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HEADER HYDROLASE 11-DEC-20 7L0A
TITLE CRYSTAL STRUCTURE OF S-FORMYLGLUTATHIONE HYDROLASE (FRMB) FROM
TITLE 2 STAPHYLOCOCCUS AUREUS, APOENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROLYL OLIGOPEPTIDASE FAMILY SERINE PEPTIDASE,PUTATIVE
COMPND 5 ESTERASE,S-FORMYLGLUTATHIONE HYDROLASE,TRIBUTYRIN ESTERASE;
COMPND 6 EC: 3.1.2.12;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: DD547_02660, DQV53_15175, EP54_00010, EQ90_02595, G0V24_06825,
SOURCE 5 G0Z18_09875, G6Y10_06490, GO746_05055, GO803_04470, GO805_09630,
SOURCE 6 GO821_02780, GO894_07900, GO942_11740, HMPREF2819_04260,
SOURCE 7 HMPREF3211_01237, NCTC10654_02801, NCTC10702_04070, NCTC10988_03042,
SOURCE 8 RK64_00235;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS FRMB, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.MILLER,J.M.JEZ,A.R.ODOM JOHN
REVDAT 3 25-AUG-21 7L0A 1 JRNL
REVDAT 2 07-JUL-21 7L0A 1 JRNL
REVDAT 1 23-DEC-20 7L0A 0
JRNL AUTH J.J.MILLER,I.T.SHAH,J.HATTEN,Y.BAREKATAIN,E.A.MUELLER,
JRNL AUTH 2 A.M.MOUSTAFA,R.L.EDWARDS,C.S.DOWD,P.J.PLANET,F.L.MULLER,
JRNL AUTH 3 J.M.JEZ,A.R.ODOM JOHN
JRNL TITL STRUCTURE-GUIDED MICROBIAL TARGETING OF ANTISTAPHYLOCOCCAL
JRNL TITL 2 PRODRUGS.
JRNL REF ELIFE V. 10 2021
JRNL REFN ESSN 2050-084X
JRNL PMID 34279224
JRNL DOI 10.7554/ELIFE.66657
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.J.MILLER,I.T.SHAH,J.HATTEN,Y.BAREKATAIN,E.A.MUELLER,
REMARK 1 AUTH 2 A.M.MOUSTAFA,R.L.EDWARDS,C.S.DOWD,P.J.PLANET,F.L.MULLER,
REMARK 1 AUTH 3 J.M.JEZ
REMARK 1 TITL STRUCTURE-GUIDED MICROBIAL TARGETING OF ANTISTAPHYLOCOCCAL
REMARK 1 TITL 2 PRODRUGS
REMARK 1 REF BIORXIV 2020
REMARK 1 REFN
REMARK 1 DOI 10.1101/2020.12.15.408237
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 78137
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.560
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 36.8100 - 3.8500 0.96 5570 146 0.1509 0.1613
REMARK 3 2 3.8500 - 3.0600 0.94 5363 141 0.1402 0.1556
REMARK 3 3 3.0600 - 2.6700 0.97 5539 145 0.1490 0.1555
REMARK 3 4 2.6700 - 2.4300 0.97 5532 146 0.1528 0.1716
REMARK 3 5 2.4300 - 2.2500 0.92 5296 139 0.1602 0.1707
REMARK 3 6 2.2500 - 2.1200 0.95 5353 141 0.1673 0.1909
REMARK 3 7 2.1200 - 2.0100 0.97 5519 144 0.1683 0.1998
REMARK 3 8 2.0100 - 1.9300 0.98 5622 148 0.1639 0.2032
REMARK 3 9 1.9300 - 1.8500 0.94 5320 139 0.2055 0.2688
REMARK 3 10 1.8500 - 1.7900 0.95 5435 143 0.1656 0.1832
REMARK 3 11 1.7900 - 1.7300 0.98 5552 146 0.1692 0.2048
REMARK 3 12 1.7300 - 1.6800 0.99 5574 146 0.1760 0.2434
REMARK 3 13 1.6800 - 1.6400 0.99 5610 148 0.1808 0.1959
REMARK 3 14 1.6400 - 1.6000 0.85 4854 126 0.1901 0.2297
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) : 19.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.79
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7L0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1000253474.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.7
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) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78193
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.41500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: 4RGY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 UL HANGING DROPS CONTAINING A 1:1
REMARK 280 MIXTURE OF PROTEIN (6 MG/ML) AND CRYSTALLIZATION BUFFER (0.1 M
REMARK 280 TRICINE PH 7.7, 15% PEG6K, 2.5 M NACL, 0.125% N-DODECYL-B-D-
REMARK 280 GLUCOSIDE), VAPOR DIFFUSION, HANGING DROP, 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 64.15150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.15150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.25000
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: 2790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 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 401 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 461 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 591 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 598 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 401 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 488 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 604 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 ILE A 165
REMARK 465 ILE A 166
REMARK 465 GLY A 167
REMARK 465 ASN A 168
REMARK 465 LEU A 169
REMARK 465 SER A 170
REMARK 465 SER A 171
REMARK 465 VAL A 172
REMARK 465 LYS A 173
REMARK 465 GLY A 174
REMARK 465 THR A 175
REMARK 465 ASP A 252
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 ASP B 252
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 120 -122.43 59.09
REMARK 500 ASN A 221 37.04 72.10
REMARK 500 ASP A 232 -167.94 -119.15
REMARK 500 SER B 120 -118.22 59.29
REMARK 500 GLU B 156 43.11 -89.45
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7L0A A 0 252 UNP A0A0D6GS23_STAAU
DBREF2 7L0A A A0A0D6GS23 1 253
DBREF1 7L0A B 0 252 UNP A0A0D6GS23_STAAU
DBREF2 7L0A B A0A0D6GS23 1 253
SEQADV 7L0A GLY A -8 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A LEU A -7 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A VAL A -6 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A PRO A -5 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A ARG A -4 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A GLY A -3 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A SER A -2 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A HIS A -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A GLY B -8 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A LEU B -7 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A VAL B -6 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A PRO B -5 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A ARG B -4 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A GLY B -3 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A SER B -2 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 7L0A HIS B -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQRES 1 A 261 GLY LEU VAL PRO ARG GLY SER HIS MET ALA TYR ILE SER
SEQRES 2 A 261 LEU ASN TYR HIS SER PRO THR ILE GLY MET HIS GLN ASN
SEQRES 3 A 261 LEU THR VAL ILE LEU PRO GLU ASP GLN SER PHE PHE ASN
SEQRES 4 A 261 SER ASP THR THR VAL LYS PRO LEU LYS THR LEU MET LEU
SEQRES 5 A 261 LEU HIS GLY LEU SER SER ASP GLU THR THR TYR MET ARG
SEQRES 6 A 261 TYR THR SER ILE GLU ARG TYR ALA ASN GLU HIS LYS LEU
SEQRES 7 A 261 ALA VAL ILE MET PRO ASN VAL ASP HIS SER ALA TYR ALA
SEQRES 8 A 261 ASN MET ALA TYR GLY HIS SER TYR TYR ASP TYR ILE LEU
SEQRES 9 A 261 GLU VAL TYR ASP TYR VAL HIS GLN ILE PHE PRO LEU SER
SEQRES 10 A 261 LYS LYS ARG ASP ASP ASN PHE ILE ALA GLY HIS SER MET
SEQRES 11 A 261 GLY GLY TYR GLY THR ILE LYS PHE ALA LEU THR GLN GLY
SEQRES 12 A 261 ASP LYS PHE ALA LYS ALA VAL PRO LEU SER ALA VAL PHE
SEQRES 13 A 261 GLU ALA GLN ASN LEU MET ASP LEU GLU TRP ASN ASP PHE
SEQRES 14 A 261 SER LYS GLU ALA ILE ILE GLY ASN LEU SER SER VAL LYS
SEQRES 15 A 261 GLY THR GLU HIS ASP PRO TYR TYR LEU LEU ASP LYS ALA
SEQRES 16 A 261 VAL ALA GLU ASP LYS GLN ILE PRO LYS LEU LEU ILE MET
SEQRES 17 A 261 CYS GLY LYS GLN ASP PHE LEU TYR GLN ASP ASN LEU ASP
SEQRES 18 A 261 PHE ILE ASP TYR LEU SER ARG ILE ASN VAL PRO TYR GLN
SEQRES 19 A 261 PHE GLU ASP GLY PRO GLY ASP HIS ASP TYR ALA TYR TRP
SEQRES 20 A 261 ASP GLN ALA ILE LYS ARG ALA ILE THR TRP MET VAL ASN
SEQRES 21 A 261 ASP
SEQRES 1 B 261 GLY LEU VAL PRO ARG GLY SER HIS MET ALA TYR ILE SER
SEQRES 2 B 261 LEU ASN TYR HIS SER PRO THR ILE GLY MET HIS GLN ASN
SEQRES 3 B 261 LEU THR VAL ILE LEU PRO GLU ASP GLN SER PHE PHE ASN
SEQRES 4 B 261 SER ASP THR THR VAL LYS PRO LEU LYS THR LEU MET LEU
SEQRES 5 B 261 LEU HIS GLY LEU SER SER ASP GLU THR THR TYR MET ARG
SEQRES 6 B 261 TYR THR SER ILE GLU ARG TYR ALA ASN GLU HIS LYS LEU
SEQRES 7 B 261 ALA VAL ILE MET PRO ASN VAL ASP HIS SER ALA TYR ALA
SEQRES 8 B 261 ASN MET ALA TYR GLY HIS SER TYR TYR ASP TYR ILE LEU
SEQRES 9 B 261 GLU VAL TYR ASP TYR VAL HIS GLN ILE PHE PRO LEU SER
SEQRES 10 B 261 LYS LYS ARG ASP ASP ASN PHE ILE ALA GLY HIS SER MET
SEQRES 11 B 261 GLY GLY TYR GLY THR ILE LYS PHE ALA LEU THR GLN GLY
SEQRES 12 B 261 ASP LYS PHE ALA LYS ALA VAL PRO LEU SER ALA VAL PHE
SEQRES 13 B 261 GLU ALA GLN ASN LEU MET ASP LEU GLU TRP ASN ASP PHE
SEQRES 14 B 261 SER LYS GLU ALA ILE ILE GLY ASN LEU SER SER VAL LYS
SEQRES 15 B 261 GLY THR GLU HIS ASP PRO TYR TYR LEU LEU ASP LYS ALA
SEQRES 16 B 261 VAL ALA GLU ASP LYS GLN ILE PRO LYS LEU LEU ILE MET
SEQRES 17 B 261 CYS GLY LYS GLN ASP PHE LEU TYR GLN ASP ASN LEU ASP
SEQRES 18 B 261 PHE ILE ASP TYR LEU SER ARG ILE ASN VAL PRO TYR GLN
SEQRES 19 B 261 PHE GLU ASP GLY PRO GLY ASP HIS ASP TYR ALA TYR TRP
SEQRES 20 B 261 ASP GLN ALA ILE LYS ARG ALA ILE THR TRP MET VAL ASN
SEQRES 21 B 261 ASP
HET MG A 301 1
HET MG B 301 1
HET MG B 302 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 3(MG 2+)
FORMUL 6 HOH *476(H2 O)
HELIX 1 AA1 ASP A 25 PHE A 29 5 5
HELIX 2 AA2 THR A 52 THR A 58 1 7
HELIX 3 AA3 SER A 59 LYS A 68 1 10
HELIX 4 AA4 ASP A 77 GLY A 87 1 11
HELIX 5 AA5 SER A 89 PHE A 105 1 17
HELIX 6 AA6 LYS A 110 ASP A 112 5 3
HELIX 7 AA7 SER A 120 GLN A 133 1 14
HELIX 8 AA8 ALA A 149 ASP A 154 5 6
HELIX 9 AA9 ASN A 158 ALA A 164 1 7
HELIX 10 AB1 ASP A 178 GLU A 189 1 12
HELIX 11 AB2 LEU A 206 ASN A 221 1 16
HELIX 12 AB3 ASP A 234 ASN A 251 1 18
HELIX 13 AB4 ASP B 25 ASN B 30 5 6
HELIX 14 AB5 THR B 52 THR B 58 1 7
HELIX 15 AB6 SER B 59 HIS B 67 1 9
HELIX 16 AB7 HIS B 78 ASN B 83 1 6
HELIX 17 AB8 SER B 89 PHE B 105 1 17
HELIX 18 AB9 LYS B 110 ASP B 112 5 3
HELIX 19 AC1 SER B 120 GLN B 133 1 14
HELIX 20 AC2 GLU B 148 LEU B 155 5 8
HELIX 21 AC3 ASN B 158 LEU B 169 1 12
HELIX 22 AC4 SER B 170 VAL B 172 5 3
HELIX 23 AC5 ASP B 178 GLU B 189 1 12
HELIX 24 AC6 LEU B 206 ILE B 220 1 15
HELIX 25 AC7 ASP B 234 ASN B 251 1 18
SHEET 1 AA116 GLN A 225 GLY A 229 0
SHEET 2 AA116 LYS A 195 GLY A 201 1 N ILE A 198 O GLN A 225
SHEET 3 AA116 LYS A 139 LEU A 143 1 N ALA A 140 O LYS A 195
SHEET 4 AA116 ASN A 114 HIS A 119 1 N GLY A 118 O LEU A 143
SHEET 5 AA116 THR A 40 LEU A 44 1 N MET A 42 O PHE A 115
SHEET 6 AA116 ALA A 70 PRO A 74 1 O ILE A 72 N LEU A 41
SHEET 7 AA116 MET A 14 PRO A 23 -1 N THR A 19 O MET A 73
SHEET 8 AA116 MET A 0 SER A 9 -1 N LEU A 5 O LEU A 18
SHEET 9 AA116 MET B 0 HIS B 8 -1 O ASN B 6 N TYR A 2
SHEET 10 AA116 HIS B 15 PRO B 23 -1 O LEU B 18 N LEU B 5
SHEET 11 AA116 ALA B 70 PRO B 74 -1 O MET B 73 N THR B 19
SHEET 12 AA116 THR B 40 LEU B 44 1 N LEU B 41 O ILE B 72
SHEET 13 AA116 ASN B 114 HIS B 119 1 O PHE B 115 N THR B 40
SHEET 14 AA116 LYS B 139 LEU B 143 1 O LEU B 143 N GLY B 118
SHEET 15 AA116 LYS B 195 GLY B 201 1 O LYS B 195 N ALA B 140
SHEET 16 AA116 GLN B 225 GLY B 229 1 O GLN B 225 N ILE B 198
LINK OG SER A 120 MG MG A 301 1555 1555 2.97
CRYST1 128.303 80.500 66.651 90.00 113.84 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 0.007794 0.000000 0.003444 0.00000
SCALE2 0.000000 0.012422 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016403 0.00000
TER 3824 ASN A 251
TER 7795 ASN B 251
MASTER 279 0 3 25 16 0 0 6 4565 2 2 42
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