Header list of 1r8u.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION/TRANSCRIPTION ACTIVATOR 28-OCT-03 1R8U
TITLE NMR STRUCTURE OF CBP TAZ1/CITED2 COMPLEX
CAVEAT 1R8U CHIRALITY ERROR AT CYS379B MODEL 13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CBP/P300-INTERACTING TRANSACTIVATOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CITED2 CAD (RESIDUES 200-269);
COMPND 5 SYNONYM: MSG-RELATED PROTEIN 1, MRG1 PROTEIN, P35SRJ, CITED2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CREB-BINDING PROTEIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: CBP TAZ1 (RESIDUES 334-433);
COMPND 11 SYNONYM: CBP;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CITED2, MRG1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS ZINC-BINDING MOTIFS, PROTEIN-PROTEIN COMPLEX, TAZ ZINC FINGER,
KEYWDS 2 TRANSCRIPTION-TRANSCRIPTION ACTIVATOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.N.DE GUZMAN,M.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
REVDAT 3 02-MAR-22 1R8U 1 REMARK LINK
REVDAT 2 24-FEB-09 1R8U 1 VERSN
REVDAT 1 23-MAR-04 1R8U 0
JRNL AUTH R.N.DE GUZMAN,M.A.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
JRNL TITL INTERACTION OF THE TAZ1 DOMAIN OF THE CREB-BINDING PROTEIN
JRNL TITL 2 WITH THE ACTIVATION DOMAIN OF CITED2: REGULATION BY
JRNL TITL 3 COMPETITION BETWEEN INTRINSICALLY UNSTRUCTURED LIGANDS FOR
JRNL TITL 4 NON-IDENTICAL BINDING SITES.
JRNL REF J.BIOL.CHEM. V. 279 3042 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14594809
JRNL DOI 10.1074/JBC.M310348200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2003, AMBER 7.0
REMARK 3 AUTHORS : DELAGLIO, BAX (NMRPIPE), DAVID CASE ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R8U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020580.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298
REMARK 210 PH : 6.8; 6.8; 6.8; 6.8
REMARK 210 IONIC STRENGTH : 16 MM; 16 MM; 16 MM; 16 MM
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM N15 TAZ1, UNLABELED
REMARK 210 CITED2, 90% H2O, 10% D2O; 0.5MM
REMARK 210 UNLABELED TAZ1, N15 CITED2, 90%
REMARK 210 H2O, 10% D2O; 0.5MM C13,N15 TAZ1,
REMARK 210 UNLABELED CITED2, 90% H2O, 10%
REMARK 210 D2O; 0.5MM UNLABELED TAZ1,
REMARK 210 CITED2, 90% H2O,10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRDRAW 4.1.3., DYANA 1.5
REMARK 210 METHOD USED : AMBER SIMULATED ANNEALING AND
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
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: A, B
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 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 B 369 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ARG B 385 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 267 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 ARG B 377 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 4 ARG B 377 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 5 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 6 ARG B 369 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 6 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 7 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 7 ARG B 350 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 7 ARG B 369 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 8 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 8 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 9 ARG B 369 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 9 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 10 ARG B 377 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 11 ARG B 350 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 11 ARG B 377 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 11 ARG B 412 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 13 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 15 ARG B 368 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 15 ARG B 369 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 15 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 16 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 17 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 17 ARG B 368 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 17 ARG B 369 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 17 ARG B 385 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 18 ARG B 368 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 18 ARG B 369 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 18 ARG B 439 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 19 ARG B 350 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 19 ARG B 369 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 20 ARG B 368 NE - CZ - NH1 ANGL. DEV. = 3.5 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 241 -41.39 -142.55
REMARK 500 1 PHE A 255 -19.70 -37.76
REMARK 500 1 THR A 257 -174.11 -68.66
REMARK 500 1 PHE A 259 39.36 -70.79
REMARK 500 1 PRO B 347 -166.97 -100.16
REMARK 500 1 ASN B 373 -28.22 -145.88
REMARK 500 2 PHE A 255 -49.36 -20.54
REMARK 500 2 ASP A 258 21.12 -146.30
REMARK 500 2 ARG A 267 -4.37 -58.55
REMARK 500 2 ALA B 345 58.72 -144.46
REMARK 500 2 ASN B 373 -18.86 -47.03
REMARK 500 2 GLU B 375 15.73 -144.09
REMARK 500 2 ALA B 378 -150.79 -120.48
REMARK 500 2 CYS B 421 -177.15 -69.01
REMARK 500 3 PHE A 253 74.90 -150.93
REMARK 500 3 PHE A 255 -41.81 -28.22
REMARK 500 3 PRO A 265 170.13 -55.46
REMARK 500 3 THR B 344 3.48 -65.31
REMARK 500 3 ASN B 373 -30.19 -142.64
REMARK 500 3 GLU B 375 20.02 -151.54
REMARK 500 3 THR B 422 -8.03 -140.42
REMARK 500 4 LYS A 241 -45.42 -133.65
REMARK 500 4 PHE A 255 -23.15 -35.18
REMARK 500 4 THR B 344 -44.83 -153.23
REMARK 500 4 ASN B 373 -33.54 -147.58
REMARK 500 4 GLU B 375 -39.60 -148.73
REMARK 500 4 VAL B 376 55.95 32.01
REMARK 500 4 ASP B 437 10.88 -61.08
REMARK 500 5 LYS A 241 -41.42 -134.43
REMARK 500 5 PHE A 255 -23.36 -35.32
REMARK 500 5 ARG A 267 8.39 -64.48
REMARK 500 5 ASN B 373 -18.57 -148.06
REMARK 500 5 GLU B 375 15.32 -143.81
REMARK 500 5 SER B 380 11.82 -140.60
REMARK 500 6 LYS A 241 -44.36 -132.68
REMARK 500 6 PHE A 255 -25.19 -39.68
REMARK 500 6 PRO B 347 -167.94 -100.15
REMARK 500 6 ASN B 373 -30.09 -148.60
REMARK 500 6 GLU B 375 25.15 -150.64
REMARK 500 6 GLN B 398 12.94 -146.09
REMARK 500 6 ASP B 425 38.51 -72.01
REMARK 500 7 PHE A 255 -35.93 -23.35
REMARK 500 7 ASP A 258 -4.50 -144.79
REMARK 500 7 PHE A 259 39.52 -78.07
REMARK 500 7 SER A 266 -40.06 -138.80
REMARK 500 7 ASN B 373 -29.29 -143.69
REMARK 500 7 GLU B 375 20.27 -149.83
REMARK 500 7 VAL B 376 92.29 -63.95
REMARK 500 7 THR B 422 -14.23 -140.50
REMARK 500 8 PHE A 255 -28.00 -35.10
REMARK 500
REMARK 500 THIS ENTRY HAS 151 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 ARG B 350 0.08 SIDE CHAIN
REMARK 500 1 HIS B 417 0.13 SIDE CHAIN
REMARK 500 2 HIS B 417 0.11 SIDE CHAIN
REMARK 500 3 HIS B 417 0.10 SIDE CHAIN
REMARK 500 4 ARG B 369 0.09 SIDE CHAIN
REMARK 500 4 HIS B 417 0.10 SIDE CHAIN
REMARK 500 5 HIS B 417 0.11 SIDE CHAIN
REMARK 500 6 ARG B 412 0.08 SIDE CHAIN
REMARK 500 6 HIS B 417 0.11 SIDE CHAIN
REMARK 500 7 HIS B 417 0.10 SIDE CHAIN
REMARK 500 8 HIS B 417 0.10 SIDE CHAIN
REMARK 500 9 HIS B 417 0.11 SIDE CHAIN
REMARK 500 10 HIS B 417 0.10 SIDE CHAIN
REMARK 500 12 HIS B 417 0.11 SIDE CHAIN
REMARK 500 13 HIS B 362 0.08 SIDE CHAIN
REMARK 500 13 HIS B 417 0.12 SIDE CHAIN
REMARK 500 15 HIS B 417 0.10 SIDE CHAIN
REMARK 500 17 HIS B 417 0.11 SIDE CHAIN
REMARK 500 18 HIS B 417 0.11 SIDE CHAIN
REMARK 500 19 HIS B 417 0.11 SIDE CHAIN
REMARK 500 20 HIS B 417 0.12 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 B 440 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 362 NE2
REMARK 620 2 CYS B 366 SG 109.6
REMARK 620 3 CYS B 379 SG 107.5 107.4
REMARK 620 4 CYS B 384 SG 110.8 111.5 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 441 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 393 NE2
REMARK 620 2 CYS B 397 SG 107.8
REMARK 620 3 CYS B 403 SG 109.4 106.9
REMARK 620 4 CYS B 408 SG 110.5 110.2 111.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 442 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 417 NE2
REMARK 620 2 CYS B 421 SG 108.8
REMARK 620 3 CYS B 426 SG 106.2 112.9
REMARK 620 4 CYS B 429 SG 111.6 105.7 111.7
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 B 440
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 442
DBREF 1R8U A 220 269 UNP Q99967 CIT2_HUMAN 220 269
DBREF 1R8U B 340 439 GB 19547885 AAL87531 334 433
SEQRES 1 A 50 THR ASP PHE ILE ASP GLU GLU VAL LEU MET SER LEU VAL
SEQRES 2 A 50 ILE GLU MET GLY LEU ASP ARG ILE LYS GLU LEU PRO GLU
SEQRES 3 A 50 LEU TRP LEU GLY GLN ASN GLU PHE ASP PHE MET THR ASP
SEQRES 4 A 50 PHE VAL CYS LYS GLN GLN PRO SER ARG VAL SER
SEQRES 1 B 100 ALA THR GLY PRO THR ALA ASP PRO GLU LYS ARG LYS LEU
SEQRES 2 B 100 ILE GLN GLN GLN LEU VAL LEU LEU LEU HIS ALA HIS LYS
SEQRES 3 B 100 CYS GLN ARG ARG GLU GLN ALA ASN GLY GLU VAL ARG ALA
SEQRES 4 B 100 CYS SER LEU PRO HIS CYS ARG THR MET LYS ASN VAL LEU
SEQRES 5 B 100 ASN HIS MET THR HIS CYS GLN ALA GLY LYS ALA CYS GLN
SEQRES 6 B 100 VAL ALA HIS CYS ALA SER SER ARG GLN ILE ILE SER HIS
SEQRES 7 B 100 TRP LYS ASN CYS THR ARG HIS ASP CYS PRO VAL CYS LEU
SEQRES 8 B 100 PRO LEU LYS ASN ALA SER ASP LYS ARG
HET ZN B 440 1
HET ZN B 441 1
HET ZN B 442 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 3(ZN 2+)
HELIX 1 1 ASP A 224 GLY A 236 1 13
HELIX 2 2 LEU A 237 ILE A 240 5 4
HELIX 3 3 GLN A 250 ASP A 254 5 5
HELIX 4 4 PRO A 265 SER A 269 5 5
HELIX 5 5 PRO B 347 ALA B 372 1 26
HELIX 6 6 HIS B 383 THR B 395 1 13
HELIX 7 7 VAL B 405 THR B 422 1 18
HELIX 8 8 VAL B 428 SER B 436 1 9
HELIX 9 9 ASP B 437 ARG B 439 5 3
LINK NE2 HIS B 362 ZN ZN B 440 1555 1555 2.09
LINK SG CYS B 366 ZN ZN B 440 1555 1555 2.30
LINK SG CYS B 379 ZN ZN B 440 1555 1555 2.29
LINK SG CYS B 384 ZN ZN B 440 1555 1555 2.30
LINK NE2 HIS B 393 ZN ZN B 441 1555 1555 2.09
LINK SG CYS B 397 ZN ZN B 441 1555 1555 2.29
LINK SG CYS B 403 ZN ZN B 441 1555 1555 2.29
LINK SG CYS B 408 ZN ZN B 441 1555 1555 2.30
LINK NE2 HIS B 417 ZN ZN B 442 1555 1555 2.07
LINK SG CYS B 421 ZN ZN B 442 1555 1555 2.30
LINK SG CYS B 426 ZN ZN B 442 1555 1555 2.28
LINK SG CYS B 429 ZN ZN B 442 1555 1555 2.30
SITE 1 AC1 4 HIS B 362 CYS B 366 CYS B 379 CYS B 384
SITE 1 AC2 4 HIS B 393 CYS B 397 CYS B 403 CYS B 408
SITE 1 AC3 4 HIS B 417 CYS B 421 CYS B 426 CYS B 429
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