Header list of 1ff1.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 24-JUL-00 1FF1
TITLE STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 IN
TITLE 2 COMPLEX WITH PTGSSSTNPFL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND EH DOMAIN;
COMPND 5 SYNONYM: EPS15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PTGSSSTNPFL PEPTIDE;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSETA;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: CHEMICALLY SYNTHESIZED PEPTIDE
KEYWDS COMPLEX, EH DOMAIN, NPF, HRB, CALCIUM BINDING, SIGNALING DOMAIN, EF-
KEYWDS 2 HAND, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.DE BEER,A.N.HOOFNAGLE,J.L.ENMON,R.C.BOWERS,M.YAMABHAI,B.K.KAY,
AUTHOR 2 M.OVERDUIN
REVDAT 4 23-FEB-22 1FF1 1 REMARK LINK
REVDAT 3 24-FEB-09 1FF1 1 VERSN
REVDAT 2 01-APR-03 1FF1 1 JRNL
REVDAT 1 01-NOV-00 1FF1 0
JRNL AUTH T.DE BEER,A.N.HOOFNAGLE,J.L.ENMON,R.C.BOWERS,M.YAMABHAI,
JRNL AUTH 2 B.K.KAY,M.OVERDUIN
JRNL TITL MOLECULAR MECHANISM OF NPF RECOGNITION BY EH DOMAINS.
JRNL REF NAT.STRUCT.BIOL. V. 7 1018 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 11062555
JRNL DOI 10.1038/80924
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, X-PLOR 3.85
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE R-6 SUMMATION METHOD WAS USED
REMARK 3 WITHIN A SIMULATED ANNEALING PROTOCOL. ALTHOUGH THE NMR DATA WAS
REMARK 3 COLLECTED ON AN 11-MER, PTGSSSTNPFL, NOES WERE ABSENT FOR THE N-
REMARK 3 TERMINAL 6 RESIDUES. THE STRUCTURES WERE THEREFORE CALCULATED
REMARK 3 WITH THE PEPTIDE FRAGMENT STNPFL.
REMARK 4
REMARK 4 1FF1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011530.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : 7.00
REMARK 210 IONIC STRENGTH : 0.15
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM {15N}-EH2 AND 5 MM PEPTIDE,
REMARK 210 20 MM PERDEUTERATED TRIS, 100 MM
REMARK 210 POTASSIUM CHLORIDE, 1 MM
REMARK 210 PERDEUTERATED DTT, 1 MM SODIUM
REMARK 210 AZIDE, 2 MM CALCIUM CHLORIDE; 1
REMARK 210 MM {15N}-EH2 AND 5 MM PEPTIDE,
REMARK 210 20 MM PERDEUTERATED TRIS, 100 MM
REMARK 210 POTASSIUM CHLORIDE, 1 MM
REMARK 210 PERDEUTERATED DTT, 1 MM SODIUM
REMARK 210 AZIDE, 2 MM CALCIUM CHLORIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1, X-PLOR 3.85
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 20 LOWEST NOE ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: DATA WAS COLLECTED ON A 15N-LABELLED EH2 SAMPLE IN THE
REMARK 210 PRESENCE OF SYNTHETIC UNLABELLED PTGSSSTNPFL AND CALCIUM
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 PRO B 102
REMARK 465 THR B 103
REMARK 465 GLY B 104
REMARK 465 SER B 105
REMARK 465 SER B 106
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 SER A 32 H LYS A 35 1.45
REMARK 500 H ALA A 8 O ALA A 93 1.45
REMARK 500 O LEU A 31 H LEU A 65 1.52
REMARK 500 O ASP A 66 H PHE A 70 1.54
REMARK 500 O TRP A 54 H ASP A 58 1.54
REMARK 500 O ILE A 49 H VAL A 53 1.56
REMARK 500 OD1 ASP A 66 H GLU A 69 1.57
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 25 92.05 84.80
REMARK 500 1 ASN A 28 19.80 52.14
REMARK 500 1 LYS A 83 -76.98 -127.17
REMARK 500 1 LEU A 90 106.96 -54.63
REMARK 500 1 LEU A 94 19.87 -152.31
REMARK 500 1 THR B 108 -30.06 179.04
REMARK 500 2 SER A 25 93.07 85.12
REMARK 500 2 VAL A 77 -60.36 -91.91
REMARK 500 2 LYS A 83 -25.95 177.73
REMARK 500 2 LEU A 90 107.48 -54.57
REMARK 500 3 SER A 25 97.19 142.46
REMARK 500 3 ASN A 28 17.04 56.78
REMARK 500 3 VAL A 77 -61.52 -91.78
REMARK 500 3 LYS A 83 -21.80 177.26
REMARK 500 3 LEU A 90 107.17 -55.28
REMARK 500 4 SER A 25 90.32 142.55
REMARK 500 4 ASP A 58 87.07 -69.01
REMARK 500 4 HIS A 61 51.98 39.58
REMARK 500 4 LYS A 83 -74.37 -103.99
REMARK 500 4 LEU A 90 107.09 -52.39
REMARK 500 4 LEU A 94 36.19 -145.52
REMARK 500 4 SER A 98 -45.52 77.43
REMARK 500 4 THR B 108 -136.24 -149.55
REMARK 500 5 SER A 25 94.75 88.31
REMARK 500 5 LYS A 83 -27.24 178.01
REMARK 500 5 THR B 108 -70.99 -54.17
REMARK 500 6 ALA A 8 -30.17 -37.71
REMARK 500 6 SER A 25 94.55 82.73
REMARK 500 6 LYS A 83 -86.88 -111.42
REMARK 500 6 PRO A 85 -160.32 -68.58
REMARK 500 6 LEU A 90 108.11 -55.76
REMARK 500 7 SER A 25 91.28 87.20
REMARK 500 7 ASN A 28 16.91 57.37
REMARK 500 7 LYS A 83 68.72 177.50
REMARK 500 7 GLU A 84 107.00 -177.54
REMARK 500 7 PRO A 85 -178.73 -66.39
REMARK 500 7 LEU A 90 107.92 -53.34
REMARK 500 8 SER A 25 95.67 85.38
REMARK 500 8 VAL A 77 -64.81 -91.28
REMARK 500 8 LYS A 83 35.98 177.74
REMARK 500 8 PRO A 85 -166.12 -70.76
REMARK 500 8 SER A 89 20.18 -162.86
REMARK 500 8 LEU A 90 120.78 59.94
REMARK 500 9 SER A 25 95.76 79.81
REMARK 500 9 ASN A 28 18.39 57.40
REMARK 500 9 LYS A 83 -27.57 177.22
REMARK 500 9 PRO A 85 -176.13 -69.94
REMARK 500 9 LEU A 90 104.99 -54.89
REMARK 500 9 THR B 108 80.58 -63.43
REMARK 500 10 SER A 25 97.15 140.36
REMARK 500
REMARK 500 THIS ENTRY HAS 113 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 52 0.14 SIDE CHAIN
REMARK 500 1 ARG A 67 0.31 SIDE CHAIN
REMARK 500 2 ARG A 52 0.27 SIDE CHAIN
REMARK 500 2 ARG A 67 0.28 SIDE CHAIN
REMARK 500 2 ARG A 100 0.30 SIDE CHAIN
REMARK 500 3 ARG A 52 0.32 SIDE CHAIN
REMARK 500 3 ARG A 67 0.32 SIDE CHAIN
REMARK 500 3 ARG A 100 0.19 SIDE CHAIN
REMARK 500 4 ARG A 52 0.31 SIDE CHAIN
REMARK 500 4 ARG A 67 0.23 SIDE CHAIN
REMARK 500 4 ARG A 100 0.31 SIDE CHAIN
REMARK 500 5 ARG A 52 0.15 SIDE CHAIN
REMARK 500 5 ARG A 67 0.30 SIDE CHAIN
REMARK 500 5 ARG A 100 0.31 SIDE CHAIN
REMARK 500 6 ARG A 52 0.12 SIDE CHAIN
REMARK 500 6 ARG A 67 0.19 SIDE CHAIN
REMARK 500 6 ARG A 100 0.31 SIDE CHAIN
REMARK 500 7 ARG A 52 0.31 SIDE CHAIN
REMARK 500 7 ARG A 67 0.29 SIDE CHAIN
REMARK 500 7 ARG A 100 0.31 SIDE CHAIN
REMARK 500 8 ARG A 52 0.32 SIDE CHAIN
REMARK 500 8 ARG A 67 0.31 SIDE CHAIN
REMARK 500 8 ARG A 100 0.27 SIDE CHAIN
REMARK 500 9 ARG A 52 0.31 SIDE CHAIN
REMARK 500 9 ARG A 67 0.31 SIDE CHAIN
REMARK 500 9 ARG A 100 0.32 SIDE CHAIN
REMARK 500 10 ARG A 67 0.25 SIDE CHAIN
REMARK 500 10 ARG A 100 0.30 SIDE CHAIN
REMARK 500 11 ARG A 52 0.21 SIDE CHAIN
REMARK 500 11 ARG A 67 0.29 SIDE CHAIN
REMARK 500 11 ARG A 100 0.20 SIDE CHAIN
REMARK 500 12 ARG A 52 0.19 SIDE CHAIN
REMARK 500 12 ARG A 67 0.29 SIDE CHAIN
REMARK 500 12 ARG A 100 0.16 SIDE CHAIN
REMARK 500 13 ARG A 52 0.32 SIDE CHAIN
REMARK 500 13 ARG A 67 0.31 SIDE CHAIN
REMARK 500 13 ARG A 100 0.24 SIDE CHAIN
REMARK 500 14 ARG A 52 0.30 SIDE CHAIN
REMARK 500 14 ARG A 67 0.23 SIDE CHAIN
REMARK 500 15 ARG A 52 0.32 SIDE CHAIN
REMARK 500 15 ARG A 67 0.24 SIDE CHAIN
REMARK 500 15 ARG A 100 0.27 SIDE CHAIN
REMARK 500 16 ARG A 52 0.32 SIDE CHAIN
REMARK 500 16 ARG A 67 0.31 SIDE CHAIN
REMARK 500 16 ARG A 100 0.17 SIDE CHAIN
REMARK 500 17 ARG A 52 0.18 SIDE CHAIN
REMARK 500 17 ARG A 67 0.19 SIDE CHAIN
REMARK 500 17 ARG A 100 0.32 SIDE CHAIN
REMARK 500 18 ARG A 52 0.29 SIDE CHAIN
REMARK 500 18 ARG A 67 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 57 PLANE DEVIATIONS.
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 113 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 58 OD1
REMARK 620 2 ASP A 60 N 87.0
REMARK 620 3 ASP A 60 OD2 154.6 67.8
REMARK 620 4 ASP A 62 OD1 80.8 110.8 110.6
REMARK 620 5 MET A 64 O 52.8 135.6 148.0 83.4
REMARK 620 6 GLU A 69 OE1 123.8 101.0 61.3 141.1 89.4
REMARK 620 7 GLU A 69 OE2 110.6 53.8 51.8 158.4 118.2 47.5
REMARK 620 N 1 2 3 4 5 6
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 113
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EH2 RELATED DB: PDB
REMARK 900 1EH2 IS THE FREE STATE OF EH2
REMARK 900 RELATED ID: 1F8H RELATED DB: PDB
REMARK 900 1F8H IS EH2 COMPLEXED WITH STNPFR
DBREF 1FF1 A 6 100 UNP P42566 EP15_HUMAN 121 215
DBREF 1FF1 B 102 112 PDB 1FF1 1FF1 102 112
SEQRES 1 A 95 PRO TRP ALA VAL LYS PRO GLU ASP LYS ALA LYS TYR ASP
SEQRES 2 A 95 ALA ILE PHE ASP SER LEU SER PRO VAL ASN GLY PHE LEU
SEQRES 3 A 95 SER GLY ASP LYS VAL LYS PRO VAL LEU LEU ASN SER LYS
SEQRES 4 A 95 LEU PRO VAL ASP ILE LEU GLY ARG VAL TRP GLU LEU SER
SEQRES 5 A 95 ASP ILE ASP HIS ASP GLY MET LEU ASP ARG ASP GLU PHE
SEQRES 6 A 95 ALA VAL ALA MET PHE LEU VAL TYR CYS ALA LEU GLU LYS
SEQRES 7 A 95 GLU PRO VAL PRO MET SER LEU PRO PRO ALA LEU VAL PRO
SEQRES 8 A 95 PRO SER LYS ARG
SEQRES 1 B 11 PRO THR GLY SER SER SER THR ASN PRO PHE LEU
HET CA A 113 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
HELIX 1 1 LYS A 10 ASP A 22 1 13
HELIX 2 2 SER A 32 ASN A 42 1 11
HELIX 3 3 PRO A 46 LEU A 56 1 11
HELIX 4 4 ASP A 66 LYS A 83 1 18
HELIX 5 5 PRO A 96 ARG A 100 5 5
LINK OD1 ASP A 58 CA CA A 113 1555 1555 2.82
LINK N ASP A 60 CA CA A 113 1555 1555 3.40
LINK OD2 ASP A 60 CA CA A 113 1555 1555 2.82
LINK OD1 ASP A 62 CA CA A 113 1555 1555 2.68
LINK O MET A 64 CA CA A 113 1555 1555 2.75
LINK OE1 GLU A 69 CA CA A 113 1555 1555 2.82
LINK OE2 GLU A 69 CA CA A 113 1555 1555 2.46
SITE 1 AC1 5 ASP A 58 ASP A 60 ASP A 62 MET A 64
SITE 2 AC1 5 GLU A 69
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 - b 23 2 Bytes