Header list of 1ry4.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 19-DEC-03 1RY4
TITLE NMR STRUCTURE OF THE CRIB-PDZ MODULE OF PAR-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CG5884-PA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CRIB-PDZ DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: PAR-6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBH
KEYWDS PDZ, CRIB, CDC-42, CELL POLARIZATION, POLARITY ADAPTOR COMPLEX, CELL
KEYWDS 2 ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.C.PETERSON,R.R.PENKERT,B.F.VOLKMAN,K.E.PREHODA
REVDAT 3 02-MAR-22 1RY4 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RY4 1 VERSN
REVDAT 1 23-MAR-04 1RY4 0
JRNL AUTH F.C.PETERSON,R.R.PENKERT,B.F.VOLKMAN,K.E.PREHODA
JRNL TITL CDC42 REGULATES THE PAR-6 PDZ DOMAIN THROUGH AN ALLOSTERIC
JRNL TITL 2 CRIB-PDZ TRANSITION.
JRNL REF MOL.CELL V. 13 665 2004
JRNL REFN ISSN 1097-2765
JRNL PMID 15023337
JRNL DOI 10.1016/S1097-2765(04)00086-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, XPLOR-NIH 2.0.6
REMARK 3 AUTHORS : BRUKER INSTRUMENTS (XWINNMR), AXEL BRUNGER AND
REMARK 3 MARIUS CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1703 RESTRAINTS, 1564 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 139 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1RY4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021137.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 50MM SODIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PAR-6 U-15C,13C, 20MM
REMARK 210 PHOSPHATE BUFFER, 0.05% SODIUM
REMARK 210 AZIDE; 0.5MM PAR-6 U-15, 20MM
REMARK 210 PHOSPHATE BUFFER, 0.05% SODIUM
REMARK 210 AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_AROMATIC_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 97.027.12.56, XEASY
REMARK 210 1.3.13, GARANT 2.1, CYANA 1.0.6
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
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 OD1 ASP A 216 H ALA A 252 1.59
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 A 129 149.68 69.00
REMARK 500 1 LYS A 130 73.41 -116.95
REMARK 500 1 PHE A 142 92.24 -179.17
REMARK 500 1 ILE A 148 88.20 -67.04
REMARK 500 1 VAL A 151 -68.30 -136.32
REMARK 500 1 ILE A 153 125.66 59.06
REMARK 500 1 HIS A 166 89.32 -152.31
REMARK 500 1 PHE A 196 -168.44 -119.08
REMARK 500 1 ASN A 222 -69.01 70.25
REMARK 500 2 PHE A 142 93.62 166.66
REMARK 500 2 ASP A 150 91.47 62.73
REMARK 500 2 VAL A 151 -72.99 -124.71
REMARK 500 2 ILE A 153 -92.88 40.29
REMARK 500 2 HIS A 166 -75.63 -139.53
REMARK 500 2 ASP A 169 -70.48 -165.14
REMARK 500 2 LEU A 211 -46.47 -145.43
REMARK 500 2 VAL A 214 -72.61 43.22
REMARK 500 2 ASN A 222 -72.09 69.59
REMARK 500 2 ASN A 241 -70.17 -93.58
REMARK 500 2 SER A 242 -41.28 60.16
REMARK 500 2 SER A 243 -73.15 -68.60
REMARK 500 2 ASN A 253 8.81 56.43
REMARK 500 3 SER A 137 93.21 -161.95
REMARK 500 3 GLU A 156 78.64 -67.93
REMARK 500 3 HIS A 166 79.07 -162.26
REMARK 500 3 SER A 198 -59.29 -121.23
REMARK 500 3 ASN A 222 -70.17 68.30
REMARK 500 4 SER A 137 73.93 58.26
REMARK 500 4 ARG A 143 89.95 -150.02
REMARK 500 4 HIS A 166 76.33 -164.99
REMARK 500 4 SER A 168 97.00 67.58
REMARK 500 4 LEU A 172 -65.56 -143.04
REMARK 500 4 ASN A 222 -74.27 65.97
REMARK 500 4 ASN A 241 -79.21 -82.31
REMARK 500 4 SER A 242 -37.31 59.59
REMARK 500 4 ASN A 253 -31.32 68.47
REMARK 500 5 ARG A 143 98.02 69.22
REMARK 500 5 ASN A 222 -66.19 70.60
REMARK 500 6 SER A 129 107.29 64.03
REMARK 500 6 PHE A 142 -64.64 -101.83
REMARK 500 6 ARG A 143 102.33 -175.77
REMARK 500 6 ASP A 150 117.43 72.63
REMARK 500 6 ILE A 153 -81.17 -80.92
REMARK 500 6 ASP A 169 108.06 71.23
REMARK 500 6 ASN A 222 -77.81 64.36
REMARK 500 6 ALA A 227 109.07 -57.59
REMARK 500 6 ASN A 253 83.74 75.16
REMARK 500 7 LYS A 130 -76.86 -153.95
REMARK 500 7 ARG A 143 24.35 40.89
REMARK 500 7 LEU A 172 -91.31 63.62
REMARK 500
REMARK 500 THIS ENTRY HAS 151 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RY4 A 130 255 GB 18860099 NP_573238 130 255
SEQADV 1RY4 GLY A 128 GB 18860099 CLONING ARTIFACT
SEQADV 1RY4 SER A 129 GB 18860099 CLONING ARTIFACT
SEQRES 1 A 128 GLY SER LYS THR LYS ALA PRO SER ILE SER ILE PRO HIS
SEQRES 2 A 128 ASP PHE ARG GLN VAL SER ALA ILE ILE ASP VAL ASP ILE
SEQRES 3 A 128 VAL PRO GLU THR HIS ARG ARG VAL ARG LEU LEU LYS HIS
SEQRES 4 A 128 GLY SER ASP LYS PRO LEU GLY PHE TYR ILE ARG ASP GLY
SEQRES 5 A 128 THR SER VAL ARG VAL THR ALA SER GLY LEU GLU LYS GLN
SEQRES 6 A 128 PRO GLY ILE PHE ILE SER ARG LEU VAL PRO GLY GLY LEU
SEQRES 7 A 128 ALA GLU SER THR GLY LEU LEU ALA VAL ASN ASP GLU VAL
SEQRES 8 A 128 ILE GLU VAL ASN GLY ILE GLU VAL ALA GLY LYS THR LEU
SEQRES 9 A 128 ASP GLN VAL THR ASP MET MET VAL ALA ASN SER SER ASN
SEQRES 10 A 128 LEU ILE ILE THR VAL LYS PRO ALA ASN GLN ARG
HELIX 1 1 GLY A 204 GLY A 210 1 7
HELIX 2 2 THR A 230 ASN A 241 1 12
HELIX 3 3 SER A 242 ASN A 244 5 3
SHEET 1 A 4 ARG A 159 LEU A 163 0
SHEET 2 A 4 LEU A 245 LYS A 250 -1 O ILE A 247 N VAL A 161
SHEET 3 A 4 GLU A 217 VAL A 221 -1 N ILE A 219 O THR A 248
SHEET 4 A 4 ILE A 224 GLU A 225 -1 O ILE A 224 N VAL A 221
SHEET 1 B 2 PHE A 174 THR A 185 0
SHEET 2 B 2 GLY A 188 LEU A 200 -1 O GLN A 192 N SER A 181
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 - r 2 2 Bytes