Header list of 1wyj.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 15-FEB-05 1WYJ
TITLE SOLUTION STRUCTURE OF MOUSE PROTOCADHERIN BETA 14 (26-137)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTOCADHERIN BETA 14;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-125;
COMPND 5 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 GENE: RIKEN CDNA 2210006M07;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031215-82;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PROTOCADHERIN BETA, SS BOND, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, NPPSFA, NATIONAL PROJECT ON
KEYWDS 3 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,K.SAITO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WYJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WYJ 1 VERSN
REVDAT 1 15-AUG-05 1WYJ 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,K.SAITO,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF MOUSE PROTOCADHERIN BETA 14 (26-137)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.8
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WYJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024155.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.96MM PROTOCADHERIN BETA 14 (26
REMARK 210 -137) U-15N,13C; 20MM D-TRIS-HCL;
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 1.0.8
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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 O ARG A 39 H THR A 43 1.51
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 SER A 3 79.71 -153.96
REMARK 500 1 SER A 5 141.66 -177.43
REMARK 500 1 SER A 6 160.43 179.43
REMARK 500 1 LEU A 18 -156.80 -59.94
REMARK 500 1 LYS A 51 157.62 68.25
REMARK 500 1 LYS A 54 112.27 67.51
REMARK 500 1 LEU A 72 173.65 -47.83
REMARK 500 1 ASP A 73 -71.37 -115.70
REMARK 500 1 ARG A 74 -82.35 159.71
REMARK 500 1 LEU A 77 -73.34 -91.08
REMARK 500 1 CYS A 78 -59.74 -148.20
REMARK 500 1 SER A 80 -58.20 77.63
REMARK 500 1 THR A 81 150.58 -38.50
REMARK 500 1 CYS A 84 68.54 81.42
REMARK 500 1 SER A 94 111.66 -35.12
REMARK 500 1 GLN A 106 81.95 -61.75
REMARK 500 1 ASP A 107 53.18 -102.12
REMARK 500 1 ASN A 109 66.25 -175.15
REMARK 500 1 ASP A 110 -48.79 -163.97
REMARK 500 1 HIS A 111 -70.62 67.63
REMARK 500 1 ALA A 112 149.34 70.38
REMARK 500 1 PHE A 115 88.86 -176.60
REMARK 500 1 MET A 116 162.68 58.44
REMARK 500 1 ASP A 118 106.55 179.41
REMARK 500 1 SER A 120 122.44 177.33
REMARK 500 1 SER A 124 154.57 176.89
REMARK 500 2 SER A 2 -59.85 75.39
REMARK 500 2 SER A 3 158.65 60.86
REMARK 500 2 SER A 6 130.49 -178.77
REMARK 500 2 ALA A 8 -58.97 -141.84
REMARK 500 2 SER A 10 -52.26 -162.52
REMARK 500 2 LEU A 18 -164.87 -57.24
REMARK 500 2 ARG A 23 103.83 -39.97
REMARK 500 2 LEU A 30 -63.28 -107.94
REMARK 500 2 LYS A 51 143.27 63.69
REMARK 500 2 LYS A 54 -63.58 179.54
REMARK 500 2 GLN A 55 104.48 60.89
REMARK 500 2 GLN A 61 -47.20 86.09
REMARK 500 2 ASP A 73 103.00 -41.40
REMARK 500 2 LEU A 77 -75.57 -63.24
REMARK 500 2 CYS A 78 100.57 -172.03
REMARK 500 2 SER A 80 81.21 37.31
REMARK 500 2 CYS A 84 75.98 71.03
REMARK 500 2 SER A 94 110.30 -33.34
REMARK 500 2 GLN A 97 145.17 -170.52
REMARK 500 2 ASN A 109 164.51 177.38
REMARK 500 2 GLU A 114 80.80 174.60
REMARK 500 2 PHE A 115 135.70 -173.59
REMARK 500 2 MET A 116 140.86 -176.14
REMARK 500 2 GLU A 117 149.56 177.72
REMARK 500
REMARK 500 THIS ENTRY HAS 387 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007113694.1 RELATED DB: TARGETDB
DBREF 1WYJ A 8 119 UNP Q6PB90 Q6PB90_MOUSE 26 137
SEQADV 1WYJ GLY A 1 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ SER A 2 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ SER A 3 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ GLY A 4 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ SER A 5 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ SER A 6 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ GLY A 7 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ SER A 120 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ GLY A 121 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ PRO A 122 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ SER A 123 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ SER A 124 UNP Q6PB90 CLONING ARTIFACT
SEQADV 1WYJ GLY A 125 UNP Q6PB90 CLONING ARTIFACT
SEQRES 1 A 125 GLY SER SER GLY SER SER GLY ALA GLY SER ALA THR ILE
SEQRES 2 A 125 THR TYR SER VAL LEU GLU GLU THR ASP ARG GLY SER LEU
SEQRES 3 A 125 VAL GLY ASN LEU ALA LYS ASP LEU GLY LEU SER LEU ARG
SEQRES 4 A 125 GLU LEU ILE THR ARG GLY ALA GLN ILE LEU SER LYS GLY
SEQRES 5 A 125 ASN LYS GLN LEU LEU GLN LEU GLU GLN LYS SER GLY ASN
SEQRES 6 A 125 LEU LEU LEU LYS GLU LYS LEU ASP ARG GLU GLU LEU CYS
SEQRES 7 A 125 GLY SER THR ASN PRO CYS ILE LEU HIS PHE GLN VAL LEU
SEQRES 8 A 125 LEU LYS SER PRO VAL GLN PHE ILE GLN GLY GLU ILE GLN
SEQRES 9 A 125 LEU GLN ASP VAL ASN ASP HIS ALA PRO GLU PHE MET GLU
SEQRES 10 A 125 ASP GLU SER GLY PRO SER SER GLY
HELIX 1 1 SER A 37 ARG A 44 1 8
SHEET 1 A 2 TYR A 15 VAL A 17 0
SHEET 2 A 2 ILE A 103 LEU A 105 1 O GLN A 104 N TYR A 15
SHEET 1 B 3 LEU A 26 ASN A 29 0
SHEET 2 B 3 ASN A 65 LEU A 68 -1 O LEU A 66 N GLY A 28
SHEET 3 B 3 LEU A 57 LEU A 59 -1 N GLN A 58 O LEU A 67
SHEET 1 C 3 GLN A 47 LEU A 49 0
SHEET 2 C 3 GLN A 89 LEU A 92 -1 O GLN A 89 N LEU A 49
SHEET 3 C 3 GLN A 97 ILE A 99 -1 O GLN A 97 N LEU A 92
SSBOND 1 CYS A 78 CYS A 84 1555 1555 2.10
CISPEP 1 ASN A 82 PRO A 83 1 -0.02
CISPEP 2 SER A 94 PRO A 95 1 0.12
CISPEP 3 ASN A 82 PRO A 83 2 -0.05
CISPEP 4 SER A 94 PRO A 95 2 0.00
CISPEP 5 ASN A 82 PRO A 83 3 0.00
CISPEP 6 SER A 94 PRO A 95 3 0.04
CISPEP 7 ASN A 82 PRO A 83 4 -0.03
CISPEP 8 SER A 94 PRO A 95 4 0.04
CISPEP 9 ASN A 82 PRO A 83 5 -0.08
CISPEP 10 SER A 94 PRO A 95 5 0.00
CISPEP 11 ASN A 82 PRO A 83 6 0.04
CISPEP 12 SER A 94 PRO A 95 6 0.05
CISPEP 13 ASN A 82 PRO A 83 7 0.02
CISPEP 14 SER A 94 PRO A 95 7 0.01
CISPEP 15 ASN A 82 PRO A 83 8 -0.02
CISPEP 16 SER A 94 PRO A 95 8 -0.02
CISPEP 17 ASN A 82 PRO A 83 9 -0.01
CISPEP 18 SER A 94 PRO A 95 9 0.02
CISPEP 19 ASN A 82 PRO A 83 10 0.07
CISPEP 20 SER A 94 PRO A 95 10 -0.01
CISPEP 21 ASN A 82 PRO A 83 11 -0.06
CISPEP 22 SER A 94 PRO A 95 11 0.01
CISPEP 23 ASN A 82 PRO A 83 12 0.07
CISPEP 24 SER A 94 PRO A 95 12 0.01
CISPEP 25 ASN A 82 PRO A 83 13 -0.04
CISPEP 26 SER A 94 PRO A 95 13 0.05
CISPEP 27 ASN A 82 PRO A 83 14 0.03
CISPEP 28 SER A 94 PRO A 95 14 0.02
CISPEP 29 ASN A 82 PRO A 83 15 -0.11
CISPEP 30 SER A 94 PRO A 95 15 -0.02
CISPEP 31 ASN A 82 PRO A 83 16 0.05
CISPEP 32 SER A 94 PRO A 95 16 0.03
CISPEP 33 ASN A 82 PRO A 83 17 0.02
CISPEP 34 SER A 94 PRO A 95 17 0.02
CISPEP 35 ASN A 82 PRO A 83 18 -0.11
CISPEP 36 SER A 94 PRO A 95 18 -0.04
CISPEP 37 ASN A 82 PRO A 83 19 0.01
CISPEP 38 SER A 94 PRO A 95 19 0.06
CISPEP 39 ASN A 82 PRO A 83 20 -0.02
CISPEP 40 SER A 94 PRO A 95 20 0.04
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 - r 2 2 Bytes