Header list of 1qry.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 16-JUN-99 1QRY
TITLE HOMEOBOX PROTEIN VND (VENTRAL NERVOUS SYSTEM DEFECTIVE PROTEIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (HOMEOBOX VENTRAL NERVOUS SYSTEM DEFECTIVE
COMPND 3 PROTEIN);
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: VND/NK2 HOMEODOMAIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS HELIX-TURN-HELIX, DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.XIANG
REVDAT 4 02-MAR-22 1QRY 1 KEYWDS REMARK
REVDAT 3 24-FEB-09 1QRY 1 VERSN
REVDAT 2 31-MAY-05 1QRY 1 JRNL REMARK COMPND
REVDAT 1 06-JUL-99 1QRY 0
JRNL AUTH K.J.HWANG,B.XIANG,J.M.GRUSCHUS,K.Y.NAM,K.T.NO,M.NIRENBERG,
JRNL AUTH 2 J.A.FERRETTI
JRNL TITL DISTORTION OF THE THREE-DIMENSIONAL STRUCTURE OF THE
JRNL TITL 2 VND/NK-2 HOMEODOMAIN BOUND TO DNA INDUCED BY AN
JRNL TITL 3 EMBRYONICALLY LETHAL A35T POINT MUTATION.
JRNL REF BIOCHEMISTRY V. 42 12522 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14580198
JRNL DOI 10.1021/BI030116I
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1146 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS AND 43 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1QRY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000009193.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM A35T VND/NK2-DNA COMPLEX;
REMARK 210 A35T VND/NK2 IS 15N SINGLE-
REMARK 210 LABELED; 90% H2O, 10% D2O; PH
REMARK 210 6.8; 0.7 MM A35T VND/NK2-DNA
REMARK 210 COMPLEX; A35T VND/NK2 IS 15N/13C
REMARK 210 DOUBLE-LABELED; 90% H2O, 10% D2O;
REMARK 210 PH 6.8; 0.7 MM A35T VND/NK2-DNA
REMARK 210 COMPLEX; A35T VND/NK2 IS 15N/13C
REMARK 210 DOUBLE-LABELED; 100% D2O; PH6.8
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 15N-1H HSQC; 3D CBCANH; 3D
REMARK 210 CBCA(CO)NH; 3D HBHA(CO)NH; 3D
REMARK 210 HNHA; 3D HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: 3D 15N EDITED NOESY-HSQC, 4D 15N/13C EDITED HMQC-NOESY
REMARK 210 -HSQC, AND 4D 13C/13C EDITED HMQC-NOESY-HSQC WERE USED FOR
REMARK 210 OBTAINING NOE RESTRAINTS.
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 HG1 THR A 20 H GLN A 23 1.29
REMARK 500 O HIS A 63 H THR A 67 1.34
REMARK 500 O PHE A 60 H ARG A 64 1.37
REMARK 500 O LEU A 37 HH12 ARG A 42 1.49
REMARK 500 O LEU A 45 H LEU A 48 1.56
REMARK 500 O ARG A 42 H LEU A 45 1.58
REMARK 500 O GLU A 43 OG1 THR A 46 2.15
REMARK 500 O LEU A 45 N LEU A 48 2.16
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 PRO A 40 C - N - CD ANGL. DEV. = -16.5 DEGREES
REMARK 500 2 PRO A 40 C - N - CD ANGL. DEV. = -16.0 DEGREES
REMARK 500 6 PRO A 40 C - N - CD ANGL. DEV. = -14.9 DEGREES
REMARK 500 7 PRO A 40 C - N - CD ANGL. DEV. = -16.2 DEGREES
REMARK 500 9 PRO A 40 C - N - CD ANGL. DEV. = -15.6 DEGREES
REMARK 500 10 PRO A 40 C - N - CD ANGL. DEV. = -14.4 DEGREES
REMARK 500 12 PRO A 40 C - N - CD ANGL. DEV. = -18.3 DEGREES
REMARK 500 14 PRO A 40 C - N - CD ANGL. DEV. = -13.9 DEGREES
REMARK 500 16 PRO A 40 C - N - CD ANGL. DEV. = -18.2 DEGREES
REMARK 500 17 PRO A 40 C - N - CD ANGL. DEV. = -18.2 DEGREES
REMARK 500 18 PRO A 40 C - N - CD ANGL. DEV. = -18.8 DEGREES
REMARK 500 19 PRO A 40 C - N - CD ANGL. DEV. = -19.9 DEGREES
REMARK 500 20 PRO A 40 C - N - CD ANGL. DEV. = -19.2 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 LYS A 12 -164.49 -77.09
REMARK 500 1 ARG A 13 42.29 -101.25
REMARK 500 1 ARG A 15 109.48 167.53
REMARK 500 1 ARG A 16 171.62 -45.44
REMARK 500 1 LEU A 18 -154.16 -148.60
REMARK 500 1 LYS A 21 -16.66 -43.49
REMARK 500 1 GLN A 23 -80.49 -40.55
REMARK 500 1 THR A 24 -35.64 -33.44
REMARK 500 1 TYR A 25 -76.25 -66.33
REMARK 500 1 LEU A 37 140.28 -35.22
REMARK 500 1 SER A 38 -141.60 -123.54
REMARK 500 1 GLU A 43 -61.86 -26.99
REMARK 500 1 THR A 46 -22.40 -36.71
REMARK 500 1 LEU A 48 -90.17 -64.71
REMARK 500 1 ILE A 49 31.86 -98.81
REMARK 500 1 ARG A 50 -2.01 45.27
REMARK 500 1 LEU A 51 95.84 -46.68
REMARK 500 1 THR A 52 129.51 -35.03
REMARK 500 1 PRO A 53 -82.09 -23.57
REMARK 500 1 THR A 67 -15.57 -42.85
REMARK 500 1 GLU A 73 -85.90 -87.47
REMARK 500 1 LYS A 74 -148.85 34.54
REMARK 500 1 GLU A 77 118.90 68.37
REMARK 500 1 HIS A 79 101.48 -172.26
REMARK 500 2 HIS A 3 110.26 51.48
REMARK 500 2 ASP A 6 107.57 56.90
REMARK 500 2 PRO A 9 23.83 -79.59
REMARK 500 2 ASN A 10 -20.39 -147.42
REMARK 500 2 LYS A 11 -42.89 81.50
REMARK 500 2 LYS A 12 143.54 56.54
REMARK 500 2 ARG A 13 43.53 -93.39
REMARK 500 2 LYS A 14 -75.58 55.34
REMARK 500 2 ARG A 16 166.26 -39.53
REMARK 500 2 VAL A 17 150.89 -48.39
REMARK 500 2 LEU A 18 -121.23 -95.59
REMARK 500 2 PHE A 19 149.46 58.27
REMARK 500 2 LYS A 21 -28.65 -36.04
REMARK 500 2 GLN A 23 -87.53 -43.70
REMARK 500 2 THR A 24 -24.94 -32.59
REMARK 500 2 TYR A 25 -75.01 -74.75
REMARK 500 2 ARG A 32 -72.41 -60.59
REMARK 500 2 LEU A 37 138.00 -32.53
REMARK 500 2 SER A 38 -140.06 -125.60
REMARK 500 2 THR A 46 -13.18 -44.07
REMARK 500 2 LEU A 48 -90.14 -70.22
REMARK 500 2 ARG A 50 -14.05 48.04
REMARK 500 2 LEU A 51 103.11 -39.11
REMARK 500 2 THR A 52 147.06 -30.44
REMARK 500 2 PRO A 53 -84.17 -51.74
REMARK 500 2 THR A 67 -15.30 -41.81
REMARK 500
REMARK 500 THIS ENTRY HAS 512 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QRY A 5 80 UNP P22808 VND_DROME 538 613
SEQRES 1 A 80 GLY SER HIS MET SER ASP GLY LEU PRO ASN LYS LYS ARG
SEQRES 2 A 80 LYS ARG ARG VAL LEU PHE THR LYS ALA GLN THR TYR GLU
SEQRES 3 A 80 LEU GLU ARG ARG PHE ARG GLN GLN ARG TYR LEU SER ALA
SEQRES 4 A 80 PRO GLU ARG GLU HIS LEU THR SER LEU ILE ARG LEU THR
SEQRES 5 A 80 PRO THR GLN VAL LYS ILE TRP PHE GLN ASN HIS ARG TYR
SEQRES 6 A 80 LYS THR LYS ARG ALA GLN ASN GLU LYS GLY TYR GLU GLY
SEQRES 7 A 80 HIS PRO
HELIX 1 1 THR A 20 GLN A 34 1 15
HELIX 2 2 SER A 38 LEU A 48 1 11
HELIX 3 3 THR A 52 LYS A 74 1 23
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