Header list of 1g47.pdb file
Complete list - b 23 2 Bytes
HEADER CELL ADHESION 26-OCT-00 1G47
TITLE 1ST LIM DOMAIN OF PINCH PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PINCH PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIM1 DOMAIN, RESIDUES 1-70;
COMPND 5 SYNONYM: PARTICULARLY INTERESTING NEW CYS-HIS PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LIMS1;
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_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMAL-C2X
KEYWDS LIM DOMAIN; ZN FINGER, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR A.VELYVIS,Y.YANG,C.WU,J.QIN
REVDAT 3 23-FEB-22 1G47 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1G47 1 VERSN
REVDAT 1 21-FEB-01 1G47 0
JRNL AUTH A.VELYVIS,Y.YANG,C.WU,J.QIN
JRNL TITL SOLUTION STRUCTURE OF THE FOCAL ADHESION ADAPTOR PINCH LIM1
JRNL TITL 2 DOMAIN AND CHARACTERIZATION OF ITS INTERACTION WITH THE
JRNL TITL 3 INTEGRIN-LINKED KINASE ANKYRIN REPEAT DOMAIN.
JRNL REF J.BIOL.CHEM. V. 276 4932 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11078733
JRNL DOI 10.1074/JBC.M007632200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843, X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER, A. (X-PLOR), BRUNGER, A. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G47 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012211.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM LIM1; 50MM PHOSPHATE;
REMARK 210 100MM NACL; 0.5MM BETA-
REMARK 210 MERCAPTOETHANOL; 0.5MM LIM1;
REMARK 210 50MM PHOSPHATE; 100MM NACL;
REMARK 210 0.5MM BETA-MERCAPTOETHANOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N/13C-SEPARATED_NOESY;
REMARK 210 HNHA; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 125
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-25
REMARK 465 RES C SSSEQI
REMARK 465 ILE A -3
REMARK 465 SER A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 TRP A 71
REMARK 465 ILE A 72
REMARK 465 LEU A 73
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 VAL A 24 H TYR A 31 1.55
REMARK 500 O PRO A 19 H ILE A 23 1.57
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 ALA A 2 -160.24 59.10
REMARK 500 1 ALA A 6 -81.03 -75.61
REMARK 500 1 CYS A 13 -25.23 -160.51
REMARK 500 1 ALA A 18 -55.38 -175.39
REMARK 500 1 ASN A 27 -44.19 71.99
REMARK 500 1 GLN A 34 44.31 -152.93
REMARK 500 1 PHE A 36 108.11 -42.57
REMARK 500 1 GLN A 40 -68.32 -104.82
REMARK 500 1 PRO A 46 -150.76 -63.91
REMARK 500 1 GLU A 47 -40.37 70.64
REMARK 500 1 LEU A 49 133.52 -177.70
REMARK 500 1 PHE A 50 -130.92 -150.78
REMARK 500 1 TYR A 51 57.47 -93.31
REMARK 500 1 GLU A 60 6.51 -66.84
REMARK 500 1 HIS A 61 -75.66 -81.27
REMARK 500 1 PHE A 67 86.24 66.26
REMARK 500 2 ALA A 8 110.99 67.29
REMARK 500 2 ALA A 18 -56.29 -174.96
REMARK 500 2 ASN A 27 -40.61 71.75
REMARK 500 2 GLN A 34 44.16 -166.89
REMARK 500 2 PHE A 36 100.58 -52.22
REMARK 500 2 ALA A 39 -17.66 -48.91
REMARK 500 2 GLN A 40 -73.22 -108.97
REMARK 500 2 PRO A 46 103.20 -58.52
REMARK 500 2 GLU A 47 43.89 30.68
REMARK 500 2 LEU A 49 70.77 45.89
REMARK 500 2 PHE A 50 -125.75 -81.68
REMARK 500 2 TYR A 51 58.59 -102.14
REMARK 500 2 LYS A 57 131.85 -171.44
REMARK 500 2 PHE A 67 75.87 62.67
REMARK 500 3 LEU A 5 130.31 69.86
REMARK 500 3 ALA A 6 -40.04 -159.66
REMARK 500 3 ALA A 18 -55.51 -174.90
REMARK 500 3 SER A 26 -113.77 -160.96
REMARK 500 3 ASN A 27 73.26 -40.11
REMARK 500 3 GLN A 34 48.99 -152.35
REMARK 500 3 PHE A 36 115.00 -38.29
REMARK 500 3 ALA A 39 -9.03 -55.80
REMARK 500 3 PRO A 46 -154.13 -65.12
REMARK 500 3 GLU A 47 -26.78 70.91
REMARK 500 3 LEU A 49 96.06 -176.92
REMARK 500 3 PHE A 50 -117.34 -105.52
REMARK 500 3 TYR A 51 45.26 -98.98
REMARK 500 3 GLU A 60 10.70 -68.91
REMARK 500 3 HIS A 61 -70.54 -86.08
REMARK 500 4 ALA A 4 -44.61 -163.92
REMARK 500 4 SER A 7 -86.03 -154.27
REMARK 500 4 CYS A 13 -26.65 -158.43
REMARK 500 4 ALA A 18 -53.18 -178.09
REMARK 500 4 ASN A 27 29.91 46.69
REMARK 500
REMARK 500 THIS ENTRY HAS 346 RAMACHANDRAN OUTLIERS.
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 998 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 CYS A 13 SG 115.0
REMARK 620 3 HIS A 32 ND1 107.1 104.8
REMARK 620 4 CYS A 35 SG 108.1 113.5 107.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 999 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 38 SG
REMARK 620 2 CYS A 41 SG 103.5
REMARK 620 3 CYS A 59 SG 102.5 115.8
REMARK 620 4 HIS A 61 ND1 123.0 97.3 114.9
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 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4884 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS FOR THIS PROTEIN DOMAIN
DBREF 1G47 A 1 70 UNP P48059 PINC_HUMAN 1 70
SEQADV 1G47 ILE A -3 UNP P48059 CLONING ARTIFACT
SEQADV 1G47 SER A -2 UNP P48059 CLONING ARTIFACT
SEQADV 1G47 GLU A -1 UNP P48059 CLONING ARTIFACT
SEQADV 1G47 PHE A 0 UNP P48059 CLONING ARTIFACT
SEQADV 1G47 TRP A 71 UNP P48059 CLONING ARTIFACT
SEQADV 1G47 ILE A 72 UNP P48059 CLONING ARTIFACT
SEQADV 1G47 LEU A 73 UNP P48059 CLONING ARTIFACT
SEQRES 1 A 77 ILE SER GLU PHE MET ALA ASN ALA LEU ALA SER ALA THR
SEQRES 2 A 77 CYS GLU ARG CYS LYS GLY GLY PHE ALA PRO ALA GLU LYS
SEQRES 3 A 77 ILE VAL ASN SER ASN GLY GLU LEU TYR HIS GLU GLN CYS
SEQRES 4 A 77 PHE VAL CYS ALA GLN CYS PHE GLN GLN PHE PRO GLU GLY
SEQRES 5 A 77 LEU PHE TYR GLU PHE GLU GLY ARG LYS TYR CYS GLU HIS
SEQRES 6 A 77 ASP PHE GLN MET LEU PHE ALA PRO CYS TRP ILE LEU
HET ZN A 998 1
HET ZN A 999 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 PHE A 45 LEU A 49 5 5
HELIX 2 2 CYS A 59 PHE A 67 1 9
SHEET 1 A 2 VAL A 24 SER A 26 0
SHEET 2 A 2 GLU A 29 TYR A 31 -1 O GLU A 29 N SER A 26
SHEET 1 B 2 TYR A 51 PHE A 53 0
SHEET 2 B 2 ARG A 56 TYR A 58 -1 O ARG A 56 N PHE A 53
LINK SG CYS A 10 ZN ZN A 998 1555 1555 2.30
LINK SG CYS A 13 ZN ZN A 998 1555 1555 2.30
LINK ND1 HIS A 32 ZN ZN A 998 1555 1555 2.00
LINK SG CYS A 35 ZN ZN A 998 1555 1555 2.31
LINK SG CYS A 38 ZN ZN A 999 1555 1555 2.31
LINK SG CYS A 41 ZN ZN A 999 1555 1555 2.30
LINK SG CYS A 59 ZN ZN A 999 1555 1555 2.30
LINK ND1 HIS A 61 ZN ZN A 999 1555 1555 2.01
SITE 1 AC1 4 CYS A 10 CYS A 13 HIS A 32 CYS A 35
SITE 1 AC2 4 CYS A 38 CYS A 41 CYS A 59 HIS A 61
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 23 2 Bytes