Header list of 3ncm.pdb file
Complete list - v 29 2 Bytes
HEADER CELL ADHESION PROTEIN 21-SEP-98 3NCM
TITLE NEURAL CELL ADHESION MOLECULE, MODULE 2, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (NEURAL CELL ADHESION MOLECULE, LARGE ISOFORM);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MODULE 2;
COMPND 5 SYNONYM: NCAM MODULE 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 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 STRAIN: ESCHERICHIA COLI STRAIN TOP 10 F';
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HIS 4 GS-115;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHIL-S1
KEYWDS CELL ADHESION, GLYCOPROTEIN, HEPARIN-BINDING, GPI-ANCHOR, NEURAL
KEYWDS 2 ADHESION MOLECULE, IMMUNOGLOBULIN FOLD, HOMOPHILIC BINDING, CELL
KEYWDS 3 ADHESION PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.H.JENSEN,V.SOROKA,N.K.THOMSEN,V.BEREZIN,E.BOCK,F.M.POULSEN
REVDAT 3 29-NOV-17 3NCM 1 REMARK HELIX
REVDAT 2 24-FEB-09 3NCM 1 VERSN
REVDAT 1 23-JUL-99 3NCM 0
JRNL AUTH P.H.JENSEN,V.SOROKA,N.K.THOMSEN,I.RALETS,V.BEREZIN,E.BOCK,
JRNL AUTH 2 F.M.POULSEN
JRNL TITL STRUCTURE AND INTERACTIONS OF NCAM MODULES 1 AND 2, BASIC
JRNL TITL 2 ELEMENTS IN NEURAL CELL ADHESION
JRNL REF NAT.STRUCT.BIOL. V. 6 486 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10331878
JRNL DOI 10.1038/8292
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.815
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NCM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007001.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 70 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% H2O/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; NOESYHSQC;
REMARK 210 TOCSYHSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : UXNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 ASN A 6 76.97 32.36
REMARK 500 1 CYS A 23 87.11 -160.08
REMARK 500 1 SER A 28 -80.52 -42.13
REMARK 500 1 LEU A 29 -63.43 -170.69
REMARK 500 1 PRO A 31 -162.94 -61.71
REMARK 500 1 THR A 32 -165.67 -170.16
REMARK 500 1 HIS A 37 150.58 63.76
REMARK 500 1 ARG A 40 88.35 56.75
REMARK 500 1 ASP A 41 84.61 55.06
REMARK 500 1 ASP A 47 171.30 -53.11
REMARK 500 1 ILE A 63 73.59 42.30
REMARK 500 1 ARG A 80 63.59 -107.98
REMARK 500 2 ASN A 6 70.92 38.88
REMARK 500 2 CYS A 23 80.49 -163.61
REMARK 500 2 SER A 28 30.57 -97.97
REMARK 500 2 PRO A 31 -170.02 -52.66
REMARK 500 2 THR A 32 -156.21 -168.93
REMARK 500 2 HIS A 37 163.79 64.06
REMARK 500 2 LYS A 38 -51.71 76.87
REMARK 500 2 ARG A 40 89.06 50.61
REMARK 500 2 ASP A 41 105.89 56.36
REMARK 500 2 ILE A 63 71.79 42.92
REMARK 500 2 LEU A 78 52.54 -91.38
REMARK 500 2 ALA A 79 -60.01 -152.20
REMARK 500 2 ARG A 80 -43.33 -135.37
REMARK 500 2 GLU A 82 -150.06 45.79
REMARK 500 3 ASN A 6 84.10 32.93
REMARK 500 3 CYS A 23 93.56 -164.85
REMARK 500 3 VAL A 26 79.46 -106.08
REMARK 500 3 SER A 28 -76.31 -45.46
REMARK 500 3 LEU A 29 -62.52 -173.04
REMARK 500 3 PRO A 31 -163.63 -62.48
REMARK 500 3 THR A 32 -166.37 -170.25
REMARK 500 3 HIS A 37 147.20 63.78
REMARK 500 3 ARG A 40 104.77 56.14
REMARK 500 3 ASP A 41 70.35 54.97
REMARK 500 3 ASP A 47 173.71 -50.57
REMARK 500 3 ILE A 63 72.10 41.47
REMARK 500 3 ARG A 80 61.67 -101.92
REMARK 500 4 ASN A 6 70.24 27.78
REMARK 500 4 SER A 28 -81.49 -46.18
REMARK 500 4 LEU A 29 -64.01 -165.93
REMARK 500 4 PRO A 31 -163.83 -61.14
REMARK 500 4 THR A 32 -162.81 -168.97
REMARK 500 4 LYS A 36 -162.68 -121.65
REMARK 500 4 HIS A 37 -166.38 69.35
REMARK 500 4 LYS A 38 19.51 58.27
REMARK 500 4 ARG A 40 -173.45 -175.29
REMARK 500 4 ILE A 63 93.72 42.30
REMARK 500 4 ARG A 80 61.99 -102.14
REMARK 500
REMARK 500 THIS ENTRY HAS 248 RAMACHANDRAN OUTLIERS.
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 1 ARG A 40 0.25 SIDE CHAIN
REMARK 500 1 ARG A 49 0.25 SIDE CHAIN
REMARK 500 1 ARG A 61 0.32 SIDE CHAIN
REMARK 500 1 ARG A 72 0.31 SIDE CHAIN
REMARK 500 1 ARG A 76 0.25 SIDE CHAIN
REMARK 500 1 ARG A 80 0.32 SIDE CHAIN
REMARK 500 2 ARG A 40 0.28 SIDE CHAIN
REMARK 500 2 ARG A 49 0.29 SIDE CHAIN
REMARK 500 2 ARG A 61 0.27 SIDE CHAIN
REMARK 500 2 ARG A 72 0.32 SIDE CHAIN
REMARK 500 2 ARG A 76 0.32 SIDE CHAIN
REMARK 500 2 ARG A 80 0.32 SIDE CHAIN
REMARK 500 3 ARG A 40 0.31 SIDE CHAIN
REMARK 500 3 ARG A 49 0.26 SIDE CHAIN
REMARK 500 3 ARG A 61 0.25 SIDE CHAIN
REMARK 500 3 ARG A 72 0.30 SIDE CHAIN
REMARK 500 3 ARG A 76 0.30 SIDE CHAIN
REMARK 500 3 ARG A 80 0.31 SIDE CHAIN
REMARK 500 4 ARG A 40 0.26 SIDE CHAIN
REMARK 500 4 ARG A 49 0.32 SIDE CHAIN
REMARK 500 4 ARG A 61 0.32 SIDE CHAIN
REMARK 500 4 ARG A 72 0.31 SIDE CHAIN
REMARK 500 4 ARG A 76 0.28 SIDE CHAIN
REMARK 500 4 ARG A 80 0.31 SIDE CHAIN
REMARK 500 5 ARG A 40 0.31 SIDE CHAIN
REMARK 500 5 ARG A 49 0.30 SIDE CHAIN
REMARK 500 5 ARG A 61 0.29 SIDE CHAIN
REMARK 500 5 ARG A 72 0.29 SIDE CHAIN
REMARK 500 5 ARG A 76 0.30 SIDE CHAIN
REMARK 500 5 ARG A 80 0.28 SIDE CHAIN
REMARK 500 6 ARG A 40 0.31 SIDE CHAIN
REMARK 500 6 ARG A 49 0.22 SIDE CHAIN
REMARK 500 6 ARG A 61 0.29 SIDE CHAIN
REMARK 500 6 ARG A 72 0.27 SIDE CHAIN
REMARK 500 6 ARG A 76 0.30 SIDE CHAIN
REMARK 500 6 ARG A 80 0.26 SIDE CHAIN
REMARK 500 7 ARG A 40 0.31 SIDE CHAIN
REMARK 500 7 ARG A 49 0.26 SIDE CHAIN
REMARK 500 7 ARG A 61 0.25 SIDE CHAIN
REMARK 500 7 ARG A 72 0.31 SIDE CHAIN
REMARK 500 7 ARG A 76 0.25 SIDE CHAIN
REMARK 500 7 ARG A 80 0.31 SIDE CHAIN
REMARK 500 8 ARG A 40 0.30 SIDE CHAIN
REMARK 500 8 ARG A 49 0.29 SIDE CHAIN
REMARK 500 8 ARG A 61 0.32 SIDE CHAIN
REMARK 500 8 ARG A 72 0.31 SIDE CHAIN
REMARK 500 8 ARG A 76 0.26 SIDE CHAIN
REMARK 500 8 ARG A 80 0.28 SIDE CHAIN
REMARK 500 9 ARG A 40 0.27 SIDE CHAIN
REMARK 500 9 ARG A 49 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 120 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3NCM A 1 92 UNP P13594 NCA12_MOUSE 117 208
SEQADV 3NCM TYR A 1 UNP P13594 LYS 117 CLONING ARTIFACT
SEQADV 3NCM VAL A 2 UNP P13594 LEU 118 CLONING ARTIFACT
SEQRES 1 A 92 TYR VAL MET PHE LYS ASN ALA PRO THR PRO GLN GLU PHE
SEQRES 2 A 92 LYS GLU GLY GLU ASP ALA VAL ILE VAL CYS ASP VAL VAL
SEQRES 3 A 92 SER SER LEU PRO PRO THR ILE ILE TRP LYS HIS LYS GLY
SEQRES 4 A 92 ARG ASP VAL ILE LEU LYS LYS ASP VAL ARG PHE ILE VAL
SEQRES 5 A 92 LEU SER ASN ASN TYR LEU GLN ILE ARG GLY ILE LYS LYS
SEQRES 6 A 92 THR ASP GLU GLY THR TYR ARG CYS GLU GLY ARG ILE LEU
SEQRES 7 A 92 ALA ARG GLY GLU ILE ASN PHE LYS ASP ILE GLN VAL ILE
SEQRES 8 A 92 VAL
HELIX 1 H1 VAL A 42 LYS A 45 5 4
HELIX 2 H2 LYS A 64 ASP A 67 5 4
SHEET 1 A 2 VAL A 2 LYS A 5 0
SHEET 2 A 2 ASP A 24 SER A 27 -1 O ASP A 24 N LYS A 5
SHEET 1 B 4 GLN A 11 GLU A 12 0
SHEET 2 B 4 GLU A 82 ILE A 91 1 O GLN A 89 N GLN A 11
SHEET 3 B 4 GLY A 69 ILE A 77 -1 N GLY A 69 O VAL A 90
SHEET 4 B 4 THR A 32 LYS A 36 -1 O THR A 32 N ARG A 76
SHEET 1 C 3 GLU A 17 ILE A 21 0
SHEET 2 C 3 LEU A 58 GLY A 62 -1 N LEU A 58 O ILE A 21
SHEET 3 C 3 PHE A 50 VAL A 52 -1 O ILE A 51 N GLN A 59
SSBOND 1 CYS A 23 CYS A 73 1555 1555 2.02
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