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HEADER HYDROLASE 31-JAN-23 8G0N
TITLE FPHI, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES I, APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROPHOSPHONATE-BINDING SERINE HYDROLASE I;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL GPG FROM EXPRESSION TAG;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA300-0114;
SOURCE 3 ORGANISM_TAXID: 1385527;
SOURCE 4 STRAIN: USA300;
SOURCE 5 GENE: EST_1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: F1012
KEYWDS FPHI, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 14-FEB-24 8G0N 0
JRNL AUTH M.FELLNER
JRNL TITL FPHI, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES I, APO FORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
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) : 1.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 87099
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.132
REMARK 3 R VALUE (WORKING SET) : 0.132
REMARK 3 FREE R VALUE : 0.145
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 4304
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 47.5400 - 3.5400 0.97 2939 149 0.1512 0.1546
REMARK 3 2 3.5400 - 2.8100 1.00 2875 153 0.1366 0.1388
REMARK 3 3 2.8100 - 2.4500 1.00 2839 145 0.1380 0.1645
REMARK 3 4 2.4500 - 2.2300 1.00 2873 128 0.1238 0.1276
REMARK 3 5 2.2300 - 2.0700 1.00 2816 145 0.1179 0.1369
REMARK 3 6 2.0700 - 1.9500 1.00 2802 159 0.1178 0.1264
REMARK 3 7 1.9500 - 1.8500 1.00 2774 162 0.1180 0.1351
REMARK 3 8 1.8500 - 1.7700 1.00 2807 140 0.1161 0.1319
REMARK 3 9 1.7700 - 1.7000 1.00 2817 133 0.1165 0.1515
REMARK 3 10 1.7000 - 1.6400 1.00 2780 160 0.1107 0.1285
REMARK 3 11 1.6400 - 1.5900 1.00 2769 138 0.1054 0.1373
REMARK 3 12 1.5900 - 1.5500 1.00 2826 138 0.0982 0.1213
REMARK 3 13 1.5500 - 1.5000 1.00 2755 154 0.1002 0.1253
REMARK 3 14 1.5000 - 1.4700 1.00 2783 134 0.1065 0.1285
REMARK 3 15 1.4700 - 1.4300 1.00 2766 154 0.1127 0.1255
REMARK 3 16 1.4300 - 1.4000 1.00 2786 148 0.1177 0.1605
REMARK 3 17 1.4000 - 1.3800 1.00 2765 144 0.1380 0.1618
REMARK 3 18 1.3800 - 1.3500 1.00 2768 140 0.1347 0.1540
REMARK 3 19 1.3500 - 1.3300 1.00 2749 138 0.1299 0.1397
REMARK 3 20 1.3300 - 1.3000 1.00 2800 150 0.1241 0.1404
REMARK 3 21 1.3000 - 1.2800 1.00 2744 142 0.1174 0.1305
REMARK 3 22 1.2800 - 1.2600 1.00 2774 150 0.1202 0.1309
REMARK 3 23 1.2600 - 1.2400 1.00 2771 126 0.1250 0.1467
REMARK 3 24 1.2400 - 1.2300 1.00 2743 158 0.1369 0.1328
REMARK 3 25 1.2300 - 1.2100 1.00 2769 139 0.1463 0.1819
REMARK 3 26 1.2100 - 1.1900 1.00 2769 134 0.1652 0.1661
REMARK 3 27 1.1900 - 1.1800 1.00 2786 139 0.1841 0.2100
REMARK 3 28 1.1800 - 1.1700 0.99 2708 155 0.2295 0.2689
REMARK 3 29 1.1700 - 1.1500 0.90 2477 134 0.2813 0.3002
REMARK 3 30 1.1500 - 1.1400 0.79 2165 115 0.3489 0.3638
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.750
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 : 0.007 NULL
REMARK 3 ANGLE : 0.981 NULL
REMARK 3 CHIRALITY : 0.082 320
REMARK 3 PLANARITY : 0.008 406
REMARK 3 DIHEDRAL : 5.362 309
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 8G0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1000271996.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9536
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20220220
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87208
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.140
REMARK 200 RESOLUTION RANGE LOW (A) : 47.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.16
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.83700
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 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL 10.2 MG/ML FPHI (20MM TRIS PH
REMARK 280 8.0, 150MM NACL) WERE MIXED WITH 0.2 UL OF RESERVOIR SOLUTION.
REMARK 280 SITTING DROP RESERVOIR CONTAINED 200MM MAGNESIUM CHLORIDE
REMARK 280 HEXAHYDRATE, 100MM MES PH 6.0 AND 20% W/V PEG 6000. CRYSTAL
REMARK 280 APPEARED WITHIN A DAY AT 16C AND GREW UNTIL DAY 2.5. CRYSTAL WAS
REMARK 280 INCUBATED FOR ~10S IN A SOLUTION OF ~25% GLYCEROL, 75% RESERVOIR
REMARK 280 PRIOR TO FREEZING., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 25.72850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.19000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.37100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.19000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.72850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.37100
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 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 PRO A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
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 O HOH A 408 O HOH A 531 1.93
REMARK 500 O HOH A 447 O HOH A 601 2.12
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 OE2 GLU A 71 O HOH A 611 3545 1.95
REMARK 500 OE2 GLU A 74 O HOH A 405 3545 2.05
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 94 -113.61 63.20
REMARK 500 SER A 94 -110.81 52.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 38 OE1
REMARK 620 2 HOH A 405 O 95.8
REMARK 620 3 HOH A 432 O 86.8 84.5
REMARK 620 4 HOH A 479 O 84.3 176.9 92.5
REMARK 620 5 HOH A 563 O 94.1 93.8 178.1 89.2
REMARK 620 6 HOH A 611 O 170.5 92.9 90.3 86.7 89.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 68 OD1
REMARK 620 2 GLU A 196 OE2 45.4
REMARK 620 3 HOH A 417 O 44.2 2.9
REMARK 620 4 HOH A 516 O 44.4 3.6 6.1
REMARK 620 5 HOH A 549 O 41.2 4.3 4.1 4.5
REMARK 620 6 HOH A 605 O 42.7 2.8 3.7 3.1 1.7
REMARK 620 N 1 2 3 4 5
DBREF 8G0N A 1 244 UNP X5DUZ9 X5DUZ9_STAAU 1 244
SEQADV 8G0N GLY A -2 UNP X5DUZ9 EXPRESSION TAG
SEQADV 8G0N PRO A -1 UNP X5DUZ9 EXPRESSION TAG
SEQADV 8G0N GLY A 0 UNP X5DUZ9 EXPRESSION TAG
SEQRES 1 A 247 GLY PRO GLY MET ARG ILE LYS THR PRO SER PRO SER TYR
SEQRES 2 A 247 LEU LYS GLY THR ASN GLY HIS ALA ILE LEU LEU LEU HIS
SEQRES 3 A 247 SER PHE THR GLY THR ASN ARG ASP VAL LYS HIS LEU ALA
SEQRES 4 A 247 ALA GLU LEU ASN ASP GLN GLY PHE SER CYS TYR ALA PRO
SEQRES 5 A 247 ASN TYR PRO GLY HIS GLY LEU LEU LEU LYS ASP PHE MET
SEQRES 6 A 247 THR TYR ASN VAL ASP ASP TRP TRP GLU GLU VAL GLU LYS
SEQRES 7 A 247 ALA TYR GLN PHE LEU VAL ASN GLU GLY TYR GLU SER ILE
SEQRES 8 A 247 SER ALA THR GLY VAL SER LEU GLY GLY LEU MET THR LEU
SEQRES 9 A 247 LYS LEU ALA GLN HIS TYR PRO LEU LYS ARG ILE ALA VAL
SEQRES 10 A 247 MET SER ALA PRO LYS GLU LYS SER ASP ASP GLY LEU ILE
SEQRES 11 A 247 GLU HIS LEU VAL TYR TYR SER GLN ARG MET SER ASN ILE
SEQRES 12 A 247 LEU ASN LEU ASP GLN GLN ALA SER SER ALA GLN LEU ALA
SEQRES 13 A 247 ALA ILE ASP ASP TYR GLU GLY GLU ILE THR LYS PHE GLN
SEQRES 14 A 247 HIS PHE ILE ASP ASP ILE MET THR ASN LEU ASN VAL ILE
SEQRES 15 A 247 LYS MET PRO ALA ASN ILE LEU PHE GLY GLY LYS ASP ALA
SEQRES 16 A 247 PRO SER TYR GLU THR SER ALA HIS PHE ILE TYR GLU HIS
SEQRES 17 A 247 LEU GLY SER VAL ASP LYS GLU LEU ASN GLY LEU LYS ASP
SEQRES 18 A 247 SER HIS HIS LEU MET THR HIS GLY GLU GLY ARG ASP ILE
SEQRES 19 A 247 LEU GLU GLU ASN VAL ILE ARG PHE PHE ASN ALA LEU THR
HET MG A 301 1
HET MG A 302 1
HET CL A 303 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 MG 2(MG 2+)
FORMUL 4 CL CL 1-
FORMUL 5 HOH *228(H2 O)
HELIX 1 AA1 THR A 28 ASP A 31 5 4
HELIX 2 AA2 VAL A 32 GLN A 42 1 11
HELIX 3 AA3 LEU A 57 MET A 62 1 6
HELIX 4 AA4 ASN A 65 GLU A 83 1 19
HELIX 5 AA5 SER A 94 TYR A 107 1 14
HELIX 6 AA6 SER A 122 ASN A 142 1 21
HELIX 7 AA7 ASP A 144 ALA A 154 1 11
HELIX 8 AA8 ILE A 155 ASP A 157 5 3
HELIX 9 AA9 TYR A 158 ASN A 175 1 18
HELIX 10 AB1 LEU A 176 ILE A 179 5 4
HELIX 11 AB2 ALA A 192 LEU A 206 1 15
HELIX 12 AB3 GLY A 228 ALA A 242 1 15
SHEET 1 AA1 7 SER A 9 LEU A 11 0
SHEET 2 AA1 7 SER A 45 ALA A 48 -1 O CYS A 46 N LEU A 11
SHEET 3 AA1 7 HIS A 17 LEU A 22 1 N HIS A 17 O SER A 45
SHEET 4 AA1 7 SER A 87 VAL A 93 1 O THR A 91 N LEU A 20
SHEET 5 AA1 7 ILE A 112 MET A 115 1 O MET A 115 N GLY A 92
SHEET 6 AA1 7 ALA A 183 GLY A 188 1 O LEU A 186 N VAL A 114
SHEET 7 AA1 7 LYS A 211 LEU A 216 1 O ASN A 214 N ILE A 185
LINK OE1 GLU A 38 MG MG A 302 1555 1555 2.16
LINK OD1 ASP A 68 MG MG A 301 1555 2555 2.07
LINK OE2 GLU A 196 MG MG A 301 1555 1555 2.07
LINK MG MG A 301 O HOH A 417 1555 1555 2.06
LINK MG MG A 301 O HOH A 516 1555 1555 2.10
LINK MG MG A 301 O HOH A 549 1555 1555 2.09
LINK MG MG A 301 O HOH A 605 1555 1555 2.07
LINK MG MG A 302 O HOH A 405 1555 1555 2.02
LINK MG MG A 302 O HOH A 432 1555 1555 2.10
LINK MG MG A 302 O HOH A 479 1555 1555 1.99
LINK MG MG A 302 O HOH A 563 1555 1555 2.01
LINK MG MG A 302 O HOH A 611 1555 1555 2.11
CRYST1 51.457 60.742 76.380 90.00 90.00 90.00 P 21 21 21 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 0.019434 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013092 0.00000
TER 4192 THR A 244
MASTER 312 0 3 12 7 0 0 6 2146 1 15 19
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