Header list of 1z9i.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 02-APR-05 1Z9I
TITLE A STRUCTURAL MODEL FOR THE MEMBRANE-BOUND FORM OF THE JUXTAMEMBRANE
TITLE 2 DOMAIN OF THE EPIDERMAL GROWTH FACTOR RECEPTOR
CAVEAT 1Z9I CHIRALITY ERROR CHIRAL CENTER CA ARG 6-12,14,16-21,23,24.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 669-721;
COMPND 5 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1;
COMPND 6 EC: 2.7.1.112;
COMPND 7 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: EGFR, ERBB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-3X
KEYWDS JUXTAMEMBRANE STRUCTURE EGFR MICELLE, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR K.CHOOWONGKOMON,C.R.CARLIN,F.D.SONNICHSEN
REVDAT 4 02-MAR-22 1Z9I 1 REMARK
REVDAT 3 24-FEB-09 1Z9I 1 VERSN
REVDAT 2 05-JUL-05 1Z9I 1 JRNL
REVDAT 1 24-MAY-05 1Z9I 0
JRNL AUTH K.CHOOWONGKOMON,C.R.CARLIN
JRNL TITL A STRUCTURAL MODEL FOR THE MEMBRANE-BOUND FORM OF THE
JRNL TITL 2 JUXTAMEMBRANE DOMAIN OF THE EPIDERMAL GROWTH FACTOR RECEPTOR
JRNL REF J.BIOL.CHEM. V. 280 24043 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15840573
JRNL DOI 10.1074/JBC.M502698200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1146 RESTRAINTS: 1249 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 55 DIHEDRAL ANGLE RESTRAINTS, 27 RDC
REMARK 3 RESTRAINTS, 21 DISTANCE RESTRAINTS FROM PARAMAGNETIC PROBE STUDIES.
REMARK 4
REMARK 4 1Z9I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032467.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5 MM JX EGFR IN 90 MM DPC
REMARK 210 15N,13C, 90% H20, 10% D20; 1.5
REMARK 210 MM JX EGFR IN 90 MM DPC 15N IN
REMARK 210 DRY ACRYLAMIDE GEL THEN COMPRESS
REMARK 210 IN THE NMR TUBE, 90% H20, 10% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; TROSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.2.1, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY AND ALSO USING RESTRAINTS FROM PARAMAGNETIC PROBE
REMARK 210 STUDIES.
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 4 ARG A 1 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 5 ARG A 1 N - CA - CB ANGL. DEV. = 11.7 DEGREES
REMARK 500 6 ARG A 1 N - CA - CB ANGL. DEV. = -83.6 DEGREES
REMARK 500 7 ARG A 1 N - CA - CB ANGL. DEV. = 20.1 DEGREES
REMARK 500 8 ARG A 1 N - CA - CB ANGL. DEV. = -73.2 DEGREES
REMARK 500 9 ARG A 1 N - CA - CB ANGL. DEV. = 24.4 DEGREES
REMARK 500 10 ARG A 1 N - CA - CB ANGL. DEV. = 23.1 DEGREES
REMARK 500 11 ARG A 1 N - CA - CB ANGL. DEV. = -84.6 DEGREES
REMARK 500 12 ARG A 1 N - CA - CB ANGL. DEV. = 110.2 DEGREES
REMARK 500 14 ARG A 1 N - CA - CB ANGL. DEV. = -37.7 DEGREES
REMARK 500 16 ARG A 1 N - CA - CB ANGL. DEV. = 100.0 DEGREES
REMARK 500 17 ARG A 1 N - CA - CB ANGL. DEV. = -58.2 DEGREES
REMARK 500 18 ARG A 1 N - CA - CB ANGL. DEV. = -52.3 DEGREES
REMARK 500 19 ARG A 1 N - CA - CB ANGL. DEV. = -61.2 DEGREES
REMARK 500 20 ARG A 1 N - CA - CB ANGL. DEV. = 105.7 DEGREES
REMARK 500 21 ARG A 1 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 22 ARG A 1 N - CA - CB ANGL. DEV. = 14.8 DEGREES
REMARK 500 23 ARG A 1 N - CA - CB ANGL. DEV. = 25.4 DEGREES
REMARK 500 24 ARG A 1 N - CA - CB ANGL. DEV. = -28.7 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 ARG A 2 -56.90 -158.69
REMARK 500 1 ARG A 3 -168.16 -111.93
REMARK 500 1 LEU A 20 -78.16 -152.85
REMARK 500 1 GLU A 22 -53.72 177.58
REMARK 500 1 ALA A 30 163.61 177.98
REMARK 500 2 ARG A 2 -63.78 -105.34
REMARK 500 2 ILE A 5 -57.62 -135.45
REMARK 500 2 VAL A 6 92.28 -59.46
REMARK 500 2 ARG A 7 -72.88 -126.37
REMARK 500 2 LEU A 11 -9.04 -59.65
REMARK 500 2 GLU A 19 21.16 48.75
REMARK 500 2 GLU A 22 68.92 66.63
REMARK 500 2 SER A 27 -79.22 -67.07
REMARK 500 2 GLU A 29 -59.18 72.22
REMARK 500 3 ARG A 3 -168.01 -104.73
REMARK 500 3 LEU A 20 -72.37 -134.63
REMARK 500 3 GLU A 22 -51.50 177.45
REMARK 500 3 SER A 27 -72.66 -91.84
REMARK 500 3 ALA A 30 147.49 -176.10
REMARK 500 4 HIS A 4 92.00 53.41
REMARK 500 4 GLU A 22 -58.92 -177.77
REMARK 500 4 LEU A 24 -42.65 -145.93
REMARK 500 4 THR A 25 100.40 69.07
REMARK 500 4 THR A 42 11.70 -151.09
REMARK 500 5 HIS A 4 -78.91 63.71
REMARK 500 5 ILE A 5 -61.58 73.64
REMARK 500 5 VAL A 21 -50.40 -145.39
REMARK 500 5 LEU A 24 -67.76 -100.33
REMARK 500 5 THR A 25 95.12 49.27
REMARK 500 5 PRO A 26 45.93 -85.12
REMARK 500 5 GLU A 29 39.12 -96.69
REMARK 500 5 THR A 42 11.79 -146.53
REMARK 500 6 ARG A 2 162.90 60.31
REMARK 500 6 HIS A 4 31.14 -99.01
REMARK 500 6 ILE A 5 -60.43 75.69
REMARK 500 6 GLU A 19 -0.44 75.54
REMARK 500 6 LEU A 20 -72.70 -145.69
REMARK 500 6 VAL A 21 -63.31 -154.30
REMARK 500 6 GLU A 22 68.13 -167.18
REMARK 500 6 SER A 27 -78.49 -77.25
REMARK 500 6 GLU A 29 -57.36 75.60
REMARK 500 7 ARG A 2 -73.26 -92.18
REMARK 500 7 HIS A 4 79.58 65.61
REMARK 500 7 ARG A 7 38.25 -96.94
REMARK 500 7 GLU A 19 47.50 -151.29
REMARK 500 7 LEU A 20 -77.98 -144.46
REMARK 500 7 GLU A 22 -55.22 179.68
REMARK 500 7 SER A 27 -62.41 -122.79
REMARK 500 7 GLU A 29 35.00 -98.36
REMARK 500 8 ARG A 2 -166.95 -105.33
REMARK 500
REMARK 500 THIS ENTRY HAS 187 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z9I A 1 53 UNP P00533 EGFR_HUMAN 669 721
SEQRES 1 A 53 ARG ARG ARG HIS ILE VAL ARG LYS ARG THR LEU ARG ARG
SEQRES 2 A 53 LEU LEU GLN GLU ARG GLU LEU VAL GLU PRO LEU THR PRO
SEQRES 3 A 53 SER GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG ILE LEU
SEQRES 4 A 53 LYS GLU THR GLU PHE LYS LYS ILE LYS VAL LEU GLY SER
SEQRES 5 A 53 GLY
HELIX 1 1 ARG A 9 GLU A 17 1 9
HELIX 2 2 ARG A 18 LEU A 20 5 3
HELIX 3 3 ALA A 30 THR A 42 1 13
HELIX 4 4 THR A 42 GLY A 51 1 10
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 - r 2 2 Bytes