Header list of 1ctl.pdb file
Complete list - b 16 2 Bytes
HEADER METAL BINDING PROTEIN 06-JAN-95 1CTL
TITLE STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH
TITLE 2 PROTEIN CRP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AVIAN CYSTEINE RICH PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: GIZZARD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAED4-LIM2
KEYWDS LIM DOMAIN CONTAINING PROTEINS, METAL-BINDING PROTEIN, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR G.C.PEREZ-ALVARADO,C.MILES,J.W.MICHELSEN,H.A.LOUIS,D.R.WINGE,
AUTHOR 2 M.C.BECKERLE,M.F.SUMMERS
REVDAT 3 16-FEB-22 1CTL 1 KEYWDS REMARK LINK
REVDAT 2 24-FEB-09 1CTL 1 VERSN
REVDAT 1 03-JUN-95 1CTL 0
JRNL AUTH G.C.PEREZ-ALVARADO,C.MILES,J.W.MICHELSEN,H.A.LOUIS,
JRNL AUTH 2 D.R.WINGE,M.C.BECKERLE,M.F.SUMMERS
JRNL TITL STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE
JRNL TITL 2 CYSTEINE RICH PROTEIN CRP.
JRNL REF NAT.STRUCT.BIOL. V. 1 388 1994
JRNL REFN ISSN 1072-8368
JRNL PMID 7664053
JRNL DOI 10.1038/NSB0694-388
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DSPACE
REMARK 3 AUTHORS : HARE RESEARCH INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CTL 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_1000172522.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 GLN A 3 146.86 64.55
REMARK 500 1 SER A 8 116.18 65.81
REMARK 500 1 ALA A 21 92.54 61.73
REMARK 500 1 VAL A 24 -168.50 -107.04
REMARK 500 1 ALA A 27 -82.43 61.54
REMARK 500 1 ALA A 39 41.77 -97.66
REMARK 500 1 LYS A 40 -48.35 -131.47
REMARK 500 1 LEU A 45 -163.63 -100.84
REMARK 500 1 ASP A 54 -95.49 60.86
REMARK 500 1 ASN A 66 62.27 -117.85
REMARK 500 1 LYS A 70 -76.13 179.98
REMARK 500 1 PHE A 74 -78.44 70.02
REMARK 500 1 ALA A 80 35.90 -166.09
REMARK 500 1 HIS A 83 -80.58 69.68
REMARK 500 2 SER A 8 -72.73 -139.94
REMARK 500 2 TYR A 19 38.89 -94.55
REMARK 500 2 ALA A 20 67.87 61.84
REMARK 500 2 ALA A 21 -64.41 -129.12
REMARK 500 2 ALA A 27 -83.22 62.75
REMARK 500 2 THR A 49 30.28 -168.60
REMARK 500 2 ALA A 51 107.97 -162.67
REMARK 500 2 LYS A 53 109.98 -166.29
REMARK 500 2 PRO A 69 91.50 -58.79
REMARK 500 2 LYS A 70 -169.12 64.38
REMARK 500 2 GLN A 76 -76.00 69.90
REMARK 500 2 ALA A 78 -162.40 61.41
REMARK 500 2 LEU A 81 -79.88 60.16
REMARK 500 2 HIS A 83 -80.44 71.58
REMARK 500 2 SER A 84 96.65 61.22
REMARK 500 3 ALA A 2 -82.71 62.29
REMARK 500 3 GLN A 3 27.17 -144.70
REMARK 500 3 ALA A 21 110.25 61.94
REMARK 500 3 ALA A 27 -82.44 61.38
REMARK 500 3 ALA A 39 41.99 -96.00
REMARK 500 3 LYS A 40 -53.57 -129.93
REMARK 500 3 LEU A 45 -163.51 -103.62
REMARK 500 3 GLU A 46 -159.26 -112.71
REMARK 500 3 THR A 49 78.68 -151.27
REMARK 500 3 LYS A 53 97.32 -175.71
REMARK 500 3 PRO A 69 91.88 -52.38
REMARK 500 3 LYS A 70 -77.45 65.22
REMARK 500 3 GLN A 76 -176.74 61.37
REMARK 500 3 ALA A 80 -82.61 62.23
REMARK 500 3 HIS A 83 -80.40 72.05
REMARK 500 3 SER A 84 -166.17 -177.27
REMARK 500 4 ALA A 2 -171.37 61.44
REMARK 500 4 ALA A 21 93.10 61.76
REMARK 500 4 PHE A 36 95.04 -60.60
REMARK 500 4 ALA A 39 41.01 -95.00
REMARK 500 4 GLU A 46 -159.34 -171.47
REMARK 500
REMARK 500 THIS ENTRY HAS 287 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 LYS A 23 VAL A 24 2 -147.70
REMARK 500 TYR A 58 CYS A 59 3 -149.98
REMARK 500 TYR A 58 CYS A 59 5 -149.26
REMARK 500 GLU A 22 LYS A 23 8 -146.14
REMARK 500 LYS A 23 VAL A 24 9 -148.59
REMARK 500 TYR A 58 CYS A 59 9 -148.59
REMARK 500 LYS A 23 VAL A 24 11 -147.16
REMARK 500 TYR A 58 CYS A 59 11 -148.81
REMARK 500 TYR A 58 CYS A 59 13 -146.04
REMARK 500 LYS A 23 VAL A 24 14 -148.96
REMARK 500 TYR A 58 CYS A 59 14 -149.91
REMARK 500 TYR A 58 CYS A 59 15 -143.39
REMARK 500 LYS A 23 VAL A 24 16 -148.03
REMARK 500 TYR A 58 CYS A 59 16 -148.24
REMARK 500 LYS A 23 VAL A 24 17 -147.33
REMARK 500 GLY A 10 CYS A 11 18 -149.59
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 8 GLU A 22 0.08 SIDE CHAIN
REMARK 500 8 HIS A 32 0.10 SIDE CHAIN
REMARK 500 9 TYR A 58 0.08 SIDE CHAIN
REMARK 500 12 HIS A 32 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 CYS A 38 -12.53
REMARK 500 1 CYS A 59 11.02
REMARK 500 1 LYS A 60 -10.92
REMARK 500 1 CYS A 62 -11.00
REMARK 500 2 VAL A 18 -10.73
REMARK 500 2 ALA A 20 10.21
REMARK 500 2 TRP A 31 -10.16
REMARK 500 3 CYS A 38 -11.95
REMARK 500 3 LYS A 60 -10.43
REMARK 500 3 CYS A 62 -10.82
REMARK 500 4 CYS A 38 -11.52
REMARK 500 5 VAL A 18 -10.74
REMARK 500 5 CYS A 38 -11.61
REMARK 500 5 CYS A 59 10.37
REMARK 500 5 LYS A 60 -10.56
REMARK 500 5 CYS A 62 -10.53
REMARK 500 6 TRP A 31 -10.91
REMARK 500 6 CYS A 38 -12.32
REMARK 500 7 LYS A 33 12.08
REMARK 500 7 CYS A 38 -11.36
REMARK 500 7 LEU A 45 10.14
REMARK 500 7 SER A 47 11.12
REMARK 500 8 VAL A 18 -13.76
REMARK 500 8 GLU A 22 11.24
REMARK 500 8 CYS A 38 -11.18
REMARK 500 8 CYS A 59 10.33
REMARK 500 8 LYS A 60 -10.61
REMARK 500 8 CYS A 62 -10.88
REMARK 500 9 TRP A 31 -10.01
REMARK 500 9 ARG A 37 -10.77
REMARK 500 9 CYS A 38 -11.15
REMARK 500 9 LYS A 60 -11.62
REMARK 500 9 CYS A 62 -10.21
REMARK 500 10 CYS A 38 -11.96
REMARK 500 10 LEU A 45 13.30
REMARK 500 10 GLU A 46 -10.85
REMARK 500 11 CYS A 11 -10.08
REMARK 500 11 LYS A 33 11.03
REMARK 500 11 CYS A 38 -12.25
REMARK 500 11 CYS A 59 10.47
REMARK 500 11 LYS A 60 -10.59
REMARK 500 11 CYS A 62 -10.63
REMARK 500 12 SER A 8 -10.07
REMARK 500 12 CYS A 38 -12.59
REMARK 500 13 GLU A 22 -11.78
REMARK 500 13 ARG A 37 -10.43
REMARK 500 13 CYS A 38 -14.76
REMARK 500 13 LEU A 45 11.90
REMARK 500 14 TRP A 31 -10.15
REMARK 500 14 CYS A 38 -11.93
REMARK 500
REMARK 500 THIS ENTRY HAS 66 MAIN CHAIN PLANARITY 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 86 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 14 SG 107.0
REMARK 620 3 HIS A 32 ND1 93.5 95.8
REMARK 620 4 CYS A 35 SG 122.2 111.2 123.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 87 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 38 SG
REMARK 620 2 CYS A 41 SG 105.5
REMARK 620 3 CYS A 59 SG 106.6 106.5
REMARK 620 4 CYS A 62 SG 125.5 105.5 106.0
REMARK 620 N 1 2 3
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 86
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 87
DBREF 1CTL A 1 85 UNP P67966 CSRP1_CHICK 107 191
SEQRES 1 A 85 MET ALA GLN LYS VAL GLY GLY SER ASP GLY CYS PRO ARG
SEQRES 2 A 85 CYS GLY GLN ALA VAL TYR ALA ALA GLU LYS VAL ILE GLY
SEQRES 3 A 85 ALA GLY LYS SER TRP HIS LYS SER CYS PHE ARG CYS ALA
SEQRES 4 A 85 LYS CYS GLY LYS SER LEU GLU SER THR THR LEU ALA ASP
SEQRES 5 A 85 LYS ASP GLY GLU ILE TYR CYS LYS GLY CYS TYR ALA LYS
SEQRES 6 A 85 ASN PHE GLY PRO LYS GLY PHE GLY PHE GLY GLN GLY ALA
SEQRES 7 A 85 GLY ALA LEU ILE HIS SER GLN
HET ZN A 86 1
HET ZN A 87 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 LYS A 60 LYS A 65 1 6
SHEET 1 A 2 GLY A 10 CYS A 11 0
SHEET 2 A 2 GLN A 16 VAL A 18 -1 O GLN A 16 N CYS A 11
SHEET 1 B 2 LYS A 23 GLY A 26 0
SHEET 2 B 2 LYS A 29 LYS A 33 -1 N TRP A 31 O VAL A 24
SHEET 1 C 2 PHE A 36 CYS A 38 0
SHEET 2 C 2 LYS A 43 LEU A 45 -1 O LYS A 43 N CYS A 38
SHEET 1 D 2 LEU A 50 LYS A 53 0
SHEET 2 D 2 GLU A 56 LYS A 60 -1 N TYR A 58 O ALA A 51
LINK SG CYS A 11 ZN ZN A 86 1555 1555 2.30
LINK SG CYS A 14 ZN ZN A 86 1555 1555 2.30
LINK ND1 HIS A 32 ZN ZN A 86 1555 1555 2.01
LINK SG CYS A 35 ZN ZN A 86 1555 1555 2.30
LINK SG CYS A 38 ZN ZN A 87 1555 1555 2.31
LINK SG CYS A 41 ZN ZN A 87 1555 1555 2.32
LINK SG CYS A 59 ZN ZN A 87 1555 1555 2.29
LINK SG CYS A 62 ZN ZN A 87 1555 1555 2.32
SITE 1 AC1 4 CYS A 11 CYS A 14 HIS A 32 CYS A 35
SITE 1 AC2 4 CYS A 38 CYS A 41 CYS A 59 CYS A 62
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 16 2 Bytes