Header list of 1rk7.pdb file
Complete list - t 27 2 Bytes
HEADER OXIDOREDUCTASE 21-NOV-03 1RK7
TITLE SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLE OF METAL
TITLE 2 IONS IN PROTEIN FOLDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
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: TOPP1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBR322 WITH HUMAN SOD GENE
KEYWDS APO FORM OF MONOMERIC MUTANT OF CU, ZN SOD; SOLUTION STRUCTURE,
KEYWDS 2 Q133M2SOD, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,F.CRAMARO,R.DEL CONTE,M.S.VIEZZOLI
REVDAT 3 27-OCT-21 1RK7 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RK7 1 VERSN
REVDAT 1 02-DEC-03 1RK7 0
JRNL AUTH L.BANCI,I.BERTINI,F.CRAMARO,R.DEL CONTE,M.S.VIEZZOLI
JRNL TITL SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLE
JRNL TITL 2 OF METAL IONS IN PROTEIN FOLDING
JRNL REF BIOCHEMISTRY V. 42 9543 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12911296
JRNL DOI 10.1021/BI034324M
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CALIBA, AMBER
REMARK 3 AUTHORS : GUENTER ET AL. (CALIBA), PEARLMAN ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE CALCULATED USING
REMARK 3 THE CONSTRAINTS: 2382 MEANINGFUL UPPER DISTANCE LIMITS, 42
REMARK 3 DIHEDRAL PHI ANGLES, 41 DIHEDRAL PSI ANGLES AND 42 PROTON PAIRS
REMARK 3 STEREOSPECIFICALLY ASSIGNED. THE DISULPHIDE BRIDGE BETWEEN C57
REMARK 3 AND C146 WAS INTRODUCED WITH THE UPPER AND LOWER DISTANCES
REMARK 3 LIMITS BETWEEN THE CB AND SG ATOMS OF THE TWO SIDE CHAINS.
REMARK 4
REMARK 4 1RK7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020828.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : APO SOD 2MM; APO SOD 2MM
REMARK 210 ENRICHED IN 15N; APO SOD 2MM
REMARK 210 ENRICHED IN 15N AND 13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCA(CO)NH,
REMARK 210 HNCACB,HNCO,HN(CA)CO,13C H(C)CH-TOCSY,13CC(CO)NH-TOCSY,13C NOESY-
REMARK 210 HSQC; HNHA,HNHB,15N HSQC NOESY,15N HSQC; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GLOMSA, DYANA, XWINNMR, PROCHECK
REMARK 210 -NMR AQUA
REMARK 210 METHOD USED : SIMULATED ANNEALING AND
REMARK 210 RESTRAINED ENERGY MINIMIZATION
REMARK 210 IN VACUUM
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY,TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE SOLUTION STRUCTURE OF APO SOD WAS DETERMINED USING
REMARK 210 TRIPLE RESONANCE THREE AND BI DIMENSIONAL AND HOMONUCLEAR
REMARK 210 BIDIMENSIONAL TECHNIQUES
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: 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 O LEU A 117 H GLY A 147 1.55
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 9 136.10 -178.29
REMARK 500 1 VAL A 14 92.78 -60.04
REMARK 500 1 ASN A 26 34.31 -152.97
REMARK 500 1 LYS A 30 97.58 -68.85
REMARK 500 1 LEU A 38 -170.93 -52.67
REMARK 500 1 GLU A 40 95.78 -40.42
REMARK 500 1 HIS A 46 173.20 -59.76
REMARK 500 1 VAL A 47 77.63 65.24
REMARK 500 1 ASP A 52 130.99 156.88
REMARK 500 1 ALA A 55 116.56 72.91
REMARK 500 1 CYS A 57 -72.33 -118.31
REMARK 500 1 THR A 58 -149.92 -114.72
REMARK 500 1 SER A 59 111.92 -178.48
REMARK 500 1 ALA A 60 -56.51 -159.63
REMARK 500 1 HIS A 63 36.95 -154.65
REMARK 500 1 PHE A 64 -149.91 67.82
REMARK 500 1 ARG A 69 -60.78 70.51
REMARK 500 1 ASP A 76 90.45 53.66
REMARK 500 1 GLU A 78 -68.02 173.89
REMARK 500 1 ARG A 79 45.54 30.90
REMARK 500 1 VAL A 81 -157.79 -97.75
REMARK 500 1 LEU A 84 -73.09 -93.28
REMARK 500 1 VAL A 87 -156.57 -117.58
REMARK 500 1 ASP A 90 -97.59 -82.96
REMARK 500 1 ASP A 92 23.20 -153.41
REMARK 500 1 VAL A 94 101.10 -39.93
REMARK 500 1 SER A 98 100.98 -164.44
REMARK 500 1 HIS A 110 63.55 -112.38
REMARK 500 1 THR A 116 85.38 -58.72
REMARK 500 1 LYS A 122 177.16 168.27
REMARK 500 1 GLU A 132 31.05 88.47
REMARK 500 1 GLN A 133 -64.64 -159.82
REMARK 500 1 THR A 137 -105.39 -124.04
REMARK 500 1 ALA A 140 -61.79 177.75
REMARK 500 1 LEU A 144 -70.44 -141.94
REMARK 500 1 CYS A 146 68.88 -156.10
REMARK 500 2 LYS A 9 117.26 -173.00
REMARK 500 2 VAL A 14 101.49 -53.25
REMARK 500 2 GLN A 22 81.04 -155.15
REMARK 500 2 LYS A 23 48.82 -85.53
REMARK 500 2 ASN A 26 33.42 -154.61
REMARK 500 2 LYS A 30 93.49 -66.00
REMARK 500 2 LEU A 38 -170.65 -54.02
REMARK 500 2 GLU A 40 122.16 -39.21
REMARK 500 2 GLU A 49 60.71 170.36
REMARK 500 2 GLU A 51 -153.50 43.63
REMARK 500 2 ASP A 52 114.16 -160.25
REMARK 500 2 ASN A 53 60.64 -179.38
REMARK 500 2 THR A 54 -51.58 -151.95
REMARK 500 2 ALA A 55 -85.22 169.50
REMARK 500
REMARK 500 THIS ENTRY HAS 1316 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BA9 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE HOLO MONOMERIC MUTANT OF CU, ZN SOD
DBREF 1RK7 A 1 153 UNP P00441 SODC_HUMAN 1 153
SEQADV 1RK7 ALA A 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1RK7 GLU A 50 UNP P00441 PHE 50 ENGINEERED MUTATION
SEQADV 1RK7 GLU A 51 UNP P00441 GLY 51 ENGINEERED MUTATION
SEQADV 1RK7 SER A 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1RK7 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
SHEET 1 A 5 ASP A 96 ASP A 101 0
SHEET 2 A 5 VAL A 29 SER A 34 -1 N VAL A 29 O ASP A 101
SHEET 3 A 5 ILE A 17 GLN A 22 -1 N ILE A 17 O SER A 34
SHEET 4 A 5 THR A 2 VAL A 7 -1 N ALA A 4 O PHE A 20
SHEET 5 A 5 GLY A 150 ALA A 152 -1 O GLY A 150 N VAL A 5
SSBOND 1 CYS A 57 CYS A 146 1555 1555 1.96
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