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HEADER HYDROLASE 15-NOV-13 4NMW
TITLE CRYSTAL STRUCTURE OF CARBOXYLESTERASE BIOH FROM SALMONELLA ENTERICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PIMELYL-[ACYL-CARRIER PROTEIN] METHYL ESTER ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BIOTIN SYNTHESIS PROTEIN BIOH, CARBOXYLESTERASE BIOH;
COMPND 5 EC: 3.1.1.85;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 3 TYPHIMURIUM;
SOURCE 4 ORGANISM_TAXID: 99287;
SOURCE 5 STRAIN: LT2;
SOURCE 6 GENE: BIOH, STM3509;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) BOLD;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG53
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 3 DISEASES, CSGID, ALPHA-BETA STRUCTURE, ALPHA-BETA-ALPHA SANDWICH,
KEYWDS 4 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,M.ZHOU,S.GRIMSHAW,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 1 04-DEC-13 4NMW 0
JRNL AUTH Y.KIM,M.ZHOU,S.GRIMSHAW,W.F.ANDERSON,A.JOACHIMIAK,
JRNL AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 3 (CSGID)
JRNL TITL CRYSTAL STRUCTURE OF CARBOXYLESTERASE BIOH FROM SALMONELLA
JRNL TITL 2 ENTERICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 42118
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.143
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2144
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 26.9677 - 3.6874 0.97 2918 167 0.1476 0.1692
REMARK 3 2 3.6874 - 2.9279 1.00 2929 155 0.1475 0.1655
REMARK 3 3 2.9279 - 2.5581 1.00 2916 167 0.1557 0.2057
REMARK 3 4 2.5581 - 2.3244 1.00 2942 153 0.1430 0.1726
REMARK 3 5 2.3244 - 2.1578 1.00 2894 175 0.1350 0.1584
REMARK 3 6 2.1578 - 2.0307 1.00 2929 151 0.1326 0.1980
REMARK 3 7 2.0307 - 1.9290 1.00 2902 170 0.1308 0.1991
REMARK 3 8 1.9290 - 1.8451 1.00 2952 125 0.1315 0.1957
REMARK 3 9 1.8451 - 1.7740 1.00 2922 148 0.1329 0.1969
REMARK 3 10 1.7740 - 1.7128 0.99 2844 158 0.1311 0.1594
REMARK 3 11 1.7128 - 1.6593 0.94 2733 155 0.1279 0.1721
REMARK 3 12 1.6593 - 1.6119 0.86 2486 130 0.1292 0.1510
REMARK 3 13 1.6119 - 1.5694 0.76 2217 111 0.1245 0.1942
REMARK 3 14 1.5694 - 1.5311 0.65 1909 95 0.1311 0.2038
REMARK 3 15 1.5311 - 1.4963 0.51 1481 84 0.1498 0.2118
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.55
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 : 0.009 2289
REMARK 3 ANGLE : 1.265 3150
REMARK 3 CHIRALITY : 0.082 344
REMARK 3 PLANARITY : 0.005 422
REMARK 3 DIHEDRAL : 14.584 848
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 4NMW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB083402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.97924
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 : 45820
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34500
REMARK 200 FOR SHELL : 2.540
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL3000, SHELXS,MLPHARE,DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESSIUM CHLORIDE, 0.1 M MES
REMARK 280 PH 6.5, 10 %(W/V) PEG4000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
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 49.52950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.10550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.52950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.10550
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A 504 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 ASN A 2
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 GLU A 11 13.12 -143.26
REMARK 500 LEU A 24 -157.73 -123.43
REMARK 500 SER A 82 -118.64 56.06
REMARK 500 ALA A 234 -127.78 -105.06
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 CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP01059 RELATED DB: TARGETTRACK
DBREF 4NMW A 1 256 UNP Q8ZLI9 BIOH_SALTY 1 256
SEQADV 4NMW SER A -2 UNP Q8ZLI9 EXPRESSION TAG
SEQADV 4NMW ASN A -1 UNP Q8ZLI9 EXPRESSION TAG
SEQADV 4NMW ALA A 0 UNP Q8ZLI9 EXPRESSION TAG
SEQRES 1 A 259 SER ASN ALA MSE ASN ASP ILE TRP TRP GLN THR TYR GLY
SEQRES 2 A 259 GLU GLY ASN CYS HIS LEU VAL LEU LEU HIS GLY TRP GLY
SEQRES 3 A 259 LEU ASN ALA GLU VAL TRP HIS CYS ILE ARG GLU GLU LEU
SEQRES 4 A 259 GLY SER HIS PHE THR LEU HIS LEU VAL ASP LEU PRO GLY
SEQRES 5 A 259 TYR GLY ARG SER SER GLY PHE GLY ALA MSE THR LEU GLU
SEQRES 6 A 259 GLU MSE THR ALA GLN VAL ALA LYS ASN ALA PRO ASP GLN
SEQRES 7 A 259 ALA ILE TRP LEU GLY TRP SER LEU GLY GLY LEU VAL ALA
SEQRES 8 A 259 SER GLN MSE ALA LEU THR HIS PRO GLU ARG VAL GLN ALA
SEQRES 9 A 259 LEU VAL THR VAL ALA SER SER PRO CYS PHE SER ALA ARG
SEQRES 10 A 259 GLU GLY TRP PRO GLY ILE LYS PRO GLU ILE LEU GLY GLY
SEQRES 11 A 259 PHE GLN GLN GLN LEU SER ASP ASP PHE GLN ARG THR VAL
SEQRES 12 A 259 GLU ARG PHE LEU ALA LEU GLN THR LEU GLY THR GLU THR
SEQRES 13 A 259 ALA ARG GLN ASP ALA ARG THR LEU LYS SER VAL VAL LEU
SEQRES 14 A 259 ALA GLN PRO MSE PRO ASP VAL GLU VAL LEU ASN GLY GLY
SEQRES 15 A 259 LEU GLU ILE LEU LYS THR VAL ASP LEU ARG GLU ALA LEU
SEQRES 16 A 259 LYS ASN VAL ASN MSE PRO PHE LEU ARG LEU TYR GLY TYR
SEQRES 17 A 259 LEU ASP GLY LEU VAL PRO ARG LYS ILE VAL PRO LEU LEU
SEQRES 18 A 259 ASP THR LEU TRP PRO HIS SER THR SER GLN ILE MSE ALA
SEQRES 19 A 259 LYS ALA ALA HIS ALA PRO PHE ILE SER HIS PRO ALA ALA
SEQRES 20 A 259 PHE CYS GLN ALA LEU MSE THR LEU LYS SER SER LEU
MODRES 4NMW MSE A 59 MET SELENOMETHIONINE
MODRES 4NMW MSE A 64 MET SELENOMETHIONINE
MODRES 4NMW MSE A 91 MET SELENOMETHIONINE
MODRES 4NMW MSE A 170 MET SELENOMETHIONINE
MODRES 4NMW MSE A 197 MET SELENOMETHIONINE
MODRES 4NMW MSE A 230 MET SELENOMETHIONINE
MODRES 4NMW MSE A 250 MET SELENOMETHIONINE
HET MSE A 59 8
HET MSE A 64 8
HET MSE A 91 8
HET MSE A 170 8
HET MSE A 197 16
HET MSE A 230 16
HET MSE A 250 16
HET CL A 301 1
HET PEG A 302 7
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 CL CL 1-
FORMUL 3 PEG C4 H10 O3
FORMUL 4 HOH *299(H2 O)
HELIX 1 1 ASN A 25 CYS A 31 5 7
HELIX 2 2 ILE A 32 SER A 38 1 7
HELIX 3 3 THR A 60 LYS A 70 1 11
HELIX 4 4 SER A 82 HIS A 95 1 14
HELIX 5 5 LYS A 121 SER A 133 1 13
HELIX 6 6 ASP A 135 LEU A 146 1 12
HELIX 7 7 THR A 153 ALA A 167 1 15
HELIX 8 8 ASP A 172 VAL A 186 1 15
HELIX 9 9 GLU A 190 VAL A 195 5 6
HELIX 10 10 LYS A 213 TRP A 222 1 10
HELIX 11 11 ALA A 236 HIS A 241 1 6
HELIX 12 12 HIS A 241 SER A 255 1 15
SHEET 1 A 7 TRP A 6 TYR A 9 0
SHEET 2 A 7 THR A 41 VAL A 45 -1 O LEU A 42 N TYR A 9
SHEET 3 A 7 HIS A 15 LEU A 19 1 N LEU A 16 O HIS A 43
SHEET 4 A 7 ALA A 76 TRP A 81 1 O ILE A 77 N VAL A 17
SHEET 5 A 7 VAL A 99 VAL A 105 1 O VAL A 103 N TRP A 78
SHEET 6 A 7 PHE A 199 GLY A 204 1 O LEU A 202 N THR A 104
SHEET 7 A 7 THR A 226 MSE A 230 1 O MSE A 230 N TYR A 203
LINK C ALA A 58 N MSE A 59 1555 1555 1.33
LINK C MSE A 59 N THR A 60 1555 1555 1.32
LINK C AGLU A 63 N MSE A 64 1555 1555 1.32
LINK C BGLU A 63 N MSE A 64 1555 1555 1.33
LINK C MSE A 64 N THR A 65 1555 1555 1.32
LINK C GLN A 90 N MSE A 91 1555 1555 1.32
LINK C MSE A 91 N ALA A 92 1555 1555 1.33
LINK C PRO A 169 N MSE A 170 1555 1555 1.32
LINK C MSE A 170 N PRO A 171 1555 1555 1.33
LINK C AASN A 196 N AMSE A 197 1555 1555 1.33
LINK C BASN A 196 N BMSE A 197 1555 1555 1.33
LINK C AMSE A 197 N PRO A 198 1555 1555 1.34
LINK C BMSE A 197 N PRO A 198 1555 1555 1.35
LINK C ILE A 229 N AMSE A 230 1555 1555 1.33
LINK C ILE A 229 N BMSE A 230 1555 1555 1.32
LINK C AMSE A 230 N ALA A 231 1555 1555 1.33
LINK C BMSE A 230 N ALA A 231 1555 1555 1.33
LINK C LEU A 249 N AMSE A 250 1555 1555 1.34
LINK C LEU A 249 N BMSE A 250 1555 1555 1.33
LINK C AMSE A 250 N THR A 251 1555 1555 1.33
LINK C BMSE A 250 N THR A 251 1555 1555 1.33
SITE 1 AC1 3 TRP A 22 SER A 82 LEU A 83
SITE 1 AC2 8 GLU A 63 GLN A 67 LYS A 70 HIS A 95
SITE 2 AC2 8 PRO A 96 GLU A 97 ARG A 98 HOH A 458
CRYST1 99.059 54.211 66.769 90.00 126.13 90.00 C 1 2 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 0.010095 0.000000 0.007370 0.00000
SCALE2 0.000000 0.018446 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018544 0.00000
TER 2208 LEU A 256
MASTER 258 0 9 12 7 0 3 6 2281 1 103 20
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