Header list of 1rgw.pdb file
Complete list - t 27 2 Bytes
HEADER STRUCTURAL PROTEIN 13-NOV-03 1RGW
TITLE SOLUTION STRUCTURE OF ZASP'S PDZ DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZASP PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: MUSCLE;
SOURCE 6 GENE: ZASP;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET9D
KEYWDS ZASP, PDZ, CYPHER, ORACLE, MUSCLE, Z-DISK, SARCOMERE, STRUCTURAL
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.AU,R.A.ATKINSON,A.PALLAVICINI,C.JOSEPH,S.R.MARTIN,F.W.MUSKETT,
AUTHOR 2 R.GUERRINI,G.FAULKNER,A.PASTORE
REVDAT 3 27-OCT-21 1RGW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RGW 1 VERSN
REVDAT 1 13-APR-04 1RGW 0
JRNL AUTH Y.AU,R.A.ATKINSON,R.GUERRINI,G.KELLY,C.JOSEPH,S.R.MARTIN,
JRNL AUTH 2 F.W.MUSKETT,A.PALLAVICINI,G.FAULKNER,A.PASTORE
JRNL TITL SOLUTION STRUCTURE OF ZASP PDZ DOMAIN; IMPLICATIONS FOR
JRNL TITL 2 SARCOMERE ULTRASTRUCTURE AND ENIGMA FAMILY REDUNDANCY.
JRNL REF STRUCTURE V. 12 611 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15062084
JRNL DOI 10.1016/J.STR.2004.02.019
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 853 NOE-DERIVED RESTAINTS FROM ASSIGNED
REMARK 3 FROM CANDID/CYANA. 7 DIRECTLY OBSERVED HYDROGEN BONDS. 97
REMARK 3 DIHEDRAL ANGLE RESTRAINTS (FROM HNHA AND TALOS).
REMARK 4
REMARK 4 1RGW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020735.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : NO ADDED SALT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM ZASP-PDZ, 20 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 0.02% SODIUM
REMARK 210 AZIDE, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; 2D
REMARK 210 TOCSY; HCCH-TOCSY; 3D_15N-
REMARK 210 SEPARATED_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA CYANA 1.0.6
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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.
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 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 2 TYR A 3 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 PHE A 23 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 2 PHE A 23 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 3 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 TYR A 3 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 6 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 7 TYR A 3 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 8 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 8 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 9 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 9 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 10 TYR A 3 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 10 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 11 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 11 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 12 TYR A 3 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 14 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 15 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 15 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 17 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 17 PHE A 15 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 17 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 TYR A 74 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 18 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 19 TYR A 3 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 19 PHE A 15 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 19 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 20 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
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 TRP A 13 -62.13 -97.88
REMARK 500 1 SER A 30 -82.48 -98.49
REMARK 500 1 SER A 41 -128.71 -90.68
REMARK 500 1 SER A 44 58.66 -151.39
REMARK 500 1 ASP A 47 -158.76 -161.23
REMARK 500 1 SER A 73 -48.79 -147.72
REMARK 500 1 SER A 83 89.47 -168.00
REMARK 500 2 SER A 30 -74.45 -90.54
REMARK 500 2 SER A 41 -142.29 -106.17
REMARK 500 2 THR A 57 48.78 -74.55
REMARK 500 2 SER A 73 -29.54 -163.68
REMARK 500 3 SER A 30 -77.56 -89.41
REMARK 500 3 SER A 41 -148.07 -89.78
REMARK 500 3 SER A 44 76.05 -151.05
REMARK 500 3 GLN A 45 103.66 -53.23
REMARK 500 3 THR A 57 33.40 -72.81
REMARK 500 3 SER A 73 -12.58 -148.74
REMARK 500 4 SER A 41 -149.57 -96.75
REMARK 500 4 ASP A 47 -164.17 -162.19
REMARK 500 4 VAL A 50 -74.34 -99.83
REMARK 500 4 SER A 73 -56.09 -160.42
REMARK 500 4 SER A 83 -69.94 -124.96
REMARK 500 5 SER A 30 -85.95 -96.98
REMARK 500 5 SER A 41 -132.49 -106.56
REMARK 500 5 SER A 44 63.67 -150.49
REMARK 500 5 GLN A 45 106.58 -42.86
REMARK 500 5 ASP A 47 -158.72 -164.00
REMARK 500 5 SER A 73 -56.13 -158.50
REMARK 500 5 SER A 83 -175.57 -68.00
REMARK 500 6 TRP A 13 84.08 40.48
REMARK 500 6 SER A 30 -85.65 -98.86
REMARK 500 6 SER A 41 -149.06 -95.55
REMARK 500 6 ASP A 53 14.47 55.32
REMARK 500 6 SER A 73 -47.08 -159.14
REMARK 500 7 ASN A 24 37.22 76.50
REMARK 500 7 SER A 30 -82.02 -102.66
REMARK 500 7 SER A 41 -153.10 -89.44
REMARK 500 7 VAL A 50 -71.13 -102.02
REMARK 500 7 THR A 57 47.74 -98.19
REMARK 500 7 SER A 73 -62.83 -156.07
REMARK 500 7 SER A 83 -23.88 93.21
REMARK 500 8 SER A 30 -77.92 -89.27
REMARK 500 8 SER A 36 -168.06 -123.51
REMARK 500 8 SER A 41 -153.36 -91.52
REMARK 500 8 SER A 44 54.22 -149.62
REMARK 500 8 GLN A 45 103.30 -53.96
REMARK 500 8 VAL A 50 -68.95 -98.46
REMARK 500 8 ASP A 53 14.34 58.84
REMARK 500 8 SER A 73 -33.00 -161.35
REMARK 500 9 LEU A 27 100.23 -59.47
REMARK 500
REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 81 LYS A 82 7 149.21
REMARK 500 GLN A 81 LYS A 82 9 142.90
REMARK 500 LYS A 82 SER A 83 10 146.96
REMARK 500 GLN A 40 SER A 41 17 -148.83
REMARK 500 LEU A 43 SER A 44 17 140.08
REMARK 500 ALA A 72 SER A 73 18 140.28
REMARK 500 PRO A 12 TRP A 13 19 143.63
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 5 TYR A 3 0.06 SIDE CHAIN
REMARK 500 5 ARG A 16 0.11 SIDE CHAIN
REMARK 500 5 ARG A 85 0.15 SIDE CHAIN
REMARK 500 7 TYR A 3 0.18 SIDE CHAIN
REMARK 500 7 ARG A 16 0.09 SIDE CHAIN
REMARK 500 8 TYR A 3 0.13 SIDE CHAIN
REMARK 500 8 ARG A 16 0.08 SIDE CHAIN
REMARK 500 8 ARG A 31 0.08 SIDE CHAIN
REMARK 500 9 PHE A 15 0.08 SIDE CHAIN
REMARK 500 9 ARG A 85 0.10 SIDE CHAIN
REMARK 500 10 PHE A 15 0.08 SIDE CHAIN
REMARK 500 10 ARG A 85 0.09 SIDE CHAIN
REMARK 500 11 ARG A 31 0.08 SIDE CHAIN
REMARK 500 12 TYR A 3 0.10 SIDE CHAIN
REMARK 500 12 ARG A 85 0.08 SIDE CHAIN
REMARK 500 13 ARG A 16 0.09 SIDE CHAIN
REMARK 500 17 ARG A 85 0.08 SIDE CHAIN
REMARK 500 19 PHE A 15 0.08 SIDE CHAIN
REMARK 500 19 ARG A 85 0.10 SIDE CHAIN
REMARK 500 20 PHE A 15 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RGW A 1 85 UNP O75112 LDB3_HUMAN 1 85
SEQADV 1RGW ALA A 2 UNP O75112 SER 2 ENGINEERED MUTATION
SEQRES 1 A 85 MET ALA TYR SER VAL THR LEU THR GLY PRO GLY PRO TRP
SEQRES 2 A 85 GLY PHE ARG LEU GLN GLY GLY LYS ASP PHE ASN MET PRO
SEQRES 3 A 85 LEU THR ILE SER ARG ILE THR PRO GLY SER LYS ALA ALA
SEQRES 4 A 85 GLN SER GLN LEU SER GLN GLY ASP LEU VAL VAL ALA ILE
SEQRES 5 A 85 ASP GLY VAL ASN THR ASP THR MET THR HIS LEU GLU ALA
SEQRES 6 A 85 GLN ASN LYS ILE LYS SER ALA SER TYR ASN LEU SER LEU
SEQRES 7 A 85 THR LEU GLN LYS SER LYS ARG
HELIX 1 1 GLY A 20 ASN A 24 5 5
HELIX 2 2 SER A 36 SER A 41 1 6
HELIX 3 3 THR A 61 LYS A 70 1 10
SHEET 1 A 4 ALA A 2 LEU A 7 0
SHEET 2 A 4 LEU A 76 GLN A 81 -1 O LEU A 80 N TYR A 3
SHEET 3 A 4 VAL A 49 ILE A 52 -1 N ALA A 51 O THR A 79
SHEET 4 A 4 VAL A 55 ASN A 56 -1 O VAL A 55 N ILE A 52
SHEET 1 B 2 PHE A 15 LEU A 17 0
SHEET 2 B 2 ILE A 29 ILE A 32 -1 O ARG A 31 N ARG A 16
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 - t 27 2 Bytes