Header list of 1iml.pdb file
Complete list - v 29 2 Bytes
HEADER METAL BINDING PROTEIN 23-DEC-95 1IML
TITLE CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE RICH INTESTINAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CRIP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;
SOURCE 3 ORGANISM_COMMON: BLACK RAT;
SOURCE 4 ORGANISM_TAXID: 10117;
SOURCE 5 ORGAN: SMALL INTESTINE;
SOURCE 6 TISSUE: SMOOTH MUSCLE;
SOURCE 7 CELL: SMOOTH MUSCLE CELLS;
SOURCE 8 GENE: CRIP;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET-3A NOVAGEN;
SOURCE 13 EXPRESSION_SYSTEM_GENE: CRIP
KEYWDS METAL-BINDING PROTEIN, LIM DOMAIN PROTEIN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 48
AUTHOR G.C.PEREZ-ALVARADO,J.L.KOSA,H.A.LOUIS,M.C.BECKERLE,D.R.WINGE,
AUTHOR 2 M.F.SUMMERS
REVDAT 3 29-NOV-17 1IML 1 KEYWDS REMARK HELIX
REVDAT 2 24-FEB-09 1IML 1 VERSN
REVDAT 1 11-JUL-96 1IML 0
JRNL AUTH G.C.PEREZ-ALVARADO,J.L.KOSA,H.A.LOUIS,M.C.BECKERLE,
JRNL AUTH 2 D.R.WINGE,M.F.SUMMERS
JRNL TITL STRUCTURE OF THE CYSTEINE-RICH INTESTINAL PROTEIN, CRIP.
JRNL REF J.MOL.BIOL. V. 257 153 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8632452
JRNL DOI 10.1006/JMBI.1996.0153
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.C.PEREZ-ALVARADO
REMARK 1 REF NMR STUDIES OF LIM DOMAIN 1995
REMARK 1 REF 2 PROTEINS
REMARK 1 PUBL BALTIMORE : UNIVERSITY OF MARYLAND, BALTIMORE COUNTY
REMARK 1 PUBL 2 (THESIS)
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.C.PEREZ-ALVARADO,C.MILES,J.W.MICHELSEN,H.A.LOUIS,
REMARK 1 AUTH 2 D.R.WINGE,M.C.BECKERLE,M.F.SUMMERS
REMARK 1 TITL STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE
REMARK 1 TITL 2 CYSTEINE RICH PROTEIN CRP
REMARK 1 REF NAT.STRUCT.BIOL. V. 1 388 1994
REMARK 1 REFN ISSN 1072-8368
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 1IML 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_1000174197.
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 : 48
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: 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 40 PHE A 12 CB - CG - CD2 ANGL. DEV. = -4.4 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 5 -73.06 -77.83
REMARK 500 1 ASP A 7 57.22 72.61
REMARK 500 1 LYS A 8 -168.78 -117.23
REMARK 500 1 SER A 18 131.83 -174.83
REMARK 500 1 LEU A 28 83.13 -62.77
REMARK 500 1 SER A 39 91.96 -61.13
REMARK 500 1 HIS A 42 -168.96 -110.86
REMARK 500 1 GLU A 46 92.84 -60.31
REMARK 500 1 LYS A 48 104.81 -177.97
REMARK 500 1 PHE A 65 -77.14 -66.81
REMARK 500 1 GLU A 71 -49.93 -165.51
REMARK 500 1 THR A 74 -166.50 -164.26
REMARK 500 1 PHE A 75 84.87 -67.80
REMARK 500 2 ASP A 7 53.33 72.29
REMARK 500 2 LYS A 8 -168.78 -111.70
REMARK 500 2 GLU A 14 44.75 -102.31
REMARK 500 2 SER A 18 132.09 -178.19
REMARK 500 2 LEU A 28 89.72 -60.02
REMARK 500 2 GLU A 31 36.95 -96.72
REMARK 500 2 LYS A 32 -44.38 -132.84
REMARK 500 2 HIS A 42 -168.91 -103.87
REMARK 500 2 GLU A 46 76.37 -61.72
REMARK 500 2 PHE A 60 30.14 -154.19
REMARK 500 2 PRO A 62 106.76 -51.86
REMARK 500 2 PHE A 65 109.69 -165.39
REMARK 500 2 SER A 72 -164.24 -106.17
REMARK 500 2 THR A 74 91.16 58.33
REMARK 500 3 LYS A 5 -74.36 -75.43
REMARK 500 3 ASP A 7 51.92 72.72
REMARK 500 3 LYS A 8 -169.01 -108.52
REMARK 500 3 GLU A 14 44.55 -101.22
REMARK 500 3 SER A 18 133.87 -170.13
REMARK 500 3 LEU A 19 18.34 59.87
REMARK 500 3 LEU A 28 84.41 -65.05
REMARK 500 3 GLU A 31 34.22 -95.80
REMARK 500 3 LYS A 32 -56.20 -131.97
REMARK 500 3 HIS A 42 -168.60 -114.14
REMARK 500 3 GLU A 46 92.21 -60.79
REMARK 500 3 LYS A 48 102.98 176.28
REMARK 500 3 PRO A 62 -82.33 -52.95
REMARK 500 3 LYS A 63 -77.35 -151.60
REMARK 500 3 ALA A 70 103.24 61.72
REMARK 500 3 SER A 72 -62.70 -100.93
REMARK 500 3 PHE A 75 -79.09 68.20
REMARK 500 4 LYS A 5 -74.09 -78.19
REMARK 500 4 ASP A 7 58.58 72.43
REMARK 500 4 LYS A 8 -168.56 -118.15
REMARK 500 4 SER A 18 133.35 -177.46
REMARK 500 4 LEU A 28 77.42 -66.16
REMARK 500 4 GLU A 31 38.59 -96.88
REMARK 500
REMARK 500 THIS ENTRY HAS 722 RAMACHANDRAN OUTLIERS.
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 PHE A 12 -11.75
REMARK 500 1 TRP A 23 -11.55
REMARK 500 1 CYS A 30 -12.40
REMARK 500 1 TYR A 50 -10.98
REMARK 500 1 CYS A 51 -12.69
REMARK 500 1 HIS A 53 -10.87
REMARK 500 2 PHE A 12 -12.34
REMARK 500 2 TRP A 23 -12.61
REMARK 500 2 CYS A 30 -11.37
REMARK 500 2 TYR A 50 -13.56
REMARK 500 2 CYS A 51 -12.69
REMARK 500 2 HIS A 53 -11.85
REMARK 500 3 PHE A 12 -12.91
REMARK 500 3 ASP A 22 -10.70
REMARK 500 3 CYS A 30 -13.63
REMARK 500 3 TYR A 50 -13.66
REMARK 500 3 CYS A 51 -11.30
REMARK 500 3 ASN A 52 -10.13
REMARK 500 3 HIS A 53 -10.31
REMARK 500 4 PHE A 12 -11.74
REMARK 500 4 TRP A 23 -11.77
REMARK 500 4 CYS A 30 -10.76
REMARK 500 4 TYR A 50 -10.04
REMARK 500 4 CYS A 51 -13.16
REMARK 500 4 HIS A 53 -10.68
REMARK 500 5 PHE A 12 -12.08
REMARK 500 5 ASP A 22 -10.44
REMARK 500 5 TRP A 23 -12.66
REMARK 500 5 CYS A 30 -11.40
REMARK 500 5 TYR A 50 -12.53
REMARK 500 5 CYS A 51 -12.22
REMARK 500 5 HIS A 53 -11.39
REMARK 500 6 ASP A 22 -10.38
REMARK 500 6 TRP A 23 -10.27
REMARK 500 6 CYS A 30 -11.49
REMARK 500 6 LYS A 32 -10.07
REMARK 500 6 TYR A 50 -13.52
REMARK 500 6 CYS A 51 -12.64
REMARK 500 6 HIS A 53 -10.88
REMARK 500 7 PHE A 12 -11.64
REMARK 500 7 TRP A 23 -11.47
REMARK 500 7 CYS A 30 -11.24
REMARK 500 7 GLY A 41 -10.07
REMARK 500 7 TYR A 50 -13.97
REMARK 500 7 CYS A 51 -11.23
REMARK 500 7 HIS A 53 -10.57
REMARK 500 8 PHE A 12 -11.90
REMARK 500 8 TRP A 23 -11.46
REMARK 500 8 CYS A 30 -11.53
REMARK 500 8 GLY A 40 10.92
REMARK 500
REMARK 500 THIS ENTRY HAS 256 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 77 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 3 SG
REMARK 620 2 CYS A 6 SG 106.6
REMARK 620 3 HIS A 24 ND1 92.9 93.2
REMARK 620 4 CYS A 27 SG 119.9 112.3 127.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 78 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 30 SG
REMARK 620 2 CYS A 33 SG 106.2
REMARK 620 3 CYS A 51 SG 105.7 106.5
REMARK 620 4 CYS A 55 SG 106.3 124.5 106.3
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 77
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 78
DBREF 1IML A 1 76 UNP P04006 CRP1_MOUSE 1 76
SEQRES 1 A 76 PRO LYS CYS PRO LYS CYS ASP LYS GLU VAL TYR PHE ALA
SEQRES 2 A 76 GLU ARG VAL THR SER LEU GLY LYS ASP TRP HIS ARG PRO
SEQRES 3 A 76 CYS LEU LYS CYS GLU LYS CYS GLY LYS THR LEU THR SER
SEQRES 4 A 76 GLY GLY HIS ALA GLU HIS GLU GLY LYS PRO TYR CYS ASN
SEQRES 5 A 76 HIS PRO CYS TYR SER ALA MET PHE GLY PRO LYS GLY PHE
SEQRES 6 A 76 GLY ARG GLY GLY ALA GLU SER HIS THR PHE LYS
HET ZN A 77 1
HET ZN A 78 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 CYS A 51 MET A 59 1 9
SHEET 1 A 2 LYS A 2 CYS A 3 0
SHEET 2 A 2 LYS A 8 TYR A 11 -1
SHEET 1 B 2 ARG A 15 SER A 18 0
SHEET 2 B 2 LYS A 21 HIS A 24 -1 N TRP A 23 O VAL A 16
SHEET 1 C 2 LEU A 28 CYS A 30 0
SHEET 2 C 2 LYS A 35 THR A 38 -1
SHEET 1 D 2 HIS A 42 HIS A 45 0
SHEET 2 D 2 LYS A 48 CYS A 51 -1 N TYR A 50 O ALA A 43
LINK ZN ZN A 77 SG CYS A 3 1555 1555 2.31
LINK ZN ZN A 77 SG CYS A 6 1555 1555 2.30
LINK ZN ZN A 77 ND1 HIS A 24 1555 1555 2.02
LINK ZN ZN A 77 SG CYS A 27 1555 1555 2.30
LINK ZN ZN A 78 SG CYS A 30 1555 1555 2.31
LINK ZN ZN A 78 SG CYS A 33 1555 1555 2.30
LINK ZN ZN A 78 SG CYS A 51 1555 1555 2.31
LINK ZN ZN A 78 SG CYS A 55 1555 1555 2.31
CISPEP 1 HIS A 53 PRO A 54 1 -23.82
CISPEP 2 HIS A 53 PRO A 54 2 -18.47
CISPEP 3 HIS A 53 PRO A 54 3 -13.43
CISPEP 4 HIS A 53 PRO A 54 4 -22.07
CISPEP 5 HIS A 53 PRO A 54 5 -17.81
CISPEP 6 HIS A 53 PRO A 54 6 -24.41
CISPEP 7 HIS A 53 PRO A 54 7 -15.80
CISPEP 8 HIS A 53 PRO A 54 8 -14.54
CISPEP 9 HIS A 53 PRO A 54 9 -13.51
CISPEP 10 HIS A 53 PRO A 54 10 -14.63
CISPEP 11 HIS A 53 PRO A 54 11 -14.46
CISPEP 12 HIS A 53 PRO A 54 12 -12.74
CISPEP 13 HIS A 53 PRO A 54 13 -15.53
CISPEP 14 HIS A 53 PRO A 54 14 -21.02
CISPEP 15 HIS A 53 PRO A 54 15 -13.06
CISPEP 16 HIS A 53 PRO A 54 16 -15.81
CISPEP 17 HIS A 53 PRO A 54 17 -11.11
CISPEP 18 HIS A 53 PRO A 54 18 -11.61
CISPEP 19 HIS A 53 PRO A 54 19 -19.11
CISPEP 20 HIS A 53 PRO A 54 20 -14.78
CISPEP 21 HIS A 53 PRO A 54 21 -13.39
CISPEP 22 HIS A 53 PRO A 54 22 -14.68
CISPEP 23 HIS A 53 PRO A 54 23 -14.34
CISPEP 24 HIS A 53 PRO A 54 24 -20.73
CISPEP 25 HIS A 53 PRO A 54 25 -13.32
CISPEP 26 HIS A 53 PRO A 54 26 -12.31
CISPEP 27 HIS A 53 PRO A 54 27 -17.24
CISPEP 28 HIS A 53 PRO A 54 28 -11.36
CISPEP 29 HIS A 53 PRO A 54 29 -12.02
CISPEP 30 HIS A 53 PRO A 54 30 -22.26
CISPEP 31 HIS A 53 PRO A 54 31 -12.52
CISPEP 32 HIS A 53 PRO A 54 32 -12.70
CISPEP 33 HIS A 53 PRO A 54 33 -13.93
CISPEP 34 HIS A 53 PRO A 54 34 -14.09
CISPEP 35 HIS A 53 PRO A 54 35 -14.19
CISPEP 36 HIS A 53 PRO A 54 36 -11.99
CISPEP 37 HIS A 53 PRO A 54 37 -11.51
CISPEP 38 HIS A 53 PRO A 54 38 -10.82
CISPEP 39 HIS A 53 PRO A 54 39 -20.70
CISPEP 40 HIS A 53 PRO A 54 40 -19.08
CISPEP 41 HIS A 53 PRO A 54 41 -12.07
CISPEP 42 HIS A 53 PRO A 54 42 -12.28
CISPEP 43 HIS A 53 PRO A 54 43 -25.35
CISPEP 44 HIS A 53 PRO A 54 44 -11.52
CISPEP 45 HIS A 53 PRO A 54 45 -10.79
CISPEP 46 HIS A 53 PRO A 54 46 -13.63
CISPEP 47 HIS A 53 PRO A 54 47 -12.69
CISPEP 48 HIS A 53 PRO A 54 48 -9.17
SITE 1 AC1 4 CYS A 3 CYS A 6 HIS A 24 CYS A 27
SITE 1 AC2 4 CYS A 30 CYS A 33 CYS A 51 CYS A 55
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 29 2 Bytes