Header list of 1wjm.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 29-MAY-04 1WJM
TITLE SOLUTION STRUCTURE OF PLECKSTRIN HOMOLOGY DOMAIN OF HUMAN BETA III
TITLE 2 SPECTRIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SPECTRIN III;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PH DOMAIN;
COMPND 5 SYNONYM: BETA-III SPECTRIN;
COMPND 6 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 HF00409;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030428-89;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PH DOMAIN, SIGNAL TRANSDUCTION, STRUCTURAL GENOMICS, SPECTRIN BETA
KEYWDS 2 CHAIN, BRAIN 2, KIAA0302, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WJM 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WJM 1 VERSN
REVDAT 1 29-NOV-04 1WJM 0
JRNL AUTH M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF PLECKSTRIN HOMOLOGY DOMAIN OF HUMAN
JRNL TITL 2 BETA III SPECTRIN
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 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WJM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023646.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.05MM PH DOMAIN U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; ECA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DELTA 2.3, NMRPIPE 20020425,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.8996,
REMARK 210 CYANA 1.0.7
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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 FUNCTION
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 H LEU A 89 O LYS A 93 1.50
REMARK 500 H GLN A 71 O GLY A 88 1.50
REMARK 500 O TRP A 108 H VAL A 112 1.52
REMARK 500 O VAL A 38 H GLY A 45 1.55
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 2 -58.42 -161.49
REMARK 500 1 SER A 5 100.00 64.68
REMARK 500 1 GLU A 19 -60.51 -94.72
REMARK 500 1 ALA A 27 -173.29 -53.61
REMARK 500 1 ALA A 28 -75.71 -108.65
REMARK 500 1 ARG A 40 142.19 -175.24
REMARK 500 1 LEU A 67 34.68 -92.97
REMARK 500 1 ARG A 69 22.81 80.37
REMARK 500 1 ASP A 77 -48.01 171.52
REMARK 500 1 TYR A 78 96.89 -41.95
REMARK 500 1 LYS A 80 -55.25 -173.24
REMARK 500 1 ALA A 103 -71.69 -69.41
REMARK 500 2 ALA A 28 -75.40 -68.22
REMARK 500 2 ARG A 40 145.41 -172.96
REMARK 500 2 LEU A 67 36.07 -91.80
REMARK 500 2 ALA A 75 75.23 -108.27
REMARK 500 2 TYR A 78 99.42 -39.29
REMARK 500 2 LYS A 80 -60.23 178.31
REMARK 500 2 ALA A 103 -70.50 -60.79
REMARK 500 2 SER A 118 94.25 -59.30
REMARK 500 2 SER A 122 -58.54 -131.10
REMARK 500 3 SER A 2 -57.89 -126.25
REMARK 500 3 SER A 3 150.35 60.59
REMARK 500 3 SER A 5 166.76 55.91
REMARK 500 3 SER A 6 -57.81 -170.50
REMARK 500 3 GLU A 19 -50.12 -124.50
REMARK 500 3 ALA A 28 -72.02 -40.63
REMARK 500 3 ARG A 30 65.59 -113.04
REMARK 500 3 ARG A 40 140.86 -172.77
REMARK 500 3 LEU A 67 45.41 -87.64
REMARK 500 3 ARG A 69 16.66 57.90
REMARK 500 3 ALA A 75 66.56 -102.16
REMARK 500 3 TYR A 78 98.69 -37.27
REMARK 500 3 LYS A 80 -81.64 -77.29
REMARK 500 3 ARG A 81 -177.71 -67.78
REMARK 500 3 ASP A 91 43.54 -104.29
REMARK 500 3 ALA A 103 -71.55 -55.81
REMARK 500 3 SER A 118 101.39 -52.42
REMARK 500 4 SER A 5 76.69 61.31
REMARK 500 4 SER A 6 150.97 178.53
REMARK 500 4 ALA A 22 173.47 173.58
REMARK 500 4 ALA A 28 -71.15 -40.03
REMARK 500 4 ARG A 30 58.78 -119.12
REMARK 500 4 ARG A 40 144.52 -172.32
REMARK 500 4 GLU A 62 160.34 -49.85
REMARK 500 4 LEU A 67 30.34 -92.60
REMARK 500 4 ALA A 75 53.41 -105.76
REMARK 500 4 ASP A 101 -175.99 -171.43
REMARK 500 4 ALA A 103 -71.39 -55.21
REMARK 500 4 SER A 122 -61.12 -133.74
REMARK 500
REMARK 500 THIS ENTRY HAS 250 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002200294.1 RELATED DB: TARGETDB
DBREF 1WJM A 8 117 UNP O15020 SPTN2_HUMAN 2219 2328
SEQADV 1WJM GLY A 1 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM SER A 2 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM SER A 3 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM GLY A 4 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM SER A 5 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM SER A 6 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM GLY A 7 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM SER A 118 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM GLY A 119 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM PRO A 120 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM SER A 121 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM SER A 122 UNP O15020 CLONING ARTIFACT
SEQADV 1WJM GLY A 123 UNP O15020 CLONING ARTIFACT
SEQRES 1 A 123 GLY SER SER GLY SER SER GLY GLU GLN MET GLU GLY MET
SEQRES 2 A 123 LEU CYS ARG LYS GLN GLU MET GLU ALA PHE GLY LYS LYS
SEQRES 3 A 123 ALA ALA ASN ARG SER TRP GLN ASN VAL TYR CYS VAL LEU
SEQRES 4 A 123 ARG ARG GLY SER LEU GLY PHE TYR LYS ASP ALA LYS ALA
SEQRES 5 A 123 ALA SER ALA GLY VAL PRO TYR HIS GLY GLU VAL PRO VAL
SEQRES 6 A 123 SER LEU ALA ARG ALA GLN GLY SER VAL ALA PHE ASP TYR
SEQRES 7 A 123 ARG LYS ARG LYS HIS VAL PHE LYS LEU GLY LEU GLN ASP
SEQRES 8 A 123 GLY LYS GLU TYR LEU PHE GLN ALA LYS ASP GLU ALA GLU
SEQRES 9 A 123 MET SER SER TRP LEU ARG VAL VAL ASN ALA ALA ILE ALA
SEQRES 10 A 123 SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 49 SER A 54 1 6
HELIX 2 2 ASP A 101 GLY A 119 1 19
SHEET 1 A 5 LYS A 25 LYS A 26 0
SHEET 2 A 5 MET A 10 ALA A 22 -1 N ALA A 22 O LYS A 25
SHEET 3 A 5 GLN A 33 ARG A 40 -1 O LEU A 39 N MET A 10
SHEET 4 A 5 SER A 43 TYR A 47 -1 O GLY A 45 N VAL A 38
SHEET 5 A 5 VAL A 65 SER A 66 -1 O VAL A 65 N LEU A 44
SHEET 1 B 5 LYS A 25 LYS A 26 0
SHEET 2 B 5 MET A 10 ALA A 22 -1 N ALA A 22 O LYS A 25
SHEET 3 B 5 GLU A 94 GLN A 98 -1 O GLU A 94 N GLU A 19
SHEET 4 B 5 VAL A 84 GLY A 88 -1 N LEU A 87 O TYR A 95
SHEET 5 B 5 GLN A 71 VAL A 74 -1 N GLN A 71 O GLY A 88
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