Header list of 1v3a.pdb file
Complete list - 2 20 Bytes
HEADER HYDROLASE 30-OCT-03 1V3A
TITLE STRUCTURE OF HUMAN PRL-3, THE PHOSPHATASE ASSOCIATED WITH CANCER
TITLE 2 METASTASIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE TYPE IVA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHATASE;
COMPND 5 EC: 3.1.3.48;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS HYDROLASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR Y.H.JEON,C.CHEONG
REVDAT 3 02-MAR-22 1V3A 1 REMARK
REVDAT 2 24-FEB-09 1V3A 1 VERSN
REVDAT 1 30-OCT-04 1V3A 0
JRNL AUTH K.A.KIM,J.S.SONG,J.JEE,M.R.SHEEN,C.LEE,T.G.LEE,S.RO,J.M.CHO,
JRNL AUTH 2 W.LEE,T.YAMAZAKI,Y.H.JEON,C.CHEONG
JRNL TITL STRUCTURE OF HUMAN PRL-3, THE PHOSPHATASE ASSOCIATED WITH
JRNL TITL 2 CANCER METASTASIS
JRNL REF FEBS LETT. V. 565 181 2004
JRNL REFN ISSN 0014-5793
JRNL PMID 15135076
JRNL DOI 10.1016/J.FEBSLET.2004.03.062
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000006151.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 RES C SSSEQI
REMARK 465 PRO A 163
REMARK 465 HIS A 164
REMARK 465 THR A 165
REMARK 465 HIS A 166
REMARK 465 LYS A 167
REMARK 465 THR A 168
REMARK 465 ARG A 169
REMARK 465 CYS A 170
REMARK 465 CYS A 171
REMARK 465 VAL A 172
REMARK 465 MET A 173
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 VAL A 12 CA - CB - CG1 ANGL. DEV. = 9.4 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 ALA A 2 -60.93 -151.72
REMARK 500 ARG A 3 2.83 -69.50
REMARK 500 MET A 17 -169.98 -175.17
REMARK 500 ASN A 24 166.01 64.09
REMARK 500 PRO A 25 -168.22 -71.88
REMARK 500 THR A 26 -146.15 -114.86
REMARK 500 ASN A 27 -78.47 52.31
REMARK 500 THR A 56 -72.14 -139.51
REMARK 500 ASP A 67 79.78 -110.44
REMARK 500 SER A 98 -165.92 52.57
REMARK 500 ALA A 111 55.09 36.46
REMARK 500 LEU A 114 -76.66 -63.83
REMARK 500 ARG A 137 104.00 100.92
REMARK 500 ARG A 138 -170.85 59.87
REMARK 500 ALA A 140 52.14 -146.07
REMARK 500 ILE A 141 16.91 -142.08
REMARK 500 SER A 143 -89.06 -73.63
REMARK 500 GLN A 156 12.05 87.39
REMARK 500 ARG A 157 -92.60 -121.25
REMARK 500 LEU A 158 47.45 -87.25
REMARK 500 ARG A 159 -76.80 -131.34
REMARK 500 LYS A 161 -42.59 -147.95
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 TYR A 14 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1V3A A 1 173 UNP O75365 TP4A3_HUMAN 1 173
SEQRES 1 A 173 MET ALA ARG MET ASN ARG PRO ALA PRO VAL GLU VAL SER
SEQRES 2 A 173 TYR LYS HIS MET ARG PHE LEU ILE THR HIS ASN PRO THR
SEQRES 3 A 173 ASN ALA THR LEU SER THR PHE ILE GLU ASP LEU LYS LYS
SEQRES 4 A 173 TYR GLY ALA THR THR VAL VAL ARG VAL CYS GLU VAL THR
SEQRES 5 A 173 TYR ASP LYS THR PRO LEU GLU LYS ASP GLY ILE THR VAL
SEQRES 6 A 173 VAL ASP TRP PRO PHE ASP ASP GLY ALA PRO PRO PRO GLY
SEQRES 7 A 173 LYS VAL VAL GLU ASP TRP LEU SER LEU VAL LYS ALA LYS
SEQRES 8 A 173 PHE CYS GLU ALA PRO GLY SER CYS VAL ALA VAL HIS CYS
SEQRES 9 A 173 VAL ALA GLY LEU GLY ARG ALA PRO VAL LEU VAL ALA LEU
SEQRES 10 A 173 ALA LEU ILE GLU SER GLY MET LYS TYR GLU ASP ALA ILE
SEQRES 11 A 173 GLN PHE ILE ARG GLN LYS ARG ARG GLY ALA ILE ASN SER
SEQRES 12 A 173 LYS GLN LEU THR TYR LEU GLU LYS TYR ARG PRO LYS GLN
SEQRES 13 A 173 ARG LEU ARG PHE LYS ASP PRO HIS THR HIS LYS THR ARG
SEQRES 14 A 173 CYS CYS VAL MET
HELIX 1 1 THR A 29 GLY A 41 1 13
HELIX 2 2 THR A 56 ASP A 61 1 6
HELIX 3 3 LYS A 79 GLU A 94 1 16
HELIX 4 4 PRO A 112 SER A 122 1 11
HELIX 5 5 LYS A 125 ARG A 134 1 10
HELIX 6 6 GLN A 135 ARG A 137 5 3
HELIX 7 7 ASN A 142 THR A 147 1 6
HELIX 8 8 TYR A 148 LYS A 151 5 4
SHEET 1 A 5 VAL A 10 SER A 13 0
SHEET 2 A 5 ARG A 18 ILE A 21 -1 O PHE A 19 N VAL A 12
SHEET 3 A 5 VAL A 100 HIS A 103 1 O VAL A 102 N LEU A 20
SHEET 4 A 5 THR A 44 ARG A 47 1 N THR A 44 O ALA A 101
SHEET 5 A 5 THR A 64 ASP A 67 1 O VAL A 66 N ARG A 47
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