HEADER TRANSFERASE 26-NOV-09 3KTY
TITLE CRYSTAL STRUCTURE OF PROBABLE METHYLTRANSFERASE FROM BORDETELLA
TITLE 2 PERTUSSIS TOHAMA I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: TARGET DOMAIN 1 - 170;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORDETELLA PERTUSSIS;
SOURCE 3 ORGANISM_TAXID: 520;
SOURCE 4 STRAIN: TOHAMA I;
SOURCE 5 GENE: BP1901;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS ALPHA-BETA-ALPHA SANDWICH, STRUCTURAL GENOMICS, PSI-2, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 3 METHYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,C.TESAR,L.KEIGHER,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 2 13-JUL-11 3KTY 1 VERSN
REVDAT 1 08-DEC-09 3KTY 0
JRNL AUTH Y.KIM,C.TESAR,L.KEIGHER,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF PROBABLE METHYLTRANSFERASE SPOU FROM
JRNL TITL 2 BORDETELLA PERTUSSIS TOHAMA I
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 22502
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1151
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 43.5315 - 4.6014 0.99 2712 151 0.1648 0.2066
REMARK 3 2 4.6014 - 3.6529 0.99 2672 146 0.1551 0.2080
REMARK 3 3 3.6529 - 3.1913 1.00 2684 133 0.1783 0.2142
REMARK 3 4 3.1913 - 2.8996 1.00 2663 144 0.1981 0.2747
REMARK 3 5 2.8996 - 2.6918 1.00 2656 148 0.2074 0.2669
REMARK 3 6 2.6918 - 2.5331 1.00 2689 136 0.2079 0.2978
REMARK 3 7 2.5331 - 2.4062 1.00 2659 147 0.2258 0.2940
REMARK 3 8 2.4062 - 2.3015 0.97 2616 146 0.2518 0.3389
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 : 0.32
REMARK 3 B_SOL : 45.37
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.52
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.51540
REMARK 3 B22 (A**2) : -1.91740
REMARK 3 B33 (A**2) : -8.59790
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.00820
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 : 0.013 3999
REMARK 3 ANGLE : 1.409 5462
REMARK 3 CHIRALITY : 0.081 646
REMARK 3 PLANARITY : 0.008 723
REMARK 3 DIHEDRAL : 19.615 1454
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4022 30.6409 104.4493
REMARK 3 T TENSOR
REMARK 3 T11: 0.0570 T22: 0.0843
REMARK 3 T33: 0.0926 T12: 0.0335
REMARK 3 T13: 0.0201 T23: -0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 2.9393 L22: 3.5531
REMARK 3 L33: 3.9265 L12: -0.7377
REMARK 3 L13: 1.6783 L23: -1.7297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0296 S12: -0.2252 S13: 0.2053
REMARK 3 S21: -0.0950 S22: 0.1310 S23: 0.0746
REMARK 3 S31: -0.2515 S32: -0.3503 S33: -0.0945
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 3KTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB056443.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22535
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 43.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
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 (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.62300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL3000, SHELXS,MLPHARE,RESOLVE,SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE MONOHYDRATE, 0.1
REMARK 280 M HEPES PH7.5, 25 % W/V POLYEHTLYENE GLYCOL 3,350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 297K
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 21.24000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.75700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 21.24000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.75700
REMARK 290 SMTRY3 4 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 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: 2820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 11.03756
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 348.18721
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: 3220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 VAL A 89
REMARK 465 ARG A 90
REMARK 465 ASP A 91
REMARK 465 LEU A 92
REMARK 465 GLY A 93
REMARK 465 ALA A 127
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
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 OG SER C 57 O4 SO4 C 181 2.16
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 NH1 ARG B 90 O HOH B 189 3445 2.11
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 SER A 57 121.74 -34.31
REMARK 500 TYR A 149 55.56 -145.45
REMARK 500 ASN A 153 142.87 -39.22
REMARK 500 ALA B 56 54.68 -97.50
REMARK 500 ALA B 127 -21.89 -145.15
REMARK 500 TYR B 149 63.01 -151.52
REMARK 500 LEU C 55 6.72 -59.70
REMARK 500 SER C 57 114.35 -37.67
REMARK 500 PRO C 95 133.65 -34.37
REMARK 500 PRO C 147 -28.79 -39.14
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 GOL B 181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 181
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC62466.2 RELATED DB: TARGETDB
DBREF 3KTY A 1 170 UNP Q7VXA3 Q7VXA3_BORPE 1 170
DBREF 3KTY B 1 170 UNP Q7VXA3 Q7VXA3_BORPE 1 170
DBREF 3KTY C 1 170 UNP Q7VXA3 Q7VXA3_BORPE 1 170
SEQADV 3KTY SER A -2 UNP Q7VXA3 EXPRESSION TAG
SEQADV 3KTY ASN A -1 UNP Q7VXA3 EXPRESSION TAG
SEQADV 3KTY ALA A 0 UNP Q7VXA3 EXPRESSION TAG
SEQADV 3KTY SER B -2 UNP Q7VXA3 EXPRESSION TAG
SEQADV 3KTY ASN B -1 UNP Q7VXA3 EXPRESSION TAG
SEQADV 3KTY ALA B 0 UNP Q7VXA3 EXPRESSION TAG
SEQADV 3KTY SER C -2 UNP Q7VXA3 EXPRESSION TAG
SEQADV 3KTY ASN C -1 UNP Q7VXA3 EXPRESSION TAG
SEQADV 3KTY ALA C 0 UNP Q7VXA3 EXPRESSION TAG
SEQRES 1 A 173 SER ASN ALA MSE THR GLN ALA PHE SER ARG VAL ARG PHE
SEQRES 2 A 173 ILE MSE THR GLN PRO SER HIS PRO GLY ASN VAL GLY SER
SEQRES 3 A 173 ALA ALA ARG ALA ILE LYS THR MSE GLY PHE GLY GLU LEU
SEQRES 4 A 173 VAL LEU VAL ALA PRO ARG PHE PRO ASP MSE THR ALA GLN
SEQRES 5 A 173 PRO GLU ALA VAL ALA LEU ALA SER GLY ALA LEU ASP VAL
SEQRES 6 A 173 LEU GLU ARG ALA ALA VAL HIS ASP THR LEU GLU GLU ALA
SEQRES 7 A 173 LEU ALA PRO VAL THR LEU ALA PHE ALA LEU THR THR ARG
SEQRES 8 A 173 VAL ARG ASP LEU GLY PRO PRO PRO CYS ASP ILE ARG GLU
SEQRES 9 A 173 ALA ALA GLY LEU ALA ARG ARG HIS LEU ASP ASP THR GLU
SEQRES 10 A 173 ALA GLY VAL VAL ALA ILE VAL LEU GLY THR GLU ARG ALA
SEQRES 11 A 173 GLY LEU THR ASN ALA GLN ILE GLU LEU CYS HIS ARG ILE
SEQRES 12 A 173 CYS HIS ILE PRO ALA ASN PRO GLN TYR SER SER LEU ASN
SEQRES 13 A 173 VAL ALA GLN ALA LEU GLN LEU ALA ALA TRP GLU LEU ARG
SEQRES 14 A 173 TYR ALA LEU LEU
SEQRES 1 B 173 SER ASN ALA MSE THR GLN ALA PHE SER ARG VAL ARG PHE
SEQRES 2 B 173 ILE MSE THR GLN PRO SER HIS PRO GLY ASN VAL GLY SER
SEQRES 3 B 173 ALA ALA ARG ALA ILE LYS THR MSE GLY PHE GLY GLU LEU
SEQRES 4 B 173 VAL LEU VAL ALA PRO ARG PHE PRO ASP MSE THR ALA GLN
SEQRES 5 B 173 PRO GLU ALA VAL ALA LEU ALA SER GLY ALA LEU ASP VAL
SEQRES 6 B 173 LEU GLU ARG ALA ALA VAL HIS ASP THR LEU GLU GLU ALA
SEQRES 7 B 173 LEU ALA PRO VAL THR LEU ALA PHE ALA LEU THR THR ARG
SEQRES 8 B 173 VAL ARG ASP LEU GLY PRO PRO PRO CYS ASP ILE ARG GLU
SEQRES 9 B 173 ALA ALA GLY LEU ALA ARG ARG HIS LEU ASP ASP THR GLU
SEQRES 10 B 173 ALA GLY VAL VAL ALA ILE VAL LEU GLY THR GLU ARG ALA
SEQRES 11 B 173 GLY LEU THR ASN ALA GLN ILE GLU LEU CYS HIS ARG ILE
SEQRES 12 B 173 CYS HIS ILE PRO ALA ASN PRO GLN TYR SER SER LEU ASN
SEQRES 13 B 173 VAL ALA GLN ALA LEU GLN LEU ALA ALA TRP GLU LEU ARG
SEQRES 14 B 173 TYR ALA LEU LEU
SEQRES 1 C 173 SER ASN ALA MSE THR GLN ALA PHE SER ARG VAL ARG PHE
SEQRES 2 C 173 ILE MSE THR GLN PRO SER HIS PRO GLY ASN VAL GLY SER
SEQRES 3 C 173 ALA ALA ARG ALA ILE LYS THR MSE GLY PHE GLY GLU LEU
SEQRES 4 C 173 VAL LEU VAL ALA PRO ARG PHE PRO ASP MSE THR ALA GLN
SEQRES 5 C 173 PRO GLU ALA VAL ALA LEU ALA SER GLY ALA LEU ASP VAL
SEQRES 6 C 173 LEU GLU ARG ALA ALA VAL HIS ASP THR LEU GLU GLU ALA
SEQRES 7 C 173 LEU ALA PRO VAL THR LEU ALA PHE ALA LEU THR THR ARG
SEQRES 8 C 173 VAL ARG ASP LEU GLY PRO PRO PRO CYS ASP ILE ARG GLU
SEQRES 9 C 173 ALA ALA GLY LEU ALA ARG ARG HIS LEU ASP ASP THR GLU
SEQRES 10 C 173 ALA GLY VAL VAL ALA ILE VAL LEU GLY THR GLU ARG ALA
SEQRES 11 C 173 GLY LEU THR ASN ALA GLN ILE GLU LEU CYS HIS ARG ILE
SEQRES 12 C 173 CYS HIS ILE PRO ALA ASN PRO GLN TYR SER SER LEU ASN
SEQRES 13 C 173 VAL ALA GLN ALA LEU GLN LEU ALA ALA TRP GLU LEU ARG
SEQRES 14 C 173 TYR ALA LEU LEU
MODRES 3KTY MSE A 1 MET SELENOMETHIONINE
MODRES 3KTY MSE A 12 MET SELENOMETHIONINE
MODRES 3KTY MSE A 31 MET SELENOMETHIONINE
MODRES 3KTY MSE A 46 MET SELENOMETHIONINE
MODRES 3KTY MSE B 1 MET SELENOMETHIONINE
MODRES 3KTY MSE B 12 MET SELENOMETHIONINE
MODRES 3KTY MSE B 31 MET SELENOMETHIONINE
MODRES 3KTY MSE B 46 MET SELENOMETHIONINE
MODRES 3KTY MSE C 1 MET SELENOMETHIONINE
MODRES 3KTY MSE C 12 MET SELENOMETHIONINE
MODRES 3KTY MSE C 31 MET SELENOMETHIONINE
MODRES 3KTY MSE C 46 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 12 8
HET MSE A 31 8
HET MSE A 46 8
HET MSE B 1 8
HET MSE B 12 8
HET MSE B 31 8
HET MSE B 46 8
HET MSE C 1 8
HET MSE C 12 8
HET MSE C 31 8
HET MSE C 46 8
HET GOL B 181 6
HET SO4 B 171 5
HET GOL B 182 6
HET SO4 C 181 5
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 8 HOH *128(H2 O)
HELIX 1 1 SER A -2 SER A 6 1 9
HELIX 2 2 HIS A 17 MSE A 31 1 15
HELIX 3 3 ASP A 45 ALA A 48 5 4
HELIX 4 4 GLN A 49 SER A 57 1 9
HELIX 5 5 ALA A 59 ARG A 65 1 7
HELIX 6 6 THR A 71 ALA A 77 1 7
HELIX 7 7 ILE A 99 THR A 113 1 15
HELIX 8 8 THR A 130 LEU A 136 1 7
HELIX 9 9 ASN A 153 LEU A 170 1 18
HELIX 10 10 ASN B -1 ARG B 7 1 9
HELIX 11 11 HIS B 17 MSE B 31 1 15
HELIX 12 12 ASP B 45 ALA B 48 5 4
HELIX 13 13 GLN B 49 ALA B 56 1 8
HELIX 14 14 ALA B 59 ARG B 65 1 7
HELIX 15 15 THR B 71 ALA B 77 1 7
HELIX 16 16 ILE B 99 THR B 113 1 15
HELIX 17 17 THR B 130 CYS B 137 1 8
HELIX 18 18 ASN B 153 LEU B 170 1 18
HELIX 19 19 GLN C 3 SER C 6 5 4
HELIX 20 20 HIS C 17 MSE C 31 1 15
HELIX 21 21 ASP C 45 ALA C 48 5 4
HELIX 22 22 GLN C 49 LEU C 55 1 7
HELIX 23 23 ALA C 59 ALA C 66 1 8
HELIX 24 24 THR C 71 ALA C 77 1 7
HELIX 25 25 ILE C 99 THR C 113 1 15
HELIX 26 26 THR C 130 CYS C 137 1 8
HELIX 27 27 ASN C 153 LEU C 170 1 18
SHEET 1 A 7 ALA A 67 HIS A 69 0
SHEET 2 A 7 LEU A 36 VAL A 39 1 N LEU A 38 O ALA A 67
SHEET 3 A 7 VAL A 8 THR A 13 1 N PHE A 10 O VAL A 37
SHEET 4 A 7 VAL A 118 LEU A 122 1 O LEU A 122 N THR A 13
SHEET 5 A 7 LEU A 81 THR A 86 1 N PHE A 83 O ALA A 119
SHEET 6 A 7 ARG A 139 HIS A 142 1 O ARG A 139 N ALA A 84
SHEET 7 A 7 CYS A 97 ASP A 98 1 N CYS A 97 O HIS A 142
SHEET 1 B 7 ALA B 67 HIS B 69 0
SHEET 2 B 7 GLU B 35 VAL B 39 1 N LEU B 38 O ALA B 67
SHEET 3 B 7 VAL B 8 THR B 13 1 N PHE B 10 O VAL B 37
SHEET 4 B 7 VAL B 118 LEU B 122 1 O LEU B 122 N THR B 13
SHEET 5 B 7 LEU B 81 THR B 86 1 N PHE B 83 O VAL B 121
SHEET 6 B 7 ARG B 139 HIS B 142 1 O CYS B 141 N ALA B 84
SHEET 7 B 7 CYS B 97 ASP B 98 1 N CYS B 97 O HIS B 142
SHEET 1 C 7 ALA C 67 HIS C 69 0
SHEET 2 C 7 GLU C 35 VAL C 39 1 N LEU C 38 O HIS C 69
SHEET 3 C 7 VAL C 8 THR C 13 1 N MSE C 12 O VAL C 37
SHEET 4 C 7 VAL C 118 LEU C 122 1 O LEU C 122 N ILE C 11
SHEET 5 C 7 LEU C 81 THR C 86 1 N LEU C 85 O VAL C 121
SHEET 6 C 7 ARG C 139 HIS C 142 1 O CYS C 141 N THR C 86
SHEET 7 C 7 CYS C 97 ASP C 98 1 N CYS C 97 O HIS C 142
LINK C MSE A 1 N THR A 2 1555 1555 1.33
LINK C MSE A 12 N THR A 13 1555 1555 1.32
LINK C MSE A 31 N GLY A 32 1555 1555 1.32
LINK C MSE A 46 N THR A 47 1555 1555 1.33
LINK C MSE B 1 N THR B 2 1555 1555 1.33
LINK C MSE B 12 N THR B 13 1555 1555 1.33
LINK C MSE B 31 N GLY B 32 1555 1555 1.34
LINK C MSE B 46 N THR B 47 1555 1555 1.33
LINK C MSE C 1 N THR C 2 1555 1555 1.34
LINK C MSE C 12 N THR C 13 1555 1555 1.32
LINK C MSE C 31 N GLY C 32 1555 1555 1.33
LINK C MSE C 46 N THR C 47 1555 1555 1.33
CISPEP 1 GLY B 93 PRO B 94 0 -1.49
CISPEP 2 GLY C 93 PRO C 94 0 -0.73
SITE 1 AC1 6 VAL A 68 HIS A 69 GLU A 74 VAL B 68
SITE 2 AC1 6 HIS B 69 GLU B 74
SITE 1 AC2 3 PRO B 96 ARG B 139 ILE B 140
SITE 1 AC3 4 ARG B 90 LEU B 129 ILE B 134 HOH B 212
SITE 1 AC4 3 TYR B 149 ARG C 26 SER C 57
CRYST1 42.480 69.514 174.802 90.00 95.16 90.00 C 1 2 1 12
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 0.023540 0.000000 0.002124 0.00000
SCALE2 0.000000 0.014386 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
