Header list of 1zu1.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 29-MAY-05 1ZU1
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGERS OF THE XENOPUS
TITLE 2 LAEVIS DOUBLE STRANDED RNA BINDING PROTEIN ZFA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA BINDING PROTEIN ZFA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DSRBP-ZFA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS ZINC FINGER PROTEIN, HELIX-LOOP-HELIX, HELIX-TURN-HELIX, RNA BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.M.MOLLER,M.A.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
REVDAT 3 02-MAR-22 1ZU1 1 REMARK LINK
REVDAT 2 24-FEB-09 1ZU1 1 VERSN
REVDAT 1 20-SEP-05 1ZU1 0
JRNL AUTH H.M.MOLLER,M.A.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGERS OF THE
JRNL TITL 2 XENOPUS LAEVIS DOUBLE-STRANDED RNA-BINDING PROTEIN ZFA
JRNL REF J.MOL.BIOL. V. 351 718 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16051273
JRNL DOI 10.1016/J.JMB.2005.06.032
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1-3.5, AMBER 8
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 D.A.CASE,T.CHEATHAM,T.DARDEN,H.GOHLKE,R.LUO,K.M.J.MERZ,
REMARK 3 A.ONUFRIEV,C.SIMMERLING,B.WANG,R.WOODS. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1142 UNIQUE NOE RESTRAINTS, 216
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1ZU1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033117.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM DSRBP-ZFA2-128 U-15N, 25MM
REMARK 210 TRIS-BUFFER, 100MM NACL, 2MM DTT,
REMARK 210 PH=6.9, 95% H2O, 5% D2O; 1MM
REMARK 210 DSRBP-ZFA2-128 U-15N,13C, 25MM
REMARK 210 TRIS-BUFFER, 100MM NACL, 2MM DTT,
REMARK 210 PH=6.9, 95% H2O, 5% D2O; 1MM
REMARK 210 DSRBP-ZFA2-128 U-15N,13C, 25MM
REMARK 210 TRIS-BUFFER, 100MM NACL, 2MM DTT,
REMARK 210 PH=6.9, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_
REMARK 210 HACAHB-COSY; 13C [13CO] AND 13C
REMARK 210 [15N] SPIN-ECHO DIFFERENCE CT
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, NMRVIEW 5.0.4,
REMARK 210 CYANA 1.0.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE PROTEIN CONSISTS OF TWO DOMAINS THAT TUMBLE MORE OR
REMARK 210 LESS INDEPENDENTLY. THE LINKER CONNECTING BOTH DOMAINS IS
REMARK 210 COMPLETELY DISORDERD.
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: 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 5 GLU A 127 CG GLU A 127 CD 0.101
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 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 ARG A 124 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 5 GLU A 127 OE1 - CD - OE2 ANGL. DEV. = 44.6 DEGREES
REMARK 500 5 GLU A 127 CG - CD - OE1 ANGL. DEV. = -34.4 DEGREES
REMARK 500 5 GLU A 127 CG - CD - OE2 ANGL. DEV. = -34.2 DEGREES
REMARK 500 6 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 9 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 10 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 11 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 13 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 13 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 13 ARG A 124 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 14 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 14 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 16 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 17 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 3.3 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 THR A 34 10.47 -143.20
REMARK 500 1 SER A 40 55.63 38.50
REMARK 500 1 ASN A 69 47.31 -71.32
REMARK 500 1 ALA A 77 36.75 -67.83
REMARK 500 1 LYS A 81 -35.58 -155.61
REMARK 500 2 PHE A 5 30.72 -152.20
REMARK 500 2 SER A 40 55.45 34.96
REMARK 500 2 ASP A 73 21.74 -141.11
REMARK 500 2 ALA A 83 70.31 -119.77
REMARK 500 2 ALA A 85 -10.62 -141.83
REMARK 500 3 SER A 40 55.92 38.44
REMARK 500 3 ILE A 44 -7.79 -56.25
REMARK 500 3 PRO A 84 39.10 -74.24
REMARK 500 3 ALA A 85 23.72 -140.50
REMARK 500 3 ASP A 89 24.92 -144.55
REMARK 500 3 ARG A 93 -75.47 -6.99
REMARK 500 3 SER A 94 -37.50 37.80
REMARK 500 4 GLU A 4 24.14 -142.54
REMARK 500 4 SER A 40 54.38 32.35
REMARK 500 4 GLU A 72 42.82 -72.51
REMARK 500 4 ALA A 85 -35.29 -156.57
REMARK 500 4 SER A 88 -64.31 -146.26
REMARK 500 4 ASP A 89 -34.09 -156.63
REMARK 500 4 ARG A 93 28.97 -76.91
REMARK 500 5 ASP A 3 -36.29 -142.15
REMARK 500 5 ASP A 12 17.31 -68.47
REMARK 500 5 VAL A 15 25.12 -140.65
REMARK 500 5 SER A 40 53.61 36.65
REMARK 500 5 ASN A 69 3.36 -65.24
REMARK 500 5 ASP A 73 48.49 -72.54
REMARK 500 5 ALA A 77 41.21 -70.81
REMARK 500 5 ILE A 87 34.83 -82.22
REMARK 500 5 GLU A 91 21.19 -141.46
REMARK 500 6 PHE A 5 -30.81 -150.22
REMARK 500 6 SER A 40 56.55 36.47
REMARK 500 6 ILE A 44 2.08 -66.53
REMARK 500 6 PRO A 76 -9.42 -58.34
REMARK 500 6 ALA A 77 45.23 -69.58
REMARK 500 6 ASP A 89 56.26 -140.28
REMARK 500 6 SER A 94 40.55 -73.28
REMARK 500 7 PHE A 5 -1.71 -155.44
REMARK 500 7 ASP A 9 -44.10 -155.16
REMARK 500 7 PRO A 14 166.86 -48.92
REMARK 500 7 VAL A 15 19.77 -144.16
REMARK 500 7 SER A 40 56.87 37.47
REMARK 500 8 PHE A 5 -39.96 -144.53
REMARK 500 8 SER A 40 58.52 37.38
REMARK 500 8 ILE A 44 1.79 -65.36
REMARK 500 8 ILE A 68 -46.08 -131.16
REMARK 500 8 GLU A 72 -39.81 -158.02
REMARK 500
REMARK 500 THIS ENTRY HAS 114 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 129 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 36 SG
REMARK 620 2 CYS A 39 SG 113.4
REMARK 620 3 HIS A 52 NE2 110.5 106.3
REMARK 620 4 HIS A 58 ND1 112.0 109.1 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 130 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 97 SG
REMARK 620 2 CYS A 100 SG 110.5
REMARK 620 3 HIS A 113 NE2 111.2 106.3
REMARK 620 4 HIS A 119 ND1 109.3 113.6 105.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 130
DBREF 1ZU1 A 2 128 UNP Q8AVN9 Q8AVN9_XENLA 2 128
SEQRES 1 A 127 ALA ASP GLU PHE GLY ASN GLY ASP ALA LEU ASP LEU PRO
SEQRES 2 A 127 VAL GLY LYS ASP ALA VAL ASN SER LEU ILE ARG GLU ASN
SEQRES 3 A 127 SER HIS ILE PHE SER ASP THR GLN CYS LYS VAL CYS SER
SEQRES 4 A 127 ALA VAL LEU ILE SER GLU SER GLN LYS LEU ALA HIS TYR
SEQRES 5 A 127 GLN SER ARG LYS HIS ALA ASN LYS VAL ARG ARG TYR MET
SEQRES 6 A 127 ALA ILE ASN GLN GLY GLU ASP SER VAL PRO ALA LYS LYS
SEQRES 7 A 127 PHE LYS ALA ALA PRO ALA GLU ILE SER ASP GLY GLU ASP
SEQRES 8 A 127 ARG SER LYS CYS CYS PRO VAL CYS ASN MET THR PHE SER
SEQRES 9 A 127 SER PRO VAL VAL ALA GLU SER HIS TYR ILE GLY LYS THR
SEQRES 10 A 127 HIS ILE LYS ASN LEU ARG LEU ARG GLU GLN
HET ZN A 129 1
HET ZN A 130 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLY A 16 ASN A 27 1 12
HELIX 2 2 SER A 45 SER A 55 1 11
HELIX 3 3 SER A 55 ASN A 69 1 15
HELIX 4 4 SER A 106 ILE A 115 1 10
HELIX 5 5 GLY A 116 GLN A 128 1 13
SHEET 1 A 2 GLN A 35 CYS A 36 0
SHEET 2 A 2 ALA A 41 VAL A 42 -1 O ALA A 41 N CYS A 36
SHEET 1 B 2 CYS A 96 CYS A 97 0
SHEET 2 B 2 MET A 102 THR A 103 -1 O MET A 102 N CYS A 97
LINK SG CYS A 36 ZN ZN A 129 1555 1555 2.30
LINK SG CYS A 39 ZN ZN A 129 1555 1555 2.29
LINK NE2 HIS A 52 ZN ZN A 129 1555 1555 2.08
LINK ND1 HIS A 58 ZN ZN A 129 1555 1555 2.08
LINK SG CYS A 97 ZN ZN A 130 1555 1555 2.29
LINK SG CYS A 100 ZN ZN A 130 1555 1555 2.29
LINK NE2 HIS A 113 ZN ZN A 130 1555 1555 2.08
LINK ND1 HIS A 119 ZN ZN A 130 1555 1555 2.09
SITE 1 AC1 4 CYS A 36 CYS A 39 HIS A 52 HIS A 58
SITE 1 AC2 4 CYS A 97 CYS A 100 HIS A 113 HIS A 119
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