HEADER TRANSFERASE 12-MAR-15 4YPA
TITLE ASH1L SET DOMAIN Q2265A MUTANT IN COMPLEX WITH S-ADENOSYL METHIONINE
TITLE 2 (SAM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE ASH1L;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: SET DOMAIN (UNP RESIDUES 2074-2293);
COMPND 5 SYNONYM: ASH1-LIKE PROTEIN,HUASH1,ABSENT SMALL AND HOMEOTIC DISKS
COMPND 6 PROTEIN 1 HOMOLOG,LYSINE N-METHYLTRANSFERASE 2H;
COMPND 7 EC: 2.1.1.43;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ASH1L, KIAA1420, KMT2H;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HISTONE METHYLATION, SET DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.S.ROGAWSKI,J.NDOJ,H.J.CHO,I.MAILLARD,J.GREMBECKA,T.CIERPICKI
REVDAT 7 27-SEP-23 4YPA 1 LINK
REVDAT 6 04-DEC-19 4YPA 1 REMARK
REVDAT 5 04-OCT-17 4YPA 1 REMARK
REVDAT 4 27-SEP-17 4YPA 1 JRNL REMARK
REVDAT 3 16-SEP-15 4YPA 1 JRNL
REVDAT 2 09-SEP-15 4YPA 1 JRNL
REVDAT 1 02-SEP-15 4YPA 0
JRNL AUTH D.S.ROGAWSKI,J.NDOJ,H.J.CHO,I.MAILLARD,J.GREMBECKA,
JRNL AUTH 2 T.CIERPICKI
JRNL TITL TWO LOOPS UNDERGOING CONCERTED DYNAMICS REGULATE THE
JRNL TITL 2 ACTIVITY OF THE ASH1L HISTONE METHYLTRANSFERASE.
JRNL REF BIOCHEMISTRY V. 54 5401 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 26292256
JRNL DOI 10.1021/ACS.BIOCHEM.5B00697
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 38087
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2758
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.26000
REMARK 3 B12 (A**2) : -0.15000
REMARK 3 B13 (A**2) : -0.15000
REMARK 3 B23 (A**2) : -0.09000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.528
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.313
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.240
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.634
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.868
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7188 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9682 ; 1.644 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 854 ; 6.788 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 380 ;38.506 ;24.105
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1264 ;18.956 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;18.546 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 980 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5556 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4272 ; 0.987 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6862 ; 1.836 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2916 ; 2.538 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2820 ; 4.041 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2069 A 2280 4
REMARK 3 1 C 2069 C 2280 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1712 ; 0.380 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1712 ; 1.060 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 2069 B 2280 4
REMARK 3 1 D 2069 D 2280 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 1712 ; 0.330 ; 0.500
REMARK 3 MEDIUM THERMAL 2 B (A**2): 1712 ; 0.860 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4YPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207830.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3-8.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40091
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.25500
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: MOLREP
REMARK 200 STARTING MODEL: 4YNM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, TRIS,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 GLY A 2281
REMARK 465 LYS A 2282
REMARK 465 SER A 2283
REMARK 465 GLN A 2284
REMARK 465 ARG A 2285
REMARK 465 VAL A 2286
REMARK 465 ASN A 2287
REMARK 465 GLY A 2288
REMARK 465 GLY B 2063
REMARK 465 ALA B 2064
REMARK 465 MET B 2065
REMARK 465 ALA B 2066
REMARK 465 GLY B 2067
REMARK 465 SER B 2068
REMARK 465 GLY B 2281
REMARK 465 LYS B 2282
REMARK 465 SER B 2283
REMARK 465 GLN B 2284
REMARK 465 ARG B 2285
REMARK 465 VAL B 2286
REMARK 465 ASN B 2287
REMARK 465 GLY B 2288
REMARK 465 GLY C 2280
REMARK 465 GLY C 2281
REMARK 465 LYS C 2282
REMARK 465 SER C 2283
REMARK 465 GLN C 2284
REMARK 465 ARG C 2285
REMARK 465 VAL C 2286
REMARK 465 ASN C 2287
REMARK 465 GLY C 2288
REMARK 465 GLY D 2063
REMARK 465 ALA D 2064
REMARK 465 MET D 2065
REMARK 465 ALA D 2066
REMARK 465 GLY D 2067
REMARK 465 SER D 2068
REMARK 465 GLY D 2280
REMARK 465 GLY D 2281
REMARK 465 LYS D 2282
REMARK 465 SER D 2283
REMARK 465 GLN D 2284
REMARK 465 ARG D 2285
REMARK 465 VAL D 2286
REMARK 465 ASN D 2287
REMARK 465 GLY D 2288
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 SG CYS B 2091 ZN ZN B 2301 0.68
REMARK 500 SG CYS D 2091 ZN ZN D 2301 1.39
REMARK 500 SG CYS A 2093 ZN ZN A 3001 1.60
REMARK 500 SG CYS D 2093 ZN ZN D 2301 1.65
REMARK 500 OE2 GLU B 2087 ND2 ASN C 2120 1.95
REMARK 500 ND2 ASN B 2261 O HOH B 2401 2.13
REMARK 500 OD1 ASP C 2097 O HOH C 2401 2.15
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 NZ LYS A 2157 SD MET B 2112 1565 1.71
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 ALA A2088 C THR A2089 N 0.147
REMARK 500 THR A2100 CB THR A2100 OG1 0.137
REMARK 500 CYS B2091 CB CYS B2091 SG 0.234
REMARK 500 CYS B2091 C ASN B2092 N 0.179
REMARK 500 ASN B2092 C CYS B2093 N 0.203
REMARK 500 ASP B2107 C CYS B2108 N 0.165
REMARK 500 ASP C2098 CG ASP C2098 OD2 -0.155
REMARK 500 GLU D2176 CD GLU D2176 OE1 0.067
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 CYS A2093 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 CYS A2104 O - C - N ANGL. DEV. = -10.8 DEGREES
REMARK 500 THR B2090 CA - C - N ANGL. DEV. = -14.9 DEGREES
REMARK 500 THR B2090 O - C - N ANGL. DEV. = 9.7 DEGREES
REMARK 500 CYS B2091 C - N - CA ANGL. DEV. = -15.0 DEGREES
REMARK 500 CYS B2091 CA - CB - SG ANGL. DEV. = 25.3 DEGREES
REMARK 500 CYS B2093 CA - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 LYS B2094 C - N - CA ANGL. DEV. = -19.4 DEGREES
REMARK 500 THR C2090 CA - CB - CG2 ANGL. DEV. = -9.1 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 ASP A2079 -64.30 -94.76
REMARK 500 GLU A2087 61.41 -111.16
REMARK 500 ALA A2088 140.62 -37.09
REMARK 500 THR A2089 36.81 115.78
REMARK 500 ASP A2099 -15.18 -44.20
REMARK 500 VAL A2105 -157.25 -68.09
REMARK 500 GLU A2149 -2.10 77.42
REMARK 500 GLN A2186 -30.14 -135.00
REMARK 500 ASN A2189 36.89 -95.36
REMARK 500 SER A2200 67.29 18.30
REMARK 500 ASN A2232 53.09 37.60
REMARK 500 THR B2090 110.35 106.75
REMARK 500 CYS B2091 179.87 -54.61
REMARK 500 LYS B2095 117.78 -29.24
REMARK 500 VAL B2105 -68.60 -109.98
REMARK 500 ASN B2130 40.70 -108.90
REMARK 500 GLN B2131 34.73 -143.98
REMARK 500 GLU B2137 49.30 -75.37
REMARK 500 GLU B2176 2.98 -65.84
REMARK 500 HIS B2188 -106.45 9.98
REMARK 500 TYR B2194 57.86 -109.89
REMARK 500 THR C2089 -148.93 -116.77
REMARK 500 PRO C2096 -177.53 -69.63
REMARK 500 VAL C2105 -160.62 -69.55
REMARK 500 GLU C2126 1.32 -68.15
REMARK 500 ASN C2130 44.20 -98.56
REMARK 500 GLN C2131 38.30 -140.39
REMARK 500 GLU C2137 49.99 -81.78
REMARK 500 GLN C2140 46.88 -101.82
REMARK 500 CYS C2141 35.04 -143.26
REMARK 500 GLU C2149 0.79 80.43
REMARK 500 ILE C2166 -51.98 -120.74
REMARK 500 GLN C2186 -36.02 -139.65
REMARK 500 ASN C2189 44.01 -101.80
REMARK 500 ASP C2199 -137.47 -143.62
REMARK 500 THR D2090 141.36 111.58
REMARK 500 GLN D2131 36.74 -143.38
REMARK 500 GLU D2137 45.02 -77.79
REMARK 500 GLU D2149 -2.49 68.57
REMARK 500 GLU D2176 28.33 -76.96
REMARK 500 GLN D2186 -42.40 -130.77
REMARK 500 HIS D2188 -79.52 -14.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 2088 THR A 2089 134.59
REMARK 500 SER B 2259 PHE B 2260 148.39
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 A3001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A2091 SG
REMARK 620 2 CYS A2108 SG 109.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A3002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A2104 SG
REMARK 620 2 CYS A2117 SG 105.2
REMARK 620 3 CYS A2122 SG 102.1 118.1
REMARK 620 4 CYS A2128 SG 118.2 109.9 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A3003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A2220 SG
REMARK 620 2 CYS A2268 SG 112.5
REMARK 620 3 CYS A2270 SG 112.8 106.5
REMARK 620 4 CYS A2275 SG 109.2 106.3 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B2093 SG
REMARK 620 2 CYS B2104 SG 107.3
REMARK 620 3 CYS B2108 SG 108.9 125.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B2104 SG
REMARK 620 2 CYS B2117 SG 120.1
REMARK 620 3 CYS B2122 SG 95.7 122.2
REMARK 620 4 CYS B2128 SG 104.7 103.6 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B2220 SG
REMARK 620 2 CYS B2268 SG 113.3
REMARK 620 3 CYS B2270 SG 112.8 113.0
REMARK 620 4 CYS B2275 SG 108.5 103.2 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C2301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C2091 SG
REMARK 620 2 CYS C2093 SG 110.8
REMARK 620 3 CYS C2104 SG 115.6 108.5
REMARK 620 4 CYS C2108 SG 110.8 107.5 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C2302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C2104 SG
REMARK 620 2 CYS C2117 SG 105.5
REMARK 620 3 CYS C2122 SG 110.9 119.2
REMARK 620 4 CYS C2128 SG 108.8 104.0 108.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C2303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C2220 SG
REMARK 620 2 CYS C2268 SG 111.7
REMARK 620 3 CYS C2270 SG 115.5 108.3
REMARK 620 4 CYS C2275 SG 109.9 103.6 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D2301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2104 SG
REMARK 620 2 CYS D2108 SG 107.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D2302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2104 SG
REMARK 620 2 CYS D2117 SG 116.6
REMARK 620 3 CYS D2122 SG 103.9 120.1
REMARK 620 4 CYS D2128 SG 107.9 106.5 100.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D2303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D2220 SG
REMARK 620 2 CYS D2268 SG 116.9
REMARK 620 3 CYS D2270 SG 115.9 107.1
REMARK 620 4 CYS D2275 SG 108.7 104.9 101.9
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 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 2304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 2301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 2302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 2303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM C 2304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 2301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 2302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 2303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM D 2304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YNM RELATED DB: PDB
REMARK 900 RELATED ID: 4YNP RELATED DB: PDB
REMARK 900 RELATED ID: 4YPE RELATED DB: PDB
DBREF 4YPA A 2069 2288 UNP Q9NR48 ASH1L_HUMAN 2074 2293
DBREF 4YPA B 2069 2288 UNP Q9NR48 ASH1L_HUMAN 2074 2293
DBREF 4YPA C 2069 2288 UNP Q9NR48 ASH1L_HUMAN 2074 2293
DBREF 4YPA D 2069 2288 UNP Q9NR48 ASH1L_HUMAN 2074 2293
SEQADV 4YPA GLY A 2063 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA A 2064 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA MET A 2065 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA A 2066 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA GLY A 2067 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA SER A 2068 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA A 2265 UNP Q9NR48 GLN 2270 ENGINEERED MUTATION
SEQADV 4YPA GLY B 2063 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA B 2064 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA MET B 2065 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA B 2066 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA GLY B 2067 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA SER B 2068 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA B 2265 UNP Q9NR48 GLN 2270 ENGINEERED MUTATION
SEQADV 4YPA GLY C 2063 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA C 2064 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA MET C 2065 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA C 2066 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA GLY C 2067 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA SER C 2068 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA C 2265 UNP Q9NR48 GLN 2270 ENGINEERED MUTATION
SEQADV 4YPA GLY D 2063 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA D 2064 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA MET D 2065 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA D 2066 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA GLY D 2067 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA SER D 2068 UNP Q9NR48 EXPRESSION TAG
SEQADV 4YPA ALA D 2265 UNP Q9NR48 GLN 2270 ENGINEERED MUTATION
SEQRES 1 A 226 GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN
SEQRES 2 A 226 VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA
SEQRES 3 A 226 THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG
SEQRES 4 A 226 LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE
SEQRES 5 A 226 ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN
SEQRES 6 A 226 CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN
SEQRES 7 A 226 CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY
SEQRES 8 A 226 ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE
SEQRES 9 A 226 ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE
SEQRES 10 A 226 ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP
SEQRES 11 A 226 HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP
SEQRES 12 A 226 SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS
SEQRES 13 A 226 SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL
SEQRES 14 A 226 ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP
SEQRES 15 A 226 MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE
SEQRES 16 A 226 HIS SER PHE ASN VAL GLU LYS ALA GLN LEU CYS LYS CYS
SEQRES 17 A 226 GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER
SEQRES 18 A 226 GLN ARG VAL ASN GLY
SEQRES 1 B 226 GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN
SEQRES 2 B 226 VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA
SEQRES 3 B 226 THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG
SEQRES 4 B 226 LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE
SEQRES 5 B 226 ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN
SEQRES 6 B 226 CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN
SEQRES 7 B 226 CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY
SEQRES 8 B 226 ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE
SEQRES 9 B 226 ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE
SEQRES 10 B 226 ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP
SEQRES 11 B 226 HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP
SEQRES 12 B 226 SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS
SEQRES 13 B 226 SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL
SEQRES 14 B 226 ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP
SEQRES 15 B 226 MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE
SEQRES 16 B 226 HIS SER PHE ASN VAL GLU LYS ALA GLN LEU CYS LYS CYS
SEQRES 17 B 226 GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER
SEQRES 18 B 226 GLN ARG VAL ASN GLY
SEQRES 1 C 226 GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN
SEQRES 2 C 226 VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA
SEQRES 3 C 226 THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG
SEQRES 4 C 226 LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE
SEQRES 5 C 226 ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN
SEQRES 6 C 226 CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN
SEQRES 7 C 226 CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY
SEQRES 8 C 226 ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE
SEQRES 9 C 226 ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE
SEQRES 10 C 226 ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP
SEQRES 11 C 226 HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP
SEQRES 12 C 226 SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS
SEQRES 13 C 226 SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL
SEQRES 14 C 226 ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP
SEQRES 15 C 226 MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE
SEQRES 16 C 226 HIS SER PHE ASN VAL GLU LYS ALA GLN LEU CYS LYS CYS
SEQRES 17 C 226 GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER
SEQRES 18 C 226 GLN ARG VAL ASN GLY
SEQRES 1 D 226 GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN
SEQRES 2 D 226 VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA
SEQRES 3 D 226 THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG
SEQRES 4 D 226 LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE
SEQRES 5 D 226 ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN
SEQRES 6 D 226 CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN
SEQRES 7 D 226 CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY
SEQRES 8 D 226 ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE
SEQRES 9 D 226 ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE
SEQRES 10 D 226 ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP
SEQRES 11 D 226 HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP
SEQRES 12 D 226 SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS
SEQRES 13 D 226 SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL
SEQRES 14 D 226 ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP
SEQRES 15 D 226 MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE
SEQRES 16 D 226 HIS SER PHE ASN VAL GLU LYS ALA GLN LEU CYS LYS CYS
SEQRES 17 D 226 GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER
SEQRES 18 D 226 GLN ARG VAL ASN GLY
HET ZN A3001 1
HET ZN A3002 1
HET ZN A3003 1
HET SAM A3004 27
HET ZN B2301 1
HET ZN B2302 1
HET ZN B2303 1
HET SAM B2304 27
HET ZN C2301 1
HET ZN C2302 1
HET ZN C2303 1
HET SAM C2304 27
HET ZN D2301 1
HET ZN D2302 1
HET ZN D2303 1
HET SAM D2304 27
HETNAM ZN ZINC ION
HETNAM SAM S-ADENOSYLMETHIONINE
FORMUL 5 ZN 12(ZN 2+)
FORMUL 8 SAM 4(C15 H22 N6 O5 S)
FORMUL 21 HOH *214(H2 O)
HELIX 1 AA1 CYS A 2108 ILE A 2113 1 6
HELIX 2 AA2 CYS A 2124 CYS A 2128 5 5
HELIX 3 AA3 GLU A 2176 GLN A 2186 1 11
HELIX 4 AA4 ASN A 2211 ILE A 2216 5 6
HELIX 5 AA5 ASP A 2254 SER A 2259 1 6
HELIX 6 AA6 ASN B 2110 PHE B 2114 5 5
HELIX 7 AA7 CYS B 2124 CYS B 2128 5 5
HELIX 8 AA8 GLN B 2177 GLN B 2186 1 10
HELIX 9 AA9 ASN B 2211 ILE B 2216 5 6
HELIX 10 AB1 ASP B 2254 HIS B 2258 5 5
HELIX 11 AB2 ASN C 2110 PHE C 2114 5 5
HELIX 12 AB3 CYS C 2124 CYS C 2128 5 5
HELIX 13 AB4 GLU C 2176 GLN C 2186 1 11
HELIX 14 AB5 ASN C 2211 ILE C 2216 5 6
HELIX 15 AB6 ASP C 2254 SER C 2259 1 6
HELIX 16 AB7 ASN D 2110 PHE D 2114 5 5
HELIX 17 AB8 CYS D 2124 CYS D 2128 5 5
HELIX 18 AB9 GLN D 2177 GLN D 2186 1 10
HELIX 19 AC1 ASN D 2211 ILE D 2216 5 6
HELIX 20 AC2 ASP D 2254 SER D 2259 5 6
SHEET 1 AA1 2 LYS A2070 LYS A2071 0
SHEET 2 AA1 2 MET A2209 GLY A2210 1 O GLY A2210 N LYS A2070
SHEET 1 AA2 4 VAL A2076 TYR A2077 0
SHEET 2 AA2 4 GLU A2172 SER A2175 1 O VAL A2173 N VAL A2076
SHEET 3 AA2 4 MET A2202 ASP A2205 -1 O VAL A2203 N VAL A2174
SHEET 4 AA2 4 CYS A2195 ASP A2199 -1 N ASP A2199 O MET A2202
SHEET 1 AA3 2 LEU A2142 ARG A2146 0
SHEET 2 AA3 2 TRP A2152 THR A2156 -1 O GLY A2153 N PHE A2145
SHEET 1 AA4 3 PHE A2165 GLU A2168 0
SHEET 2 AA4 3 VAL A2234 ALA A2241 -1 O LEU A2239 N ILE A2167
SHEET 3 AA4 3 CYS A2224 VAL A2231 -1 N VAL A2231 O VAL A2234
SHEET 1 AA5 2 ASN A2217 HIS A2218 0
SHEET 2 AA5 2 THR A2252 TYR A2253 1 O TYR A2253 N ASN A2217
SHEET 1 AA6 2 GLN A2266 LEU A2267 0
SHEET 2 AA6 2 ILE A2278 ILE A2279 -1 O ILE A2279 N GLN A2266
SHEET 1 AA7 2 LYS B2070 LYS B2071 0
SHEET 2 AA7 2 MET B2209 GLY B2210 1 O GLY B2210 N LYS B2070
SHEET 1 AA8 4 VAL B2076 TYR B2077 0
SHEET 2 AA8 4 GLU B2172 SER B2175 1 O VAL B2173 N VAL B2076
SHEET 3 AA8 4 MET B2202 ASP B2205 -1 O VAL B2203 N VAL B2174
SHEET 4 AA8 4 CYS B2195 ASN B2197 -1 N LEU B2196 O ILE B2204
SHEET 1 AA9 2 LEU B2142 ARG B2146 0
SHEET 2 AA9 2 TRP B2152 THR B2156 -1 O ARG B2155 N GLU B2143
SHEET 1 AB1 3 PHE B2165 GLU B2168 0
SHEET 2 AB1 3 VAL B2234 ALA B2241 -1 O LEU B2239 N ILE B2166
SHEET 3 AB1 3 CYS B2224 VAL B2231 -1 N GLU B2225 O TYR B2240
SHEET 1 AB2 2 ASN B2217 HIS B2218 0
SHEET 2 AB2 2 THR B2252 TYR B2253 1 O TYR B2253 N ASN B2217
SHEET 1 AB3 2 GLN B2266 LEU B2267 0
SHEET 2 AB3 2 ILE B2278 ILE B2279 -1 O ILE B2279 N GLN B2266
SHEET 1 AB4 2 LYS C2070 LYS C2071 0
SHEET 2 AB4 2 MET C2209 GLY C2210 1 O GLY C2210 N LYS C2070
SHEET 1 AB5 4 VAL C2076 TYR C2077 0
SHEET 2 AB5 4 GLU C2172 SER C2175 1 O VAL C2173 N VAL C2076
SHEET 3 AB5 4 MET C2202 ASP C2205 -1 O VAL C2203 N VAL C2174
SHEET 4 AB5 4 CYS C2195 ASP C2199 -1 N LEU C2196 O ILE C2204
SHEET 1 AB6 2 LEU C2142 ARG C2146 0
SHEET 2 AB6 2 TRP C2152 THR C2156 -1 O GLY C2153 N PHE C2145
SHEET 1 AB7 3 PHE C2165 GLU C2168 0
SHEET 2 AB7 3 VAL C2234 ALA C2241 -1 O LEU C2239 N ILE C2166
SHEET 3 AB7 3 CYS C2224 VAL C2231 -1 N VAL C2231 O VAL C2234
SHEET 1 AB8 2 ASN C2217 HIS C2218 0
SHEET 2 AB8 2 THR C2252 TYR C2253 1 O TYR C2253 N ASN C2217
SHEET 1 AB9 2 GLN C2266 LEU C2267 0
SHEET 2 AB9 2 ILE C2278 ILE C2279 -1 O ILE C2279 N GLN C2266
SHEET 1 AC1 2 LYS D2070 LYS D2071 0
SHEET 2 AC1 2 MET D2209 GLY D2210 1 O GLY D2210 N LYS D2070
SHEET 1 AC2 4 VAL D2076 TYR D2077 0
SHEET 2 AC2 4 GLU D2172 SER D2175 1 O VAL D2173 N VAL D2076
SHEET 3 AC2 4 MET D2202 ASP D2205 -1 O ASP D2205 N GLU D2172
SHEET 4 AC2 4 CYS D2195 ASN D2197 -1 N LEU D2196 O ILE D2204
SHEET 1 AC3 2 LEU D2142 ARG D2146 0
SHEET 2 AC3 2 TRP D2152 THR D2156 -1 O GLY D2153 N PHE D2145
SHEET 1 AC4 3 PHE D2165 GLU D2168 0
SHEET 2 AC4 3 VAL D2234 ALA D2241 -1 O LEU D2239 N ILE D2167
SHEET 3 AC4 3 CYS D2224 VAL D2231 -1 N GLU D2225 O TYR D2240
SHEET 1 AC5 2 ASN D2217 HIS D2218 0
SHEET 2 AC5 2 THR D2252 TYR D2253 1 O TYR D2253 N ASN D2217
SHEET 1 AC6 2 GLN D2266 LEU D2267 0
SHEET 2 AC6 2 ILE D2278 ILE D2279 -1 O ILE D2279 N GLN D2266
SSBOND 1 CYS A 2093 CYS A 2104 1555 1555 2.33
SSBOND 2 CYS B 2091 CYS B 2093 1555 1555 2.30
SSBOND 3 CYS B 2091 CYS B 2104 1555 1555 2.82
SSBOND 4 CYS B 2091 CYS B 2108 1555 1555 2.40
SSBOND 5 CYS D 2091 CYS D 2093 1555 1555 2.26
LINK SG CYS A2091 ZN ZN A3001 1555 1555 2.40
LINK SG CYS A2104 ZN ZN A3002 1555 1555 2.63
LINK SG CYS A2108 ZN ZN A3001 1555 1555 2.42
LINK SG CYS A2117 ZN ZN A3002 1555 1555 2.29
LINK SG CYS A2122 ZN ZN A3002 1555 1555 2.52
LINK SG CYS A2128 ZN ZN A3002 1555 1555 2.38
LINK SG CYS A2220 ZN ZN A3003 1555 1555 2.25
LINK SG CYS A2268 ZN ZN A3003 1555 1555 2.32
LINK SG CYS A2270 ZN ZN A3003 1555 1555 2.27
LINK SG CYS A2275 ZN ZN A3003 1555 1555 2.35
LINK SG CYS B2093 ZN ZN B2301 1555 1555 2.29
LINK SG CYS B2104 ZN ZN B2301 1555 1555 2.34
LINK SG CYS B2104 ZN ZN B2302 1555 1555 2.30
LINK SG CYS B2108 ZN ZN B2301 1555 1555 2.23
LINK SG CYS B2117 ZN ZN B2302 1555 1555 2.49
LINK SG CYS B2122 ZN ZN B2302 1555 1555 2.26
LINK SG CYS B2128 ZN ZN B2302 1555 1555 2.39
LINK SG CYS B2220 ZN ZN B2303 1555 1555 2.30
LINK SG CYS B2268 ZN ZN B2303 1555 1555 2.29
LINK SG CYS B2270 ZN ZN B2303 1555 1555 2.27
LINK SG CYS B2275 ZN ZN B2303 1555 1555 2.41
LINK SG CYS C2091 ZN ZN C2301 1555 1555 2.21
LINK SG CYS C2093 ZN ZN C2301 1555 1555 2.18
LINK SG CYS C2104 ZN ZN C2301 1555 1555 2.37
LINK SG CYS C2104 ZN ZN C2302 1555 1555 2.15
LINK SG CYS C2108 ZN ZN C2301 1555 1555 2.27
LINK SG CYS C2117 ZN ZN C2302 1555 1555 2.35
LINK SG CYS C2122 ZN ZN C2302 1555 1555 2.16
LINK SG CYS C2128 ZN ZN C2302 1555 1555 2.35
LINK SG CYS C2220 ZN ZN C2303 1555 1555 2.35
LINK SG CYS C2268 ZN ZN C2303 1555 1555 2.25
LINK SG CYS C2270 ZN ZN C2303 1555 1555 2.23
LINK SG CYS C2275 ZN ZN C2303 1555 1555 2.40
LINK SG CYS D2104 ZN ZN D2301 1555 1555 2.40
LINK SG CYS D2104 ZN ZN D2302 1555 1555 2.21
LINK SG CYS D2108 ZN ZN D2301 1555 1555 2.41
LINK SG CYS D2117 ZN ZN D2302 1555 1555 2.48
LINK SG CYS D2122 ZN ZN D2302 1555 1555 2.31
LINK SG CYS D2128 ZN ZN D2302 1555 1555 2.21
LINK SG CYS D2220 ZN ZN D2303 1555 1555 2.32
LINK SG CYS D2268 ZN ZN D2303 1555 1555 2.14
LINK SG CYS D2270 ZN ZN D2303 1555 1555 2.21
LINK SG CYS D2275 ZN ZN D2303 1555 1555 2.44
SITE 1 AC1 4 CYS A2091 CYS A2093 CYS A2104 CYS A2108
SITE 1 AC2 4 CYS A2104 CYS A2117 CYS A2122 CYS A2128
SITE 1 AC3 4 CYS A2220 CYS A2268 CYS A2270 CYS A2275
SITE 1 AC4 18 LYS A2150 TRP A2152 SER A2191 ASP A2192
SITE 2 AC4 18 HIS A2193 TYR A2194 ARG A2214 PHE A2215
SITE 3 AC4 18 ILE A2216 ASN A2217 HIS A2218 TYR A2255
SITE 4 AC4 18 GLN A2266 LEU A2267 CYS A2268 LYS A2269
SITE 5 AC4 18 ILE A2279 HOH A3131
SITE 1 AC5 4 CYS B2091 CYS B2093 CYS B2104 CYS B2108
SITE 1 AC6 4 CYS B2104 CYS B2117 CYS B2122 CYS B2128
SITE 1 AC7 4 CYS B2220 CYS B2268 CYS B2270 CYS B2275
SITE 1 AC8 13 LYS B2150 TRP B2152 ASP B2192 HIS B2193
SITE 2 AC8 13 TYR B2194 ARG B2214 ASN B2217 HIS B2218
SITE 3 AC8 13 TYR B2255 GLN B2266 LEU B2267 LYS B2269
SITE 4 AC8 13 ILE B2279
SITE 1 AC9 4 CYS C2091 CYS C2093 CYS C2104 CYS C2108
SITE 1 AD1 4 CYS C2104 CYS C2117 CYS C2122 CYS C2128
SITE 1 AD2 4 CYS C2220 CYS C2268 CYS C2270 CYS C2275
SITE 1 AD3 16 LYS C2150 TRP C2152 SER C2191 ASP C2192
SITE 2 AD3 16 HIS C2193 TYR C2194 ARG C2214 PHE C2215
SITE 3 AD3 16 ASN C2217 HIS C2218 TYR C2255 GLN C2266
SITE 4 AD3 16 LEU C2267 CYS C2268 LYS C2269 ILE C2279
SITE 1 AD4 5 CYS D2091 CYS D2093 CYS D2104 CYS D2108
SITE 2 AD4 5 ZN D2302
SITE 1 AD5 5 CYS D2104 CYS D2117 CYS D2122 CYS D2128
SITE 2 AD5 5 ZN D2301
SITE 1 AD6 4 CYS D2220 CYS D2268 CYS D2270 CYS D2275
SITE 1 AD7 16 LYS D2150 GLY D2151 TRP D2152 ASP D2192
SITE 2 AD7 16 HIS D2193 TYR D2194 ARG D2214 ASN D2217
SITE 3 AD7 16 HIS D2218 TYR D2255 GLN D2266 LEU D2267
SITE 4 AD7 16 CYS D2268 LYS D2269 ILE D2279 HOH D2419
CRYST1 53.682 61.773 73.233 91.57 93.83 90.46 P 1 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 0.018628 0.000150 0.001253 0.00000
SCALE2 0.000000 0.016189 0.000455 0.00000
SCALE3 0.000000 0.000000 0.013691 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
