Header list of 1t6w.pdb file
Complete list - t 27 2 Bytes
HEADER METAL BINDING PROTEIN 07-MAY-04 1T6W
TITLE RATIONAL DESIGN OF A CALCIUM-BINDING ADHESION PROTEIN NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN XP_346638;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS CALCIUM-BINDING PROTEIN, CD2, DESIGN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.YANG,A.L.WILKINS,Y.YE,Z.-R.LIU,J.L.URBAUER,A.KEARNEY,P.A.VAN DER
AUTHOR 2 MERWE,J.J.YANG
REVDAT 4 27-OCT-21 1T6W 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1T6W 1 VERSN
REVDAT 2 22-FEB-05 1T6W 1 JRNL
REVDAT 1 15-FEB-05 1T6W 0
JRNL AUTH W.YANG,A.L.WILKINS,Y.YE,Z.R.LIU,S.Y.LI,J.L.URBAUER,
JRNL AUTH 2 H.W.HELLINGA,A.KEARNEY,P.A.VAN DER MERWE,J.J.YANG
JRNL TITL DESIGN OF A CALCIUM-BINDING PROTEIN WITH DESIRED STRUCTURE
JRNL TITL 2 IN A CELL ADHESION MOLECULE.
JRNL REF J.AM.CHEM.SOC. V. 127 2085 2005
JRNL REFN ISSN 0002-7863
JRNL PMID 15713084
JRNL DOI 10.1021/JA0431307
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T6W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022387.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 95% H2O, 5% D2O, PROTEIN 1 MM,
REMARK 210 KCL 130 MM, CACL2 10 MM, PIPES
REMARK 210 20 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_TOCSY; 15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1
REMARK 210 METHOD USED : ANNEAL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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
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 ASP A 2 78.94 -100.03
REMARK 500 1 SER A 3 -74.94 -83.03
REMARK 500 1 ILE A 14 136.28 163.29
REMARK 500 1 MET A 23 75.20 -68.78
REMARK 500 1 ALA A 40 113.23 -167.20
REMARK 500 1 LYS A 45 39.40 -82.44
REMARK 500 1 MET A 46 -166.19 41.91
REMARK 500 1 SER A 52 165.97 179.05
REMARK 500 1 ASN A 60 33.25 -97.06
REMARK 500 1 ILE A 88 -67.31 -104.12
REMARK 500 2 ASP A 2 92.21 -62.27
REMARK 500 2 ILE A 14 136.33 160.36
REMARK 500 2 ALA A 40 111.86 -165.76
REMARK 500 2 ARG A 44 -88.98 -51.71
REMARK 500 2 LYS A 45 48.65 -82.59
REMARK 500 2 ASN A 60 31.91 -96.53
REMARK 500 3 ASP A 2 79.96 60.38
REMARK 500 3 ILE A 14 136.19 162.03
REMARK 500 3 ALA A 40 111.31 -166.06
REMARK 500 3 LYS A 45 -47.32 82.48
REMARK 500 3 ASN A 60 32.81 -96.13
REMARK 500 4 ASP A 2 -68.57 68.33
REMARK 500 4 ILE A 14 136.61 161.24
REMARK 500 4 ALA A 40 114.38 -174.73
REMARK 500 4 LYS A 45 46.72 -82.56
REMARK 500 4 MET A 46 -171.86 177.59
REMARK 500 4 LYS A 51 -90.33 -38.88
REMARK 500 4 ASN A 60 31.94 -96.24
REMARK 500 5 ILE A 14 136.02 163.31
REMARK 500 5 ALA A 40 112.17 -167.47
REMARK 500 5 ARG A 44 90.27 -59.83
REMARK 500 5 LYS A 45 -45.56 80.85
REMARK 500 5 ASN A 60 33.33 -96.76
REMARK 500 6 SER A 3 108.05 60.48
REMARK 500 6 ILE A 14 136.00 163.79
REMARK 500 6 ALA A 40 110.17 -166.60
REMARK 500 6 LYS A 45 46.35 -82.19
REMARK 500 6 MET A 46 -172.40 176.19
REMARK 500 6 LEU A 58 165.75 -49.19
REMARK 500 6 ASN A 60 33.11 -96.21
REMARK 500 6 ILE A 88 -69.30 -93.95
REMARK 500 7 ILE A 14 137.24 161.70
REMARK 500 7 ALA A 40 111.57 -166.64
REMARK 500 7 ARG A 44 94.40 -55.76
REMARK 500 7 LYS A 45 -46.98 81.66
REMARK 500 7 ASN A 60 33.12 -96.57
REMARK 500 7 ILE A 88 -70.71 -82.20
REMARK 500 8 ILE A 14 136.65 162.19
REMARK 500 8 ALA A 40 112.55 -162.34
REMARK 500 8 LYS A 45 39.10 -82.24
REMARK 500
REMARK 500 THIS ENTRY HAS 130 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 CA A 100 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 15 OD2
REMARK 620 2 ASP A 17 OD1 80.8
REMARK 620 3 ASN A 60 OD1 139.3 134.0
REMARK 620 4 ASP A 62 OD1 100.1 79.6 72.8
REMARK 620 5 ASP A 62 OD2 51.8 73.7 110.4 48.3
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 CA A 100
DBREF 1T6W A 1 99 UNP P08921 CD2_RAT 23 121
SEQADV 1T6W ASP A 15 UNP P08921 ASN 37 ENGINEERED MUTATION
SEQADV 1T6W ASP A 17 UNP P08921 ASN 39 ENGINEERED MUTATION
SEQRES 1 A 99 ARG ASP SER GLY THR VAL TRP GLY ALA LEU GLY HIS GLY
SEQRES 2 A 99 ILE ASP LEU ASP ILE PRO ASN PHE GLN MET THR ASP ASP
SEQRES 3 A 99 ILE ASP GLU VAL ARG TRP GLU ARG GLY SER THR LEU VAL
SEQRES 4 A 99 ALA GLU PHE LYS ARG LYS MET LYS PRO PHE LEU LYS SER
SEQRES 5 A 99 GLY ALA PHE GLU ILE LEU ALA ASN GLY ASP LEU LYS ILE
SEQRES 6 A 99 LYS ASN LEU THR ARG ASP ASP SER GLY THR TYR ASN VAL
SEQRES 7 A 99 THR VAL TYR SER THR ASN GLY THR ARG ILE LEU ASN LYS
SEQRES 8 A 99 ALA LEU ASP LEU ARG ILE LEU GLU
HET CA A 100 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 THR A 69 SER A 73 5 5
SHEET 1 A 6 THR A 5 ALA A 9 0
SHEET 2 A 6 ARG A 87 LEU A 98 1 O LEU A 98 N GLY A 8
SHEET 3 A 6 GLY A 74 SER A 82 -1 N VAL A 80 O ILE A 88
SHEET 4 A 6 ILE A 27 ARG A 34 -1 N GLU A 33 O ASN A 77
SHEET 5 A 6 THR A 37 LYS A 43 -1 O PHE A 42 N VAL A 30
SHEET 6 A 6 PHE A 49 LEU A 50 -1 O PHE A 49 N GLU A 41
SHEET 1 B 3 ILE A 14 LEU A 16 0
SHEET 2 B 3 LEU A 63 ILE A 65 -1 O ILE A 65 N ILE A 14
SHEET 3 B 3 PHE A 55 ILE A 57 -1 N GLU A 56 O LYS A 64
LINK OD2 ASP A 15 CA CA A 100 1555 1555 2.81
LINK OD1 ASP A 17 CA CA A 100 1555 1555 2.80
LINK OD1 ASN A 60 CA CA A 100 1555 1555 2.81
LINK OD1 ASP A 62 CA CA A 100 1555 1555 2.48
LINK OD2 ASP A 62 CA CA A 100 1555 1555 2.83
SITE 1 AC1 4 ASP A 15 ASP A 17 ASN A 60 ASP 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 - t 27 2 Bytes