Header list of 1inz.pdb file
Complete list - p 9 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 05-DEC-00 1INZ
TITLE SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF
TITLE 2 HUMAN EPSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPS15-INTERACTING PROTEIN(EPSIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ENTH DOMAIN(RESIDUES 1-144);
COMPND 5 SYNONYM: EH DOMAIN-BINDING MITOTIC PHOSPHOPROTEIN;
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: EPSIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX2T
KEYWDS ALPHA-HELIX, EPSIN, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 2 RSGI, STRUCTURAL GENOMICS, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.KOSHIBA,T.KIGAWA,A.KIKUCHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 09-SEP-20 1INZ 1 COMPND REMARK
REVDAT 4 24-FEB-09 1INZ 1 VERSN
REVDAT 3 21-JAN-03 1INZ 1 REMARK
REVDAT 2 16-MAY-01 1INZ 1 DBREF
REVDAT 1 09-MAY-01 1INZ 0
JRNL AUTH S.KOSHIBA,T.KIGAWA,A.KIKUCHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH)
JRNL TITL 2 DOMAIN OF HUMAN EPSIN
JRNL REF J.STRUCT.FUNCT.GENOM. V. 2 1 2001
JRNL REFN ISSN 1345-711X
JRNL PMID 12836669
JRNL DOI 10.1023/A:1011397007366
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1 AND 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1INZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000005106.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.0
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 400MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM EPSIN ENTH DOMAIN U-15N;
REMARK 210 20MM NA PHOSPHATE BUFFER; 400MM
REMARK 210 NACL; 2MM DTT; 0.01% SODIUM
REMARK 210 AZIDE; 90% H2O, 10% D2O; 1MM
REMARK 210 EPSIN ENTH DOMAIN U-15N,13C;
REMARK 210 20MM NA PHOSPHATE BUFFER; 400MM
REMARK 210 NACL; 2MM DTT; 0.01% SODIUM
REMARK 210 AZIDE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 4.0.3, X-PLOR
REMARK 210 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
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: 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 -61.10 -129.61
REMARK 500 1 SER A 4 105.75 -58.89
REMARK 500 1 LEU A 6 149.70 64.83
REMARK 500 1 ARG A 7 -83.75 -118.82
REMARK 500 1 MET A 10 -157.06 -80.79
REMARK 500 1 LYS A 11 -152.41 -77.79
REMARK 500 1 ASN A 16 77.93 -101.13
REMARK 500 1 TYR A 17 109.10 -45.76
REMARK 500 1 SER A 29 105.68 178.28
REMARK 500 1 PRO A 32 -162.90 -68.27
REMARK 500 1 TRP A 33 -164.43 -112.41
REMARK 500 1 SER A 37 -71.54 -101.74
REMARK 500 1 SER A 38 67.31 -163.65
REMARK 500 1 ASN A 49 -157.48 -56.68
REMARK 500 1 VAL A 51 -71.91 -84.54
REMARK 500 1 ILE A 56 -70.07 -80.96
REMARK 500 1 ASP A 66 -169.42 -52.40
REMARK 500 1 LYS A 69 -37.15 -144.96
REMARK 500 1 LYS A 86 -82.40 -97.28
REMARK 500 1 SER A 89 176.16 176.61
REMARK 500 1 PHE A 109 90.24 -59.02
REMARK 500 1 ASP A 113 172.47 56.95
REMARK 500 1 ARG A 135 88.46 -155.96
REMARK 500 1 LEU A 140 108.97 55.04
REMARK 500 1 ARG A 141 -162.16 -69.67
REMARK 500 1 GLU A 142 65.03 -175.25
REMARK 500 2 SER A -2 48.14 -144.30
REMARK 500 2 SER A 5 -141.98 49.06
REMARK 500 2 LYS A 11 -58.49 -135.49
REMARK 500 2 GLU A 19 16.20 56.52
REMARK 500 2 SER A 29 -79.51 -76.16
REMARK 500 2 PRO A 32 -158.65 -65.32
REMARK 500 2 PRO A 35 -165.00 -65.54
REMARK 500 2 VAL A 50 -59.04 -10.20
REMARK 500 2 ASN A 65 35.27 -99.66
REMARK 500 2 LYS A 69 -88.56 -83.29
REMARK 500 2 SER A 89 150.14 74.28
REMARK 500 2 PHE A 109 95.43 -60.01
REMARK 500 2 TYR A 111 100.49 -166.73
REMARK 500 2 ASP A 113 -174.86 67.59
REMARK 500 2 ASP A 118 99.63 -43.59
REMARK 500 2 ASP A 136 -38.32 -146.16
REMARK 500 2 LEU A 140 178.23 -58.73
REMARK 500 2 GLU A 142 -164.75 -103.17
REMARK 500 2 GLU A 143 41.21 -164.57
REMARK 500 3 SER A -1 -158.83 -61.15
REMARK 500 3 SER A 5 -171.49 52.63
REMARK 500 3 MET A 10 -145.76 -132.41
REMARK 500 3 GLU A 19 48.69 175.26
REMARK 500 3 SER A 29 106.42 -179.60
REMARK 500
REMARK 500 THIS ENTRY HAS 527 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 0 0.32 SIDE CHAIN
REMARK 500 1 ARG A 7 0.27 SIDE CHAIN
REMARK 500 1 ARG A 8 0.18 SIDE CHAIN
REMARK 500 1 ARG A 25 0.22 SIDE CHAIN
REMARK 500 1 ARG A 63 0.08 SIDE CHAIN
REMARK 500 1 ARG A 72 0.21 SIDE CHAIN
REMARK 500 1 ARG A 91 0.17 SIDE CHAIN
REMARK 500 1 ARG A 114 0.30 SIDE CHAIN
REMARK 500 1 ARG A 124 0.32 SIDE CHAIN
REMARK 500 1 ARG A 135 0.30 SIDE CHAIN
REMARK 500 1 ARG A 139 0.32 SIDE CHAIN
REMARK 500 1 ARG A 141 0.31 SIDE CHAIN
REMARK 500 1 ARG A 144 0.15 SIDE CHAIN
REMARK 500 2 ARG A 0 0.25 SIDE CHAIN
REMARK 500 2 ARG A 7 0.32 SIDE CHAIN
REMARK 500 2 ARG A 8 0.28 SIDE CHAIN
REMARK 500 2 ARG A 25 0.17 SIDE CHAIN
REMARK 500 2 ARG A 63 0.27 SIDE CHAIN
REMARK 500 2 ARG A 72 0.29 SIDE CHAIN
REMARK 500 2 ARG A 91 0.21 SIDE CHAIN
REMARK 500 2 ARG A 114 0.12 SIDE CHAIN
REMARK 500 2 ARG A 124 0.29 SIDE CHAIN
REMARK 500 2 ARG A 135 0.31 SIDE CHAIN
REMARK 500 2 ARG A 139 0.20 SIDE CHAIN
REMARK 500 2 ARG A 144 0.18 SIDE CHAIN
REMARK 500 3 ARG A 0 0.31 SIDE CHAIN
REMARK 500 3 ARG A 7 0.24 SIDE CHAIN
REMARK 500 3 ARG A 8 0.29 SIDE CHAIN
REMARK 500 3 ARG A 25 0.25 SIDE CHAIN
REMARK 500 3 ARG A 63 0.32 SIDE CHAIN
REMARK 500 3 ARG A 91 0.32 SIDE CHAIN
REMARK 500 3 ARG A 114 0.21 SIDE CHAIN
REMARK 500 3 ARG A 124 0.12 SIDE CHAIN
REMARK 500 3 ARG A 135 0.31 SIDE CHAIN
REMARK 500 3 ARG A 141 0.22 SIDE CHAIN
REMARK 500 3 ARG A 144 0.32 SIDE CHAIN
REMARK 500 4 ARG A 0 0.19 SIDE CHAIN
REMARK 500 4 ARG A 7 0.28 SIDE CHAIN
REMARK 500 4 ARG A 8 0.32 SIDE CHAIN
REMARK 500 4 ARG A 25 0.31 SIDE CHAIN
REMARK 500 4 ARG A 63 0.20 SIDE CHAIN
REMARK 500 4 ARG A 72 0.27 SIDE CHAIN
REMARK 500 4 ARG A 91 0.20 SIDE CHAIN
REMARK 500 4 ARG A 114 0.27 SIDE CHAIN
REMARK 500 4 ARG A 124 0.27 SIDE CHAIN
REMARK 500 4 ARG A 135 0.26 SIDE CHAIN
REMARK 500 4 ARG A 139 0.16 SIDE CHAIN
REMARK 500 4 ARG A 141 0.20 SIDE CHAIN
REMARK 500 4 ARG A 144 0.31 SIDE CHAIN
REMARK 500 5 ARG A 0 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 247 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NHS001016601.1 RELATED DB: TARGETDB
DBREF 1INZ A 1 144 UNP Q9Y6I3 EPN1_HUMAN 1 144
SEQADV 1INZ GLY A -3 UNP Q9Y6I3 SEE REMARK 999
SEQADV 1INZ SER A -2 UNP Q9Y6I3 SEE REMARK 999
SEQADV 1INZ SER A -1 UNP Q9Y6I3 SEE REMARK 999
SEQADV 1INZ ARG A 0 UNP Q9Y6I3 SEE REMARK 999
SEQRES 1 A 148 GLY SER SER ARG MET SER THR SER SER LEU ARG ARG GLN
SEQRES 2 A 148 MET LYS ASN ILE VAL HIS ASN TYR SER GLU ALA GLU ILE
SEQRES 3 A 148 LYS VAL ARG GLU ALA THR SER ASN ASP PRO TRP GLY PRO
SEQRES 4 A 148 SER SER SER LEU MET SER GLU ILE ALA ASP LEU THR TYR
SEQRES 5 A 148 ASN VAL VAL ALA PHE SER GLU ILE MET SER MET ILE TRP
SEQRES 6 A 148 LYS ARG LEU ASN ASP HIS GLY LYS ASN TRP ARG HIS VAL
SEQRES 7 A 148 TYR LYS ALA MET THR LEU MET GLU TYR LEU ILE LYS THR
SEQRES 8 A 148 GLY SER GLU ARG VAL SER GLN GLN CYS LYS GLU ASN MET
SEQRES 9 A 148 TYR ALA VAL GLN THR LEU LYS ASP PHE GLN TYR VAL ASP
SEQRES 10 A 148 ARG ASP GLY LYS ASP GLN GLY VAL ASN VAL ARG GLU LYS
SEQRES 11 A 148 ALA LYS GLN LEU VAL ALA LEU LEU ARG ASP GLU ASP ARG
SEQRES 12 A 148 LEU ARG GLU GLU ARG
HELIX 1 1 GLU A 19 ALA A 27 1 9
HELIX 2 2 MET A 40 TYR A 48 1 9
HELIX 3 3 PHE A 53 LEU A 64 1 12
HELIX 4 4 TRP A 71 LEU A 84 1 14
HELIX 5 5 GLU A 90 ASN A 99 1 10
HELIX 6 6 MET A 100 LYS A 107 1 8
HELIX 7 7 VAL A 121 LEU A 134 1 14
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 - p 9 2 Bytes