Header list of 1kmg.pdb file
Complete list - t 27 2 Bytes
HEADER OXIDOREDUCTASE 15-DEC-01 1KMG
TITLE THE SOLUTION STRUCTURE OF MONOMERIC COPPER-FREE SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 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: SOD1;
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: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPHSOD1IQ
KEYWDS OXIDOREDUCTASE, SUPEROXIDE DISMUTASE, COPPER-FREE PROTEIN, BETA-
KEYWDS 2 BARREL
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR L.BANCI,I.BERTINI,F.CANTINI,M.D'ONOFRIO,M.S.VIEZZOLI
REVDAT 4 27-OCT-21 1KMG 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1KMG 1 VERSN
REVDAT 2 01-APR-03 1KMG 1 JRNL
REVDAT 1 02-OCT-02 1KMG 0
JRNL AUTH L.BANCI,I.BERTINI,F.CANTINI,M.D'ONOFRIO,M.S.VIEZZOLI
JRNL TITL STRUCTURE AND DYNAMICS OF COPPER-FREE SOD: THE PROTEIN
JRNL TITL 2 BEFORE BINDING COPPER.
JRNL REF PROTEIN SCI. V. 11 2479 2002
JRNL REFN ISSN 0961-8368
JRNL PMID 12237469
JRNL DOI 10.1110/PS.0210802
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, AMBER 5.0
REMARK 3 AUTHORS : PEARLMAN, D.A., CASE, D.A., CALDWELL, J.W., ROSS,
REMARK 3 W.S., CHEATHAM, T.E., FERGUSON, D.M., SEIBEL, G.L.,
REMARK 3 SINGH, U.C., WEINER, P.K., AND KOLLMAN, P.A.
REMARK 3 (1997) (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KMG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015109.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : 20 MM PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM OF 15N AND 13C ENRICHED
REMARK 210 SUPEROXIDE DISMUTASE; 2MM OF 15N
REMARK 210 AND 13C ENRICHED SUPEROXIDE
REMARK 210 DISMUTASE; 2MM UNLABELLED
REMARK 210 SUPEROXIDE DISMUTASE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; CBCA(CO)NH;
REMARK 210 CBCANH; HNCO; HN(CA)CO; CC(CO)NH-
REMARK 210 TOCSY; 13C-HCCH-TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 700 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3, DIANA 1.5, CORMA,
REMARK 210 GARANT 2.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
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 3 CYS A 146 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 11 CYS A 57 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 18 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 32 ARG A 115 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 34 PHE A 20 CB - CG - CD2 ANGL. DEV. = -5.0 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 2 121.38 92.53
REMARK 500 1 LYS A 9 -52.05 -135.22
REMARK 500 1 SER A 25 -68.55 -101.69
REMARK 500 1 GLU A 49 -103.39 -51.30
REMARK 500 1 GLU A 51 -107.39 -73.99
REMARK 500 1 THR A 54 -55.21 -170.22
REMARK 500 1 ALA A 55 -53.01 -170.37
REMARK 500 1 THR A 58 7.74 -156.41
REMARK 500 1 SER A 59 -40.67 -176.00
REMARK 500 1 LEU A 67 -65.70 -155.84
REMARK 500 1 SER A 68 71.45 -154.95
REMARK 500 1 ARG A 79 160.57 177.33
REMARK 500 1 VAL A 81 39.62 -79.49
REMARK 500 1 ASP A 90 -90.38 -74.11
REMARK 500 1 LYS A 91 -34.37 -158.23
REMARK 500 1 ASP A 109 -105.60 55.10
REMARK 500 1 GLU A 121 -71.96 -50.82
REMARK 500 1 LEU A 126 -13.71 72.63
REMARK 500 1 ASN A 131 -78.54 -141.42
REMARK 500 1 GLU A 132 -54.06 179.56
REMARK 500 1 SER A 134 -77.13 -29.57
REMARK 500 1 ASN A 139 57.13 36.25
REMARK 500 1 LEU A 144 -72.64 -120.32
REMARK 500 1 ILE A 151 57.00 -98.65
REMARK 500 2 LYS A 9 -47.97 -139.77
REMARK 500 2 ASN A 26 83.04 -161.47
REMARK 500 2 LEU A 38 -168.16 -72.14
REMARK 500 2 GLU A 40 175.95 -51.24
REMARK 500 2 GLU A 51 -153.31 -80.61
REMARK 500 2 ASN A 53 -84.15 -152.79
REMARK 500 2 CYS A 57 29.49 -74.79
REMARK 500 2 SER A 59 68.74 177.69
REMARK 500 2 ALA A 60 -86.49 -141.61
REMARK 500 2 HIS A 63 57.57 -62.17
REMARK 500 2 PHE A 64 77.40 35.88
REMARK 500 2 LEU A 67 -66.63 -155.33
REMARK 500 2 SER A 68 74.71 -154.40
REMARK 500 2 ARG A 79 147.36 156.37
REMARK 500 2 LYS A 91 -55.99 -168.35
REMARK 500 2 SER A 98 70.40 -156.95
REMARK 500 2 GLU A 121 -72.15 -45.16
REMARK 500 2 LEU A 126 -7.61 81.55
REMARK 500 2 ASN A 131 -89.48 177.64
REMARK 500 2 GLU A 132 -57.35 -170.38
REMARK 500 2 THR A 137 -52.28 -132.53
REMARK 500 2 SER A 142 -179.71 -67.76
REMARK 500 2 LEU A 144 -85.27 -121.50
REMARK 500 2 ILE A 151 55.39 -92.11
REMARK 500 3 LYS A 9 -53.20 -132.23
REMARK 500 3 PRO A 13 40.59 -77.52
REMARK 500
REMARK 500 THIS ENTRY HAS 814 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 THR A 58 SER A 59 1 -126.12
REMARK 500 THR A 58 SER A 59 2 -115.75
REMARK 500 ILE A 99 GLU A 100 2 145.91
REMARK 500 LEU A 38 THR A 39 3 149.73
REMARK 500 THR A 58 SER A 59 3 105.09
REMARK 500 ASP A 83 LEU A 84 3 147.03
REMARK 500 ALA A 152 GLN A 153 3 141.55
REMARK 500 THR A 58 SER A 59 4 -141.24
REMARK 500 THR A 58 SER A 59 5 -119.01
REMARK 500 THR A 58 SER A 59 6 -121.75
REMARK 500 THR A 58 SER A 59 7 -142.53
REMARK 500 GLY A 82 ASP A 83 7 143.98
REMARK 500 ASP A 96 VAL A 97 7 145.46
REMARK 500 THR A 58 SER A 59 8 -110.98
REMARK 500 ARG A 79 HIS A 80 8 147.08
REMARK 500 CYS A 57 THR A 58 9 -142.64
REMARK 500 THR A 58 SER A 59 9 -143.07
REMARK 500 GLY A 82 ASP A 83 9 146.64
REMARK 500 THR A 58 SER A 59 10 -117.95
REMARK 500 ARG A 79 HIS A 80 10 145.85
REMARK 500 VAL A 94 ALA A 95 10 149.18
REMARK 500 ASP A 96 VAL A 97 10 -148.31
REMARK 500 THR A 58 SER A 59 11 -123.62
REMARK 500 THR A 58 SER A 59 12 -133.26
REMARK 500 ALA A 152 GLN A 153 12 144.60
REMARK 500 LEU A 38 THR A 39 13 146.18
REMARK 500 THR A 58 SER A 59 13 -146.71
REMARK 500 THR A 58 SER A 59 14 -136.01
REMARK 500 ALA A 152 GLN A 153 14 139.82
REMARK 500 THR A 58 SER A 59 15 82.27
REMARK 500 LYS A 75 ASP A 76 15 -145.10
REMARK 500 GLY A 82 ASP A 83 15 149.78
REMARK 500 ALA A 152 GLN A 153 15 129.61
REMARK 500 THR A 58 SER A 59 16 -128.00
REMARK 500 ALA A 152 GLN A 153 16 142.32
REMARK 500 ASP A 11 GLY A 12 17 148.94
REMARK 500 THR A 58 SER A 59 17 -144.02
REMARK 500 ILE A 99 GLU A 100 17 149.31
REMARK 500 ILE A 35 LYS A 36 18 149.63
REMARK 500 THR A 58 SER A 59 18 139.99
REMARK 500 THR A 58 SER A 59 19 -115.65
REMARK 500 ASP A 83 LEU A 84 19 141.53
REMARK 500 THR A 58 SER A 59 20 -101.63
REMARK 500 THR A 58 SER A 59 21 -115.43
REMARK 500 THR A 58 SER A 59 22 143.46
REMARK 500 THR A 58 SER A 59 23 143.36
REMARK 500 THR A 58 SER A 59 24 -137.87
REMARK 500 THR A 58 SER A 59 25 -141.66
REMARK 500 THR A 58 SER A 59 26 -137.38
REMARK 500 VAL A 5 ALA A 6 27 148.98
REMARK 500
REMARK 500 THIS ENTRY HAS 71 NON CIS, NON-TRANS OMEGA 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 HIS A 43 0.09 SIDE CHAIN
REMARK 500 1 ARG A 79 0.10 SIDE CHAIN
REMARK 500 1 HIS A 80 0.12 SIDE CHAIN
REMARK 500 1 ARG A 115 0.12 SIDE CHAIN
REMARK 500 2 ARG A 79 0.10 SIDE CHAIN
REMARK 500 2 HIS A 80 0.10 SIDE CHAIN
REMARK 500 3 HIS A 43 0.09 SIDE CHAIN
REMARK 500 3 HIS A 80 0.13 SIDE CHAIN
REMARK 500 3 ARG A 115 0.09 SIDE CHAIN
REMARK 500 4 HIS A 43 0.09 SIDE CHAIN
REMARK 500 4 HIS A 80 0.14 SIDE CHAIN
REMARK 500 4 ARG A 115 0.08 SIDE CHAIN
REMARK 500 5 ARG A 79 0.12 SIDE CHAIN
REMARK 500 5 HIS A 80 0.10 SIDE CHAIN
REMARK 500 5 ARG A 115 0.12 SIDE CHAIN
REMARK 500 6 PHE A 20 0.10 SIDE CHAIN
REMARK 500 6 HIS A 43 0.09 SIDE CHAIN
REMARK 500 6 HIS A 80 0.14 SIDE CHAIN
REMARK 500 7 HIS A 80 0.13 SIDE CHAIN
REMARK 500 8 ARG A 69 0.07 SIDE CHAIN
REMARK 500 8 HIS A 80 0.14 SIDE CHAIN
REMARK 500 9 PHE A 20 0.10 SIDE CHAIN
REMARK 500 9 HIS A 43 0.08 SIDE CHAIN
REMARK 500 9 HIS A 80 0.14 SIDE CHAIN
REMARK 500 9 ARG A 143 0.08 SIDE CHAIN
REMARK 500 10 HIS A 43 0.09 SIDE CHAIN
REMARK 500 10 HIS A 80 0.14 SIDE CHAIN
REMARK 500 10 ARG A 115 0.10 SIDE CHAIN
REMARK 500 11 HIS A 43 0.10 SIDE CHAIN
REMARK 500 11 HIS A 80 0.11 SIDE CHAIN
REMARK 500 11 ARG A 143 0.08 SIDE CHAIN
REMARK 500 12 HIS A 43 0.09 SIDE CHAIN
REMARK 500 12 HIS A 80 0.14 SIDE CHAIN
REMARK 500 13 HIS A 80 0.13 SIDE CHAIN
REMARK 500 14 PHE A 20 0.09 SIDE CHAIN
REMARK 500 14 HIS A 43 0.09 SIDE CHAIN
REMARK 500 14 HIS A 80 0.15 SIDE CHAIN
REMARK 500 15 HIS A 43 0.08 SIDE CHAIN
REMARK 500 15 ARG A 69 0.12 SIDE CHAIN
REMARK 500 15 ARG A 79 0.20 SIDE CHAIN
REMARK 500 15 HIS A 80 0.12 SIDE CHAIN
REMARK 500 15 ARG A 115 0.12 SIDE CHAIN
REMARK 500 16 HIS A 43 0.09 SIDE CHAIN
REMARK 500 16 HIS A 80 0.15 SIDE CHAIN
REMARK 500 16 ARG A 115 0.10 SIDE CHAIN
REMARK 500 17 PHE A 20 0.09 SIDE CHAIN
REMARK 500 17 HIS A 43 0.09 SIDE CHAIN
REMARK 500 17 HIS A 80 0.13 SIDE CHAIN
REMARK 500 18 HIS A 43 0.08 SIDE CHAIN
REMARK 500 18 ARG A 69 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 99 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 ZN A 154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 HIS A 71 ND1 116.8
REMARK 620 3 HIS A 80 ND1 119.6 121.5
REMARK 620 4 ASP A 83 OD2 82.0 111.3 91.0
REMARK 620 5 THR A 137 O 79.7 87.4 88.1 158.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 154
DBREF 1KMG A 1 153 UNP P00441 SODC_HUMAN 1 153
SEQADV 1KMG ALA A 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1KMG GLU A 50 UNP P00441 PHE 50 ENGINEERED MUTATION
SEQADV 1KMG GLU A 51 UNP P00441 GLY 51 ENGINEERED MUTATION
SEQADV 1KMG SER A 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1KMG 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
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLU A 132 THR A 137 1 6
SHEET 1 A 3 ALA A 4 LEU A 8 0
SHEET 2 A 3 GLY A 16 GLU A 21 -1 O PHE A 20 N ALA A 4
SHEET 3 A 3 LYS A 30 GLY A 33 -1 O TRP A 32 N ASN A 19
SHEET 1 B 4 ASP A 83 ALA A 89 0
SHEET 2 B 4 GLY A 41 HIS A 48 -1 N PHE A 45 O GLY A 85
SHEET 3 B 4 THR A 116 HIS A 120 -1 O VAL A 118 N HIS A 46
SHEET 4 B 4 ARG A 143 VAL A 148 -1 O ALA A 145 N VAL A 119
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.09
LINK ND1 HIS A 63 ZN ZN A 154 1555 1555 2.23
LINK ND1 HIS A 71 ZN ZN A 154 1555 1555 2.06
LINK ND1 HIS A 80 ZN ZN A 154 1555 1555 2.19
LINK OD2 ASP A 83 ZN ZN A 154 1555 1555 1.90
LINK O THR A 137 ZN ZN A 154 1555 1555 1.88
SITE 1 AC1 5 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 2 AC1 5 THR A 137
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