Header list of 2btt.pdb file
Complete list - n 15 2 Bytes
HEADER CONTRACTILE PROTEIN 06-JUN-05 2BTT
TITLE NMR STRUCTURE OF MYO3-SH3 DOMAIN FROM MYOSIN-TYPEI FROM S. CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-3 ISOFORM;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 1122-1190;
COMPND 5 SYNONYM: MYO3-SH3 DOMAIN, MYO3-SH3 ISOFORM;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SH3 DOMAIN, MYOSIN-TYPE I, MUSCLE PROTEIN, CONTRACTILE PROTEIN,
KEYWDS 2 ACTIN-BINDING, ATP-BINDING, MOTOR PROTEIN, MYOSIN, NUCLEOTIDE-
KEYWDS 3 BINDING, PHOSPHORYLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.MUSI,B.BIRDSALL,A.PASTORE
REVDAT 5 15-JAN-20 2BTT 1 REMARK
REVDAT 4 17-JAN-18 2BTT 1 JRNL
REVDAT 3 24-FEB-09 2BTT 1 VERSN
REVDAT 2 20-DEC-06 2BTT 1 JRNL
REVDAT 1 12-APR-06 2BTT 0
JRNL AUTH V.MUSI,B.BIRDSALL,G.FERNANDEZ-BALLESTER,R.GUERRINI,
JRNL AUTH 2 S.SALVATORI,L.SERRANO,A.PASTORE
JRNL TITL NEW APPROACHES TO HIGH-THROUGHPUT STRUCTURE CHARACTERIZATION
JRNL TITL 2 OF SH3 COMPLEXES: THE EXAMPLE OF MYOSIN-3 AND MYOSIN-5 SH3
JRNL TITL 3 DOMAINS FROM S. CEREVISIAE.
JRNL REF PROTEIN SCI. V. 15 795 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16600966
JRNL DOI 10.1110/PS.051785506
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : LINGE,HABECK,RIEPING,NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BTT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1290024122.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-15N-NOESY-HSQC; 1H-15N- TOCSY
REMARK 210 -HSQC; HNHA; HNHB; CBCACONH;
REMARK 210 CBCANH; HNCO; HCCH- TOCSY; 2D-
REMARK 210 NOESY; 2D COSY; 2D-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, SPARKY
REMARK 210 METHOD USED : ARIA 1.2
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED MYO3_SH3.
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 OD2 ASP A 1123 HZ2 LYS A 1163 1.60
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 SER A1137 -166.11 50.28
REMARK 500 1 SER A1138 -62.36 70.88
REMARK 500 1 LYS A1145 107.72 -55.29
REMARK 500 1 PRO A1156 6.14 -66.91
REMARK 500 1 THR A1187 108.77 -49.53
REMARK 500 2 SER A1135 42.98 -78.76
REMARK 500 2 LYS A1145 109.05 -50.42
REMARK 500 2 PRO A1156 3.01 -64.39
REMARK 500 2 LEU A1164 150.26 -49.35
REMARK 500 2 LYS A1182 84.59 -69.30
REMARK 500 3 SER A1138 53.79 -151.85
REMARK 500 3 LYS A1145 104.31 -48.75
REMARK 500 3 PRO A1156 3.20 -63.93
REMARK 500 3 LYS A1182 83.83 -63.86
REMARK 500 3 ASP A1183 -70.14 -126.71
REMARK 500 3 THR A1187 122.54 78.37
REMARK 500 4 SER A1138 -82.55 70.90
REMARK 500 4 LYS A1145 100.60 -57.76
REMARK 500 4 LYS A1182 83.84 -65.77
REMARK 500 4 ASP A1183 -68.01 -141.21
REMARK 500 4 THR A1187 -44.21 75.64
REMARK 500 5 SER A1137 -168.04 -72.24
REMARK 500 5 SER A1138 -74.78 -49.94
REMARK 500 5 LYS A1145 106.19 -51.90
REMARK 500 5 PRO A1156 4.95 -66.55
REMARK 500 5 THR A1184 39.42 -87.65
REMARK 500 5 ARG A1185 -65.09 -149.51
REMARK 500 6 LYS A1145 107.46 -52.67
REMARK 500 6 PRO A1156 6.71 -65.82
REMARK 500 6 LYS A1182 84.33 -60.10
REMARK 500 6 ASN A1186 -52.06 -120.12
REMARK 500 7 SER A1138 -70.22 67.84
REMARK 500 7 SER A1139 30.37 -81.30
REMARK 500 7 LYS A1182 83.00 -67.26
REMARK 500 8 SER A1138 38.19 -142.93
REMARK 500 8 LYS A1145 104.74 -59.35
REMARK 500 8 PRO A1156 5.14 -66.92
REMARK 500 8 THR A1184 102.35 -48.45
REMARK 500 8 ASN A1186 -55.51 -123.30
REMARK 500 8 THR A1187 -68.93 -143.22
REMARK 500 9 PRO A1133 76.32 -69.63
REMARK 500 9 SER A1135 89.78 -54.13
REMARK 500 9 PRO A1156 1.16 -64.12
REMARK 500 9 LYS A1169 130.49 -171.50
REMARK 500 9 ASP A1183 -81.36 -88.39
REMARK 500 9 ARG A1185 -33.34 178.15
REMARK 500 10 PRO A1133 95.58 -69.22
REMARK 500 10 SER A1135 21.13 -164.35
REMARK 500 10 SER A1138 49.60 -152.89
REMARK 500 10 PRO A1142 109.92 -59.23
REMARK 500
REMARK 500 THIS ENTRY HAS 102 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RUW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SH3 DOMAIN FROM S . CEREVISIAE MYO3
REMARK 900 RELATED ID: 6197 RELATED DB: BMRB
DBREF 2BTT A 1122 1190 UNP P36006 MYO3_YEAST 1122 1190
SEQRES 1 A 69 LYS ASP PRO LYS PHE GLU ALA ALA TYR ASP PHE PRO GLY
SEQRES 2 A 69 SER GLY SER SER SER GLU LEU PRO LEU LYS LYS GLY ASP
SEQRES 3 A 69 ILE VAL PHE ILE SER ARG ASP GLU PRO SER GLY TRP SER
SEQRES 4 A 69 LEU ALA LYS LEU LEU ASP GLY SER LYS GLU GLY TRP VAL
SEQRES 5 A 69 PRO THR ALA TYR MET THR PRO TYR LYS ASP THR ARG ASN
SEQRES 6 A 69 THR VAL PRO VAL
SHEET 1 AA 5 GLU A1170 PRO A1174 0
SHEET 2 AA 5 TRP A1159 LEU A1164 -1 O SER A1160 N VAL A1173
SHEET 3 AA 5 ILE A1148 GLU A1155 -1 O PHE A1150 N LYS A1163
SHEET 4 AA 5 LYS A1125 ALA A1128 -1 O PHE A1126 N VAL A1149
SHEET 5 AA 5 MET A1178 PRO A1180 -1 O THR A1179 N GLU A1127
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 - n 15 2 Bytes