HEADER TRANSFERASE 05-JUN-16 5B75
TITLE CRYSTAL STRUCTURE OF MOZ DOUBLE PHD FINGER IN COMPLEX WITH HISTONE H3
TITLE 2 BUTYRYLATION AT K14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE KAT6A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 194-323;
COMPND 5 SYNONYM: MOZ;
COMPND 6 EC: 2.3.1.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE H3;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 2-26;
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: MOZ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS MOZ DOUBLE PHD FINGER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,X.XIONG
REVDAT 3 08-NOV-23 5B75 1 REMARK
REVDAT 2 30-NOV-16 5B75 1 JRNL
REVDAT 1 26-OCT-16 5B75 0
JRNL AUTH X.XIONG,T.PANCHENKO,S.YANG,S.ZHAO,P.YAN,W.ZHANG,W.XIE,Y.LI,
JRNL AUTH 2 Y.ZHAO,C.D.ALLIS,H.LI
JRNL TITL SELECTIVE RECOGNITION OF HISTONE CROTONYLATION BY DOUBLE PHD
JRNL TITL 2 FINGERS OF MOZ AND DPF2
JRNL REF NAT.CHEM.BIOL. V. 12 1111 2016
JRNL REFN ESSN 1552-4469
JRNL PMID 27775714
JRNL DOI 10.1038/NCHEMBIO.2218
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 19643
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 997
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.8735 - 3.2592 0.99 2820 138 0.1613 0.1920
REMARK 3 2 3.2592 - 2.5874 1.00 2712 142 0.1810 0.1951
REMARK 3 3 2.5874 - 2.2604 1.00 2648 149 0.1611 0.1958
REMARK 3 4 2.2604 - 2.0538 1.00 2645 151 0.1594 0.1597
REMARK 3 5 2.0538 - 1.9066 1.00 2640 139 0.1750 0.2239
REMARK 3 6 1.9066 - 1.7942 1.00 2643 140 0.1892 0.2162
REMARK 3 7 1.7942 - 1.7044 0.97 2538 138 0.2086 0.2342
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 1139
REMARK 3 ANGLE : 1.000 1528
REMARK 3 CHIRALITY : 0.054 162
REMARK 3 PLANARITY : 0.008 200
REMARK 3 DIHEDRAL : 13.922 722
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5B75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1300000653.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19643
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 29.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4LLB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 4000, LITHIUM
REMARK 280 SULFATE, TRIS, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.83850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.09550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.06100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.09550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.83850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.06100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 193
REMARK 465 ARG A 313
REMARK 465 LYS A 314
REMARK 465 LYS A 315
REMARK 465 GLY A 316
REMARK 465 ARG A 317
REMARK 465 LYS A 318
REMARK 465 LEU A 319
REMARK 465 LEU A 320
REMARK 465 GLN A 321
REMARK 465 LYS A 322
REMARK 465 LYS A 323
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HD22 ASN A 235 O HOH A 505 1.58
REMARK 500 O HOH A 608 O HOH A 613 1.95
REMARK 500 O HOH A 600 O HOH A 621 1.96
REMARK 500 O1 SO4 B 101 O HOH B 201 2.06
REMARK 500 O HOH A 527 O HOH A 624 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 568 O HOH A 577 4445 1.98
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 LYS A 198 3.17 -64.53
REMARK 500 PRO A 207 37.45 -83.30
REMARK 500 GLN A 271 -68.61 -102.80
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 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 209 SG
REMARK 620 2 CYS A 212 SG 111.3
REMARK 620 3 HIS A 238 ND1 99.6 98.0
REMARK 620 4 CYS A 241 SG 111.7 113.4 121.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 230 SG
REMARK 620 2 CYS A 233 SG 105.6
REMARK 620 3 CYS A 259 SG 112.0 115.8
REMARK 620 4 CYS A 262 SG 108.1 114.0 101.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 265 SG
REMARK 620 2 CYS A 268 SG 109.6
REMARK 620 3 HIS A 289 ND1 103.8 98.1
REMARK 620 4 CYS A 292 SG 116.6 115.1 111.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 281 SG
REMARK 620 2 CYS A 284 SG 106.4
REMARK 620 3 CYS A 307 SG 108.5 112.2
REMARK 620 4 CYS A 310 SG 112.2 106.0 111.6
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 101
DBREF 5B75 A 194 323 UNP Q92794 KAT6A_HUMAN 194 323
DBREF 5B75 B 1 25 UNP K7EMV3 K7EMV3_HUMAN 2 26
SEQADV 5B75 SER A 193 UNP Q92794 EXPRESSION TAG
SEQRES 1 A 131 SER LEU PRO HIS GLU LYS ASP LYS PRO VAL ALA GLU PRO
SEQRES 2 A 131 ILE PRO ILE CYS SER PHE CYS LEU GLY THR LYS GLU GLN
SEQRES 3 A 131 ASN ARG GLU LYS LYS PRO GLU GLU LEU ILE SER CYS ALA
SEQRES 4 A 131 ASP CYS GLY ASN SER GLY HIS PRO SER CYS LEU LYS PHE
SEQRES 5 A 131 SER PRO GLU LEU THR VAL ARG VAL LYS ALA LEU ARG TRP
SEQRES 6 A 131 GLN CYS ILE GLU CYS LYS THR CYS SER SER CYS ARG ASP
SEQRES 7 A 131 GLN GLY LYS ASN ALA ASP ASN MET LEU PHE CYS ASP SER
SEQRES 8 A 131 CYS ASP ARG GLY PHE HIS MET GLU CYS CYS ASP PRO PRO
SEQRES 9 A 131 LEU THR ARG MET PRO LYS GLY MET TRP ILE CYS GLN ILE
SEQRES 10 A 131 CYS ARG PRO ARG LYS LYS GLY ARG LYS LEU LEU GLN LYS
SEQRES 11 A 131 LYS
SEQRES 1 B 25 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 B 25 BTK ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
MODRES 5B75 BTK B 14 LYS MODIFIED RESIDUE
HET BTK B 14 32
HET ZN A 401 1
HET ZN A 402 1
HET ZN A 403 1
HET ZN A 404 1
HET SO4 B 101 5
HETNAM BTK N~6~-BUTANOYL-L-LYSINE
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 2 BTK C10 H20 N2 O3
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *188(H2 O)
HELIX 1 AA1 HIS A 238 LYS A 243 1 6
HELIX 2 AA2 SER A 245 ALA A 254 1 10
HELIX 3 AA3 ASN A 274 ASN A 277 5 4
HELIX 4 AA4 HIS A 289 CYS A 293 5 5
HELIX 5 AA5 LYS B 4 GLY B 12 1 9
HELIX 6 AA6 PRO B 16 ALA B 25 1 10
SHEET 1 AA1 2 ILE A 228 SER A 229 0
SHEET 2 AA1 2 SER A 236 GLY A 237 -1 O GLY A 237 N ILE A 228
SHEET 1 AA2 3 GLY A 287 PHE A 288 0
SHEET 2 AA2 3 LEU A 279 PHE A 280 -1 N LEU A 279 O PHE A 288
SHEET 3 AA2 3 ARG B 2 THR B 3 -1 O ARG B 2 N PHE A 280
LINK C GLY B 13 N BTK B 14 1555 1555 1.32
LINK C BTK B 14 N ALA B 15 1555 1555 1.33
LINK SG CYS A 209 ZN ZN A 403 1555 1555 2.32
LINK SG CYS A 212 ZN ZN A 403 1555 1555 2.34
LINK SG CYS A 230 ZN ZN A 404 1555 1555 2.37
LINK SG CYS A 233 ZN ZN A 404 1555 1555 2.31
LINK ND1 HIS A 238 ZN ZN A 403 1555 1555 2.08
LINK SG CYS A 241 ZN ZN A 403 1555 1555 2.29
LINK SG CYS A 259 ZN ZN A 404 1555 1555 2.35
LINK SG CYS A 262 ZN ZN A 404 1555 1555 2.35
LINK SG CYS A 265 ZN ZN A 402 1555 1555 2.35
LINK SG CYS A 268 ZN ZN A 402 1555 1555 2.31
LINK SG CYS A 281 ZN ZN A 401 1555 1555 2.31
LINK SG CYS A 284 ZN ZN A 401 1555 1555 2.37
LINK ND1 HIS A 289 ZN ZN A 402 1555 1555 2.14
LINK SG CYS A 292 ZN ZN A 402 1555 1555 2.31
LINK SG CYS A 307 ZN ZN A 401 1555 1555 2.32
LINK SG CYS A 310 ZN ZN A 401 1555 1555 2.33
CISPEP 1 ASP A 294 PRO A 295 0 2.59
SITE 1 AC1 4 CYS A 281 CYS A 284 CYS A 307 CYS A 310
SITE 1 AC2 4 CYS A 265 CYS A 268 HIS A 289 CYS A 292
SITE 1 AC3 4 CYS A 209 CYS A 212 HIS A 238 CYS A 241
SITE 1 AC4 4 CYS A 230 CYS A 233 CYS A 259 CYS A 262
SITE 1 AC5 5 PRO B 16 ARG B 17 HOH B 201 HOH B 202
SITE 2 AC5 5 HOH B 206
CRYST1 47.677 48.122 76.191 90.00 90.00 90.00 P 21 21 21 4
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 0.020974 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020781 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013125 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
