Header list of 1m3g.pdb file
Complete list - 27 20 Bytes
HEADER HYDROLASE 27-JUN-02 1M3G
TITLE SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1:
TITLE 2 INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY PROTEIN PHOSPHATASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 170-314;
COMPND 5 SYNONYM: MAPK PHOSPHATASE PAC-1, DUAL SPECIFICITY PROTEIN PHOSPHATASE
COMPND 6 PAC-1;
COMPND 7 EC: 3.1.3.48, 3.1.3.16;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: 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: PET15B
KEYWDS CATALYTIC DOMAIN, MAPK PHOSPHATASE, PAC-1, HYDROLASE
EXPDTA SOLUTION NMR
AUTHOR A.FAROOQ,M.-M.ZHOU
REVDAT 4 27-OCT-21 1M3G 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1M3G 1 VERSN
REVDAT 2 03-FEB-04 1M3G 1 SPRSDE
REVDAT 1 27-JUN-03 1M3G 0
SPRSDE 03-FEB-04 1M3G 1IKZ
JRNL AUTH A.FAROOQ,O.PLOTNIKOVA,G.CHATURVEDI,S.YAN,L.ZENG,Q.ZHANG,
JRNL AUTH 2 M.-M.ZHOU
JRNL TITL SOLUTION STRUCTURE OF THE MAPK PHOSPHATASE PAC-1 CATALYTIC
JRNL TITL 2 DOMAIN INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION
JRNL TITL 3 OF MKP
JRNL REF STRUCTURE V. 11 155 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12575935
JRNL DOI 10.1016/S0969-2126(02)00943-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR/ARIA, XPLOR/ARIA
REMARK 3 AUTHORS : BRUNGER (X-PLOR), NILGES, O'DONOGHUE (ARIA)
REMARK 3 (XPLOR/ARIA), BRUNGER (X-PLOR)/ NILGES, O'DONOGHUE
REMARK 3 (ARIA) (XPLOR/ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M3G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016549.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM CATALYTIC DOMAIN MAPK
REMARK 210 PHOSPHATASE U-15N,13C; 5MM
REMARK 210 PHOSPHATE BUFFER PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_ 15N
REMARK 210 -SEPARATED_NOESY; HNHA
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 : XWINNMR, NMRPIPE, NMRVIEW
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 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: 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 LEU A 177 174.85 54.38
REMARK 500 SER A 184 -63.09 -172.23
REMARK 500 CYS A 185 -151.57 -110.80
REMARK 500 THR A 200 -61.68 -124.02
REMARK 500 ASN A 204 90.86 -68.56
REMARK 500 VAL A 205 78.50 -69.85
REMARK 500 SER A 206 -77.30 -125.34
REMARK 500 ALA A 207 -143.58 -170.88
REMARK 500 CYS A 209 -175.58 50.29
REMARK 500 PRO A 210 84.99 -57.92
REMARK 500 HIS A 212 74.40 -116.49
REMARK 500 GLU A 214 59.35 -175.10
REMARK 500 PHE A 217 -79.06 -168.56
REMARK 500 GLN A 228 -87.89 55.03
REMARK 500 MET A 229 27.92 -149.21
REMARK 500 VAL A 230 101.37 53.71
REMARK 500 SER A 249 -49.68 -149.99
REMARK 500 GLN A 258 21.43 -155.02
REMARK 500 ALA A 259 29.85 -173.05
REMARK 500 ARG A 279 165.93 55.68
REMARK 500 LYS A 288 -171.28 -171.11
REMARK 500 ARG A 290 -154.53 -64.12
REMARK 500 ARG A 291 95.97 54.58
REMARK 500 SER A 295 173.83 54.29
REMARK 500 PRO A 296 99.80 -63.88
REMARK 500 ASN A 297 39.27 -162.38
REMARK 500 LEU A 304 -69.20 -157.83
REMARK 500 LEU A 312 -74.37 -88.90
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M3G A 170 314 UNP Q05923 DUS2_HUMAN 170 314
SEQADV 1M3G SER A 257 UNP Q05923 CYS 257 ENGINEERED MUTATION
SEQRES 1 A 145 GLN GLY GLY PRO VAL GLU ILE LEU PRO TYR LEU PHE LEU
SEQRES 2 A 145 GLY SER CYS SER HIS SER SER ASP LEU GLN GLY LEU GLN
SEQRES 3 A 145 ALA CYS GLY ILE THR ALA VAL LEU ASN VAL SER ALA SER
SEQRES 4 A 145 CYS PRO ASN HIS PHE GLU GLY LEU PHE ARG TYR LYS SER
SEQRES 5 A 145 ILE PRO VAL GLU ASP ASN GLN MET VAL GLU ILE SER ALA
SEQRES 6 A 145 TRP PHE GLN GLU ALA ILE GLY PHE ILE ASP TRP VAL LYS
SEQRES 7 A 145 ASN SER GLY GLY ARG VAL LEU VAL HIS SER GLN ALA GLY
SEQRES 8 A 145 ILE SER ARG SER ALA THR ILE CYS LEU ALA TYR LEU MET
SEQRES 9 A 145 GLN SER ARG ARG VAL ARG LEU ASP GLU ALA PHE ASP PHE
SEQRES 10 A 145 VAL LYS GLN ARG ARG GLY VAL ILE SER PRO ASN PHE SER
SEQRES 11 A 145 PHE MET GLY GLN LEU LEU GLN PHE GLU THR GLN VAL LEU
SEQRES 12 A 145 CYS HIS
HELIX 1 1 HIS A 187 GLY A 198 1 12
HELIX 2 2 TRP A 235 SER A 249 1 15
HELIX 3 3 SER A 262 SER A 275 1 14
HELIX 4 4 VAL A 278 LYS A 288 1 11
HELIX 5 5 LEU A 304 LEU A 312 1 9
SHEET 1 A 6 VAL A 174 ILE A 176 0
SHEET 2 A 6 LEU A 180 LEU A 182 -1 O LEU A 182 N VAL A 174
SHEET 3 A 6 VAL A 253 VAL A 255 1 O VAL A 253 N PHE A 181
SHEET 4 A 6 ALA A 201 ASN A 204 1 N LEU A 203 O LEU A 254
SHEET 5 A 6 ARG A 218 SER A 221 1 O ARG A 218 N VAL A 202
SHEET 6 A 6 ASN A 211 PHE A 213 -1 N PHE A 213 O TYR A 219
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 - 27 20 Bytes