Header list of 1cmz.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNALING PROTEIN REGULATION 12-MAY-99 1CMZ
TITLE SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR
TITLE 2 OF G PROTEIN SIGNALING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RGS BOX;
COMPND 5 SYNONYM: GALPHA INTERACTING PROTEIN;
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_PLASMID: PGEX-2T
KEYWDS GAIP, RGS, REGULATOR OF G PROTEIN, SIGNALING PROTEIN REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.DE ALBA,L.DE VRIES,M.G.FARQUHAR,N.TJANDRA
REVDAT 4 16-FEB-22 1CMZ 1 REMARK
REVDAT 3 24-FEB-09 1CMZ 1 VERSN
REVDAT 2 01-APR-03 1CMZ 1 JRNL
REVDAT 1 10-NOV-99 1CMZ 0
JRNL AUTH E.DE ALBA,L.DE VRIES,M.G.FARQUHAR,N.TJANDRA
JRNL TITL SOLUTION STRUCTURE OF HUMAN GAIP (GALPHA INTERACTING
JRNL TITL 2 PROTEIN): A REGULATOR OF G PROTEIN SIGNALING.
JRNL REF J.MOL.BIOL. V. 291 927 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10452897
JRNL DOI 10.1006/JMBI.1999.2989
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.DE VRIES,M.MOUSLI,A.WURMSER,M.G.FARQUHAR
REMARK 1 TITL GAIP, A PROTEIN THAT SPECIFICALLY INTERACTS WITH THE
REMARK 1 TITL 2 TRIMERIC G PROTEIN G(ALPHAI3), IS A MEMBER OF A PROTEIN
REMARK 1 TITL 3 FAMILY WITH A HIGHLY CONSERVED CORE DOMAIN
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 92 11916 1995
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE CALCULATED USING
REMARK 3 THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS
REMARK 3 LETT. 229, 129-136, USING THE PROGRAM X-PLOR 3.1 (BRUNGER)
REMARK 3 MODIFIED TO INCORPORATE DIPOLAR COUPLING RESTRAINTS TJANDRA ET
REMARK 3 AL. (1997) NATURE STRUCT. BIOL. 4, 732-738.
REMARK 4
REMARK 4 1CMZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001056.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 7.2; 8.3
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : NULL; NULL
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCACONH; CBCANH; HBHACONH;
REMARK 210 HNCA; HCCH-TOCSY; C-CNOESY; N-
REMARK 210 CNOESY; H-HNOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, PIPP, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 167
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: TRIPLE-RESONANCE NMR SPECTROSCOPY USED ON 13C, 15N-LABELED
REMARK 210 GAIP
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 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 SER A 68
REMARK 465 PRO A 69
REMARK 465 GLY A 70
REMARK 465 ILE A 71
REMARK 465 SER A 72
REMARK 465 GLY A 73
REMARK 465 GLY A 74
REMARK 465 GLY A 75
REMARK 465 GLY A 76
REMARK 465 GLY A 77
REMARK 465 ILE A 78
REMARK 465 PRO A 207
REMARK 465 TRP A 208
REMARK 465 VAL A 209
REMARK 465 ASP A 210
REMARK 465 SER A 211
REMARK 465 SER A 212
REMARK 465 SER A 213
REMARK 465 SER A 214
REMARK 465 LEU A 215
REMARK 465 ILE A 216
REMARK 465 HIS A 217
REMARK 465 ARG A 218
REMARK 465 ASP A 219
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 O ARG A 140 H GLU A 144 1.50
REMARK 500 O GLU A 82 H SER A 86 1.55
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 PRO A 81 1.52 -53.33
REMARK 500 1 GLU A 111 7.67 -59.59
REMARK 500 1 ALA A 128 30.47 -82.62
REMARK 500 1 GLU A 129 -75.21 -140.72
REMARK 500 1 ALA A 130 21.75 46.03
REMARK 500 1 ASN A 131 -110.14 -72.91
REMARK 500 1 GLN A 132 -47.98 -170.54
REMARK 500 1 TYR A 146 -82.02 -132.44
REMARK 500 1 VAL A 147 -37.79 -37.66
REMARK 500 1 SER A 148 -86.80 -76.35
REMARK 500 1 LEU A 150 -35.92 -174.52
REMARK 500 1 SER A 151 163.87 178.81
REMARK 500 1 PRO A 152 -5.92 -58.02
REMARK 500 1 LYS A 153 36.16 -83.06
REMARK 500 1 SER A 156 87.95 -66.03
REMARK 500 1 ASP A 158 100.36 160.76
REMARK 500 1 SER A 159 -148.97 -173.48
REMARK 500 1 ALA A 174 42.59 -79.27
REMARK 500 1 HIS A 175 33.11 -171.76
REMARK 500 1 ASP A 178 -33.99 -35.37
REMARK 500 2 ALA A 128 30.78 -77.37
REMARK 500 2 GLU A 129 -67.97 -141.57
REMARK 500 2 ALA A 130 15.23 47.55
REMARK 500 2 ASN A 131 -144.48 -64.89
REMARK 500 2 GLN A 132 -17.20 -144.73
REMARK 500 2 TYR A 146 -79.92 -121.15
REMARK 500 2 VAL A 147 -31.58 -39.89
REMARK 500 2 LEU A 150 -37.00 -172.71
REMARK 500 2 PRO A 152 -0.89 -57.49
REMARK 500 2 LYS A 153 -102.27 -83.02
REMARK 500 2 GLU A 154 124.84 62.54
REMARK 500 2 ASP A 158 103.28 160.39
REMARK 500 2 SER A 159 -156.90 -168.21
REMARK 500 2 GLU A 171 66.00 34.59
REMARK 500 2 PRO A 172 -169.09 -65.94
REMARK 500 2 SER A 173 40.83 -174.97
REMARK 500 2 ALA A 174 -44.27 66.45
REMARK 500 2 HIS A 175 38.14 -79.40
REMARK 500 3 PRO A 81 -2.93 -52.41
REMARK 500 3 HIS A 96 30.08 -85.06
REMARK 500 3 ARG A 101 -15.65 -44.05
REMARK 500 3 GLU A 111 -1.80 -51.82
REMARK 500 3 SER A 113 52.73 -118.60
REMARK 500 3 LEU A 126 -19.80 -47.79
REMARK 500 3 ALA A 130 -27.04 71.95
REMARK 500 3 ASN A 131 -158.18 -57.63
REMARK 500 3 GLN A 132 -9.05 -148.97
REMARK 500 3 TYR A 146 31.32 -147.34
REMARK 500 3 VAL A 147 -46.05 -150.54
REMARK 500 3 SER A 148 -154.15 -59.13
REMARK 500
REMARK 500 THIS ENTRY HAS 420 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CMZ A 68 219 UNP P49795 RGS19_HUMAN 68 217
SEQADV 1CMZ SER A 68 UNP P49795 GLN 68 SEE REMARK 999
SEQADV 1CMZ PRO A 69 UNP P49795 PRO 69 SEE REMARK 999
SEQADV 1CMZ GLY A 70 UNP P49795 LEU 70 SEE REMARK 999
SEQADV 1CMZ ILE A 71 UNP P49795 PRO 71 SEE REMARK 999
SEQADV 1CMZ SER A 72 UNP P49795 SER 72 SEE REMARK 999
SEQADV 1CMZ GLY A 73 UNP P49795 CYS 73 SEE REMARK 999
SEQADV 1CMZ GLY A 74 UNP P49795 GLU 74 SEE REMARK 999
SEQADV 1CMZ GLY A 75 UNP P49795 VAL 75 SEE REMARK 999
SEQADV 1CMZ GLY A 76 UNP P49795 CYS 76 SEE REMARK 999
SEQADV 1CMZ GLY A 77 UNP P49795 ALA 77 SEE REMARK 999
SEQADV 1CMZ ILE A 78 UNP P49795 THR 78 SEE REMARK 999
SEQADV 1CMZ PRO A 207 UNP P49795 LEU 207 SEE REMARK 999
SEQADV 1CMZ TRP A 208 UNP P49795 GLN 208 SEE REMARK 999
SEQADV 1CMZ VAL A 209 UNP P49795 GLY 209 SEE REMARK 999
SEQADV 1CMZ ASP A 210 UNP P49795 PRO 210 SEE REMARK 999
SEQADV 1CMZ SER A 212 UNP P49795 GLN 212 SEE REMARK 999
SEQADV 1CMZ LEU A 215 UNP P49795 SER 215 SEE REMARK 999
SEQADV 1CMZ ILE A 216 UNP P49795 GLU 216 SEE REMARK 999
SEQADV 1CMZ HIS A 217 UNP P49795 ALA 217 SEE REMARK 999
SEQADV 1CMZ ARG A 218 UNP P49795 SEE REMARK 999
SEQADV 1CMZ ASP A 219 UNP P49795 SEE REMARK 999
SEQRES 1 A 152 SER PRO GLY ILE SER GLY GLY GLY GLY GLY ILE PRO SER
SEQRES 2 A 152 PRO GLU GLU VAL GLN SER TRP ALA GLN SER PHE ASP LYS
SEQRES 3 A 152 LEU MET HIS SER PRO ALA GLY ARG SER VAL PHE ARG ALA
SEQRES 4 A 152 PHE LEU ARG THR GLU TYR SER GLU GLU ASN MET LEU PHE
SEQRES 5 A 152 TRP LEU ALA CYS GLU GLU LEU LYS ALA GLU ALA ASN GLN
SEQRES 6 A 152 HIS VAL VAL ASP GLU LYS ALA ARG LEU ILE TYR GLU ASP
SEQRES 7 A 152 TYR VAL SER ILE LEU SER PRO LYS GLU VAL SER LEU ASP
SEQRES 8 A 152 SER ARG VAL ARG GLU GLY ILE ASN LYS LYS MET GLN GLU
SEQRES 9 A 152 PRO SER ALA HIS THR PHE ASP ASP ALA GLN LEU GLN ILE
SEQRES 10 A 152 TYR THR LEU MET HIS ARG ASP SER TYR PRO ARG PHE LEU
SEQRES 11 A 152 SER SER PRO THR TYR ARG ALA LEU LEU PRO TRP VAL ASP
SEQRES 12 A 152 SER SER SER SER LEU ILE HIS ARG ASP
HELIX 1 1 PRO A 81 TRP A 87 1 7
HELIX 2 2 ASP A 92 MET A 95 1 4
HELIX 3 3 PRO A 98 GLU A 111 1 14
HELIX 4 4 GLU A 115 ALA A 128 1 14
HELIX 5 5 HIS A 133 ASP A 145 1 13
HELIX 6 6 ARG A 160 LYS A 168 1 9
HELIX 7 7 ASP A 178 ASP A 191 1 14
HELIX 8 8 TYR A 193 SER A 198 1 6
HELIX 9 9 PRO A 200 ARG A 203 1 4
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 - b 16 2 Bytes