Header list of 1p9j.pdb file
Complete list - g 9 2 Bytes
HEADER HORMONE/GROWTH FACTOR 12-MAY-03 1P9J
TITLE SOLUTION STRUCTURE AND DYNAMICS OF THE EGF/TGF-ALPHA CHIMERA T1E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHIMERA OF EPIDERMAL GROWTH FACTOR(EGF) AND TRANSFORMING
COMPND 3 GROWTH FACTOR ALPHA (TGF-ALPHA);
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: TGF-ALPHA (RESIDUES 1-7), EGF (RESIDUES 8-54);
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: TGF-ALPHA AND EGF;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X33
KEYWDS CHIMERA, EGF, TGF-ALPHA, ERBB1, ERBB3, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 36
AUTHOR M.WINGENS,T.WALMA,H.VAN INGEN,C.STORTELERS,J.E.VAN LEEUWEN,E.J.VAN
AUTHOR 2 ZOELEN,G.W.VUISTER
REVDAT 4 14-JUN-23 1P9J 1 REMARK
REVDAT 3 05-FEB-20 1P9J 1 REMARK
REVDAT 2 24-FEB-09 1P9J 1 VERSN
REVDAT 1 07-OCT-03 1P9J 0
JRNL AUTH M.WINGENS,T.WALMA,H.VAN INGEN,C.STORTELERS,J.E.VAN LEEUWEN,
JRNL AUTH 2 E.J.VAN ZOELEN,G.W.VUISTER
JRNL TITL STRUCTURAL ANALYSIS OF AN EPIDERMAL GROWTH
JRNL TITL 2 FACTOR/TRANSFORMING GROWTH FACTOR-ALPHA CHIMERA WITH UNIQUE
JRNL TITL 3 ERBB BINDING SPECIFICITY.
JRNL REF J.BIOL.CHEM. V. 278 39114 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12869572
JRNL DOI 10.1074/JBC.M305603200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 0203, X-PLOR 3.851, CHARMM 22
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), BRUNGER, A. (X-PLOR),
REMARK 3 MACKERELL, A.D. (CHARMM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 660 ARE NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 98 DIHEDRAL ANGLE RESTRAINTS, AND 9 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1P9J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019177.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8MM T1E, 15N-LABELLED, 50MM
REMARK 210 PHOSPHATE BUFFER, 95% H20, 5%D20,
REMARK 210 PH 6.3, 20UG/ML PEFABLOC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY FOLLOWED BY
REMARK 210 BRIEF MOLECULAR DYNAMICS RUN IN
REMARK 210 WATER.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 98
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 36
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: 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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 6 TYR A 24 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 7 CYS A 8 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 8 TYR A 24 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 8 TYR A 46 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 8 TYR A 46 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 9 ARG A 43 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 11 TYR A 24 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 11 TYR A 24 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 11 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 12 TYR A 24 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 12 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 13 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 TYR A 24 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 15 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 17 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 18 ARG A 43 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 19 TYR A 31 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 19 TYR A 31 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 20 TYR A 24 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 20 TYR A 24 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 20 TYR A 46 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 22 TYR A 24 CB - CG - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 22 TYR A 24 CB - CG - CD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 23 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 27 TYR A 24 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 28 CYS A 8 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 29 TYR A 24 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 29 TYR A 46 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 29 TYR A 46 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 31 TYR A 24 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 31 TYR A 24 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 31 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 32 TYR A 24 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 32 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 32 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 33 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 35 TYR A 24 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 35 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
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 ASP A 13 35.33 -99.72
REMARK 500 1 ASP A 19 62.96 68.61
REMARK 500 2 CYS A 8 96.70 -52.00
REMARK 500 2 HIS A 18 30.21 73.62
REMARK 500 2 ASP A 19 80.88 77.06
REMARK 500 2 ASP A 29 16.82 80.73
REMARK 500 3 ASP A 19 79.75 59.74
REMARK 500 3 GLU A 53 46.18 -70.28
REMARK 500 4 ASP A 19 81.06 58.04
REMARK 500 4 ASP A 29 31.06 81.04
REMARK 500 4 GLU A 53 59.78 -91.65
REMARK 500 5 SER A 3 -53.71 -130.40
REMARK 500 5 CYS A 8 79.77 -114.63
REMARK 500 5 ASP A 19 74.54 56.22
REMARK 500 5 GLU A 53 72.15 -103.94
REMARK 500 6 ASP A 19 76.86 59.47
REMARK 500 6 ASP A 29 9.08 84.25
REMARK 500 6 GLU A 53 63.71 -100.32
REMARK 500 7 HIS A 12 -39.21 -150.14
REMARK 500 7 ASP A 19 74.53 51.45
REMARK 500 8 HIS A 12 72.91 -15.88
REMARK 500 8 GLU A 53 64.55 -102.83
REMARK 500 9 ASP A 7 97.74 -160.90
REMARK 500 9 HIS A 12 93.87 -16.66
REMARK 500 10 HIS A 12 34.78 -150.02
REMARK 500 10 ILE A 40 -165.12 -129.55
REMARK 500 10 GLU A 53 73.41 -107.32
REMARK 500 11 ASP A 19 72.28 33.08
REMARK 500 11 ASP A 29 51.22 71.23
REMARK 500 11 ARG A 43 37.95 -94.75
REMARK 500 11 CYS A 44 31.72 71.28
REMARK 500 12 CYS A 8 107.50 -57.74
REMARK 500 12 ASP A 29 7.39 83.49
REMARK 500 12 GLU A 53 73.77 -113.15
REMARK 500 14 SER A 3 55.04 -99.92
REMARK 500 14 ASP A 19 80.13 73.77
REMARK 500 15 SER A 3 -49.03 -130.40
REMARK 500 15 HIS A 12 114.36 -20.69
REMARK 500 15 GLU A 53 69.11 -103.56
REMARK 500 16 PRO A 9 -64.26 -103.42
REMARK 500 16 HIS A 18 45.85 78.09
REMARK 500 16 GLU A 53 44.84 -93.07
REMARK 500 17 ASP A 13 35.33 -99.72
REMARK 500 17 ASP A 19 62.96 68.61
REMARK 500 18 ASP A 7 97.74 -160.90
REMARK 500 18 HIS A 12 93.87 -16.66
REMARK 500 19 ASP A 19 40.19 72.04
REMARK 500 19 ASP A 29 10.22 84.48
REMARK 500 19 CYS A 44 70.55 54.38
REMARK 500 20 SER A 3 -50.30 -120.72
REMARK 500
REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 11 HIS A 12 8 -148.85
REMARK 500 SER A 11 HIS A 12 9 -147.73
REMARK 500 SER A 11 HIS A 12 18 -147.73
REMARK 500 SER A 11 HIS A 12 29 -148.85
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 2 ARG A 43 0.09 SIDE CHAIN
REMARK 500 5 ARG A 43 0.14 SIDE CHAIN
REMARK 500 6 ARG A 43 0.10 SIDE CHAIN
REMARK 500 9 ARG A 47 0.09 SIDE CHAIN
REMARK 500 10 TYR A 46 0.08 SIDE CHAIN
REMARK 500 11 TYR A 39 0.09 SIDE CHAIN
REMARK 500 12 ARG A 43 0.15 SIDE CHAIN
REMARK 500 15 ARG A 43 0.09 SIDE CHAIN
REMARK 500 18 ARG A 47 0.09 SIDE CHAIN
REMARK 500 22 TYR A 24 0.08 SIDE CHAIN
REMARK 500 23 ARG A 43 0.09 SIDE CHAIN
REMARK 500 26 ARG A 43 0.14 SIDE CHAIN
REMARK 500 27 ARG A 43 0.10 SIDE CHAIN
REMARK 500 30 TYR A 46 0.08 SIDE CHAIN
REMARK 500 31 TYR A 39 0.09 SIDE CHAIN
REMARK 500 32 ARG A 43 0.15 SIDE CHAIN
REMARK 500 35 ARG A 43 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5801 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT, J COUPLING CONSTANTS AND RELAXATION DATA
DBREF 1P9J A 1 7 UNP P01135 TGFA_HUMAN 40 46
DBREF 1P9J A 8 54 UNP P01133 EGF_HUMAN 976 1022
SEQRES 1 A 54 VAL VAL SER HIS PHE ASN ASP CYS PRO LEU SER HIS ASP
SEQRES 2 A 54 GLY TYR CYS LEU HIS ASP GLY VAL CYS MET TYR ILE GLU
SEQRES 3 A 54 ALA LEU ASP LYS TYR ALA CYS ASN CYS VAL VAL GLY TYR
SEQRES 4 A 54 ILE GLY GLU ARG CYS GLN TYR ARG ASP LEU LYS TRP TRP
SEQRES 5 A 54 GLU LEU
SHEET 1 A 2 VAL A 21 ILE A 25 0
SHEET 2 A 2 LYS A 30 ASN A 34 -1 O LYS A 30 N ILE A 25
SHEET 1 B 2 TYR A 39 ILE A 40 0
SHEET 2 B 2 TYR A 46 ARG A 47 -1 O TYR A 46 N ILE A 40
SSBOND 1 CYS A 8 CYS A 22 1555 1555 2.03
SSBOND 2 CYS A 16 CYS A 33 1555 1555 2.03
SSBOND 3 CYS A 35 CYS A 44 1555 1555 2.03
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 - g 9 2 Bytes