HEADER CALCIUM-BINDING PROTEIN 15-APR-97 1TBO
TITLE NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, 30
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE C, GAMMA TYPE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYS2 DOMAIN;
COMPND 5 SYNONYM: RAT BRAIN PKC-G;
COMPND 6 EC: 2.7.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;
SOURCE 3 ORGANISM_COMMON: BLACK RAT;
SOURCE 4 ORGANISM_TAXID: 10117;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS CALCIUM-BINDING PROTEIN, PROTEIN KINASE C, PKC, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR R.X.XU,T.PAWELCZYK,T.XIA,S.C.BROWN
REVDAT 3 02-MAR-22 1TBO 1 REMARK LINK
REVDAT 2 24-FEB-09 1TBO 1 VERSN
REVDAT 1 29-APR-98 1TBO 0
JRNL AUTH R.X.XU,T.PAWELCZYK,T.H.XIA,S.C.BROWN
JRNL TITL NMR STRUCTURE OF A PROTEIN KINASE C-GAMMA PHORBOL-BINDING
JRNL TITL 2 DOMAIN AND STUDY OF PROTEIN-LIPID MICELLE INTERACTIONS.
JRNL REF BIOCHEMISTRY V. 36 10709 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9271501
JRNL DOI 10.1021/BI970833A
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.ZHANG,M.G.KAZANIETZ,P.M.BLUMBERG,J.H.HURLEY
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CYS2 ACTIVATOR-BINDING DOMAIN OF
REMARK 1 TITL 2 PROTEIN KINASE C DELTA IN COMPLEX WITH PHORBOL ESTER
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 81 917 1995
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.ICHIKAWA,H.HATANAKA,Y.TAKEUCHI,S.OHNO,F.INAGAKI
REMARK 1 TITL SOLUTION STRUCTURE OF CYSTEINE-RICH DOMAIN OF PROTEIN KINASE
REMARK 1 TITL 2 C ALPHA
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 117 566 1995
REMARK 1 REFN ISSN 0021-924X
REMARK 1 REFERENCE 3
REMARK 1 AUTH U.HOMMEL,M.ZURINI,M.LUYTEN
REMARK 1 TITL SOLUTION STRUCTURE OF A CYSTEINE RICH DOMAIN OF RAT PROTEIN
REMARK 1 TITL 2 KINASE C
REMARK 1 REF NAT.STRUCT.BIOL. V. 1 383 1994
REMARK 1 REFN ISSN 1072-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TBO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176599.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : 6.5
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 : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DG-SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 92
REMARK 465 PRO A 93
REMARK 465 GLY A 160
REMARK 465 ARG A 161
REMARK 465 LEU A 162
REMARK 465 GLN A 163
REMARK 465 LEU A 164
REMARK 465 GLU A 165
REMARK 465 ILE A 166
REMARK 465 ARG A 167
REMARK 465 ALA A 168
REMARK 465 PRO A 169
REMARK 465 THR A 170
REMARK 465 SER A 171
REMARK 465 ASP A 172
REMARK 465 GLU A 173
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 THR A 95 -41.11 -156.37
REMARK 500 1 ASN A 100 -136.16 -128.67
REMARK 500 1 HIS A 102 154.16 -44.81
REMARK 500 1 LYS A 103 47.95 -94.15
REMARK 500 1 SER A 110 -59.84 161.81
REMARK 500 1 LEU A 121 151.92 -43.54
REMARK 500 1 LEU A 125 -38.34 -138.39
REMARK 500 1 GLN A 128 -72.51 -138.26
REMARK 500 1 SER A 133 44.25 -83.85
REMARK 500 1 CYS A 134 -40.56 -150.11
REMARK 500 1 GLU A 136 81.76 76.13
REMARK 500 1 SER A 149 89.95 61.34
REMARK 500 1 ASP A 154 -169.95 -114.88
REMARK 500 2 PRO A 98 -159.13 -77.35
REMARK 500 2 ARG A 99 -140.63 -81.09
REMARK 500 2 LYS A 103 46.34 -90.56
REMARK 500 2 PHE A 104 148.55 -39.80
REMARK 500 2 LEU A 122 90.21 -68.72
REMARK 500 2 TYR A 123 -172.57 -53.17
REMARK 500 2 GLN A 128 -75.46 77.99
REMARK 500 2 SER A 133 38.52 -84.40
REMARK 500 2 CYS A 134 -38.45 -150.49
REMARK 500 2 GLU A 136 74.96 62.48
REMARK 500 2 SER A 149 93.94 64.68
REMARK 500 3 LYS A 103 43.02 -89.96
REMARK 500 3 SER A 110 -25.67 160.83
REMARK 500 3 LEU A 122 35.93 -86.57
REMARK 500 3 HIS A 127 107.59 -50.10
REMARK 500 3 GLN A 128 -87.52 63.77
REMARK 500 3 SER A 133 45.11 -84.51
REMARK 500 3 CYS A 134 -39.26 -146.84
REMARK 500 3 GLU A 136 73.03 70.66
REMARK 500 3 SER A 149 75.65 75.96
REMARK 500 3 HIS A 155 50.00 -165.15
REMARK 500 3 THR A 156 95.03 47.18
REMARK 500 4 THR A 95 43.86 -98.99
REMARK 500 4 ARG A 99 31.87 -142.24
REMARK 500 4 LYS A 103 49.07 -89.67
REMARK 500 4 PHE A 104 137.46 -39.57
REMARK 500 4 TYR A 123 177.08 -48.81
REMARK 500 4 HIS A 127 92.45 -50.07
REMARK 500 4 GLN A 128 -91.37 62.39
REMARK 500 4 SER A 133 45.70 -84.53
REMARK 500 4 CYS A 134 -39.06 -148.83
REMARK 500 4 GLU A 136 76.49 62.04
REMARK 500 4 PRO A 148 40.38 -80.54
REMARK 500 4 CYS A 151 62.39 -103.83
REMARK 500 5 ASP A 96 -175.40 -58.61
REMARK 500 5 ASP A 97 66.44 -158.63
REMARK 500 5 ARG A 99 134.35 -177.47
REMARK 500
REMARK 500 THIS ENTRY HAS 428 RAMACHANDRAN OUTLIERS.
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 1 ARG A 99 0.18 SIDE CHAIN
REMARK 500 1 ARG A 105 0.10 SIDE CHAIN
REMARK 500 1 ARG A 141 0.32 SIDE CHAIN
REMARK 500 1 ARG A 142 0.30 SIDE CHAIN
REMARK 500 1 ARG A 145 0.27 SIDE CHAIN
REMARK 500 1 ARG A 158 0.32 SIDE CHAIN
REMARK 500 1 ARG A 159 0.31 SIDE CHAIN
REMARK 500 2 ARG A 99 0.31 SIDE CHAIN
REMARK 500 2 ARG A 105 0.32 SIDE CHAIN
REMARK 500 2 ARG A 141 0.26 SIDE CHAIN
REMARK 500 2 ARG A 142 0.15 SIDE CHAIN
REMARK 500 2 ARG A 145 0.32 SIDE CHAIN
REMARK 500 2 ARG A 158 0.31 SIDE CHAIN
REMARK 500 2 ARG A 159 0.27 SIDE CHAIN
REMARK 500 3 ARG A 99 0.25 SIDE CHAIN
REMARK 500 3 ARG A 105 0.22 SIDE CHAIN
REMARK 500 3 ARG A 141 0.09 SIDE CHAIN
REMARK 500 3 ARG A 142 0.32 SIDE CHAIN
REMARK 500 3 ARG A 145 0.30 SIDE CHAIN
REMARK 500 3 ARG A 158 0.26 SIDE CHAIN
REMARK 500 3 ARG A 159 0.30 SIDE CHAIN
REMARK 500 4 ARG A 99 0.20 SIDE CHAIN
REMARK 500 4 ARG A 105 0.31 SIDE CHAIN
REMARK 500 4 ARG A 141 0.24 SIDE CHAIN
REMARK 500 4 ARG A 142 0.30 SIDE CHAIN
REMARK 500 4 ARG A 145 0.22 SIDE CHAIN
REMARK 500 4 ARG A 158 0.12 SIDE CHAIN
REMARK 500 4 ARG A 159 0.23 SIDE CHAIN
REMARK 500 5 ARG A 99 0.09 SIDE CHAIN
REMARK 500 5 ARG A 105 0.25 SIDE CHAIN
REMARK 500 5 ARG A 141 0.09 SIDE CHAIN
REMARK 500 5 ARG A 142 0.17 SIDE CHAIN
REMARK 500 5 ARG A 145 0.28 SIDE CHAIN
REMARK 500 5 ARG A 158 0.31 SIDE CHAIN
REMARK 500 5 ARG A 159 0.23 SIDE CHAIN
REMARK 500 6 ARG A 99 0.20 SIDE CHAIN
REMARK 500 6 ARG A 105 0.12 SIDE CHAIN
REMARK 500 6 ARG A 141 0.31 SIDE CHAIN
REMARK 500 6 ARG A 142 0.30 SIDE CHAIN
REMARK 500 6 ARG A 145 0.27 SIDE CHAIN
REMARK 500 6 ARG A 158 0.22 SIDE CHAIN
REMARK 500 6 ARG A 159 0.28 SIDE CHAIN
REMARK 500 7 ARG A 99 0.27 SIDE CHAIN
REMARK 500 7 ARG A 105 0.28 SIDE CHAIN
REMARK 500 7 ARG A 141 0.31 SIDE CHAIN
REMARK 500 7 ARG A 142 0.22 SIDE CHAIN
REMARK 500 7 ARG A 145 0.30 SIDE CHAIN
REMARK 500 7 ARG A 158 0.20 SIDE CHAIN
REMARK 500 7 ARG A 159 0.32 SIDE CHAIN
REMARK 500 8 ARG A 99 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 204 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 102 ND1
REMARK 620 2 CYS A 132 SG 123.1
REMARK 620 3 CYS A 135 SG 127.8 106.0
REMARK 620 4 CYS A 151 SG 90.3 89.0 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 115 SG
REMARK 620 2 CYS A 118 SG 90.4
REMARK 620 3 HIS A 140 ND1 97.5 87.4
REMARK 620 4 CYS A 143 SG 138.9 118.7 111.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TBN RELATED DB: PDB
DBREF 1TBO A 92 173 UNP P05697 KPCG_MOUSE 91 172
SEQRES 1 A 82 GLY PRO GLN THR ASP ASP PRO ARG ASN LYS HIS LYS PHE
SEQRES 2 A 82 ARG LEU HIS SER TYR SER SER PRO THR PHE CYS ASP HIS
SEQRES 3 A 82 CYS GLY SER LEU LEU TYR GLY LEU VAL HIS GLN GLY MET
SEQRES 4 A 82 LYS CYS SER CYS CYS GLU MET ASN VAL HIS ARG ARG CYS
SEQRES 5 A 82 VAL ARG SER VAL PRO SER LEU CYS GLY VAL ASP HIS THR
SEQRES 6 A 82 GLU ARG ARG GLY ARG LEU GLN LEU GLU ILE ARG ALA PRO
SEQRES 7 A 82 THR SER ASP GLU
HET ZN A 1 1
HET ZN A 2 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
SHEET 1 A 2 PHE A 104 LEU A 106 0
SHEET 2 A 2 MET A 130 CYS A 132 -1 N LYS A 131 O ARG A 105
LINK ZN ZN A 1 ND1 HIS A 102 1555 1555 1.78
LINK ZN ZN A 1 SG CYS A 132 1555 1555 2.47
LINK ZN ZN A 1 SG CYS A 135 1555 1555 2.11
LINK ZN ZN A 1 SG CYS A 151 1555 1555 2.74
LINK ZN ZN A 2 SG CYS A 115 1555 1555 2.11
LINK ZN ZN A 2 SG CYS A 118 1555 1555 2.41
LINK ZN ZN A 2 ND1 HIS A 140 1555 1555 1.96
LINK ZN ZN A 2 SG CYS A 143 1555 1555 2.42
SITE 1 AC1 4 HIS A 102 CYS A 132 CYS A 135 CYS A 151
SITE 1 AC2 4 CYS A 115 CYS A 118 HIS A 140 CYS A 143
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
(ATOM LINES ARE NOT SHOWN.)
END
