Header list of 1r6h.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 15-OCT-03 1R6H
TITLE SOLUTION STRUCTURE OF HUMAN PRL-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE TYPE IVA, MEMBER 3 ISOFORM 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PRL-3 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS DUAL SPECIFICITY PHOSPHATASE FOLD, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.KOZLOV,K.GEHRING,I.EKIEL
REVDAT 4 02-MAR-22 1R6H 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1R6H 1 VERSN
REVDAT 2 23-MAR-04 1R6H 1 JRNL
REVDAT 1 13-JAN-04 1R6H 0
JRNL AUTH G.KOZLOV,J.CHENG,E.ZIOMEK,D.BANVILLE,K.GEHRING,I.EKIEL
JRNL TITL STRUCTURAL INSIGHTS INTO MOLECULAR FUNCTION OF THE
JRNL TITL 2 METASTASIS-ASSOCIATED PHOSPHATASE PRL-3.
JRNL REF J.BIOL.CHEM. V. 279 11882 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14704153
JRNL DOI 10.1074/JBC.M312905200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2320 RESTRAINTS, 1969 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 275 DIHEDRAL ANGLE RESTRAINTS, 76 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1R6H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020495.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.1M NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM PRL-3 U-15N, 50MM PHOSPHATE
REMARK 210 BUFFER, 0.1M NACL, 10MM DTT,
REMARK 210 0.1MM NAN3, 90% H2O, 10% D2O;
REMARK 210 3MM PRL-3 U-15N,13C, 50MM
REMARK 210 PHOSPHATE BUFFER, 0.1M NACL,
REMARK 210 10MM DTT, 0.1MM NAN3, 90% H2O,
REMARK 210 10% D2O; 3MM PRL-3, 50MM
REMARK 210 PHOSPHATE BUFFER, 0.1M NACL,
REMARK 210 10MM DTT, 0.1MM NAN3, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 3D_13C-SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.31, ARIA 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: THE STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 -RESONANCE NMR SPECTROSCOPY
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: 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
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 HIS A 3 35.86 -142.26
REMARK 500 1 MET A 7 157.42 60.74
REMARK 500 1 LYS A 18 -88.76 65.93
REMARK 500 1 PRO A 78 108.13 -59.98
REMARK 500 1 SER A 101 -164.45 -101.08
REMARK 500 1 MET A 127 76.92 -62.90
REMARK 500 1 ASN A 145 -78.09 -114.03
REMARK 500 1 SER A 146 -61.23 -101.32
REMARK 500 1 ARG A 162 40.45 -96.23
REMARK 500 1 THR A 171 -52.28 -143.17
REMARK 500 2 LYS A 18 -86.62 55.06
REMARK 500 2 PRO A 78 97.10 -40.16
REMARK 500 2 PRO A 80 151.72 -47.67
REMARK 500 2 SER A 101 -165.10 -101.21
REMARK 500 2 MET A 127 78.67 -62.53
REMARK 500 2 ASN A 145 -77.32 -113.89
REMARK 500 2 SER A 146 -60.68 -100.67
REMARK 500 2 PHE A 163 -56.01 -120.88
REMARK 500 2 LYS A 164 110.98 59.29
REMARK 500 3 ASN A 8 -73.08 -82.00
REMARK 500 3 PRO A 10 96.58 -52.49
REMARK 500 3 LYS A 18 -97.81 51.08
REMARK 500 3 PRO A 78 99.39 -43.32
REMARK 500 3 PRO A 80 153.97 -47.46
REMARK 500 3 SER A 101 -163.85 -101.23
REMARK 500 3 MET A 127 71.18 -63.20
REMARK 500 3 ASN A 145 -76.87 -113.25
REMARK 500 3 SER A 146 -61.01 -99.60
REMARK 500 3 PHE A 163 -66.33 -108.90
REMARK 500 3 HIS A 167 37.93 -177.60
REMARK 500 3 LYS A 170 -47.38 -148.46
REMARK 500 3 THR A 171 -62.08 -120.39
REMARK 500 4 ARG A 6 -65.92 -132.20
REMARK 500 4 ASN A 8 31.86 -163.75
REMARK 500 4 ARG A 9 112.34 -175.89
REMARK 500 4 PRO A 10 109.85 -50.30
REMARK 500 4 LYS A 18 -78.47 44.71
REMARK 500 4 ASP A 74 -175.62 178.85
REMARK 500 4 PRO A 78 101.00 -47.02
REMARK 500 4 SER A 101 -161.80 -101.05
REMARK 500 4 MET A 127 72.25 -63.55
REMARK 500 4 ASN A 145 -76.72 -113.13
REMARK 500 4 SER A 146 -60.71 -99.75
REMARK 500 5 MET A 4 -60.93 -150.07
REMARK 500 5 PRO A 10 90.94 -69.16
REMARK 500 5 LYS A 18 -90.73 64.59
REMARK 500 5 PRO A 78 101.89 -49.71
REMARK 500 5 MET A 127 78.39 -63.42
REMARK 500 5 ASN A 145 -77.38 -113.66
REMARK 500 5 SER A 146 -60.80 -100.49
REMARK 500
REMARK 500 THIS ENTRY HAS 208 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1R6H A 4 172 UNP O75365 TP4A3_HUMAN 1 169
SEQADV 1R6H GLY A 1 UNP O75365 CLONING ARTIFACT
SEQADV 1R6H SER A 2 UNP O75365 CLONING ARTIFACT
SEQADV 1R6H HIS A 3 UNP O75365 CLONING ARTIFACT
SEQRES 1 A 172 GLY SER HIS MET ALA ARG MET ASN ARG PRO ALA PRO VAL
SEQRES 2 A 172 GLU VAL SER TYR LYS HIS MET ARG PHE LEU ILE THR HIS
SEQRES 3 A 172 ASN PRO THR ASN ALA THR LEU SER THR PHE ILE GLU ASP
SEQRES 4 A 172 LEU LYS LYS TYR GLY ALA THR THR VAL VAL ARG VAL CYS
SEQRES 5 A 172 GLU VAL THR TYR ASP LYS THR PRO LEU GLU LYS ASP GLY
SEQRES 6 A 172 ILE THR VAL VAL ASP TRP PRO PHE ASP ASP GLY ALA PRO
SEQRES 7 A 172 PRO PRO GLY LYS VAL VAL GLU ASP TRP LEU SER LEU VAL
SEQRES 8 A 172 LYS ALA LYS PHE CYS GLU ALA PRO GLY SER CYS VAL ALA
SEQRES 9 A 172 VAL HIS CYS VAL ALA GLY LEU GLY ARG ALA PRO VAL LEU
SEQRES 10 A 172 VAL ALA LEU ALA LEU ILE GLU SER GLY MET LYS TYR GLU
SEQRES 11 A 172 ASP ALA ILE GLN PHE ILE ARG GLN LYS ARG ARG GLY ALA
SEQRES 12 A 172 ILE ASN SER LYS GLN LEU THR TYR LEU GLU LYS TYR ARG
SEQRES 13 A 172 PRO LYS GLN ARG LEU ARG PHE LYS ASP PRO HIS THR HIS
SEQRES 14 A 172 LYS THR ARG
HELIX 1 1 THR A 32 GLY A 44 1 13
HELIX 2 2 ASP A 57 GLY A 65 1 9
HELIX 3 3 GLY A 81 ALA A 98 1 18
HELIX 4 4 ARG A 113 ILE A 123 1 11
HELIX 5 5 GLU A 124 GLY A 126 5 3
HELIX 6 6 MET A 127 LYS A 139 1 13
HELIX 7 7 SER A 146 ARG A 156 1 11
SHEET 1 A 5 VAL A 13 TYR A 17 0
SHEET 2 A 5 MET A 20 THR A 25 -1 O ILE A 24 N VAL A 13
SHEET 3 A 5 CYS A 102 HIS A 106 1 O VAL A 105 N THR A 25
SHEET 4 A 5 VAL A 48 VAL A 51 1 N VAL A 49 O ALA A 104
SHEET 5 A 5 VAL A 68 TRP A 71 1 O VAL A 69 N VAL A 48
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