Header list of 1ba9.pdb file
Complete list - v 3 2 Bytes
HEADER OXIDOREDUCTASE 24-APR-98 1BA9
TITLE THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR,
TITLE 2 36 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SOD;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSOD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOPP 1 (STRATAGENE);
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PBR322;
SOURCE 11 EXPRESSION_SYSTEM_GENE: HSOD
KEYWDS OXIDOREDUCTASE, SUPEROXIDE DISMUTASE, COPPER-ZINC ENZYME, DISMUTATION
KEYWDS 2 OF UPEROXIDE RADICALS TO MOLECULAR OXYGEN AND HYDROGEN PEROXIDE
EXPDTA SOLUTION NMR
NUMMDL 36
AUTHOR L.BANCI,M.BENEDETTO,I.BERTINI,R.DEL CONTE,M.PICCIOLI,M.S.VIEZZOLI
REVDAT 3 03-NOV-21 1BA9 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1BA9 1 VERSN
REVDAT 1 16-SEP-98 1BA9 0
JRNL AUTH L.BANCI,M.BENEDETTO,I.BERTINI,R.DEL CONTE,M.PICCIOLI,
JRNL AUTH 2 M.S.VIEZZOLI
JRNL TITL SOLUTION STRUCTURE OF REDUCED MONOMERIC Q133M2 COPPER, ZINC
JRNL TITL 2 SUPEROXIDE DISMUTASE (SOD). WHY IS SOD A DIMERIC ENZYME?.
JRNL REF BIOCHEMISTRY V. 37 11780 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9718300
JRNL DOI 10.1021/BI9803473
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1BA9 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_1000171518.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O AND D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCA; 3D HN(CO)CA; 3DHNCAHA;
REMARK 210 3DHN(CO)CAHA; 3D HNCO; (HCA)
REMARK 210 CO(CA)NH; 3D HNHA; H(C)CH-TOCSY;
REMARK 210 (H)CCH-TOCSY; (H)C(CO)NH-TOCSY;
REMARK 210 1H-NOESY; 1H-15N-HSQC; 15N-NOESY-
REMARK 210 HSQC; 13C-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 600; DRX 600; AVANCE 800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY (ETH (ETH, ZURICH)
REMARK 210 METHOD USED : TORTION ANGLES DYNAMIC (DYANA)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 36
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 36
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N LABELED SOD.
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 5 ASP A 124 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 17 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 20 HIS A 120 CB - CG - CD2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 27 PRO A 62 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 29 ASP A 124 CB - CG - OD2 ANGL. DEV. = -5.5 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 LYS A 3 88.98 -175.39
REMARK 500 1 LYS A 23 -60.99 66.66
REMARK 500 1 SER A 34 103.21 -161.03
REMARK 500 1 GLU A 49 -82.73 -34.05
REMARK 500 1 THR A 58 -38.75 -35.03
REMARK 500 1 ALA A 60 74.22 -170.67
REMARK 500 1 LEU A 84 44.18 -83.89
REMARK 500 1 SER A 98 95.62 -168.86
REMARK 500 1 ILE A 104 -169.33 -76.15
REMARK 500 1 SER A 105 -19.53 -148.03
REMARK 500 1 LEU A 106 -4.33 66.92
REMARK 500 1 SER A 107 85.91 170.69
REMARK 500 1 HIS A 110 45.57 -94.52
REMARK 500 1 SER A 111 109.24 -46.06
REMARK 500 2 VAL A 14 107.44 -41.19
REMARK 500 2 LYS A 23 -58.64 74.25
REMARK 500 2 GLU A 49 -153.57 -78.77
REMARK 500 2 GLU A 50 -62.82 69.11
REMARK 500 2 GLU A 51 154.18 69.00
REMARK 500 2 ASP A 52 73.20 8.50
REMARK 500 2 ASN A 53 -41.31 -157.33
REMARK 500 2 CYS A 57 18.31 59.85
REMARK 500 2 THR A 58 -75.45 -71.59
REMARK 500 2 PRO A 66 -70.94 -84.82
REMARK 500 2 SER A 98 98.06 -163.33
REMARK 500 2 LEU A 106 -23.83 72.52
REMARK 500 2 SER A 107 89.11 -169.00
REMARK 500 2 HIS A 110 48.57 -84.26
REMARK 500 2 SER A 111 100.56 -57.98
REMARK 500 2 GLN A 133 -72.27 -53.14
REMARK 500 3 LYS A 3 78.00 -159.30
REMARK 500 3 VAL A 14 101.63 -58.99
REMARK 500 3 GLN A 22 -67.72 -166.96
REMARK 500 3 LYS A 23 -52.37 67.45
REMARK 500 3 SER A 34 101.75 -163.12
REMARK 500 3 LEU A 38 -167.19 -70.69
REMARK 500 3 GLU A 50 168.48 80.65
REMARK 500 3 GLU A 51 -103.08 -154.37
REMARK 500 3 ASN A 53 -40.67 -162.18
REMARK 500 3 THR A 54 46.43 -75.20
REMARK 500 3 SER A 68 99.48 77.66
REMARK 500 3 LEU A 84 38.96 -95.08
REMARK 500 3 SER A 98 81.47 -166.32
REMARK 500 3 VAL A 103 -63.09 -94.24
REMARK 500 3 LEU A 106 43.52 -102.15
REMARK 500 3 SER A 111 91.44 -17.80
REMARK 500 3 ASP A 125 5.68 -68.78
REMARK 500 3 GLN A 133 -73.72 -50.59
REMARK 500 4 VAL A 14 102.72 -43.56
REMARK 500 4 LYS A 23 -50.60 71.29
REMARK 500
REMARK 500 THIS ENTRY HAS 652 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 HIS A 80 VAL A 81 9 147.52
REMARK 500 PRO A 62 HIS A 63 27 143.12
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 HIS A 71 0.09 SIDE CHAIN
REMARK 500 2 PHE A 64 0.08 SIDE CHAIN
REMARK 500 2 ARG A 79 0.08 SIDE CHAIN
REMARK 500 4 HIS A 71 0.09 SIDE CHAIN
REMARK 500 4 HIS A 80 0.12 SIDE CHAIN
REMARK 500 11 HIS A 71 0.08 SIDE CHAIN
REMARK 500 14 ARG A 115 0.12 SIDE CHAIN
REMARK 500 15 PHE A 45 0.09 SIDE CHAIN
REMARK 500 16 PHE A 45 0.08 SIDE CHAIN
REMARK 500 16 HIS A 71 0.10 SIDE CHAIN
REMARK 500 17 HIS A 71 0.09 SIDE CHAIN
REMARK 500 18 HIS A 71 0.09 SIDE CHAIN
REMARK 500 19 ARG A 115 0.08 SIDE CHAIN
REMARK 500 20 HIS A 80 0.10 SIDE CHAIN
REMARK 500 20 ARG A 115 0.08 SIDE CHAIN
REMARK 500 22 HIS A 80 0.12 SIDE CHAIN
REMARK 500 24 HIS A 71 0.09 SIDE CHAIN
REMARK 500 24 ARG A 115 0.09 SIDE CHAIN
REMARK 500 27 HIS A 71 0.11 SIDE CHAIN
REMARK 500 30 HIS A 80 0.09 SIDE CHAIN
REMARK 500 31 HIS A 80 0.09 SIDE CHAIN
REMARK 500 32 HIS A 80 0.09 SIDE CHAIN
REMARK 500 33 HIS A 80 0.09 SIDE CHAIN
REMARK 500 34 HIS A 80 0.09 SIDE CHAIN
REMARK 500 35 HIS A 80 0.09 SIDE CHAIN
REMARK 500 36 HIS A 80 0.09 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 CU1 A 155 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 144.9
REMARK 620 3 HIS A 120 NE2 95.4 115.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 HIS A 71 ND1 93.6
REMARK 620 3 HIS A 80 ND1 114.2 117.8
REMARK 620 4 ASP A 83 OD1 106.3 110.6 112.5
REMARK 620 5 ASP A 83 OD2 158.4 77.0 87.2 60.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CU
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: REDUCED COPPER ION (CU1+) IS COORDINATED BY
REMARK 800 THREE HISTIDINES: HIS 46, METAL COORDINATED THROUGH ND1; HIS 48,
REMARK 800 METAL COORDINATED THROUGH NE2; HIS 120 METAL COORDINATED THROUGH
REMARK 800 NE2. THE THREE MENTIONED HISTIDINES ARE PROTONATED ON THE OTHER
REMARK 800 N POSITION OF THE IMIDAZOLE RING, I.E. HIS 46 IS HIS-E, HIS 48
REMARK 800 IS HIS-D, HIS 120 IS HIS-D. THERE ARE DIRECT SPECTROSCOPIC
REMARK 800 EVIDENCES FOR THE ABOVE FINDINGS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC ION (ZN2+) IS COORDINATED BY THREE
REMARK 800 HISTIDINES AND BY AN ASPARTIC ACID RESIDUE. HIS 63, HIS 71 AND
REMARK 800 HIS 80 ARE METAL COORDINATED THROUGH THE ND1 ATOM. ASP 83 IS
REMARK 800 METAL COORDINATED THROUGH OD1. THE THREE HISTIDINES COORDINATED
REMARK 800 TO THE ZN ION ARE PROTONATED AT THE OTHER N POSITION OF THE
REMARK 800 IMIDAZOLE RING, I.E. HIS 63, HIS 71 AND HIS 80 ARE ALL HIS-E.
REMARK 800 THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE COORDINATION
REMARK 800 AND PROTONATION PROPERTIES OF THE HIS RESIDUES. IN ADDITION,
REMARK 800 THERE ARE SPECTROSCOPIC EVIDENCES THAT THE NON METAL COORDINATED
REMARK 800 RESIDUE HIS 43 IS PROTONATED ON BOTH N IMIDAZOLE POSITION, I.E.
REMARK 800 HIS 43 IS HIS-H.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 155
DBREF 1BA9 A 1 153 UNP P00441 SODC_HUMAN 1 153
SEQADV 1BA9 ALA A 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1BA9 GLU A 50 UNP P00441 PHE 50 ENGINEERED MUTATION
SEQADV 1BA9 GLU A 51 UNP P00441 GLY 51 ENGINEERED MUTATION
SEQADV 1BA9 SER A 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1BA9 GLN A 133 UNP P00441 GLU 133 ENGINEERED MUTATION
SEQRES 1 A 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 A 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 A 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 A 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU GLU GLU ASP
SEQRES 5 A 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 A 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 A 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 A 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 A 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 A 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 A 153 ASN GLU GLN SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 A 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET ZN A 154 1
HET CU1 A 155 1
HETNAM ZN ZINC ION
HETNAM CU1 COPPER (I) ION
FORMUL 2 ZN ZN 2+
FORMUL 3 CU1 CU 1+
HELIX 1 2 GLU A 132 THR A 137 1 6
SHEET 1 A 5 ARG A 143 ILE A 151 0
SHEET 2 A 5 LYS A 3 LYS A 9 -1 N VAL A 5 O GLY A 150
SHEET 3 A 5 GLN A 15 GLU A 21 -1 N PHE A 20 O ALA A 4
SHEET 4 A 5 VAL A 29 LYS A 36 -1 N LYS A 36 O GLN A 15
SHEET 5 A 5 ASP A 96 ASP A 101 -1 N ASP A 101 O VAL A 29
SHEET 1 B 2 GLY A 41 HIS A 48 0
SHEET 2 B 2 ASP A 83 ALA A 89 -1 N ALA A 89 O GLY A 41
SHEET 1 C 2 PHE A 45 HIS A 48 0
SHEET 2 C 2 THR A 116 HIS A 120 -1 N VAL A 118 O HIS A 46
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.09
LINK ND1 HIS A 46 CU CU1 A 155 1555 1555 2.05
LINK NE2 HIS A 48 CU CU1 A 155 1555 1555 1.98
LINK ND1 HIS A 63 ZN ZN A 154 1555 1555 2.11
LINK ND1 HIS A 71 ZN ZN A 154 1555 1555 1.97
LINK ND1 HIS A 80 ZN ZN A 154 1555 1555 2.04
LINK OD1 ASP A 83 ZN ZN A 154 1555 1555 1.89
LINK OD2 ASP A 83 ZN ZN A 154 1555 1555 2.39
LINK NE2 HIS A 120 CU CU1 A 155 1555 1555 1.98
SITE 1 CU 4 HIS A 46 HIS A 48 HIS A 120 CU1 A 155
SITE 1 ZN 4 HIS A 63 HIS A 71 HIS A 80 ZN A 154
SITE 1 AC1 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC2 4 HIS A 46 HIS A 48 HIS A 63 HIS A 120
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 - v 3 2 Bytes