HEADER PHOSPHORIC DIESTER HYDROLASE 13-JUN-94 2HSP
TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHOSPHOLIPASE CGAMMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE C-GAMMA (SH3 DOMAIN);
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.4.11;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GRB2
KEYWDS PHOSPHORIC DIESTER HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.KOHDA,H.HATANAKA,M.ODAKA,F.INAGAKI
REVDAT 4 29-NOV-17 2HSP 1 REMARK HELIX
REVDAT 3 24-FEB-09 2HSP 1 VERSN
REVDAT 2 01-APR-03 2HSP 1 JRNL
REVDAT 1 31-AUG-94 2HSP 0
SPRSDE 31-AUG-94 2HSP 1HSP
JRNL AUTH D.KOHDA,H.HATANAKA,M.ODAKA,V.MANDIYAN,A.ULLRICH,
JRNL AUTH 2 J.SCHLESSINGER,F.INAGAKI
JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHOSPHOLIPASE
JRNL TITL 2 C-GAMMA.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 72 953 1993
JRNL REFN ISSN 0092-8674
JRNL PMID 7681365
JRNL DOI 10.1016/0092-8674(93)90583-C
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.KOHDA,H.TERASAWA,S.ICHIKAWA,K.OGURA,H.HATANAKA,V.MANDIYAN,
REMARK 1 AUTH 2 A.ULLRICH,J.SCHLESSINGER,F.INAGAKI
REMARK 1 TITL SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE C-TERMINAL
REMARK 1 TITL 2 SH3 DOMAIN OF GRB2
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : NILGES (DSPACE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HSP 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_1000178226.
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
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 : 20
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 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: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 TRP A 42 CG TRP A 42 CD2 -0.108
REMARK 500 1 HIS A 69 CG HIS A 69 ND1 -0.101
REMARK 500 2 TRP A 42 CG TRP A 42 CD2 -0.109
REMARK 500 2 HIS A 69 CG HIS A 69 ND1 -0.098
REMARK 500 3 TRP A 42 CG TRP A 42 CD2 -0.108
REMARK 500 3 HIS A 69 CG HIS A 69 ND1 -0.100
REMARK 500 4 TRP A 42 CG TRP A 42 CD2 -0.114
REMARK 500 4 HIS A 69 CG HIS A 69 ND1 -0.099
REMARK 500 5 TRP A 42 CG TRP A 42 CD2 -0.116
REMARK 500 5 HIS A 69 CG HIS A 69 ND1 -0.102
REMARK 500 6 TRP A 42 CG TRP A 42 CD2 -0.114
REMARK 500 6 TRP A 53 CG TRP A 53 CD2 -0.107
REMARK 500 6 HIS A 69 CG HIS A 69 ND1 -0.102
REMARK 500 7 TRP A 42 CG TRP A 42 CD2 -0.116
REMARK 500 7 HIS A 69 CG HIS A 69 ND1 -0.100
REMARK 500 8 TRP A 42 CG TRP A 42 CD2 -0.114
REMARK 500 8 TRP A 53 CG TRP A 53 CD2 -0.103
REMARK 500 8 HIS A 69 CG HIS A 69 ND1 -0.102
REMARK 500 9 TRP A 42 CG TRP A 42 CD2 -0.116
REMARK 500 9 HIS A 69 CG HIS A 69 ND1 -0.101
REMARK 500 10 TRP A 42 CG TRP A 42 CD2 -0.117
REMARK 500 10 TRP A 53 CG TRP A 53 CD2 -0.104
REMARK 500 10 HIS A 69 CG HIS A 69 ND1 -0.102
REMARK 500 11 TRP A 42 CG TRP A 42 CD2 -0.115
REMARK 500 11 HIS A 69 CG HIS A 69 ND1 -0.103
REMARK 500 12 TRP A 42 CG TRP A 42 CD2 -0.109
REMARK 500 12 HIS A 69 CG HIS A 69 ND1 -0.104
REMARK 500 13 TRP A 42 CG TRP A 42 CD2 -0.119
REMARK 500 13 TRP A 53 CG TRP A 53 CD2 -0.103
REMARK 500 13 HIS A 69 CG HIS A 69 ND1 -0.101
REMARK 500 14 TRP A 42 CG TRP A 42 CD2 -0.110
REMARK 500 14 HIS A 69 CG HIS A 69 ND1 -0.100
REMARK 500 15 TRP A 42 CG TRP A 42 CD2 -0.112
REMARK 500 15 TRP A 53 CG TRP A 53 CD2 -0.105
REMARK 500 15 HIS A 69 CG HIS A 69 ND1 -0.101
REMARK 500 16 TRP A 42 CG TRP A 42 CD2 -0.111
REMARK 500 16 HIS A 69 CG HIS A 69 ND1 -0.103
REMARK 500 17 TRP A 42 CG TRP A 42 CD2 -0.120
REMARK 500 17 HIS A 69 CG HIS A 69 ND1 -0.102
REMARK 500 18 TRP A 42 CG TRP A 42 CD2 -0.111
REMARK 500 18 TRP A 53 CG TRP A 53 CD2 -0.103
REMARK 500 18 HIS A 69 CG HIS A 69 ND1 -0.103
REMARK 500 19 TRP A 42 CG TRP A 42 CD2 -0.116
REMARK 500 19 HIS A 69 CG HIS A 69 ND1 -0.102
REMARK 500 20 TRP A 42 CG TRP A 42 CD2 -0.109
REMARK 500 20 TRP A 53 CG TRP A 53 CD2 -0.105
REMARK 500 20 HIS A 69 CG HIS A 69 ND1 -0.100
REMARK 500
REMARK 500 REMARK: NULL
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 1 TRP A 41 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 TRP A 41 NE1 - CE2 - CZ2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 1 TRP A 41 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TRP A 42 CG - CD1 - NE1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 1 TRP A 42 CD1 - NE1 - CE2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 1 TRP A 42 NE1 - CE2 - CZ2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 1 TRP A 42 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 TRP A 53 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TRP A 53 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 TRP A 53 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 1 TRP A 53 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 41 CD1 - NE1 - CE2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 2 TRP A 41 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 2 TRP A 41 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP A 42 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 2 TRP A 42 CD1 - NE1 - CE2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 2 TRP A 42 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 2 TRP A 53 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP A 53 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 2 TRP A 53 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 TRP A 53 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 41 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 3 TRP A 41 NE1 - CE2 - CZ2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 3 TRP A 41 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 TRP A 42 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 3 TRP A 42 CD1 - NE1 - CE2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 3 TRP A 53 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 3 TRP A 53 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 3 TRP A 53 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 3 TRP A 53 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 4 TRP A 41 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 TRP A 41 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 4 TRP A 41 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 4 TRP A 41 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 TRP A 42 CG - CD1 - NE1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 4 TRP A 42 CD1 - NE1 - CE2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 4 TRP A 42 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 4 TRP A 42 NE1 - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 TRP A 53 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 4 TRP A 53 CD1 - NE1 - CE2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 4 TRP A 53 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 4 TRP A 53 NE1 - CE2 - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 5 TRP A 41 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 TRP A 41 CD1 - NE1 - CE2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 5 TRP A 41 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 5 TRP A 41 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 5 TRP A 42 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 5 TRP A 42 CD1 - NE1 - CE2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 5 TRP A 42 NE1 - CE2 - CZ2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 5 TRP A 42 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 219 ANGLE DEVIATIONS.
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 PHE A 5 -163.62 -58.46
REMARK 500 1 LYS A 6 156.61 55.66
REMARK 500 1 ALA A 11 120.95 -38.60
REMARK 500 1 ALA A 17 -50.78 -125.34
REMARK 500 1 GLN A 18 -38.74 76.30
REMARK 500 1 ARG A 19 73.99 -175.60
REMARK 500 1 ASP A 21 -7.89 112.46
REMARK 500 1 SER A 28 -5.97 110.29
REMARK 500 1 ASN A 33 87.73 46.90
REMARK 500 1 GLU A 35 107.35 -174.64
REMARK 500 1 GLU A 38 81.73 -32.12
REMARK 500 1 GLN A 51 68.69 71.90
REMARK 500 1 LEU A 52 -136.37 -97.73
REMARK 500 1 GLU A 61 82.08 -56.62
REMARK 500 1 MET A 62 100.26 38.52
REMARK 500 1 PRO A 65 -140.92 -56.65
REMARK 500 1 GLU A 66 166.94 55.56
REMARK 500 1 ARG A 70 -132.55 -68.11
REMARK 500 2 PRO A 3 21.70 -68.47
REMARK 500 2 ALA A 11 117.30 -35.26
REMARK 500 2 LYS A 16 64.30 -150.11
REMARK 500 2 GLN A 18 -28.54 68.61
REMARK 500 2 ARG A 19 79.92 -173.80
REMARK 500 2 GLU A 20 4.84 -150.50
REMARK 500 2 ASP A 21 -4.11 106.90
REMARK 500 2 LYS A 27 93.02 -68.20
REMARK 500 2 SER A 28 -18.05 149.95
REMARK 500 2 ILE A 30 63.99 -111.20
REMARK 500 2 ASN A 33 97.62 56.59
REMARK 500 2 GLU A 35 128.07 173.48
REMARK 500 2 LYS A 36 172.89 -51.20
REMARK 500 2 GLU A 38 14.31 42.62
REMARK 500 2 TYR A 46 72.51 -152.36
REMARK 500 2 LYS A 49 169.19 -45.62
REMARK 500 2 GLN A 51 73.06 64.19
REMARK 500 2 LEU A 52 -138.05 -96.93
REMARK 500 2 GLU A 61 83.19 -45.51
REMARK 500 2 MET A 62 101.87 43.71
REMARK 500 2 VAL A 63 111.76 33.99
REMARK 500 2 ASN A 64 96.01 -29.42
REMARK 500 2 PRO A 65 32.01 -82.65
REMARK 500 2 GLU A 66 117.59 -38.86
REMARK 500 2 ILE A 68 -142.84 -114.73
REMARK 500 2 HIS A 69 -153.65 -167.51
REMARK 500 2 ARG A 70 171.60 -43.79
REMARK 500 3 VAL A 9 -152.14 -139.97
REMARK 500 3 LYS A 10 78.00 -167.23
REMARK 500 3 ALA A 11 113.29 -29.87
REMARK 500 3 LYS A 16 59.39 -149.52
REMARK 500 3 GLN A 18 -33.03 71.34
REMARK 500
REMARK 500 THIS ENTRY HAS 458 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 19 0.17 SIDE CHAIN
REMARK 500 1 ARG A 43 0.20 SIDE CHAIN
REMARK 500 1 ARG A 70 0.28 SIDE CHAIN
REMARK 500 2 ARG A 19 0.32 SIDE CHAIN
REMARK 500 2 ARG A 43 0.24 SIDE CHAIN
REMARK 500 2 TYR A 46 0.06 SIDE CHAIN
REMARK 500 2 ARG A 70 0.29 SIDE CHAIN
REMARK 500 3 ARG A 19 0.16 SIDE CHAIN
REMARK 500 3 ARG A 43 0.21 SIDE CHAIN
REMARK 500 3 TYR A 46 0.06 SIDE CHAIN
REMARK 500 3 ARG A 70 0.29 SIDE CHAIN
REMARK 500 4 ARG A 19 0.27 SIDE CHAIN
REMARK 500 4 ARG A 43 0.29 SIDE CHAIN
REMARK 500 4 TYR A 46 0.06 SIDE CHAIN
REMARK 500 4 ARG A 70 0.32 SIDE CHAIN
REMARK 500 5 ARG A 19 0.31 SIDE CHAIN
REMARK 500 5 ARG A 43 0.28 SIDE CHAIN
REMARK 500 5 TYR A 46 0.07 SIDE CHAIN
REMARK 500 5 ARG A 70 0.27 SIDE CHAIN
REMARK 500 6 ARG A 19 0.21 SIDE CHAIN
REMARK 500 6 ARG A 43 0.26 SIDE CHAIN
REMARK 500 6 ARG A 70 0.30 SIDE CHAIN
REMARK 500 7 ARG A 19 0.27 SIDE CHAIN
REMARK 500 8 ARG A 19 0.30 SIDE CHAIN
REMARK 500 8 ARG A 43 0.25 SIDE CHAIN
REMARK 500 8 ARG A 70 0.20 SIDE CHAIN
REMARK 500 9 ARG A 19 0.27 SIDE CHAIN
REMARK 500 9 ARG A 43 0.13 SIDE CHAIN
REMARK 500 9 ARG A 70 0.14 SIDE CHAIN
REMARK 500 10 ARG A 19 0.23 SIDE CHAIN
REMARK 500 10 ARG A 70 0.30 SIDE CHAIN
REMARK 500 11 ARG A 43 0.09 SIDE CHAIN
REMARK 500 11 ARG A 70 0.28 SIDE CHAIN
REMARK 500 12 ARG A 19 0.12 SIDE CHAIN
REMARK 500 12 TYR A 46 0.06 SIDE CHAIN
REMARK 500 12 ARG A 70 0.26 SIDE CHAIN
REMARK 500 13 ARG A 19 0.32 SIDE CHAIN
REMARK 500 13 ARG A 43 0.12 SIDE CHAIN
REMARK 500 13 ARG A 70 0.17 SIDE CHAIN
REMARK 500 14 ARG A 19 0.32 SIDE CHAIN
REMARK 500 14 ARG A 43 0.23 SIDE CHAIN
REMARK 500 14 ARG A 70 0.20 SIDE CHAIN
REMARK 500 15 ARG A 19 0.32 SIDE CHAIN
REMARK 500 15 ARG A 43 0.20 SIDE CHAIN
REMARK 500 15 TYR A 46 0.06 SIDE CHAIN
REMARK 500 15 ARG A 70 0.17 SIDE CHAIN
REMARK 500 16 ARG A 43 0.12 SIDE CHAIN
REMARK 500 16 TYR A 46 0.06 SIDE CHAIN
REMARK 500 16 ARG A 70 0.27 SIDE CHAIN
REMARK 500 17 ARG A 43 0.12 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 62 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HSQ RELATED DB: PDB
DBREF 2HSP A 3 64 UNP P19174 PLCG1_HUMAN 790 851
SEQRES 1 A 71 GLY SER PRO THR PHE LYS CYS ALA VAL LYS ALA LEU PHE
SEQRES 2 A 71 ASP TYR LYS ALA GLN ARG GLU ASP GLU LEU THR PHE ILE
SEQRES 3 A 71 LYS SER ALA ILE ILE GLN ASN VAL GLU LYS GLN GLU GLY
SEQRES 4 A 71 GLY TRP TRP ARG GLY ASP TYR GLY GLY LYS LYS GLN LEU
SEQRES 5 A 71 TRP PHE PRO SER ASN TYR VAL GLU GLU MET VAL ASN PRO
SEQRES 6 A 71 GLU GLY ILE HIS ARG ASP
HELIX 1 GH SER A 56 TYR A 58 53/10 HELIX 3
SHEET 1 B1 3 ALA A 29 GLN A 32 0
SHEET 2 B1 3 CYS A 7 ALA A 11 -1 O VAL A 9 N ILE A 31
SHEET 3 B1 3 VAL A 59 MET A 62 -1 O GLU A 60 N LYS A 10
SHEET 1 B2 2 PHE A 13 LYS A 16 0
SHEET 2 B2 2 THR A 24 ILE A 26 -1 O PHE A 25 N TYR A 15
SHEET 1 B3A 3 VAL A 34 LYS A 36 0
SHEET 2 B3A 3 TRP A 41 TYR A 46 -1 O ARG A 43 N GLU A 35
SHEET 3 B3A 3 LYS A 49 LYS A 50 -1 O LYS A 49 N TYR A 46
SHEET 1 B3B 3 VAL A 34 LYS A 36 0
SHEET 2 B3B 3 TRP A 41 TYR A 46 -1 O ARG A 43 N GLU A 35
SHEET 3 B3B 3 LEU A 52 PRO A 55 -1 O PHE A 54 N TRP A 42
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
