE A 37 ILE A 39 HEC A 153
SITE 1 AC2 10 VAL A 13 THR A 14 PHE A 15 HIS A 20
SITE 2 AC2 10 CYS A 29 CYS A 49 CYS A 52 HIS A 53
SITE 3 AC2 10 ASN A 56 HEC A 130
SITE 1 AC3 11 ASN A 8 ALA A 9 VAL A 13 ASP A 40
SITE 2 AC3 11 LYS A 41 ALA A 44 HIS A 45 THR A 60
SITE 3 AC3 11 CYS A 62 CYS A 65 HIS A 66
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 - t 27 2 Bytes