HEADER CELL ADHESION 16-DEC-96 2NCM
TITLE NEURAL CELL ADHESION MOLECULE, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEURAL CELL ADHESION MOLECULE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN 1;
COMPND 5 SYNONYM: NCAM DOMAIN 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 STRAIN: C57BL/6;
SOURCE 6 ORGAN: BRAIN;
SOURCE 7 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHIL-S1
KEYWDS CELL ADHESION, GLYCOPROTEIN, HEPARIN-BINDING, GPI-ANCHOR, NEURAL
KEYWDS 2 ADHESION MOLECULE, IMMUNOGLOBULIN FOLD
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.K.THOMSEN,F.M.POULSEN
REVDAT 3 29-NOV-17 2NCM 1 REMARK HELIX
REVDAT 2 24-FEB-09 2NCM 1 VERSN
REVDAT 1 12-MAR-97 2NCM 0
SPRSDE 12-MAR-97 2NCM 1NCM
JRNL AUTH N.K.THOMSEN,V.SOROKA,P.H.JENSEN,V.BEREZIN,V.V.KISELYOV,
JRNL AUTH 2 E.BOCK,F.M.POULSEN
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST DOMAIN OF
JRNL TITL 2 NEURAL CELL ADHESION MOLECULE.
JRNL REF NAT.STRUCT.BIOL. V. 3 581 1996
JRNL REFN ISSN 1072-8368
JRNL PMID 8673600
JRNL DOI 10.1038/NSB0796-581
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NCM 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_1000178399.
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 : 20
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 VAL A 2 -43.59 -156.49
REMARK 500 1 LYS A 20 119.52 -164.16
REMARK 500 1 ASP A 29 37.97 -173.32
REMARK 500 1 LYS A 31 -167.87 60.22
REMARK 500 1 PRO A 40 -16.85 -49.93
REMARK 500 1 ASN A 48 65.86 -118.34
REMARK 500 1 GLN A 49 -59.70 -126.11
REMARK 500 1 ASN A 57 -80.35 -110.51
REMARK 500 1 ASP A 58 -176.45 -56.24
REMARK 500 1 ASP A 60 22.68 -152.78
REMARK 500 1 TYR A 67 -113.88 -60.20
REMARK 500 1 ASN A 68 94.17 -55.21
REMARK 500 1 ALA A 74 107.81 -51.37
REMARK 500 1 THR A 87 103.46 -58.52
REMARK 500 2 VAL A 2 37.29 -152.87
REMARK 500 2 LYS A 31 -86.48 59.98
REMARK 500 2 LYS A 33 106.47 -3.63
REMARK 500 2 GLN A 50 -72.73 -156.67
REMARK 500 2 ASN A 57 -80.77 -91.16
REMARK 500 2 ASP A 58 -177.92 -65.26
REMARK 500 2 TYR A 67 -113.46 -59.57
REMARK 500 2 ASN A 68 96.14 -53.28
REMARK 500 2 THR A 87 108.30 -57.92
REMARK 500 3 VAL A 2 49.28 -159.64
REMARK 500 3 ALA A 30 -178.80 -68.48
REMARK 500 3 PRO A 40 -74.00 -29.12
REMARK 500 3 GLU A 43 -168.72 71.04
REMARK 500 3 ASN A 48 63.60 -152.69
REMARK 500 3 GLN A 49 -73.58 -64.11
REMARK 500 3 GLN A 50 -74.51 -147.84
REMARK 500 3 ASN A 57 -79.97 -98.72
REMARK 500 3 ASP A 58 -177.63 -62.64
REMARK 500 3 ASP A 60 17.89 -149.37
REMARK 500 3 TYR A 67 -107.59 -58.36
REMARK 500 3 ASN A 68 95.74 -56.42
REMARK 500 3 THR A 87 107.81 -59.55
REMARK 500 4 LEU A 3 118.16 -168.72
REMARK 500 4 LYS A 20 118.99 -166.79
REMARK 500 4 ASP A 29 42.72 -106.87
REMARK 500 4 LYS A 31 -85.47 57.96
REMARK 500 4 ASP A 32 -31.76 -37.48
REMARK 500 4 LYS A 33 80.73 -12.52
REMARK 500 4 PRO A 40 -9.15 -58.18
REMARK 500 4 ASN A 48 56.50 -117.19
REMARK 500 4 GLN A 49 -80.46 -76.01
REMARK 500 4 GLN A 50 -72.68 -155.78
REMARK 500 4 ASN A 57 -76.34 -114.09
REMARK 500 4 ASP A 58 -173.41 -55.92
REMARK 500 4 ASP A 60 28.61 -156.57
REMARK 500 4 TYR A 67 -111.84 -60.46
REMARK 500
REMARK 500 THIS ENTRY HAS 257 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2NCM A 3 99 UNP P13594 NCA12_MOUSE 20 116
SEQRES 1 A 99 ARG VAL LEU GLN VAL ASP ILE VAL PRO SER GLN GLY GLU
SEQRES 2 A 99 ILE SER VAL GLY GLU SER LYS PHE PHE LEU CYS GLN VAL
SEQRES 3 A 99 ALA GLY ASP ALA LYS ASP LYS ASP ILE SER TRP PHE SER
SEQRES 4 A 99 PRO ASN GLY GLU LYS LEU SER PRO ASN GLN GLN ARG ILE
SEQRES 5 A 99 SER VAL VAL TRP ASN ASP ASP ASP SER SER THR LEU THR
SEQRES 6 A 99 ILE TYR ASN ALA ASN ILE ASP ASP ALA GLY ILE TYR LYS
SEQRES 7 A 99 CYS VAL VAL THR ALA GLU ASP GLY THR GLN SER GLU ALA
SEQRES 8 A 99 THR VAL ASN VAL LYS ILE PHE GLN
SHEET 1 A 4 LEU A 3 VAL A 8 0
SHEET 2 A 4 SER A 19 GLY A 28 -1 N ALA A 27 O GLN A 4
SHEET 3 A 4 SER A 61 TYR A 67 -1 N ILE A 66 O LYS A 20
SHEET 4 A 4 ILE A 52 ASN A 57 -1 N ASN A 57 O SER A 61
SHEET 1 B 5 GLN A 11 SER A 15 0
SHEET 2 B 5 THR A 87 PHE A 98 1 N ASN A 94 O GLY A 12
SHEET 3 B 5 GLY A 75 ALA A 83 -1 N ALA A 83 O THR A 87
SHEET 4 B 5 ASP A 34 SER A 39 -1 N PHE A 38 O LYS A 78
SHEET 5 B 5 GLU A 43 LEU A 45 -1 N LEU A 45 O TRP A 37
SSBOND 1 CYS A 24 CYS A 79 1555 1555 2.03
CISPEP 1 VAL A 8 PRO A 9 1 -0.50
CISPEP 2 VAL A 8 PRO A 9 2 -0.08
CISPEP 3 VAL A 8 PRO A 9 3 0.05
CISPEP 4 VAL A 8 PRO A 9 4 -0.15
CISPEP 5 VAL A 8 PRO A 9 5 0.16
CISPEP 6 VAL A 8 PRO A 9 6 -0.22
CISPEP 7 VAL A 8 PRO A 9 7 -0.06
CISPEP 8 VAL A 8 PRO A 9 8 -0.20
CISPEP 9 VAL A 8 PRO A 9 9 -0.05
CISPEP 10 VAL A 8 PRO A 9 10 -0.07
CISPEP 11 VAL A 8 PRO A 9 11 0.01
CISPEP 12 VAL A 8 PRO A 9 12 -0.23
CISPEP 13 VAL A 8 PRO A 9 13 0.03
CISPEP 14 VAL A 8 PRO A 9 14 0.12
CISPEP 15 VAL A 8 PRO A 9 15 -0.43
CISPEP 16 VAL A 8 PRO A 9 16 0.20
CISPEP 17 VAL A 8 PRO A 9 17 0.04
CISPEP 18 VAL A 8 PRO A 9 18 -0.34
CISPEP 19 VAL A 8 PRO A 9 19 -0.06
CISPEP 20 VAL A 8 PRO A 9 20 -0.24
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
(ATOM LINES ARE NOT SHOWN.)
END
