Header list of 1fi6.pdb file
Complete list - b 23 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 03-AUG-00 1FI6
TITLE SOLUTION STRUCTURE OF THE REPS1 EH DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EH DOMAIN PROTEIN REPS1;
COMPND 3 CHAIN: A;
COMPND 4 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX2T
KEYWDS EPS15 HOMOLOGY DOMAIN, EF HAND, CALCIUM, RAS SIGNAL TRANSDUCTION,
KEYWDS 2 ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR S.KIM,J.D.BALEJA
REVDAT 4 23-FEB-22 1FI6 1 REMARK LINK
REVDAT 3 24-FEB-09 1FI6 1 VERSN
REVDAT 2 01-APR-03 1FI6 1 JRNL
REVDAT 1 18-JUL-01 1FI6 0
JRNL AUTH S.KIM,D.N.CULLIS,L.A.FEIG,J.D.BALEJA
JRNL TITL SOLUTION STRUCTURE OF THE REPS1 EH DOMAIN AND
JRNL TITL 2 CHARACTERIZATION OF ITS BINDING TO NPF TARGET SEQUENCES.
JRNL REF BIOCHEMISTRY V. 40 6776 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11389591
JRNL DOI 10.1021/BI002700M
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.KIM
REMARK 1 TITL CHAPTER 3: STUDIES OF PROTEIN STRUCTURE AND INTERACTION
REMARK 1 TITL 2 USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY:APPLICATIONS
REMARK 1 TITL 3 TO THE REPS1 EH DOMAIN AND MICROCINB17 PROPEPTIDE
REMARK 1 REF THESIS 2000
REMARK 1 PUBL TUFTS UNIVERSITY MEDICAL SCHOOL
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.7, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER/BIOSYM (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1265 RESTRAINTS, 1143 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 122
REMARK 3 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1FI6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011612.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 30
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 10MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM REPS1 EH DOMAIN U-15N,13C;
REMARK 210 10MM D-IMIDAZOLE BUFFER, 1.5MM
REMARK 210 CACL2; 90% H2O, 10% D2O; 1MM
REMARK 210 REPS1 EH DOMAIN U-15N; 10MM D-
REMARK 210 IMIDAZOLE BUFFER, 1.5MM CACL2;
REMARK 210 90% H2O, 10% D2O; 1MM REPS1 EH
REMARK 210 DOMAIN; 10MM D-IMIDAZOLE BUFFER,
REMARK 210 1.5MM CACL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; DQF-
REMARK 210 COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.7, FELIX 1.1.2, X-PLOR
REMARK 210 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR 2D AND 3D
REMARK 210 NMR SPECTROSCOPY.
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
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 LEU A 27 25.48 -67.54
REMARK 500 1 LYS A 44 -55.01 163.52
REMARK 500 1 ILE A 47 -37.39 -38.95
REMARK 500 1 ASP A 58 59.98 -98.77
REMARK 500 1 PHE A 59 -19.49 -47.76
REMARK 500 1 ASN A 82 51.02 -140.82
REMARK 500 1 PRO A 87 -145.55 -72.66
REMARK 500 1 GLU A 88 77.85 -174.36
REMARK 500 1 SER A 93 36.48 -141.61
REMARK 500 1 LEU A 94 49.69 -142.62
REMARK 500 1 PRO A 96 67.80 -61.73
REMARK 500 2 ASN A 28 41.83 -97.67
REMARK 500 2 LYS A 61 41.63 82.63
REMARK 500 2 ASN A 82 47.28 173.85
REMARK 500 2 ASP A 85 154.00 -45.24
REMARK 500 2 GLU A 92 -138.16 -99.24
REMARK 500 3 LYS A 7 128.99 -171.23
REMARK 500 3 GLN A 24 72.33 -114.88
REMARK 500 3 LEU A 27 -16.38 -48.36
REMARK 500 3 ASN A 28 39.77 -95.52
REMARK 500 3 ASP A 58 53.77 -99.08
REMARK 500 3 TYR A 84 111.44 39.49
REMARK 500 3 PRO A 87 -140.11 -75.02
REMARK 500 3 LYS A 89 -44.45 -165.30
REMARK 500 3 GLU A 92 0.36 -53.34
REMARK 500 3 LEU A 94 52.37 -141.18
REMARK 500 3 PRO A 96 -178.02 -64.78
REMARK 500 4 LYS A 7 96.95 -64.63
REMARK 500 4 GLN A 24 54.28 -105.97
REMARK 500 4 SER A 34 -75.64 -92.36
REMARK 500 4 LYS A 44 -40.08 151.33
REMARK 500 4 ILE A 47 -33.32 -38.56
REMARK 500 4 ASP A 58 51.20 -96.35
REMARK 500 4 PHE A 59 -8.59 -54.89
REMARK 500 4 LYS A 61 49.79 71.45
REMARK 500 4 ASN A 82 57.51 -168.22
REMARK 500 4 GLU A 88 68.61 157.41
REMARK 500 4 SER A 93 -115.53 -137.50
REMARK 500 4 MET A 95 97.21 -30.38
REMARK 500 4 PRO A 96 57.45 -69.01
REMARK 500 5 LYS A 7 126.65 69.83
REMARK 500 5 ASP A 26 29.25 -160.58
REMARK 500 5 LEU A 27 -139.43 -90.27
REMARK 500 5 LYS A 44 -54.27 165.96
REMARK 500 5 LEU A 48 -75.08 -45.73
REMARK 500 5 ASP A 58 49.11 -98.74
REMARK 500 5 PHE A 59 -4.69 -52.76
REMARK 500 5 TYR A 84 -36.53 -156.73
REMARK 500 5 LEU A 86 104.83 68.30
REMARK 500 5 GLU A 88 59.11 -66.15
REMARK 500
REMARK 500 THIS ENTRY HAS 298 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 100 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 58 OD1
REMARK 620 2 ASP A 60 OD1 71.5
REMARK 620 3 ASP A 60 OD2 103.2 59.7
REMARK 620 4 ASP A 62 OD1 91.3 69.8 118.2
REMARK 620 5 ASP A 62 OD2 129.7 78.7 95.1 39.7
REMARK 620 6 ALA A 64 O 112.3 137.5 144.0 67.9 66.8
REMARK 620 7 GLU A 69 OE1 80.5 144.2 107.6 134.1 137.1 73.8
REMARK 620 8 GLU A 69 OE2 131.8 131.6 72.7 133.9 98.3 79.2 57.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 100
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4788 RELATED DB: BMRB
REMARK 900 BMRB-4788 IS 1H, 13C, AND 15N RESONANCE ASSIGNMENTS
DBREF 1FI6 A 6 97 UNP O54916 REPS1_MOUSE 227 318
SEQRES 1 A 92 TRP LYS ILE THR ASP GLU GLN ARG GLN TYR TYR VAL ASN
SEQRES 2 A 92 GLN PHE LYS THR ILE GLN PRO ASP LEU ASN GLY PHE ILE
SEQRES 3 A 92 PRO GLY SER ALA ALA LYS GLU PHE PHE THR LYS SER LYS
SEQRES 4 A 92 LEU PRO ILE LEU GLU LEU SER HIS ILE TRP GLU LEU SER
SEQRES 5 A 92 ASP PHE ASP LYS ASP GLY ALA LEU THR LEU ASP GLU PHE
SEQRES 6 A 92 CYS ALA ALA PHE HIS LEU VAL VAL ALA ARG LYS ASN GLY
SEQRES 7 A 92 TYR ASP LEU PRO GLU LYS LEU PRO GLU SER LEU MET PRO
SEQRES 8 A 92 LYS
HET CA A 100 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 THR A 9 LYS A 21 1 13
HELIX 2 2 GLY A 33 LYS A 44 1 12
HELIX 3 3 PRO A 46 ASP A 58 1 13
HELIX 4 4 LEU A 67 GLY A 83 1 17
SHEET 1 A 2 PHE A 30 PRO A 32 0
SHEET 2 A 2 ALA A 64 THR A 66 -1 N LEU A 65 O ILE A 31
LINK OD1 ASP A 58 CA CA A 100 1555 1555 2.09
LINK OD1 ASP A 60 CA CA A 100 1555 1555 2.21
LINK OD2 ASP A 60 CA CA A 100 1555 1555 2.15
LINK OD1 ASP A 62 CA CA A 100 1555 1555 2.10
LINK OD2 ASP A 62 CA CA A 100 1555 1555 3.36
LINK O ALA A 64 CA CA A 100 1555 1555 2.19
LINK OE1 GLU A 69 CA CA A 100 1555 1555 2.27
LINK OE2 GLU A 69 CA CA A 100 1555 1555 2.28
SITE 1 AC1 5 ASP A 58 ASP A 60 ASP A 62 ALA A 64
SITE 2 AC1 5 GLU A 69
CRYST1 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 - b 23 2 Bytes