Header list of 1x5l.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 16-MAY-05 1X5L
TITLE SOLUTION STRUCTURE OF THE SECOND FN3 DOMAIN OF EPH RECEPTOR A8 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 8;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FN3 DOMAIN;
COMPND 5 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR EEK, EPH-AND ELK-RELATED
COMPND 6 KINASE, HEK3;
COMPND 7 EC: 2.7.1.112;
COMPND 8 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: KAZUSA CDNA FH16961;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040705-14;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS FN3 DOMAIN, EPHRIN TYPE-A RECEPTOR 8 PRECURSOR/TYROSINE-PROTEIN
KEYWDS 2 KINASE RECEPTOR EEK, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS 3 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5L 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5L 1 VERSN
REVDAT 1 16-NOV-05 1X5L 0
JRNL AUTH X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND FN3 DOMAIN OF EPH RECEPTOR
JRNL TITL 2 A8 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X5L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024407.
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 : 1.42MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9296, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE 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: SPECTROMETER_ID 1 FOR 3D_15N_SEPARATED_NOESY,
REMARK 210 SPECTROMETER_ID 2 FOR 3D_13C_SEPARATED_NOESY
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 2 GLU A 50 107.30 -55.39
REMARK 500 2 ALA A 97 105.31 -55.79
REMARK 500 3 SER A 12 171.25 -59.24
REMARK 500 3 GLU A 50 108.56 -59.10
REMARK 500 3 ALA A 97 102.77 -54.62
REMARK 500 3 PRO A 105 96.10 -69.76
REMARK 500 3 PRO A 108 89.88 -69.80
REMARK 500 4 ALA A 97 102.23 -58.39
REMARK 500 4 PRO A 105 2.80 -69.77
REMARK 500 5 ARG A 93 176.89 -55.68
REMARK 500 5 SER A 95 178.06 -59.34
REMARK 500 5 ALA A 97 104.56 -56.49
REMARK 500 5 PRO A 108 85.90 -69.70
REMARK 500 6 MET A 55 -179.66 -52.62
REMARK 500 6 SER A 95 178.12 -57.61
REMARK 500 6 ALA A 97 102.14 -56.67
REMARK 500 7 PRO A 105 2.76 -69.83
REMARK 500 8 PRO A 11 -179.32 -69.74
REMARK 500 8 GLU A 50 108.80 -57.18
REMARK 500 8 SER A 95 174.50 -58.08
REMARK 500 8 ALA A 97 102.07 -52.03
REMARK 500 8 PRO A 108 -176.51 -69.82
REMARK 500 9 GLN A 8 108.97 -56.88
REMARK 500 9 GLU A 50 109.60 -53.29
REMARK 500 9 ARG A 93 176.62 -54.53
REMARK 500 9 ALA A 97 105.17 -57.44
REMARK 500 9 PRO A 105 0.90 -69.72
REMARK 500 10 PRO A 108 89.05 -69.76
REMARK 500 11 PRO A 11 -164.86 -69.73
REMARK 500 11 PRO A 34 -164.72 -69.75
REMARK 500 11 PRO A 37 5.43 -69.80
REMARK 500 11 GLN A 56 -68.55 -98.00
REMARK 500 11 PRO A 108 90.67 -69.70
REMARK 500 12 GLU A 50 105.48 -53.59
REMARK 500 12 SER A 95 174.44 -59.35
REMARK 500 12 ALA A 97 102.93 -52.03
REMARK 500 12 THR A 102 179.08 -52.06
REMARK 500 12 PRO A 105 2.47 -69.76
REMARK 500 13 THR A 25 31.99 39.73
REMARK 500 13 PRO A 34 -178.20 -69.72
REMARK 500 13 GLU A 50 109.93 -52.63
REMARK 500 13 ALA A 97 102.53 -56.06
REMARK 500 13 PRO A 105 5.95 -69.80
REMARK 500 13 PRO A 108 2.79 -69.71
REMARK 500 14 GLU A 54 -64.77 -95.58
REMARK 500 14 PHE A 94 172.50 -58.32
REMARK 500 14 SER A 95 -70.86 -81.36
REMARK 500 14 PRO A 108 1.14 -69.77
REMARK 500 15 GLU A 20 -70.20 -97.99
REMARK 500 15 ARG A 21 -66.35 -97.62
REMARK 500
REMARK 500 THIS ENTRY HAS 74 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001431.2 RELATED DB: TARGETDB
DBREF 1X5L A 8 105 UNP P29322 EPHA8_HUMAN 437 534
SEQADV 1X5L GLY A 1 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L SER A 2 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L SER A 3 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L GLY A 4 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L SER A 5 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L SER A 6 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L GLY A 7 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L SER A 106 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L GLY A 107 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L PRO A 108 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L SER A 109 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L SER A 110 UNP P29322 CLONING ARTIFACT
SEQADV 1X5L GLY A 111 UNP P29322 CLONING ARTIFACT
SEQRES 1 A 111 GLY SER SER GLY SER SER GLY GLN ALA ALA PRO SER GLN
SEQRES 2 A 111 VAL VAL VAL ILE ARG GLN GLU ARG ALA GLY GLN THR SER
SEQRES 3 A 111 VAL SER LEU LEU TRP GLN GLU PRO GLU GLN PRO ASN GLY
SEQRES 4 A 111 ILE ILE LEU GLU TYR GLU ILE LYS TYR TYR GLU LYS ASP
SEQRES 5 A 111 LYS GLU MET GLN SER TYR SER THR LEU LYS ALA VAL THR
SEQRES 6 A 111 THR ARG ALA THR VAL SER GLY LEU LYS PRO GLY THR ARG
SEQRES 7 A 111 TYR VAL PHE GLN VAL ARG ALA ARG THR SER ALA GLY CYS
SEQRES 8 A 111 GLY ARG PHE SER GLN ALA MET GLU VAL GLU THR GLY LYS
SEQRES 9 A 111 PRO SER GLY PRO SER SER GLY
SHEET 1 A 3 ILE A 17 ARG A 18 0
SHEET 2 A 3 VAL A 27 TRP A 31 -1 O LEU A 30 N ARG A 18
SHEET 3 A 3 ARG A 67 VAL A 70 -1 O VAL A 70 N VAL A 27
SHEET 1 B 4 SER A 59 ALA A 63 0
SHEET 2 B 4 GLU A 43 GLU A 50 -1 N TYR A 44 O ALA A 63
SHEET 3 B 4 VAL A 83 THR A 87 -1 O ARG A 84 N GLU A 45
SHEET 4 B 4 GLY A 90 CYS A 91 -1 O GLY A 90 N THR A 87
SHEET 1 C 4 SER A 59 ALA A 63 0
SHEET 2 C 4 GLU A 43 GLU A 50 -1 N TYR A 44 O ALA A 63
SHEET 3 C 4 ARG A 78 PHE A 81 -1 O VAL A 80 N TYR A 49
SHEET 4 C 4 MET A 98 GLU A 101 -1 O VAL A 100 N TYR A 79
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