HEADER TRANSFERASE 23-NOV-15 5EX3
TITLE CRYSTAL STRUCTURE OF HUMAN SMYD3 IN COMPLEX WITH A VEGFR1 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SMYD3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SET AND MYND DOMAIN-CONTAINING PROTEIN 3,ZINC FINGER MYND
COMPND 5 DOMAIN-CONTAINING PROTEIN 1;
COMPND 6 EC: 2.1.1.43;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: VEGFR1 PEPTIDE;
COMPND 11 CHAIN: D;
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: SMYD3, ZMYND1, ZNFN3A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS SET DOMAIN, METHYLATION, CHROMATIN, CANCER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.QIAO,W.FU,N.LIU,M.WANG,J.MIN,B.ZHU,R.M.XU,N.YANG
REVDAT 3 18-OCT-17 5EX3 1 JRNL REMARK
REVDAT 2 25-MAY-16 5EX3 1 JRNL
REVDAT 1 09-MAR-16 5EX3 0
JRNL AUTH W.FU,N.LIU,Q.QIAO,M.WANG,J.MIN,B.ZHU,R.M.XU,N.YANG
JRNL TITL STRUCTURAL BASIS FOR SUBSTRATE PREFERENCE OF SMYD3, A SET
JRNL TITL 2 DOMAIN-CONTAINING PROTEIN LYSINE METHYLTRANSFERASE
JRNL REF J.BIOL.CHEM. V. 291 9173 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 26929412
JRNL DOI 10.1074/JBC.M115.709832
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.210
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 24925
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.710
REMARK 3 FREE R VALUE TEST SET COUNT : 1922
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 30.0053 - 5.1801 0.99 2565 215 0.1924 0.2073
REMARK 3 2 5.1801 - 4.1150 1.00 2455 204 0.1395 0.1626
REMARK 3 3 4.1150 - 3.5958 0.99 2411 200 0.1520 0.1973
REMARK 3 4 3.5958 - 3.2675 0.99 2389 202 0.1805 0.2411
REMARK 3 5 3.2675 - 3.0335 0.98 2359 199 0.2092 0.2534
REMARK 3 6 3.0335 - 2.8548 0.97 2317 192 0.2234 0.3056
REMARK 3 7 2.8548 - 2.7119 0.95 2265 186 0.2299 0.2930
REMARK 3 8 2.7119 - 2.5940 0.93 2220 189 0.2276 0.3018
REMARK 3 9 2.5940 - 2.4941 0.91 2147 179 0.2347 0.3118
REMARK 3 10 2.4941 - 2.4081 0.80 1875 156 0.2395 0.2952
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 57.74
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.15190
REMARK 3 B22 (A**2) : 9.61470
REMARK 3 B33 (A**2) : -15.76660
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 3596
REMARK 3 ANGLE : 1.153 4838
REMARK 3 CHIRALITY : 0.075 528
REMARK 3 PLANARITY : 0.004 628
REMARK 3 DIHEDRAL : 19.468 1384
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 5EX3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215635.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.9788
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26005
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52900
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: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8M NAAC, PH 7.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 26.68900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.79950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.32950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.79950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.68900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.32950
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: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 -7
REMARK 465 PRO A -6
REMARK 465 LEU A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 PRO A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 LEU D 827
REMARK 465 ARG D 835
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 O ASN A 134 O HOH A 601 2.00
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 ARG A 51 -64.60 -91.09
REMARK 500 ARG A 66 15.82 54.52
REMARK 500 ASN A 187 -167.70 -69.02
REMARK 500 GLU A 189 31.70 -89.79
REMARK 500 LYS A 271 -0.45 80.64
REMARK 500 PHE A 362 65.80 -118.53
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 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 49 SG
REMARK 620 2 CYS A 52 SG 103.3
REMARK 620 3 CYS A 71 SG 112.5 107.3
REMARK 620 4 CYS A 75 SG 112.3 116.8 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 62 SG
REMARK 620 2 CYS A 65 SG 111.1
REMARK 620 3 HIS A 83 NE2 110.0 109.7
REMARK 620 4 CYS A 87 SG 111.3 109.6 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 208 SG
REMARK 620 2 CYS A 261 SG 112.4
REMARK 620 3 CYS A 263 SG 108.8 106.6
REMARK 620 4 CYS A 266 SG 91.3 115.9 120.9
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EX0 RELATED DB: PDB
DBREF 5EX3 A 1 428 UNP Q9H7B4 SMYD3_HUMAN 1 428
DBREF 5EX3 D 827 835 PDB 5EX3 5EX3 827 835
SEQADV 5EX3 GLY A -7 UNP Q9H7B4 EXPRESSION TAG
SEQADV 5EX3 PRO A -6 UNP Q9H7B4 EXPRESSION TAG
SEQADV 5EX3 LEU A -5 UNP Q9H7B4 EXPRESSION TAG
SEQADV 5EX3 GLY A -4 UNP Q9H7B4 EXPRESSION TAG
SEQADV 5EX3 SER A -3 UNP Q9H7B4 EXPRESSION TAG
SEQADV 5EX3 PRO A -2 UNP Q9H7B4 EXPRESSION TAG
SEQADV 5EX3 GLU A -1 UNP Q9H7B4 EXPRESSION TAG
SEQADV 5EX3 PHE A 0 UNP Q9H7B4 EXPRESSION TAG
SEQADV 5EX3 ASN A 13 UNP Q9H7B4 LYS 13 ENGINEERED MUTATION
SEQADV 5EX3 ARG A 140 UNP Q9H7B4 LYS 140 ENGINEERED MUTATION
SEQRES 1 A 436 GLY PRO LEU GLY SER PRO GLU PHE MET GLU PRO LEU LYS
SEQRES 2 A 436 VAL GLU LYS PHE ALA THR ALA ASN ARG GLY ASN GLY LEU
SEQRES 3 A 436 ARG ALA VAL THR PRO LEU ARG PRO GLY GLU LEU LEU PHE
SEQRES 4 A 436 ARG SER ASP PRO LEU ALA TYR THR VAL CYS LYS GLY SER
SEQRES 5 A 436 ARG GLY VAL VAL CYS ASP ARG CYS LEU LEU GLY LYS GLU
SEQRES 6 A 436 LYS LEU MET ARG CYS SER GLN CYS ARG VAL ALA LYS TYR
SEQRES 7 A 436 CYS SER ALA LYS CYS GLN LYS LYS ALA TRP PRO ASP HIS
SEQRES 8 A 436 LYS ARG GLU CYS LYS CYS LEU LYS SER CYS LYS PRO ARG
SEQRES 9 A 436 TYR PRO PRO ASP SER VAL ARG LEU LEU GLY ARG VAL VAL
SEQRES 10 A 436 PHE LYS LEU MET ASP GLY ALA PRO SER GLU SER GLU LYS
SEQRES 11 A 436 LEU TYR SER PHE TYR ASP LEU GLU SER ASN ILE ASN LYS
SEQRES 12 A 436 LEU THR GLU ASP ARG LYS GLU GLY LEU ARG GLN LEU VAL
SEQRES 13 A 436 MET THR PHE GLN HIS PHE MET ARG GLU GLU ILE GLN ASP
SEQRES 14 A 436 ALA SER GLN LEU PRO PRO ALA PHE ASP LEU PHE GLU ALA
SEQRES 15 A 436 PHE ALA LYS VAL ILE CYS ASN SER PHE THR ILE CYS ASN
SEQRES 16 A 436 ALA GLU MET GLN GLU VAL GLY VAL GLY LEU TYR PRO SER
SEQRES 17 A 436 ILE SER LEU LEU ASN HIS SER CYS ASP PRO ASN CYS SER
SEQRES 18 A 436 ILE VAL PHE ASN GLY PRO HIS LEU LEU LEU ARG ALA VAL
SEQRES 19 A 436 ARG ASP ILE GLU VAL GLY GLU GLU LEU THR ILE CYS TYR
SEQRES 20 A 436 LEU ASP MET LEU MET THR SER GLU GLU ARG ARG LYS GLN
SEQRES 21 A 436 LEU ARG ASP GLN TYR CYS PHE GLU CYS ASP CYS PHE ARG
SEQRES 22 A 436 CYS GLN THR GLN ASP LYS ASP ALA ASP MET LEU THR GLY
SEQRES 23 A 436 ASP GLU GLN VAL TRP LYS GLU VAL GLN GLU SER LEU LYS
SEQRES 24 A 436 LYS ILE GLU GLU LEU LYS ALA HIS TRP LYS TRP GLU GLN
SEQRES 25 A 436 VAL LEU ALA MET CYS GLN ALA ILE ILE SER SER ASN SER
SEQRES 26 A 436 GLU ARG LEU PRO ASP ILE ASN ILE TYR GLN LEU LYS VAL
SEQRES 27 A 436 LEU ASP CYS ALA MET ASP ALA CYS ILE ASN LEU GLY LEU
SEQRES 28 A 436 LEU GLU GLU ALA LEU PHE TYR GLY THR ARG THR MET GLU
SEQRES 29 A 436 PRO TYR ARG ILE PHE PHE PRO GLY SER HIS PRO VAL ARG
SEQRES 30 A 436 GLY VAL GLN VAL MET LYS VAL GLY LYS LEU GLN LEU HIS
SEQRES 31 A 436 GLN GLY MET PHE PRO GLN ALA MET LYS ASN LEU ARG LEU
SEQRES 32 A 436 ALA PHE ASP ILE MET ARG VAL THR HIS GLY ARG GLU HIS
SEQRES 33 A 436 SER LEU ILE GLU ASP LEU ILE LEU LEU LEU GLU GLU CYS
SEQRES 34 A 436 ASP ALA ASN ILE ARG ALA SER
SEQRES 1 D 9 LEU LYS LEU GLY MLY SER LEU GLY ARG
HET MLY D 831 11
HET ZN A 501 1
HET ZN A 502 1
HET ZN A 503 1
HET SAH A 504 26
HET ACY A 505 4
HET ACY A 506 4
HET ACY A 507 4
HET ACY A 508 4
HETNAM MLY N-DIMETHYL-LYSINE
HETNAM ZN ZINC ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM ACY ACETIC ACID
FORMUL 2 MLY C8 H18 N2 O2
FORMUL 3 ZN 3(ZN 2+)
FORMUL 6 SAH C14 H20 N6 O5 S
FORMUL 7 ACY 4(C2 H4 O2)
FORMUL 11 HOH *96(H2 O)
HELIX 1 AA1 LYS A 42 ARG A 45 5 4
HELIX 2 AA2 SER A 72 LYS A 94 1 23
HELIX 3 AA3 PRO A 99 LEU A 112 1 14
HELIX 4 AA4 SER A 118 LYS A 122 5 5
HELIX 5 AA5 SER A 125 LEU A 129 5 5
HELIX 6 AA6 ASN A 132 LEU A 136 5 5
HELIX 7 AA7 THR A 137 MET A 155 1 19
HELIX 8 AA8 ASP A 161 LEU A 165 5 5
HELIX 9 AA9 ASP A 170 ASN A 181 1 12
HELIX 10 AB1 SER A 200 LEU A 204 5 5
HELIX 11 AB2 THR A 245 CYS A 258 1 14
HELIX 12 AB3 CYS A 263 GLN A 269 1 7
HELIX 13 AB4 LYS A 271 LEU A 276 1 6
HELIX 14 AB5 ASP A 279 HIS A 299 1 21
HELIX 15 AB6 LYS A 301 SER A 317 1 17
HELIX 16 AB7 ASN A 324 LEU A 341 1 18
HELIX 17 AB8 LEU A 343 PHE A 362 1 20
HELIX 18 AB9 HIS A 366 GLN A 383 1 18
HELIX 19 AC1 MET A 385 HIS A 404 1 20
HELIX 20 AC2 HIS A 408 ARG A 426 1 19
SHEET 1 AA1 2 VAL A 6 ALA A 10 0
SHEET 2 AA1 2 ASN A 16 ALA A 20 -1 O GLY A 17 N PHE A 9
SHEET 1 AA2 3 LEU A 29 SER A 33 0
SHEET 2 AA2 3 HIS A 220 ALA A 225 -1 O LEU A 221 N SER A 33
SHEET 3 AA2 3 CYS A 212 ASN A 217 -1 N SER A 213 O ARG A 224
SHEET 1 AA3 3 ALA A 37 VAL A 40 0
SHEET 2 AA3 3 GLU A 192 LEU A 197 -1 O LEU A 197 N ALA A 37
SHEET 3 AA3 3 SER A 182 CYS A 186 -1 N PHE A 183 O GLY A 196
SHEET 1 AA4 2 MET A 60 ARG A 61 0
SHEET 2 AA4 2 LYS A 69 TYR A 70 -1 O TYR A 70 N MET A 60
SHEET 1 AA5 2 ASN A 205 HIS A 206 0
SHEET 2 AA5 2 THR A 236 ILE A 237 1 O ILE A 237 N ASN A 205
LINK SG CYS A 49 ZN ZN A 501 1555 1555 2.35
LINK SG CYS A 52 ZN ZN A 501 1555 1555 2.51
LINK SG CYS A 62 ZN ZN A 502 1555 1555 2.48
LINK SG CYS A 65 ZN ZN A 502 1555 1555 2.30
LINK SG CYS A 71 ZN ZN A 501 1555 1555 2.46
LINK SG CYS A 75 ZN ZN A 501 1555 1555 2.28
LINK NE2 HIS A 83 ZN ZN A 502 1555 1555 2.21
LINK SG CYS A 87 ZN ZN A 502 1555 1555 2.51
LINK SG CYS A 208 ZN ZN A 503 1555 1555 2.45
LINK SG CYS A 261 ZN ZN A 503 1555 1555 2.42
LINK SG CYS A 263 ZN ZN A 503 1555 1555 2.43
LINK SG CYS A 266 ZN ZN A 503 1555 1555 2.56
LINK C GLY D 830 N MLY D 831 1555 1555 1.33
LINK C MLY D 831 N SER D 832 1555 1555 1.33
CISPEP 1 LYS A 94 PRO A 95 0 1.75
SITE 1 AC1 4 CYS A 49 CYS A 52 CYS A 71 CYS A 75
SITE 1 AC2 4 CYS A 62 CYS A 65 HIS A 83 CYS A 87
SITE 1 AC3 4 CYS A 208 CYS A 261 CYS A 263 CYS A 266
SITE 1 AC4 13 ARG A 14 ASN A 16 TYR A 124 ASN A 132
SITE 2 AC4 13 SER A 202 LEU A 203 ASN A 205 HIS A 206
SITE 3 AC4 13 TYR A 239 TYR A 257 PHE A 259 HOH A 643
SITE 4 AC4 13 MLY D 831
SITE 1 AC5 4 GLN A 160 ASP A 161 HOH A 617 HOH A 665
SITE 1 AC6 3 LEU A 276 THR A 277 GLY A 278
SITE 1 AC7 4 ALA A 73 ARG A 394 PHE A 397 ASP A 398
CRYST1 53.378 104.659 117.599 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 0.018734 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009555 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008503 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
