Header list of 1xr0.pdb file
Complete list - 2 20 Bytes
HEADER SIGNALING PROTEIN/GROWTH FACTOR RECEPTOR13-OCT-04 1XR0
TITLE STRUCTURAL BASIS OF SNT PTB DOMAIN INTERACTIONS WITH DISTINCT
TITLE 2 NEUROTROPHIC RECEPTORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BASIC FIBROBLAST GROWTH FACTOR RECEPTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 409-430 FROM THE JUXTAMEMBRANE
COMPND 5 REGION OF HFGFR1;
COMPND 6 SYNONYM: FGFR-1, BFGF-R, FMS-LIKE TYROSINE KINASE-2, C-FGR;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: FGFR SIGNALLING ADAPTOR SNT-1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: PTB DOMAIN AT THE N TERMINUS;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 IS TAKEN FROM HOMO SAPIENS (HUMAN).;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FGFR, SNT, PHOSPHOTYROSINE BINDING DOMAIN, PTB, TRK, NPXPY MOTIF,
KEYWDS 2 SIGNALING PROTEIN-GROWTH FACTOR RECEPTOR COMPLEX
EXPDTA SOLUTION NMR
AUTHOR C.DHALLUIN,K.S.YAN,O.PLOTNIKOVA,K.W.LEE,L.ZENG,M.KUTI,S.MUJTABA,
AUTHOR 2 M.P.GOLDFARB,M.-M.ZHOU
REVDAT 3 02-MAR-22 1XR0 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1XR0 1 VERSN
REVDAT 1 02-NOV-04 1XR0 0
JRNL AUTH C.DHALLUIN,K.S.YAN,O.PLOTNIKOVA,K.W.LEE,L.ZENG,M.KUTI,
JRNL AUTH 2 S.MUJTABA,M.P.GOLDFARB,M.-M.ZHOU
JRNL TITL STRUCTURAL BASIS OF SNT PTB DOMAIN INTERACTIONS WITH
JRNL TITL 2 DISTINCT NEUROTROPHIC RECEPTORS
JRNL REF MOL.CELL V. 6 921 2000
JRNL REFN ISSN 1097-2765
JRNL PMID 11090629
JRNL DOI 10.1016/S1097-2765(05)00087-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, ARIA 1.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), M. NILGES AND S. O'DONOGHUE
REMARK 3 (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030666.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 15 MM DTT-D10, AND 0.5 MM EDTA00
REMARK 210 MM PHOSPHATE BUFFER,
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : SNT-1 PTB DOMAIN/HFGFR1 PEPTIDE
REMARK 210 COMPLEX (1:1) OF ~0.5 MM IN 100
REMARK 210 MM PHOSPHATE BUFFER OF PH 6.5, 5
REMARK 210 MM DTT-D10, AND 0.5 MM EDTA IN
REMARK 210 H2O/2H2O (9/1) OR 2H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 3D_13C-SEPARATED_NOESY;
REMARK 210 3D_15N-SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : STRUCTURES OF THE SNT-1 PTB
REMARK 210 DOMAIN IN COMPLEX WITH THE
REMARK 210 HFGFR1 PEPTIDE WERE CALCULATED
REMARK 210 WITH A DISTANCE GEOMETRY AND
REMARK 210 SIMULATED ANNEALING PROTOCOL BY
REMARK 210 USING THE X-PLOR PROGRAM ([4]).
REMARK 210 NOE DISTANCE AND DIHEDRAL ANGLE
REMARK 210 RESTRAINTS WERE TREATED WITH A
REMARK 210 SQUARE-WELL POTENTIAL OF 50 KCAL
REMARK 210 MOL?1 ?2. A TOTAL OF 2448
REMARK 210 MANUALLY ASSIGNED NOE-DERIVED
REMARK 210 DISTANCE RESTRAINTS WERE
REMARK 210 OBTAINED FROM THE 15N- OR 13C-
REMARK 210 EDITED NOESY DATA. INCLUDED IN
REMARK 210 THIS FIGURE ARE 251 INTRAPEPTIDE
REMARK 210 AND 258 INTERMOLECULAR DISTANCE
REMARK 210 RESTRAINTS. ADDITIONALLY, 255
REMARK 210 UNAMBIGUOUS AND 52 AMBIGUOUS
REMARK 210 DISTANCE RESTRAINTS WERE
REMARK 210 IDENTIFIED FROM THE NOE DATA BY
REMARK 210 USING ARIA. THE FINAL STRUCTURE
REMARK 210 CALCULATIONS EMPLOYED A TOTAL OF
REMARK 210 2755 NOE RESTRAINTS OBTAINED
REMARK 210 FROM THE MANUAL AND THE ARIA-
REMARK 210 ASSISTED ASSIGNMENTS, 2703 OF
REMARK 210 WHICH WERE UNAMBIGUOUSLY
REMARK 210 ASSIGNED NOE-DERIVED DISTANCE
REMARK 210 RESTRAINTS THAT COMPRISE 1072
REMARK 210 INTRARESIDUE, 466 SEQUENTIAL,
REMARK 210 216 MEDIUM-RANGE, AND 949 LONG-
REMARK 210 RANGE NOES. IN ADDITION, 70
REMARK 210 HYDROGEN-BOND DISTANCE
REMARK 210 RESTRAINTS FOR 35 HYDROGEN BONDS
REMARK 210 AND 19 -ANGLE RESTRAINTS WERE
REMARK 210 ALSO USED IN THE STRUCTURE
REMARK 210 CALCULATIONS. FOR THE ENSEMBLE
REMARK 210 OF THE FINAL 20 STRUCTURES, NO
REMARK 210 DISTANCE OR TORSIONAL ANGLE
REMARK 210 RESTRAINT WAS VIOLATED BY MORE
REMARK 210 THAN 0.4 OR 5, RESPECTIVELY. THE
REMARK 210 DISTANCE-VIOLATION, DIHEDRAL-
REMARK 210 VIOLATION, AND TOTAL ENERGIES
REMARK 210 WERE 74.4 1.7 KCAL MOL/1, 0.82
REMARK 210 0.08 KCAL MOL/1, AND 262.0 6.0
REMARK 210 KCAL MOL/1, RESPECTIVELY. THE
REMARK 210 LENNARD-JONES POTENTIAL, WHICH
REMARK 210 WAS NOT USED DURING ANY
REMARK 210 REFINEMENT STAGE, WAS 659.3 23.1
REMARK 210 KCAL MOL/1 FOR THE FINAL
REMARK 210 STRUCTURES. RAMACHANDRAN PLOT
REMARK 210 ANALYSIS BY PROCHECK-NMR SHOWED
REMARK 210 THAT IN THE FINAL STRUCTURES OF
REMARK 210 THE COMPLEX, 98.1% OF THE
REMARK 210 BACKBONE GEOMETRIES OF THE NON-
REMARK 210 GLY AND NON-PRO RESIDUES IN THE
REMARK 210 COMPLEX (PROTEIN RESIDUES 18-116
REMARK 210 AND PEPTIDE RESIDUES (412-430)
REMARK 210 AND NEARLY 100% IN THE SECONDARY
REMARK 210 STRUCTURE (PROTEIN RESIDUES 19-
REMARK 210 24, 35-40, 45-49, 52-57, 63-68,
REMARK 210 71-76, 85-90, 94-107, AND 111-
REMARK 210 115 AND PEPTIDE RESIDUES 426-430)
REMARK 210 LIE WITHIN ENERGETICALLY
REMARK 210 FAVORABLE OR ALLOWED REGIONS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 NMR SPECTRA WERE ACQUIRED AT 30C ON A BRUKER DRX600 OR DRX500
REMARK 210 SPECTROMETER. THE BACKBONE AND
REMARK 210 SIDE CHAIN 1H, 13C, AND 15N RESONANCES OF THE PROTEIN WERE
REMARK 210 ASSIGNED USING DEUTERIUM-DECOUPLED
REMARK 210 TRIPLE-RESONANCE EXPERIMENTS OF HNCA, HN(CO)CA, HNCACB, HN(CO)
REMARK 210 CACB, AND
REMARK 210 (H)C(CO)NH-TOCSY ([34 AND 30]) RECORDED BY USING UNIFORMLY 15N/
REMARK 210 13C-LABELED AND FRACTIONALLY
REMARK 210 DEUTERATED PROTEIN IN COMPLEX WITH A NONISOTOPICALLY LABELED
REMARK 210 HFGFR1 PEPTIDE. THE SIDE CHAIN
REMARK 210 ASSIGNMENTS WERE COMPLETED USING 3D HCCH-TOCSY ([7]) DATA
REMARK 210 COLLECTED FROM A UNIFORMLY 15N/13C
REMARK 210 LABELED-PROTEIN/NONLABELED-PEPTIDE COMPLEX. NOE-DERIVED
REMARK 210 DISTANCE RESTRAINTS WERE OBTAINED FROM
REMARK 210 15N- OR 13C-EDITED 3D NOESY SPECTRA ([7]). -ANGLE RESTRAINTS
REMARK 210 WERE DETERMINED FROM 3JHN,H
REMARK 210 COUPLING CONSTANTS MEASURED IN A 3D HNHA-J SPECTRUM ([7]).
REMARK 210 SLOWLY EXCHANGING AMIDE PROTONS WERE
REMARK 210 IDENTIFIED FROM A SERIES OF 2D 15N-HSQC SPECTRA RECORDED AFTER
REMARK 210 THE H2O BUFFER WAS CHANGED TO 2H2O
REMARK 210 BUFFER. THE PEPTIDE RESONANCES WERE ASSIGNED USING 13C/15N-
REMARK 210 FILTERED 2D NOESY AND TOCSY SPECTRA
REMARK 210 ([30]) COLLECTED FROM A 15N/13C LABELED-PROTEIN/NONLABELED-
REMARK 210 PEPTIDE COMPLEX. THE INTERMOLECULAR NOES
REMARK 210 USED IN DEFINING THE STRUCTURE OF THE SNT-1 PTB DOMAIN/HFGFR1
REMARK 210 COMPLEX WERE DETECTED IN 13C- OR
REMARK 210 15N-EDITED (F 1), 13C/15N-FILTERED (F 3) 3D NOESY SPECTRA. ALL
REMARK 210 NMR SPECTRA WERE PROCESSED WITH
REMARK 210 NMRPIPE/NMRDRAW ([8]) AND ANALYZED USING NMRVIEW.
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 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 GLN A 411 -86.34 61.86
REMARK 500 MET A 412 -178.00 50.11
REMARK 500 VAL A 414 95.77 -42.03
REMARK 500 HIS A 415 -173.67 -65.40
REMARK 500 PRO A 422 75.09 -64.72
REMARK 500 GLN A 426 73.55 -161.08
REMARK 500 ASP B 11 33.08 -161.25
REMARK 500 ASN B 16 74.34 -64.62
REMARK 500 HIS B 17 54.30 -160.75
REMARK 500 LYS B 22 82.99 -59.15
REMARK 500 GLU B 32 141.03 60.75
REMARK 500 SER B 35 122.05 167.68
REMARK 500 LEU B 40 66.83 -119.24
REMARK 500 THR B 41 -167.57 -54.15
REMARK 500 THR B 43 54.06 -163.83
REMARK 500 GLU B 44 139.61 178.49
REMARK 500 LEU B 45 67.50 -101.64
REMARK 500 LYS B 51 27.05 47.92
REMARK 500 ARG B 52 -52.35 -152.46
REMARK 500 HIS B 58 32.03 -96.59
REMARK 500 TYR B 59 -80.57 70.02
REMARK 500 LEU B 62 -152.33 -59.81
REMARK 500 ARG B 63 -44.63 -151.73
REMARK 500 SER B 69 -84.68 56.85
REMARK 500 ARG B 79 -74.75 -156.49
REMARK 500 CYS B 80 -155.55 178.88
REMARK 500 GLN B 81 -85.89 69.85
REMARK 500 PHE B 98 -70.83 -49.11
REMARK 500 VAL B 112 54.28 -143.95
REMARK 500 VAL B 113 99.72 -44.22
REMARK 500 VAL B 117 34.88 -146.65
REMARK 500 VAL B 118 96.12 41.10
REMARK 500 ASN B 121 -80.70 61.70
REMARK 500 ASN B 122 119.78 179.43
REMARK 500 GLU B 128 -49.25 -166.21
REMARK 500 THR B 135 79.25 66.04
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XR0 A 409 430 UNP P11362 FGFR1_HUMAN 409 430
DBREF 1XR0 B 11 136 UNP Q8WU20 FRS2_HUMAN 11 136
SEQADV 1XR0 MET B 8 UNP Q8WU20 CLONING ARTIFACT
SEQADV 1XR0 GLY B 9 UNP Q8WU20 CLONING ARTIFACT
SEQADV 1XR0 SER B 10 UNP Q8WU20 CLONING ARTIFACT
SEQRES 1 A 22 HIS SER GLN MET ALA VAL HIS LYS LEU ALA LYS SER ILE
SEQRES 2 A 22 PRO LEU ARG ARG GLN VAL THR VAL SER
SEQRES 1 B 129 MET GLY SER ASP THR VAL PRO ASP ASN HIS ARG ASN LYS
SEQRES 2 B 129 PHE LYS VAL ILE ASN VAL ASP ASP ASP GLY ASN GLU LEU
SEQRES 3 B 129 GLY SER GLY ILE MET GLU LEU THR ASP THR GLU LEU ILE
SEQRES 4 B 129 LEU TYR THR ARG LYS ARG ASP SER VAL LYS TRP HIS TYR
SEQRES 5 B 129 LEU CYS LEU ARG ARG TYR GLY TYR ASP SER ASN LEU PHE
SEQRES 6 B 129 SER PHE GLU SER GLY ARG ARG CYS GLN THR GLY GLN GLY
SEQRES 7 B 129 ILE PHE ALA PHE LYS CYS ALA ARG ALA GLU GLU LEU PHE
SEQRES 8 B 129 ASN MET LEU GLN GLU ILE MET GLN ASN ASN SER ILE ASN
SEQRES 9 B 129 VAL VAL GLU GLU PRO VAL VAL GLU ARG ASN ASN HIS GLN
SEQRES 10 B 129 THR GLU LEU GLU VAL PRO ARG THR PRO ARG THR PRO
HELIX 1 1 ARG B 93 ASN B 108 1 16
SHEET 1 A 2 VAL A 427 THR A 428 0
SHEET 2 A 2 VAL B 113 GLU B 114 -1 O VAL B 113 N THR A 428
SHEET 1 B 7 ASP B 53 TRP B 57 0
SHEET 2 B 7 LEU B 45 THR B 49 -1 N LEU B 47 O VAL B 55
SHEET 3 B 7 GLY B 36 LEU B 40 -1 N ILE B 37 O TYR B 48
SHEET 4 B 7 LYS B 20 VAL B 26 -1 N VAL B 23 O GLY B 36
SHEET 5 B 7 GLY B 85 LYS B 90 -1 O ALA B 88 N VAL B 26
SHEET 6 B 7 LEU B 71 SER B 76 -1 N PHE B 74 O PHE B 87
SHEET 7 B 7 LEU B 62 TYR B 67 -1 N GLY B 66 O SER B 73
CISPEP 1 VAL B 129 PRO B 130 0 0.34
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
Complete list - 2 20 Bytes