HEADER TRANSFERASE 08-JAN-19 6J46
TITLE LEPI-SAH COMPLEX STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: O-METHYLTRANSFERASE LEPI;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LEPORINS BIOSYNTHESIS PROTEIN I;
COMPND 5 EC: 2.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS FLAVUS (STRAIN ATCC 200026 / FGSC
SOURCE 3 A1120 / NRRL 3357 / JCM 12722 / SRRC 167);
SOURCE 4 ORGANISM_TAXID: 332952;
SOURCE 5 STRAIN: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167;
SOURCE 6 GENE: LEPI, AFLA_066940;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.QIU,C.WEI
REVDAT 4 20-MAR-24 6J46 1 SOURCE
REVDAT 3 22-NOV-23 6J46 1 REMARK
REVDAT 2 13-NOV-19 6J46 1 JRNL
REVDAT 1 01-MAY-19 6J46 0
JRNL AUTH Q.SUN,Y.HU,Y.GU,J.HUANG,J.HE,L.LUO,Y.YANG,S.YIN,C.DOU,
JRNL AUTH 2 T.WANG,X.FU,L.HE,S.QI,X.ZHU,S.YANG,X.WEI,W.CHENG
JRNL TITL DECIPHERING THE REGULATORY AND CATALYTIC MECHANISMS OF AN
JRNL TITL 2 UNUSUAL SAM-DEPENDENT ENZYME.
JRNL REF SIGNAL TRANSDUCT TARGET THER V. 4 17 2019
JRNL REFN ESSN 2059-3635
JRNL PMID 31149354
JRNL DOI 10.1038/S41392-019-0052-Y
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 28554
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1413
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 53.2130 - 5.6441 0.97 2973 138 0.1735 0.2027
REMARK 3 2 5.6441 - 4.4806 0.99 2965 157 0.1875 0.2475
REMARK 3 3 4.4806 - 3.9145 1.00 2947 155 0.1868 0.1962
REMARK 3 4 3.9145 - 3.5566 1.00 2928 179 0.2083 0.2438
REMARK 3 5 3.5566 - 3.3018 0.95 2821 123 0.2492 0.2641
REMARK 3 6 3.3018 - 3.1071 0.99 2931 146 0.2543 0.2931
REMARK 3 7 3.1071 - 2.9515 0.99 2911 136 0.2605 0.3193
REMARK 3 8 2.9515 - 2.8230 0.99 2926 145 0.2757 0.2990
REMARK 3 9 2.8230 - 2.7144 0.99 2889 173 0.2873 0.3510
REMARK 3 10 2.7144 - 2.6207 0.30 850 61 0.3941 0.4360
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.600
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 : 0.003 6339
REMARK 3 ANGLE : 0.583 8623
REMARK 3 CHIRALITY : 0.041 965
REMARK 3 PLANARITY : 0.004 1126
REMARK 3 DIHEDRAL : 17.580 3885
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 6J46 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010339.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-17
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 : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X CDTE 1M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28684
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.621
REMARK 200 RESOLUTION RANGE LOW (A) : 53.202
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.82700
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: PHENIX
REMARK 200 STARTING MODEL: 6J1O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.10M BIS-TRIS PH 7.0, 35% PEG 400,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 79.90850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.16650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.90850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.16650
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: 9900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 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 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 103 19.99 59.50
REMARK 500 TYR A 154 70.15 58.27
REMARK 500 GLU A 219 56.60 -148.33
REMARK 500 ASP A 252 -165.89 -165.31
REMARK 500 ARG B 103 19.66 59.22
REMARK 500 ASN B 137 -70.41 -108.39
REMARK 500 GLU B 219 57.87 -147.05
REMARK 500 ASP B 252 -165.22 -165.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 401
DBREF 6J46 A 1 387 UNP B8NJH3 LEPI_ASPFN 1 387
DBREF 6J46 B 1 387 UNP B8NJH3 LEPI_ASPFN 1 387
SEQRES 1 A 387 MET GLU THR VAL ALA ALA ILE LYS THR LEU ILE GLN GLN
SEQRES 2 A 387 LEU ALA GLN SER THR ASP GLN PHE GLY ARG ALA GLU ILE
SEQRES 3 A 387 ASN ASP ALA LEU ARG GLU LEU GLN TYR SER LEU GLU THR
SEQRES 4 A 387 PRO PHE ASP THR VAL MET ARG MET SER LEU ASP THR CYS
SEQRES 5 A 387 GLN VAL ALA VAL ALA ARG ILE GLY SER ASP LEU GLY LEU
SEQRES 6 A 387 PHE LYS HIS LEU SER GLN CYS ALA SER PRO GLN SER ALA
SEQRES 7 A 387 GLU GLU LEU ALA ASP HIS LEU GLY CYS GLY ARG GLU LEU
SEQRES 8 A 387 MET SER ARG LEU LEU ARG TYR MET ALA SER VAL ARG MET
SEQRES 9 A 387 VAL GLN GLN THR ASP ASP ILE LYS TYR ILE SER SER ASN
SEQRES 10 A 387 ILE THR GLN THR LEU ALA VAL PRO GLY LEU GLU ALA GLY
SEQRES 11 A 387 MET ARG HIS ALA PHE GLU ASN LEU TRP PRO VAL LEU MET
SEQRES 12 A 387 ALA LEU PRO ASP PHE LEU ALA GLU ARG LYS TYR PRO ASP
SEQRES 13 A 387 ILE VAL ASP ALA LYS ASP THR ALA PHE GLN LYS ALA PHE
SEQRES 14 A 387 ASN THR ASP GLN ASP CYS PHE HIS TRP LEU ALA THR GLN
SEQRES 15 A 387 PRO THR ARG ILE ALA ASN PHE LYS VAL LEU LEU THR ASP
SEQRES 16 A 387 GLU ARG THR PRO ASN PHE LEU SER THR PHE PRO LEU GLU
SEQRES 17 A 387 LYS GLU LEU GLY SER TRP SER ALA GLU PRO GLU LYS ALA
SEQRES 18 A 387 LEU PHE VAL ASP ILE GLY GLY GLY MET GLY HIS ALA CYS
SEQRES 19 A 387 ILE ARG LEU ARG GLU LYS TYR PRO ASN GLN PRO GLY ARG
SEQRES 20 A 387 VAL ILE LEU GLN ASP LEU PRO PRO VAL LEU GLN ALA ALA
SEQRES 21 A 387 GLN ALA THR LEU PRO LEU SER GLY ILE GLU SER MET PRO
SEQRES 22 A 387 HIS ASN PHE HIS THR PRO GLN PRO VAL GLN GLY ALA LYS
SEQRES 23 A 387 PHE TYR PHE LEU ARG LEU ILE LEU ARG ASP PHE PRO ASP
SEQRES 24 A 387 HIS GLN ALA LEU GLU ILE LEU GLN ASN ILE VAL PRO ALA
SEQRES 25 A 387 MET ASP ALA GLU SER ARG ILE VAL ILE ASP ASP GLY VAL
SEQRES 26 A 387 PRO PRO GLU LYS GLY ALA ARG TRP ALA GLU THR GLY THR
SEQRES 27 A 387 ASP ILE CYS ILE MET SER ALA LEU GLY SER LYS GLU ARG
SEQRES 28 A 387 THR GLN ARG GLN TRP GLU GLU LEU ALA ALA LYS ALA GLY
SEQRES 29 A 387 LEU GLN LEU GLN ALA LEU TYR GLN TYR THR TRP PRO VAL
SEQRES 30 A 387 VAL ASN ALA ALA MET VAL PHE SER LEU GLN
SEQRES 1 B 387 MET GLU THR VAL ALA ALA ILE LYS THR LEU ILE GLN GLN
SEQRES 2 B 387 LEU ALA GLN SER THR ASP GLN PHE GLY ARG ALA GLU ILE
SEQRES 3 B 387 ASN ASP ALA LEU ARG GLU LEU GLN TYR SER LEU GLU THR
SEQRES 4 B 387 PRO PHE ASP THR VAL MET ARG MET SER LEU ASP THR CYS
SEQRES 5 B 387 GLN VAL ALA VAL ALA ARG ILE GLY SER ASP LEU GLY LEU
SEQRES 6 B 387 PHE LYS HIS LEU SER GLN CYS ALA SER PRO GLN SER ALA
SEQRES 7 B 387 GLU GLU LEU ALA ASP HIS LEU GLY CYS GLY ARG GLU LEU
SEQRES 8 B 387 MET SER ARG LEU LEU ARG TYR MET ALA SER VAL ARG MET
SEQRES 9 B 387 VAL GLN GLN THR ASP ASP ILE LYS TYR ILE SER SER ASN
SEQRES 10 B 387 ILE THR GLN THR LEU ALA VAL PRO GLY LEU GLU ALA GLY
SEQRES 11 B 387 MET ARG HIS ALA PHE GLU ASN LEU TRP PRO VAL LEU MET
SEQRES 12 B 387 ALA LEU PRO ASP PHE LEU ALA GLU ARG LYS TYR PRO ASP
SEQRES 13 B 387 ILE VAL ASP ALA LYS ASP THR ALA PHE GLN LYS ALA PHE
SEQRES 14 B 387 ASN THR ASP GLN ASP CYS PHE HIS TRP LEU ALA THR GLN
SEQRES 15 B 387 PRO THR ARG ILE ALA ASN PHE LYS VAL LEU LEU THR ASP
SEQRES 16 B 387 GLU ARG THR PRO ASN PHE LEU SER THR PHE PRO LEU GLU
SEQRES 17 B 387 LYS GLU LEU GLY SER TRP SER ALA GLU PRO GLU LYS ALA
SEQRES 18 B 387 LEU PHE VAL ASP ILE GLY GLY GLY MET GLY HIS ALA CYS
SEQRES 19 B 387 ILE ARG LEU ARG GLU LYS TYR PRO ASN GLN PRO GLY ARG
SEQRES 20 B 387 VAL ILE LEU GLN ASP LEU PRO PRO VAL LEU GLN ALA ALA
SEQRES 21 B 387 GLN ALA THR LEU PRO LEU SER GLY ILE GLU SER MET PRO
SEQRES 22 B 387 HIS ASN PHE HIS THR PRO GLN PRO VAL GLN GLY ALA LYS
SEQRES 23 B 387 PHE TYR PHE LEU ARG LEU ILE LEU ARG ASP PHE PRO ASP
SEQRES 24 B 387 HIS GLN ALA LEU GLU ILE LEU GLN ASN ILE VAL PRO ALA
SEQRES 25 B 387 MET ASP ALA GLU SER ARG ILE VAL ILE ASP ASP GLY VAL
SEQRES 26 B 387 PRO PRO GLU LYS GLY ALA ARG TRP ALA GLU THR GLY THR
SEQRES 27 B 387 ASP ILE CYS ILE MET SER ALA LEU GLY SER LYS GLU ARG
SEQRES 28 B 387 THR GLN ARG GLN TRP GLU GLU LEU ALA ALA LYS ALA GLY
SEQRES 29 B 387 LEU GLN LEU GLN ALA LEU TYR GLN TYR THR TRP PRO VAL
SEQRES 30 B 387 VAL ASN ALA ALA MET VAL PHE SER LEU GLN
HET SAH A 401 26
HET SAH B 401 26
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 3 SAH 2(C14 H20 N6 O5 S)
FORMUL 5 HOH *20(H2 O)
HELIX 1 AA1 MET A 1 THR A 18 1 18
HELIX 2 AA2 ASP A 19 LEU A 37 1 19
HELIX 3 AA3 THR A 39 ASP A 50 1 12
HELIX 4 AA4 THR A 51 GLY A 64 1 14
HELIX 5 AA5 GLY A 64 GLN A 71 1 8
HELIX 6 AA6 SER A 77 GLY A 86 1 10
HELIX 7 AA7 GLY A 88 VAL A 102 1 15
HELIX 8 AA8 SER A 116 VAL A 124 1 9
HELIX 9 AA9 VAL A 124 ASN A 137 1 14
HELIX 10 AB1 ASN A 137 ARG A 152 1 16
HELIX 11 AB2 THR A 163 ASN A 170 1 8
HELIX 12 AB3 ASP A 174 THR A 181 1 8
HELIX 13 AB4 GLN A 182 LEU A 193 1 12
HELIX 14 AB5 ASN A 200 THR A 204 5 5
HELIX 15 AB6 PRO A 206 GLY A 212 1 7
HELIX 16 AB7 GLY A 231 TYR A 241 1 11
HELIX 17 AB8 LEU A 253 GLN A 261 1 9
HELIX 18 AB9 ALA A 262 LEU A 264 5 3
HELIX 19 AC1 ILE A 293 PHE A 297 5 5
HELIX 20 AC2 PRO A 298 ASN A 308 1 11
HELIX 21 AC3 ILE A 309 MET A 313 5 5
HELIX 22 AC4 ARG A 332 GLY A 347 1 16
HELIX 23 AC5 THR A 352 ALA A 363 1 12
HELIX 24 AC6 GLU B 2 THR B 18 1 17
HELIX 25 AC7 ASP B 19 GLU B 38 1 20
HELIX 26 AC8 THR B 39 ASP B 50 1 12
HELIX 27 AC9 THR B 51 GLY B 64 1 14
HELIX 28 AD1 GLY B 64 GLN B 71 1 8
HELIX 29 AD2 SER B 77 GLY B 86 1 10
HELIX 30 AD3 GLY B 88 VAL B 102 1 15
HELIX 31 AD4 SER B 116 VAL B 124 1 9
HELIX 32 AD5 VAL B 124 ASN B 137 1 14
HELIX 33 AD6 ASN B 137 ARG B 152 1 16
HELIX 34 AD7 THR B 163 ASN B 170 1 8
HELIX 35 AD8 ASP B 174 THR B 181 1 8
HELIX 36 AD9 GLN B 182 THR B 194 1 13
HELIX 37 AE1 ASN B 200 THR B 204 5 5
HELIX 38 AE2 PRO B 206 GLY B 212 1 7
HELIX 39 AE3 GLY B 231 TYR B 241 1 11
HELIX 40 AE4 LEU B 253 GLN B 261 1 9
HELIX 41 AE5 ILE B 293 PHE B 297 5 5
HELIX 42 AE6 PRO B 298 ASN B 308 1 11
HELIX 43 AE7 ILE B 309 MET B 313 5 5
HELIX 44 AE8 ARG B 332 GLY B 347 1 16
HELIX 45 AE9 THR B 352 ALA B 363 1 12
SHEET 1 AA1 2 GLN A 106 GLN A 107 0
SHEET 2 AA1 2 TYR A 113 ILE A 114 -1 O ILE A 114 N GLN A 106
SHEET 1 AA2 7 ILE A 269 PRO A 273 0
SHEET 2 AA2 7 ARG A 247 ASP A 252 1 N LEU A 250 O GLU A 270
SHEET 3 AA2 7 ALA A 221 ILE A 226 1 N ASP A 225 O ILE A 249
SHEET 4 AA2 7 PHE A 287 ARG A 291 1 O PHE A 289 N VAL A 224
SHEET 5 AA2 7 ARG A 318 GLY A 324 1 O VAL A 320 N TYR A 288
SHEET 6 AA2 7 ASN A 379 SER A 385 -1 O PHE A 384 N ILE A 319
SHEET 7 AA2 7 GLN A 366 GLN A 372 -1 N GLN A 368 O VAL A 383
SHEET 1 AA3 2 GLN B 106 GLN B 107 0
SHEET 2 AA3 2 TYR B 113 ILE B 114 -1 O ILE B 114 N GLN B 106
SHEET 1 AA4 7 ILE B 269 PRO B 273 0
SHEET 2 AA4 7 ARG B 247 ASP B 252 1 N LEU B 250 O GLU B 270
SHEET 3 AA4 7 ALA B 221 ILE B 226 1 N PHE B 223 O ILE B 249
SHEET 4 AA4 7 PHE B 287 ARG B 291 1 O PHE B 289 N VAL B 224
SHEET 5 AA4 7 ARG B 318 GLY B 324 1 O VAL B 320 N TYR B 288
SHEET 6 AA4 7 ASN B 379 SER B 385 -1 O PHE B 384 N ILE B 319
SHEET 7 AA4 7 GLN B 366 GLN B 372 -1 N GLN B 368 O VAL B 383
CISPEP 1 THR A 198 PRO A 199 0 -0.76
CISPEP 2 GLU A 217 PRO A 218 0 -0.64
CISPEP 3 TRP A 375 PRO A 376 0 -1.69
CISPEP 4 THR B 198 PRO B 199 0 0.10
CISPEP 5 GLU B 217 PRO B 218 0 -0.93
CISPEP 6 TRP B 375 PRO B 376 0 -1.41
SITE 1 AC1 12 LEU A 193 GLY A 227 GLY A 228 GLY A 229
SITE 2 AC1 12 ASP A 252 LEU A 253 VAL A 256 HIS A 274
SITE 3 AC1 12 ASN A 275 PHE A 276 HIS A 277 ARG A 291
SITE 1 AC2 10 LEU B 193 GLY B 227 GLY B 229 ASP B 252
SITE 2 AC2 10 VAL B 256 HIS B 274 ASN B 275 PHE B 276
SITE 3 AC2 10 ARG B 291 HOH B 508
CRYST1 159.817 62.333 112.735 90.00 112.45 90.00 C 1 2 1 8
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 0.006257 0.000000 0.002585 0.00000
SCALE2 0.000000 0.016043 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END