Header list of 2hgh.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION/RNA 27-JUN-06 2HGH
TITLE TRANSCRIPTION FACTOR IIIA ZINC FINGERS 4-6 BOUND TO 5S RRNA 55MER (NMR
TITLE 2 STRUCTURE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 55-MER;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TRANSCRIPTION FACTOR IIIA;
COMPND 7 CHAIN: A;
COMPND 8 FRAGMENT: ZINC FINGERS 4-6 (RESIDUES 127-212);
COMPND 9 SYNONYM: FACTOR A, TFIIIA, S-TFIIIA/O-TFIIIA;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: RNA WAS SYNTHESIZED BY IN VITRO TRANSCRIPTION FROM
SOURCE 4 LINEARIZED PUC18 PLASMID CONTAINING THE 55MER SEQUENCE AND THE
SOURCE 5 PRIMER BINDING SITE FOR T7 RNA POLYMERASE;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 8 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 9 ORGANISM_TAXID: 8355;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS ZINC FINGER, TRANSCRIPTION-RNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.M.LEE
REVDAT 4 09-MAR-22 2HGH 1 REMARK SEQADV LINK
REVDAT 3 14-APR-10 2HGH 1 REMARK
REVDAT 2 24-FEB-09 2HGH 1 VERSN
REVDAT 1 01-AUG-06 2HGH 0
JRNL AUTH B.M.LEE,J.XU,B.K.CLARKSON,M.A.MARTINEZ-YAMOUT,J.H.DYSON,
JRNL AUTH 2 D.A.CASE,J.M.GOTTESFELD,P.E.WRIGHT
JRNL TITL INDUCED FIT AND 'LOCK AND KEY' RECOGNITION OF 5 S RNA BY
JRNL TITL 2 ZINC FINGERS OF TRANSCRIPTION FACTOR IIIA
JRNL REF J.MOL.BIOL. V. 357 275 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16405997
JRNL DOI 10.1016/J.JMB.2005.12.010
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, AMBER 8
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HGH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038320.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 291
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : U-15N, 90% H2O, 10% D2O; U-13C;U
REMARK 210 -15N, D2O; U-2H;U-13C;U-15N, 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ; 750 MHZ; 600
REMARK 210 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX; DMX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.4, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 MOLECULAR DYNAMICS, GENERALIZED
REMARK 210 BORN SOLVATION MODEL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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: 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 1 A B 8 C3' - C2' - C1' ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 A B 25 C3' - C2' - C1' ANGL. DEV. = -4.4 DEGREES
REMARK 500 1 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.6 DEGREES
REMARK 500 1 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 A B 6 O4' - C4' - C3' ANGL. DEV. = 5.4 DEGREES
REMARK 500 2 U B 11 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 A B 25 C3' - C2' - C1' ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 A B 25 C3' - C2' - C1' ANGL. DEV. = -5.8 DEGREES
REMARK 500 3 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 A B 6 O4' - C4' - C3' ANGL. DEV. = 5.0 DEGREES
REMARK 500 4 G B 26 C5' - C4' - O4' ANGL. DEV. = 6.2 DEGREES
REMARK 500 4 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.6 DEGREES
REMARK 500 4 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 4 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 4 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 U B 11 C5' - C4' - O4' ANGL. DEV. = 5.6 DEGREES
REMARK 500 5 A B 25 C3' - C2' - C1' ANGL. DEV. = -4.5 DEGREES
REMARK 500 5 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 5 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 VAL A 158 CG1 - CB - CG2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 6 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.6 DEGREES
REMARK 500 6 VAL A 158 CG1 - CB - CG2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 7 A B 6 O4' - C4' - C3' ANGL. DEV. = 5.3 DEGREES
REMARK 500 7 U B 11 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 7 C B 19 C5' - C4' - O4' ANGL. DEV. = 5.8 DEGREES
REMARK 500 7 A B 25 C3' - C2' - C1' ANGL. DEV. = -5.8 DEGREES
REMARK 500 7 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 7 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 7 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 7 VAL A 158 CG1 - CB - CG2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 8 A B 6 O4' - C4' - C3' ANGL. DEV. = 4.9 DEGREES
REMARK 500 8 A B 25 C3' - C2' - C1' ANGL. DEV. = -6.2 DEGREES
REMARK 500 8 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 8 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 8 VAL A 158 CG1 - CB - CG2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 9 A B 25 C3' - C2' - C1' ANGL. DEV. = -5.0 DEGREES
REMARK 500 9 U B 38 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 9 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 9 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 9 ARG A 154 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 10 A B 6 O4' - C4' - C3' ANGL. DEV. = 5.1 DEGREES
REMARK 500 10 A B 25 C3' - C2' - C1' ANGL. DEV. = -5.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 113 ANGLE DEVIATIONS.
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 CYS A 112 -79.63 -84.63
REMARK 500 1 ASP A 143 13.53 -148.03
REMARK 500 1 LYS A 165 12.13 -142.34
REMARK 500 2 CYS A 112 -78.46 -84.18
REMARK 500 2 ASP A 143 16.85 -149.85
REMARK 500 3 CYS A 112 -78.82 -84.41
REMARK 500 3 ASP A 143 19.36 -151.28
REMARK 500 3 LYS A 165 12.38 -142.48
REMARK 500 3 SER A 171 4.81 -151.67
REMARK 500 4 CYS A 112 -78.56 -84.30
REMARK 500 4 ASP A 143 13.24 -146.06
REMARK 500 4 LYS A 165 13.51 -142.23
REMARK 500 4 GLN A 189 14.37 -149.45
REMARK 500 5 CYS A 112 -78.39 -84.95
REMARK 500 5 ASP A 143 11.71 -148.05
REMARK 500 5 SER A 171 5.75 -152.53
REMARK 500 6 CYS A 112 -79.82 -85.25
REMARK 500 6 ASP A 143 18.36 -151.90
REMARK 500 6 LYS A 165 12.11 -143.50
REMARK 500 7 CYS A 112 -78.41 -85.04
REMARK 500 7 ASP A 143 17.05 -148.93
REMARK 500 7 LYS A 165 13.52 -142.61
REMARK 500 7 SER A 171 8.34 -153.29
REMARK 500 8 CYS A 112 -78.48 -84.56
REMARK 500 8 ASP A 143 14.94 -153.54
REMARK 500 8 LYS A 165 13.12 -143.12
REMARK 500 8 SER A 171 6.55 -152.99
REMARK 500 9 CYS A 112 -78.42 -85.10
REMARK 500 9 ASP A 143 12.15 -145.13
REMARK 500 9 LYS A 165 12.01 -141.98
REMARK 500 10 CYS A 112 -79.18 -84.89
REMARK 500 10 ASP A 143 11.70 -145.92
REMARK 500 11 CYS A 112 -79.02 -85.59
REMARK 500 11 ASP A 143 13.40 -145.55
REMARK 500 11 LYS A 165 13.10 -142.08
REMARK 500 12 CYS A 112 -78.63 -84.90
REMARK 500 12 ASP A 143 10.79 -145.78
REMARK 500 12 LYS A 165 13.46 -145.22
REMARK 500 13 CYS A 112 -78.95 -83.92
REMARK 500 13 ASP A 143 12.21 -144.44
REMARK 500 13 LYS A 165 12.50 -142.77
REMARK 500 14 CYS A 112 -78.94 -84.79
REMARK 500 14 ASP A 143 14.47 -148.40
REMARK 500 15 CYS A 112 -78.87 -84.28
REMARK 500 15 ASP A 143 15.90 -150.24
REMARK 500 15 LYS A 165 12.30 -142.04
REMARK 500 16 CYS A 112 -78.43 -83.82
REMARK 500 16 ASP A 143 11.52 -148.30
REMARK 500 16 LYS A 165 13.23 -142.74
REMARK 500 17 CYS A 112 -78.82 -84.75
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 1 C B 4 0.06 SIDE CHAIN
REMARK 500 1 U B 7 0.07 SIDE CHAIN
REMARK 500 1 A B 8 0.06 SIDE CHAIN
REMARK 500 1 U B 24 0.06 SIDE CHAIN
REMARK 500 1 G B 26 0.14 SIDE CHAIN
REMARK 500 1 U B 27 0.08 SIDE CHAIN
REMARK 500 1 U B 33 0.07 SIDE CHAIN
REMARK 500 1 C B 35 0.07 SIDE CHAIN
REMARK 500 1 G B 37 0.07 SIDE CHAIN
REMARK 500 1 A B 43 0.06 SIDE CHAIN
REMARK 500 1 U B 51 0.16 SIDE CHAIN
REMARK 500 1 G B 52 0.07 SIDE CHAIN
REMARK 500 2 U B 7 0.08 SIDE CHAIN
REMARK 500 2 U B 27 0.07 SIDE CHAIN
REMARK 500 2 A B 28 0.07 SIDE CHAIN
REMARK 500 2 U B 33 0.07 SIDE CHAIN
REMARK 500 2 C B 35 0.07 SIDE CHAIN
REMARK 500 2 G B 37 0.07 SIDE CHAIN
REMARK 500 2 A B 43 0.06 SIDE CHAIN
REMARK 500 2 G B 50 0.06 SIDE CHAIN
REMARK 500 2 U B 51 0.14 SIDE CHAIN
REMARK 500 2 G B 52 0.09 SIDE CHAIN
REMARK 500 2 ARG A 145 0.08 SIDE CHAIN
REMARK 500 2 ARG A 154 0.10 SIDE CHAIN
REMARK 500 3 U B 7 0.08 SIDE CHAIN
REMARK 500 3 A B 8 0.06 SIDE CHAIN
REMARK 500 3 C B 10 0.06 SIDE CHAIN
REMARK 500 3 U B 27 0.06 SIDE CHAIN
REMARK 500 3 A B 28 0.07 SIDE CHAIN
REMARK 500 3 U B 33 0.07 SIDE CHAIN
REMARK 500 3 C B 35 0.07 SIDE CHAIN
REMARK 500 3 G B 37 0.07 SIDE CHAIN
REMARK 500 3 A B 43 0.05 SIDE CHAIN
REMARK 500 3 U B 51 0.17 SIDE CHAIN
REMARK 500 3 G B 52 0.08 SIDE CHAIN
REMARK 500 3 ARG A 145 0.13 SIDE CHAIN
REMARK 500 4 C B 4 0.06 SIDE CHAIN
REMARK 500 4 U B 7 0.09 SIDE CHAIN
REMARK 500 4 G B 26 0.07 SIDE CHAIN
REMARK 500 4 U B 27 0.09 SIDE CHAIN
REMARK 500 4 A B 28 0.07 SIDE CHAIN
REMARK 500 4 U B 33 0.07 SIDE CHAIN
REMARK 500 4 C B 35 0.07 SIDE CHAIN
REMARK 500 4 G B 37 0.07 SIDE CHAIN
REMARK 500 4 A B 43 0.05 SIDE CHAIN
REMARK 500 4 G B 50 0.06 SIDE CHAIN
REMARK 500 4 U B 51 0.14 SIDE CHAIN
REMARK 500 4 G B 52 0.09 SIDE CHAIN
REMARK 500 4 ARG A 145 0.11 SIDE CHAIN
REMARK 500 4 ARG A 154 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 246 PLANE DEVIATIONS.
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 191 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 107 SG
REMARK 620 2 CYS A 112 SG 112.2
REMARK 620 3 HIS A 125 NE2 118.1 101.9
REMARK 620 4 HIS A 129 NE2 113.4 109.0 101.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 192 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 137 SG
REMARK 620 2 CYS A 142 SG 108.6
REMARK 620 3 HIS A 155 NE2 108.4 112.5
REMARK 620 4 HIS A 159 NE2 111.5 109.5 106.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 193 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 164 SG
REMARK 620 2 CYS A 170 SG 107.5
REMARK 620 3 HIS A 183 NE2 110.5 112.8
REMARK 620 4 HIS A 188 NE2 101.2 112.4 111.7
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 191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 193
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TF3 RELATED DB: PDB
REMARK 900 RELATED ID: 1ZNF RELATED DB: PDB
DBREF 2HGH A 105 190 UNP P03001 TF3A_XENLA 127 212
DBREF 2HGH B 1 55 PDB 2HGH 2HGH 1 55
SEQADV 2HGH MET A 104 UNP P03001 INITIATING METHIONINE
SEQRES 1 B 55 G G G C C A U A C C U C U
SEQRES 2 B 55 U G G G C C U G G U U A G
SEQRES 3 B 55 U A C C U C U U C G G U G
SEQRES 4 B 55 G G A A U A C C A G G U G
SEQRES 5 B 55 C C C
SEQRES 1 A 87 MET TYR VAL CYS HIS PHE GLU ASN CYS GLY LYS ALA PHE
SEQRES 2 A 87 LYS LYS HIS ASN GLN LEU LYS VAL HIS GLN PHE SER HIS
SEQRES 3 A 87 THR GLN GLN LEU PRO TYR GLU CYS PRO HIS GLU GLY CYS
SEQRES 4 A 87 ASP LYS ARG PHE SER LEU PRO SER ARG LEU LYS ARG HIS
SEQRES 5 A 87 GLU LYS VAL HIS ALA GLY TYR PRO CYS LYS LYS ASP ASP
SEQRES 6 A 87 SER CYS SER PHE VAL GLY LYS THR TRP THR LEU TYR LEU
SEQRES 7 A 87 LYS HIS VAL ALA GLU CYS HIS GLN ASP
HET ZN A 191 1
HET ZN A 192 1
HET ZN A 193 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 3(ZN 2+)
HELIX 1 1 LYS A 118 GLN A 131 1 14
HELIX 2 2 LEU A 148 GLY A 161 1 14
HELIX 3 3 THR A 176 HIS A 188 1 13
SHEET 1 A 2 TYR A 105 VAL A 106 0
SHEET 2 A 2 ALA A 115 PHE A 116 -1 O PHE A 116 N TYR A 105
SHEET 1 B 2 TYR A 135 GLU A 136 0
SHEET 2 B 2 ARG A 145 PHE A 146 -1 O PHE A 146 N TYR A 135
SHEET 1 C 2 TYR A 162 PRO A 163 0
SHEET 2 C 2 VAL A 173 GLY A 174 -1 O GLY A 174 N TYR A 162
LINK SG CYS A 107 ZN ZN A 191 1555 1555 2.28
LINK SG CYS A 112 ZN ZN A 191 1555 1555 2.24
LINK NE2 HIS A 125 ZN ZN A 191 1555 1555 2.06
LINK NE2 HIS A 129 ZN ZN A 191 1555 1555 2.06
LINK SG CYS A 137 ZN ZN A 192 1555 1555 2.27
LINK SG CYS A 142 ZN ZN A 192 1555 1555 2.27
LINK NE2 HIS A 155 ZN ZN A 192 1555 1555 2.06
LINK NE2 HIS A 159 ZN ZN A 192 1555 1555 2.06
LINK SG CYS A 164 ZN ZN A 193 1555 1555 2.25
LINK SG CYS A 170 ZN ZN A 193 1555 1555 2.27
LINK NE2 HIS A 183 ZN ZN A 193 1555 1555 2.07
LINK NE2 HIS A 188 ZN ZN A 193 1555 1555 2.06
SITE 1 AC1 4 CYS A 107 CYS A 112 HIS A 125 HIS A 129
SITE 1 AC2 4 CYS A 137 CYS A 142 HIS A 155 HIS A 159
SITE 1 AC3 4 CYS A 164 CYS A 170 HIS A 183 HIS A 188
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 9 2 Bytes