Header list of 1z60.pdb file
Complete list - 10 20 Bytes
HEADER TRANSCRIPTION 21-MAR-05 1Z60
TITLE SOLUTION STRUCTURE OF THE CARBOXY-TERMINAL DOMAIN OF HUMAN TFIIH P44
TITLE 2 SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TFIIH BASAL TRANSCRIPTION FACTOR COMPLEX P44 SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: TFIIH P44 SUBUNIT, BASIC TRANSCRIPTION FACTOR 2 44 KDA
COMPND 6 SUBUNIT, BTF2-P44, GENERAL TRANSCRIPTION FACTOR IIH POLYPEPTIDE 2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS BASIC TRANSCRIPTION FACTOR, ZINC BINDING PROTEIN, RING FINGER,
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR E.KELLENBERGER,C.DOMINGUEZ,S.FRIBOURG,E.WASIELEWSKI,D.MORAS,
AUTHOR 2 A.POTERSZMAN,R.BOELENS,B.KIEFFER
REVDAT 4 10-NOV-21 1Z60 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1Z60 1 VERSN
REVDAT 2 19-JUL-05 1Z60 1 JRNL
REVDAT 1 12-APR-05 1Z60 0
SPRSDE 12-APR-05 1Z60 1E53
JRNL AUTH E.KELLENBERGER,C.DOMINGUEZ,S.FRIBOURG,E.WASIELEWSKI,D.MORAS,
JRNL AUTH 2 A.POTERSZMAN,R.BOELENS,B.KIEFFER
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF TFIIH P44
JRNL TITL 2 SUBUNIT REVEALS A NOVEL TYPE OF C4C4 RING DOMAIN INVOLVED IN
JRNL TITL 3 PROTEIN-PROTEIN INTERACTIONS.
JRNL REF J.BIOL.CHEM. V. 280 20785 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15790571
JRNL DOI 10.1074/JBC.M412999200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.FRIBOURG,E.KELLENBERGER,H.ROGNIAUX,A.POTERSZMAN,
REMARK 1 AUTH 2 A.VAN DORSSELAER,J.C.THIERRY,J.M.EGLY,D.MORAS,B.KIEFFER
REMARK 1 TITL STRUCTURAL CHARACTERIZATION OF THE CYSTEINE-RICH DOMAIN OF
REMARK 1 TITL 2 TFIIH P44 SUBUNIT
REMARK 1 REF J.BIOL.CHEM. V. 275 31963 2000
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 10882739
REMARK 1 DOI 10.1074/JBC.M004960200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA / CNS 1.2., XPLOR-NIH 2.0.6
REMARK 3 AUTHORS : NILGES (ARIA / CNS),
REMARK 3 C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AUTOMATED ASSIGNMENT OF THE NOE WAS
REMARK 3 PERFORMED, THE STRUCTURES ARE BASED ON 1294 UNAMBIGUOUS NOE-
REMARK 3 DERIVED DISTANCE CONSTRAINTS, 32 DIHEDRAL ANGLE RESTRAINTS AND
REMARK 3 17 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. GEOMETRY OF THE ZINC
REMARK 3 BINDING SITE II IS DISTORDED DUE TO CONFORMATIONAL EXCHANGE
REMARK 3 AVERAGING.
REMARK 4
REMARK 4 1Z60 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032341.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 303
REMARK 210 PH : 7; 7
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM P44 U-15N; 20MM DEUTERATED
REMARK 210 TRISHCL BUFFER, 20MM NACL AND
REMARK 210 0.5MM DTT; 0.5MM P44; 20MM
REMARK 210 DEUTERATED TRISHCL BUFFER, 20MM
REMARK 210 NACL AND 0.5MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-EDITED TOCSY AND NOESY;
REMARK 210 2D TOCSY AND NOESY; HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.2, XWINNMR 2.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 113CD-1H HSQC SPECTRUM WAS RECORDED USING A BROADBAND Z
REMARK 210 -GRADIENT PROBE AT 293 K
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 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 1 GLN A 364 C ASN A 365 N -0.182
REMARK 500 1 ASN A 365 N ASN A 365 CA -0.138
REMARK 500 1 CYS A 368 CB CYS A 368 SG -0.158
REMARK 500 2 PHE A 344 CA PHE A 344 CB -0.144
REMARK 500 2 GLN A 364 C ASN A 365 N -0.140
REMARK 500 2 HIS A 380 CG HIS A 380 CD2 0.074
REMARK 500 3 GLN A 364 C ASN A 365 N -0.168
REMARK 500 3 ASN A 365 N ASN A 365 CA -0.135
REMARK 500 4 CYS A 368 CB CYS A 368 SG -0.113
REMARK 500 5 CYS A 363 C CYS A 363 O -0.125
REMARK 500 5 GLN A 364 N GLN A 364 CA 0.145
REMARK 500 5 GLN A 364 CB GLN A 364 CG -0.178
REMARK 500 6 CYS A 363 CA CYS A 363 CB -0.097
REMARK 500 6 PHE A 367 CB PHE A 367 CG -0.123
REMARK 500 7 CYS A 368 CB CYS A 368 SG -0.100
REMARK 500 8 PHE A 344 CA PHE A 344 CB -0.138
REMARK 500 8 GLN A 364 C ASN A 365 N -0.141
REMARK 500 9 GLN A 364 N GLN A 364 CA 0.164
REMARK 500 9 ASN A 365 N ASN A 365 CA -0.121
REMARK 500 10 TYR A 346 CE2 TYR A 346 CD2 -0.133
REMARK 500 10 GLN A 364 C ASN A 365 N -0.175
REMARK 500 10 ASN A 365 N ASN A 365 CA -0.149
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 CYS A 368 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 1 CYS A 368 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 1 ASP A 370 CB - CA - C ANGL. DEV. = -19.8 DEGREES
REMARK 500 1 CYS A 371 CB - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 2 CYS A 348 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 2 PHE A 367 CB - CG - CD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 2 CYS A 368 CB - CA - C ANGL. DEV. = -13.8 DEGREES
REMARK 500 2 CYS A 368 CA - CB - SG ANGL. DEV. = 8.7 DEGREES
REMARK 500 2 ASP A 370 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 2 CYS A 371 CB - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 4 CYS A 363 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 4 CYS A 368 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 4 ASP A 370 CB - CA - C ANGL. DEV. = -21.7 DEGREES
REMARK 500 4 ASP A 370 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 4 CYS A 371 CB - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 5 PHE A 331 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 TYR A 339 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 5 TYR A 339 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 5 TYR A 346 N - CA - CB ANGL. DEV. = -14.4 DEGREES
REMARK 500 5 TYR A 346 CA - CB - CG ANGL. DEV. = 12.3 DEGREES
REMARK 500 5 CYS A 363 CB - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 5 CYS A 363 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 5 GLN A 364 N - CA - CB ANGL. DEV. = 13.3 DEGREES
REMARK 500 5 CYS A 368 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 6 TYR A 339 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 6 TYR A 339 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 6 CYS A 360 N - CA - CB ANGL. DEV. = 10.2 DEGREES
REMARK 500 7 PHE A 331 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 7 CYS A 360 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 7 PHE A 367 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 7 PHE A 367 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 7 CYS A 368 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 8 CYS A 360 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 9 TYR A 346 CB - CG - CD2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 9 CYS A 360 N - CA - CB ANGL. DEV. = 9.5 DEGREES
REMARK 500 10 PHE A 344 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 10 TYR A 346 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 10 TYR A 346 CB - CG - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 10 TYR A 346 CB - CG - CD1 ANGL. DEV. = 5.7 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 GLU A 342 108.76 -59.18
REMARK 500 1 GLN A 355 -47.61 -157.30
REMARK 500 1 GLN A 364 -19.78 56.16
REMARK 500 1 ASP A 377 -65.97 -94.16
REMARK 500 1 LEU A 379 -109.38 -116.95
REMARK 500 2 GLN A 355 -49.06 -156.67
REMARK 500 2 GLN A 364 -20.60 24.29
REMARK 500 2 ASP A 377 -80.70 -91.47
REMARK 500 2 SER A 381 -43.58 -178.80
REMARK 500 3 ALA A 330 -83.15 -52.18
REMARK 500 3 LEU A 352 -122.68 -88.55
REMARK 500 3 GLN A 355 -32.08 177.93
REMARK 500 3 GLN A 364 -20.30 50.60
REMARK 500 3 LEU A 379 -103.86 -144.39
REMARK 500 4 PHE A 344 -169.84 44.57
REMARK 500 4 GLN A 355 -47.89 -168.79
REMARK 500 4 GLN A 364 -5.88 52.58
REMARK 500 4 ASP A 377 -143.47 -99.19
REMARK 500 4 HIS A 380 178.51 152.36
REMARK 500 5 LYS A 353 22.59 -67.40
REMARK 500 5 GLN A 355 -43.10 -173.96
REMARK 500 5 HIS A 376 -131.13 -170.57
REMARK 500 5 HIS A 380 175.25 -54.22
REMARK 500 6 ASP A 329 -40.49 -157.17
REMARK 500 6 GLN A 332 164.42 179.68
REMARK 500 6 GLN A 355 -43.47 -158.88
REMARK 500 6 ALA A 361 -11.05 67.12
REMARK 500 6 VAL A 362 -67.93 -129.43
REMARK 500 6 GLN A 364 -1.20 52.54
REMARK 500 6 ASP A 377 -27.54 85.15
REMARK 500 6 HIS A 380 -179.10 156.13
REMARK 500 7 ARG A 343 -134.46 68.29
REMARK 500 7 PHE A 344 141.22 44.53
REMARK 500 7 GLN A 355 -34.14 -162.51
REMARK 500 7 ALA A 361 -15.55 66.42
REMARK 500 7 GLN A 364 -5.98 58.27
REMARK 500 7 SER A 378 -12.61 167.95
REMARK 500 7 HIS A 380 173.28 161.88
REMARK 500 8 PHE A 331 64.37 39.69
REMARK 500 8 CYS A 348 -40.22 -131.13
REMARK 500 8 GLU A 351 135.42 111.28
REMARK 500 8 GLN A 355 -58.20 -163.58
REMARK 500 8 ALA A 361 -17.60 52.78
REMARK 500 8 CYS A 363 88.12 -169.87
REMARK 500 8 GLN A 364 -23.59 80.28
REMARK 500 8 ASP A 377 -69.89 -95.85
REMARK 500 8 LEU A 379 -142.94 -110.90
REMARK 500 9 PRO A 335 24.12 -76.52
REMARK 500 9 LEU A 336 -47.87 74.33
REMARK 500 9 GLN A 355 -53.02 -163.85
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 5 TYR A 346 0.08 SIDE CHAIN
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 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 345 SG
REMARK 620 2 CYS A 348 SG 102.6
REMARK 620 3 CYS A 368 SG 92.0 123.4
REMARK 620 4 ASP A 370 OD2 168.8 78.7 78.3
REMARK 620 5 CYS A 371 SG 100.1 113.1 117.6 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 360 SG
REMARK 620 2 CYS A 363 SG 95.9
REMARK 620 3 CYS A 382 SG 115.9 105.3
REMARK 620 4 CYS A 385 SG 115.5 106.5 114.8
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
DBREF 1Z60 A 328 386 UNP Q13888 TF2H2_HUMAN 328 386
SEQADV 1Z60 SER A 381 UNP Q13888 CYS 381 ENGINEERED MUTATION
SEQRES 1 A 59 LEU ASP ALA PHE GLN GLU ILE PRO LEU GLU GLU TYR ASN
SEQRES 2 A 59 GLY GLU ARG PHE CYS TYR GLY CYS GLN GLY GLU LEU LYS
SEQRES 3 A 59 ASP GLN HIS VAL TYR VAL CYS ALA VAL CYS GLN ASN VAL
SEQRES 4 A 59 PHE CYS VAL ASP CYS ASP VAL PHE VAL HIS ASP SER LEU
SEQRES 5 A 59 HIS SER CYS PRO GLY CYS ILE
HET ZN A 1 1
HET ZN A 2 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 LEU A 336 ASN A 340 1 5
HELIX 2 2 CYS A 368 PHE A 374 1 7
SHEET 1 A 2 GLU A 333 PRO A 335 0
SHEET 2 A 2 HIS A 356 TYR A 358 -1 O VAL A 357 N ILE A 334
SHEET 1 B 2 PHE A 344 CYS A 345 0
SHEET 2 B 2 GLY A 350 GLU A 351 -1 O GLY A 350 N CYS A 345
LINK ZN ZN A 1 SG CYS A 345 1555 1555 2.22
LINK ZN ZN A 1 SG CYS A 348 1555 1555 2.35
LINK ZN ZN A 1 SG CYS A 368 1555 1555 2.35
LINK ZN ZN A 1 OD2 ASP A 370 1555 1555 2.02
LINK ZN ZN A 1 SG CYS A 371 1555 1555 2.36
LINK ZN ZN A 2 SG CYS A 360 1555 1555 2.32
LINK ZN ZN A 2 SG CYS A 363 1555 1555 2.25
LINK ZN ZN A 2 SG CYS A 382 1555 1555 2.32
LINK ZN ZN A 2 SG CYS A 385 1555 1555 2.35
SITE 1 AC1 5 CYS A 345 CYS A 348 CYS A 368 ASP A 370
SITE 2 AC1 5 CYS A 371
SITE 1 AC2 4 CYS A 360 CYS A 363 CYS A 382 CYS A 385
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 - 10 20 Bytes