HEADER TRANSFERASE 12-FEB-10 3LST
TITLE CRYSTAL STRUCTURE OF CALO1, METHYLTRANSFERASE IN CALICHEAMICIN
TITLE 2 BIOSYNTHESIS, SAH BOUND FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALO1 METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA ECHINOSPORA;
SOURCE 3 ORGANISM_COMMON: MICROMONOSPORA PURPUREA;
SOURCE 4 ORGANISM_TAXID: 1877;
SOURCE 5 GENE: CALO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834 P(RARE2);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS CALICHEAMICIN, METHYLTRANSFERASE, CALO1, ENEDIYNE, SAH, STRUCTURAL
KEYWDS 2 GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, CENTER FOR EUKARYOTIC
KEYWDS 3 STRUCTURAL GENOMICS, CESG, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHANG,S.SINGH,C.A.BINGMAN,J.S.THORSON,G.N.PHILLIPS JR.,CENTER FOR
AUTHOR 2 EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 3 01-NOV-17 3LST 1 REMARK
REVDAT 2 16-MAR-11 3LST 1 JRNL
REVDAT 1 02-MAR-10 3LST 0
JRNL AUTH A.CHANG,S.SINGH,C.A.BINGMAN,J.S.THORSON,G.N.PHILLIPS
JRNL TITL STRUCTURAL CHARACTERIZATION OF CALO1: A PUTATIVE ORSELLINIC
JRNL TITL 2 ACID METHYLTRANSFERASE IN THE CALICHEAMICIN-BIOSYNTHETIC
JRNL TITL 3 PATHWAY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 67 197 2011
JRNL REFN ISSN 0907-4449
JRNL PMID 21358050
JRNL DOI 10.1107/S090744491100360X
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.320
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 27959
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1411
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 48.1830 - 5.1690 1.00 2847 167 0.1730 0.2040
REMARK 3 2 5.1690 - 4.1030 1.00 2771 142 0.1450 0.2050
REMARK 3 3 4.1030 - 3.5850 1.00 2721 138 0.1690 0.2350
REMARK 3 4 3.5850 - 3.2570 1.00 2743 131 0.2170 0.2370
REMARK 3 5 3.2570 - 3.0240 1.00 2665 152 0.2280 0.2900
REMARK 3 6 3.0240 - 2.8450 1.00 2708 130 0.2220 0.2850
REMARK 3 7 2.8450 - 2.7030 1.00 2671 159 0.2290 0.2800
REMARK 3 8 2.7030 - 2.5850 0.99 2639 126 0.2500 0.3310
REMARK 3 9 2.5850 - 2.4860 0.93 2503 144 0.2450 0.3300
REMARK 3 10 2.4860 - 2.4000 0.86 2280 122 0.2590 0.3030
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 : 40.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50800
REMARK 3 B22 (A**2) : -2.32600
REMARK 3 B33 (A**2) : 1.89100
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 : 0.004 5222
REMARK 3 ANGLE : 0.717 7098
REMARK 3 CHIRALITY : 0.049 808
REMARK 3 PLANARITY : 0.002 938
REMARK 3 DIHEDRAL : 14.893 1882
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 3LST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057685.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-09
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 : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794, 0.9641
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATER
REMARK 200 OPTICS : ADJUSTABLE FOCUSING MIRRORS IN K
REMARK 200 -B GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28057
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 97.7
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
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) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.00
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION 20MG/ML CALO1
REMARK 280 PROTEIN, 20MM TRIS PH 8, MIXED IN A 1:1 RATIO WITH THE WELL
REMARK 280 SOLUTION 20% MEPEG 5K, 0.2M GLYCINE, 0.1M BTP PH 7.0.
REMARK 280 CRYOPROTECTED WITH 20% ETHYLENE GLYCOL, 20% MEPEG 5K, 0.2M
REMARK 280 GLYCINE, 0.1M BTP PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 120.48550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 120.48550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 31.75750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.80150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.75750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.80150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 120.48550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.75750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.80150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 120.48550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.75750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.80150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER. THERE ARE HALF OF 2
REMARK 300 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT. THE DIMER GENERATED FROM
REMARK 300 THE MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: X, -Y,-Z AND -
REMARK 300 X, Y,-Z+1/2
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: 8500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 93.60300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 240.97100
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 8920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 120.48550
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 398 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 429 LIES ON A SPECIAL POSITION.
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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 GLN A 2
REMARK 465 ARG A 3
REMARK 465 GLN A 4
REMARK 465 ARG A 5
REMARK 465 PRO A 6
REMARK 465 PRO A 7
REMARK 465 SER A 8
REMARK 465 ARG A 9
REMARK 465 ALA A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 12
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 GLN B 2
REMARK 465 ARG B 3
REMARK 465 GLN B 4
REMARK 465 ARG B 5
REMARK 465 PRO B 6
REMARK 465 PRO B 7
REMARK 465 SER B 8
REMARK 465 ARG B 9
REMARK 465 ALA B 10
REMARK 465 GLY B 11
REMARK 465 GLY B 12
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 133 69.29 63.92
REMARK 500 ASP A 212 -178.88 -170.06
REMARK 500 ILE A 253 -65.00 -108.53
REMARK 500 LEU A 327 96.13 -62.79
REMARK 500 ARG B 133 77.16 56.84
REMARK 500 SER B 142 152.77 179.08
REMARK 500 HIS B 220 152.28 -43.86
REMARK 500 ASP B 223 42.26 -81.71
REMARK 500 VAL B 272 30.52 -99.85
REMARK 500 SER B 334 2.42 -69.74
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 346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 347
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 347
DBREF 3LST A 1 345 UNP Q8KNE5 Q8KNE5_MICEC 1 345
DBREF 3LST B 1 345 UNP Q8KNE5 Q8KNE5_MICEC 1 345
SEQADV 3LST GLY A -2 UNP Q8KNE5 EXPRESSION TAG
SEQADV 3LST SER A -1 UNP Q8KNE5 EXPRESSION TAG
SEQADV 3LST HIS A 0 UNP Q8KNE5 EXPRESSION TAG
SEQADV 3LST GLY B -2 UNP Q8KNE5 EXPRESSION TAG
SEQADV 3LST SER B -1 UNP Q8KNE5 EXPRESSION TAG
SEQADV 3LST HIS B 0 UNP Q8KNE5 EXPRESSION TAG
SEQRES 1 A 348 GLY SER HIS MSE GLN ARG GLN ARG PRO PRO SER ARG ALA
SEQRES 2 A 348 GLY GLY ASP MSE ASP ARG LEU GLN SER ALA LEU ALA LEU
SEQRES 3 A 348 TYR GLU GLU ALA MSE GLY TYR THR TYR ALA ALA ALA LEU
SEQRES 4 A 348 ARG ALA ALA ALA ALA VAL GLY VAL ALA ASP HIS LEU VAL
SEQRES 5 A 348 ASP GLY PRO ARG THR PRO ALA GLU LEU ALA ALA ALA THR
SEQRES 6 A 348 GLY THR ASP ALA ASP ALA LEU ARG ARG VAL LEU ARG LEU
SEQRES 7 A 348 LEU ALA VAL ARG ASP VAL VAL ARG GLU SER ASP GLY ARG
SEQRES 8 A 348 PHE ALA LEU THR ASP LYS GLY ALA ALA LEU ARG SER ASP
SEQRES 9 A 348 SER PRO VAL PRO ALA ARG ALA GLY ILE LEU MSE PHE THR
SEQRES 10 A 348 ASP THR MSE PHE TRP THR MSE SER HIS ARG VAL ALA SER
SEQRES 11 A 348 ALA LEU GLY PRO GLU ARG PRO ALA PHE ALA ASP ILE PHE
SEQRES 12 A 348 GLY SER SER LEU ASP ALA TYR PHE ASP GLY ASP ALA GLU
SEQRES 13 A 348 VAL GLU ALA LEU TYR TYR GLU GLY MSE GLU THR VAL SER
SEQRES 14 A 348 ALA ALA GLU HIS LEU ILE LEU ALA ARG ALA GLY ASP PHE
SEQRES 15 A 348 PRO ALA THR GLY THR VAL ALA ASP VAL GLY GLY GLY ARG
SEQRES 16 A 348 GLY GLY PHE LEU LEU THR VAL LEU ARG GLU HIS PRO GLY
SEQRES 17 A 348 LEU GLN GLY VAL LEU LEU ASP ARG ALA GLU VAL VAL ALA
SEQRES 18 A 348 ARG HIS ARG LEU ASP ALA PRO ASP VAL ALA GLY ARG TRP
SEQRES 19 A 348 LYS VAL VAL GLU GLY ASP PHE LEU ARG GLU VAL PRO HIS
SEQRES 20 A 348 ALA ASP VAL HIS VAL LEU LYS ARG ILE LEU HIS ASN TRP
SEQRES 21 A 348 GLY ASP GLU ASP SER VAL ARG ILE LEU THR ASN CYS ARG
SEQRES 22 A 348 ARG VAL MSE PRO ALA HIS GLY ARG VAL LEU VAL ILE ASP
SEQRES 23 A 348 ALA VAL VAL PRO GLU GLY ASN ASP ALA HIS GLN SER LYS
SEQRES 24 A 348 GLU MSE ASP PHE MSE MSE LEU ALA ALA ARG THR GLY GLN
SEQRES 25 A 348 GLU ARG THR ALA ALA GLU LEU GLU PRO LEU PHE THR ALA
SEQRES 26 A 348 ALA GLY LEU ARG LEU ASP ARG VAL VAL GLY THR SER SER
SEQRES 27 A 348 VAL MSE SER ILE ALA VAL GLY VAL PRO ALA
SEQRES 1 B 348 GLY SER HIS MSE GLN ARG GLN ARG PRO PRO SER ARG ALA
SEQRES 2 B 348 GLY GLY ASP MSE ASP ARG LEU GLN SER ALA LEU ALA LEU
SEQRES 3 B 348 TYR GLU GLU ALA MSE GLY TYR THR TYR ALA ALA ALA LEU
SEQRES 4 B 348 ARG ALA ALA ALA ALA VAL GLY VAL ALA ASP HIS LEU VAL
SEQRES 5 B 348 ASP GLY PRO ARG THR PRO ALA GLU LEU ALA ALA ALA THR
SEQRES 6 B 348 GLY THR ASP ALA ASP ALA LEU ARG ARG VAL LEU ARG LEU
SEQRES 7 B 348 LEU ALA VAL ARG ASP VAL VAL ARG GLU SER ASP GLY ARG
SEQRES 8 B 348 PHE ALA LEU THR ASP LYS GLY ALA ALA LEU ARG SER ASP
SEQRES 9 B 348 SER PRO VAL PRO ALA ARG ALA GLY ILE LEU MSE PHE THR
SEQRES 10 B 348 ASP THR MSE PHE TRP THR MSE SER HIS ARG VAL ALA SER
SEQRES 11 B 348 ALA LEU GLY PRO GLU ARG PRO ALA PHE ALA ASP ILE PHE
SEQRES 12 B 348 GLY SER SER LEU ASP ALA TYR PHE ASP GLY ASP ALA GLU
SEQRES 13 B 348 VAL GLU ALA LEU TYR TYR GLU GLY MSE GLU THR VAL SER
SEQRES 14 B 348 ALA ALA GLU HIS LEU ILE LEU ALA ARG ALA GLY ASP PHE
SEQRES 15 B 348 PRO ALA THR GLY THR VAL ALA ASP VAL GLY GLY GLY ARG
SEQRES 16 B 348 GLY GLY PHE LEU LEU THR VAL LEU ARG GLU HIS PRO GLY
SEQRES 17 B 348 LEU GLN GLY VAL LEU LEU ASP ARG ALA GLU VAL VAL ALA
SEQRES 18 B 348 ARG HIS ARG LEU ASP ALA PRO ASP VAL ALA GLY ARG TRP
SEQRES 19 B 348 LYS VAL VAL GLU GLY ASP PHE LEU ARG GLU VAL PRO HIS
SEQRES 20 B 348 ALA ASP VAL HIS VAL LEU LYS ARG ILE LEU HIS ASN TRP
SEQRES 21 B 348 GLY ASP GLU ASP SER VAL ARG ILE LEU THR ASN CYS ARG
SEQRES 22 B 348 ARG VAL MSE PRO ALA HIS GLY ARG VAL LEU VAL ILE ASP
SEQRES 23 B 348 ALA VAL VAL PRO GLU GLY ASN ASP ALA HIS GLN SER LYS
SEQRES 24 B 348 GLU MSE ASP PHE MSE MSE LEU ALA ALA ARG THR GLY GLN
SEQRES 25 B 348 GLU ARG THR ALA ALA GLU LEU GLU PRO LEU PHE THR ALA
SEQRES 26 B 348 ALA GLY LEU ARG LEU ASP ARG VAL VAL GLY THR SER SER
SEQRES 27 B 348 VAL MSE SER ILE ALA VAL GLY VAL PRO ALA
MODRES 3LST MSE A 14 MET SELENOMETHIONINE
MODRES 3LST MSE A 28 MET SELENOMETHIONINE
MODRES 3LST MSE A 112 MET SELENOMETHIONINE
MODRES 3LST MSE A 117 MET SELENOMETHIONINE
MODRES 3LST MSE A 121 MET SELENOMETHIONINE
MODRES 3LST MSE A 162 MET SELENOMETHIONINE
MODRES 3LST MSE A 273 MET SELENOMETHIONINE
MODRES 3LST MSE A 298 MET SELENOMETHIONINE
MODRES 3LST MSE A 301 MET SELENOMETHIONINE
MODRES 3LST MSE A 302 MET SELENOMETHIONINE
MODRES 3LST MSE A 337 MET SELENOMETHIONINE
MODRES 3LST MSE B 14 MET SELENOMETHIONINE
MODRES 3LST MSE B 28 MET SELENOMETHIONINE
MODRES 3LST MSE B 112 MET SELENOMETHIONINE
MODRES 3LST MSE B 117 MET SELENOMETHIONINE
MODRES 3LST MSE B 121 MET SELENOMETHIONINE
MODRES 3LST MSE B 162 MET SELENOMETHIONINE
MODRES 3LST MSE B 273 MET SELENOMETHIONINE
MODRES 3LST MSE B 298 MET SELENOMETHIONINE
MODRES 3LST MSE B 301 MET SELENOMETHIONINE
MODRES 3LST MSE B 302 MET SELENOMETHIONINE
MODRES 3LST MSE B 337 MET SELENOMETHIONINE
HET MSE A 14 8
HET MSE A 28 8
HET MSE A 112 8
HET MSE A 117 8
HET MSE A 121 8
HET MSE A 162 8
HET MSE A 273 8
HET MSE A 298 8
HET MSE A 301 8
HET MSE A 302 8
HET MSE A 337 8
HET MSE B 14 8
HET MSE B 28 8
HET MSE B 112 8
HET MSE B 117 8
HET MSE B 121 8
HET MSE B 162 8
HET MSE B 273 8
HET MSE B 298 8
HET MSE B 301 8
HET MSE B 302 8
HET MSE B 337 8
HET SAH A 346 26
HET EDO A 347 4
HET SAH B 346 26
HET EDO B 347 4
HETNAM MSE SELENOMETHIONINE
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 3 SAH 2(C14 H20 N6 O5 S)
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 7 HOH *181(H2 O)
HELIX 1 1 ASP A 15 MSE A 28 1 14
HELIX 2 2 TYR A 30 GLY A 43 1 14
HELIX 3 3 VAL A 44 VAL A 49 5 6
HELIX 4 4 THR A 54 GLY A 63 1 10
HELIX 5 5 ASP A 65 ARG A 79 1 15
HELIX 6 6 GLY A 95 ARG A 99 5 5
HELIX 7 7 ALA A 106 THR A 114 1 9
HELIX 8 8 ASP A 115 ARG A 124 1 10
HELIX 9 9 ARG A 124 LEU A 129 1 6
HELIX 10 10 ALA A 135 GLY A 141 1 7
HELIX 11 11 SER A 143 ASP A 149 1 7
HELIX 12 12 ASP A 151 ALA A 168 1 18
HELIX 13 13 GLU A 169 GLY A 177 1 9
HELIX 14 14 GLY A 193 HIS A 203 1 11
HELIX 15 15 ARG A 213 ALA A 218 1 6
HELIX 16 16 ALA A 224 ALA A 228 5 5
HELIX 17 17 ILE A 253 TRP A 257 5 5
HELIX 18 18 GLY A 258 VAL A 272 1 15
HELIX 19 19 HIS A 293 ALA A 305 1 13
HELIX 20 20 THR A 312 ALA A 323 1 12
HELIX 21 21 ASP B 15 MSE B 28 1 14
HELIX 22 22 TYR B 30 GLY B 43 1 14
HELIX 23 23 VAL B 44 LEU B 48 5 5
HELIX 24 24 THR B 54 GLY B 63 1 10
HELIX 25 25 ASP B 65 ARG B 79 1 15
HELIX 26 26 GLY B 95 ARG B 99 5 5
HELIX 27 27 ALA B 106 THR B 114 1 9
HELIX 28 28 ASP B 115 ARG B 124 1 10
HELIX 29 29 ALA B 126 GLY B 130 5 5
HELIX 30 30 ALA B 135 GLY B 141 1 7
HELIX 31 31 SER B 143 ASP B 151 1 9
HELIX 32 32 ASP B 151 GLY B 177 1 27
HELIX 33 33 GLY B 193 HIS B 203 1 11
HELIX 34 34 ARG B 213 ALA B 218 1 6
HELIX 35 35 ALA B 224 ALA B 228 5 5
HELIX 36 36 ILE B 253 TRP B 257 5 5
HELIX 37 37 GLY B 258 VAL B 272 1 15
HELIX 38 38 HIS B 293 ARG B 306 1 14
HELIX 39 39 THR B 312 ALA B 323 1 12
SHEET 1 A 2 VAL A 82 SER A 85 0
SHEET 2 A 2 ARG A 88 LEU A 91 -1 O ALA A 90 N ARG A 83
SHEET 1 B 7 TRP A 231 GLU A 235 0
SHEET 2 B 7 LEU A 206 ASP A 212 1 N LEU A 210 O VAL A 234
SHEET 3 B 7 GLY A 183 VAL A 188 1 N VAL A 185 O VAL A 209
SHEET 4 B 7 VAL A 247 LYS A 251 1 O VAL A 249 N ALA A 186
SHEET 5 B 7 ARG A 278 ASP A 283 1 O LEU A 280 N HIS A 248
SHEET 6 B 7 SER A 338 PRO A 344 -1 O ALA A 340 N VAL A 281
SHEET 7 B 7 LEU A 325 GLY A 332 -1 N ARG A 329 O VAL A 341
SHEET 1 C 2 VAL B 82 SER B 85 0
SHEET 2 C 2 ARG B 88 LEU B 91 -1 O ARG B 88 N SER B 85
SHEET 1 D 7 TRP B 231 GLU B 235 0
SHEET 2 D 7 GLN B 207 ASP B 212 1 N LEU B 210 O VAL B 234
SHEET 3 D 7 THR B 184 VAL B 188 1 N VAL B 185 O VAL B 209
SHEET 4 D 7 VAL B 247 LYS B 251 1 O VAL B 247 N ALA B 186
SHEET 5 D 7 ARG B 278 ASP B 283 1 O LEU B 280 N HIS B 248
SHEET 6 D 7 SER B 338 PRO B 344 -1 O SER B 338 N ASP B 283
SHEET 7 D 7 LEU B 325 VAL B 331 -1 N ARG B 329 O VAL B 341
LINK C ASP A 13 N MSE A 14 1555 1555 1.33
LINK C MSE A 14 N ASP A 15 1555 1555 1.33
LINK C ALA A 27 N MSE A 28 1555 1555 1.33
LINK C MSE A 28 N GLY A 29 1555 1555 1.33
LINK C LEU A 111 N MSE A 112 1555 1555 1.33
LINK C MSE A 112 N PHE A 113 1555 1555 1.33
LINK C THR A 116 N MSE A 117 1555 1555 1.33
LINK C MSE A 117 N PHE A 118 1555 1555 1.33
LINK C THR A 120 N MSE A 121 1555 1555 1.33
LINK C MSE A 121 N SER A 122 1555 1555 1.33
LINK C GLY A 161 N MSE A 162 1555 1555 1.33
LINK C MSE A 162 N GLU A 163 1555 1555 1.33
LINK C VAL A 272 N MSE A 273 1555 1555 1.33
LINK C MSE A 273 N PRO A 274 1555 1555 1.34
LINK C GLU A 297 N MSE A 298 1555 1555 1.33
LINK C MSE A 298 N ASP A 299 1555 1555 1.33
LINK C PHE A 300 N MSE A 301 1555 1555 1.33
LINK C MSE A 301 N MSE A 302 1555 1555 1.33
LINK C MSE A 302 N LEU A 303 1555 1555 1.33
LINK C VAL A 336 N MSE A 337 1555 1555 1.33
LINK C MSE A 337 N SER A 338 1555 1555 1.33
LINK C ASP B 13 N MSE B 14 1555 1555 1.33
LINK C MSE B 14 N ASP B 15 1555 1555 1.33
LINK C ALA B 27 N MSE B 28 1555 1555 1.33
LINK C MSE B 28 N GLY B 29 1555 1555 1.33
LINK C LEU B 111 N MSE B 112 1555 1555 1.33
LINK C MSE B 112 N PHE B 113 1555 1555 1.33
LINK C THR B 116 N MSE B 117 1555 1555 1.33
LINK C MSE B 117 N PHE B 118 1555 1555 1.33
LINK C THR B 120 N MSE B 121 1555 1555 1.33
LINK C MSE B 121 N SER B 122 1555 1555 1.33
LINK C GLY B 161 N MSE B 162 1555 1555 1.33
LINK C MSE B 162 N GLU B 163 1555 1555 1.33
LINK C VAL B 272 N MSE B 273 1555 1555 1.33
LINK C MSE B 273 N PRO B 274 1555 1555 1.34
LINK C GLU B 297 N MSE B 298 1555 1555 1.33
LINK C MSE B 298 N ASP B 299 1555 1555 1.33
LINK C PHE B 300 N MSE B 301 1555 1555 1.33
LINK C MSE B 301 N MSE B 302 1555 1555 1.33
LINK C MSE B 302 N LEU B 303 1555 1555 1.33
LINK C VAL B 336 N MSE B 337 1555 1555 1.33
LINK C MSE B 337 N SER B 338 1555 1555 1.33
CISPEP 1 THR A 62 GLY A 63 0 -3.33
CISPEP 2 PHE B 140 GLY B 141 0 -3.83
SITE 1 AC1 14 SER A 166 GLY A 189 GLY A 190 ASP A 212
SITE 2 AC1 14 ARG A 213 VAL A 216 ASP A 237 PHE A 238
SITE 3 AC1 14 LYS A 251 ARG A 252 ILE A 253 TRP A 257
SITE 4 AC1 14 HOH A 359 HOH A 390
SITE 1 AC2 4 GLU A 26 TYR A 32 ARG A 79 HOH A 381
SITE 1 AC3 12 GLY B 189 ASP B 212 ARG B 213 VAL B 216
SITE 2 AC3 12 GLY B 236 ASP B 237 PHE B 238 LYS B 251
SITE 3 AC3 12 ARG B 252 ILE B 253 TRP B 257 HOH B 354
SITE 1 AC4 4 GLU B 26 GLY B 29 TYR B 32 ARG B 79
CRYST1 63.515 93.603 240.971 90.00 90.00 90.00 C 2 2 21 16
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 0.015744 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010683 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004150 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
