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HEADER HYDROLASE 04-APR-23 8SBQ
TITLE FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES E, FLUOROPHOSPHONATE JB101 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROPHOSPHONATE-BINDING SERINE HYDROLASES E;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL GPG FROM EXPRESSION TAG;
COMPND 5 EC: 3.-.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA100-CA-126;
SOURCE 3 ORGANISM_TAXID: 1385546;
SOURCE 4 GENE: SAUSA300_2518;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: F1010
KEYWDS FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
KEYWDS 2 HYDROLASES E, FLUOROPHOSPHONATE JB101 BOUND, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 17-APR-24 8SBQ 0
JRNL AUTH M.FELLNER
JRNL TITL FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES E, FLUOROPHOSPHONATE JB101 BOUND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 81176
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 4130
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 40.0900 - 4.6000 1.00 2745 143 0.1476 0.1594
REMARK 3 2 4.6000 - 3.6600 1.00 2701 145 0.1285 0.1367
REMARK 3 3 3.6600 - 3.1900 1.00 2670 166 0.1508 0.1805
REMARK 3 4 3.1900 - 2.9000 1.00 2689 127 0.1704 0.1811
REMARK 3 5 2.9000 - 2.6900 1.00 2652 170 0.1756 0.2234
REMARK 3 6 2.6900 - 2.5300 1.00 2676 149 0.1787 0.1904
REMARK 3 7 2.5300 - 2.4100 1.00 2661 132 0.1791 0.2135
REMARK 3 8 2.4100 - 2.3000 1.00 2706 133 0.1731 0.2001
REMARK 3 9 2.3000 - 2.2100 1.00 2655 128 0.1738 0.2050
REMARK 3 10 2.2100 - 2.1400 1.00 2657 152 0.1686 0.2051
REMARK 3 11 2.1400 - 2.0700 1.00 2678 146 0.1660 0.1979
REMARK 3 12 2.0700 - 2.0100 1.00 2707 107 0.1698 0.1765
REMARK 3 13 2.0100 - 1.9600 1.00 2617 137 0.1692 0.2075
REMARK 3 14 1.9600 - 1.9100 1.00 2715 141 0.1764 0.1898
REMARK 3 15 1.9100 - 1.8700 1.00 2635 151 0.1807 0.2299
REMARK 3 16 1.8700 - 1.8300 1.00 2678 152 0.1770 0.2272
REMARK 3 17 1.8300 - 1.7900 1.00 2673 130 0.1836 0.2125
REMARK 3 18 1.7900 - 1.7600 1.00 2628 132 0.1799 0.2105
REMARK 3 19 1.7600 - 1.7300 1.00 2663 145 0.1823 0.2158
REMARK 3 20 1.7300 - 1.7000 1.00 2678 128 0.1851 0.2172
REMARK 3 21 1.7000 - 1.6700 1.00 2689 109 0.1886 0.1938
REMARK 3 22 1.6700 - 1.6400 1.00 2658 148 0.1961 0.2352
REMARK 3 23 1.6400 - 1.6200 1.00 2616 180 0.1956 0.2225
REMARK 3 24 1.6200 - 1.6000 1.00 2644 156 0.2143 0.2127
REMARK 3 25 1.6000 - 1.5800 1.00 2631 137 0.2109 0.2623
REMARK 3 26 1.5800 - 1.5500 1.00 2675 150 0.2236 0.2267
REMARK 3 27 1.5500 - 1.5400 1.00 2656 157 0.2469 0.2612
REMARK 3 28 1.5400 - 1.5200 1.00 2570 160 0.2643 0.2718
REMARK 3 29 1.5200 - 1.5000 0.90 2423 119 0.3109 0.3294
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.960
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 : 0.006 4656
REMARK 3 ANGLE : 0.914 6330
REMARK 3 CHIRALITY : 0.077 682
REMARK 3 PLANARITY : 0.008 840
REMARK 3 DIHEDRAL : 10.454 653
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9745 -11.0148 7.5107
REMARK 3 T TENSOR
REMARK 3 T11: 0.1105 T22: 0.1034
REMARK 3 T33: 0.1302 T12: 0.0063
REMARK 3 T13: 0.0150 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 1.1121 L22: 0.8357
REMARK 3 L33: 1.1953 L12: 0.2158
REMARK 3 L13: 0.2062 L23: -0.0102
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: -0.0258 S13: 0.1135
REMARK 3 S21: -0.0099 S22: -0.0107 S23: 0.0295
REMARK 3 S31: -0.0595 S32: 0.0249 S33: 0.0072
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 167 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.0751 -15.1118 -24.1972
REMARK 3 T TENSOR
REMARK 3 T11: 0.1617 T22: 0.1652
REMARK 3 T33: 0.2025 T12: 0.0207
REMARK 3 T13: 0.0066 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.0172 L22: 1.4770
REMARK 3 L33: 2.5837 L12: 0.5315
REMARK 3 L13: 0.4113 L23: 0.6165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0408 S12: 0.0399 S13: -0.1402
REMARK 3 S21: -0.0180 S22: -0.0641 S23: 0.0070
REMARK 3 S31: 0.2091 S32: 0.0826 S33: 0.0347
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7185 -6.9105 -24.6075
REMARK 3 T TENSOR
REMARK 3 T11: 0.1695 T22: 0.1650
REMARK 3 T33: 0.1654 T12: 0.0053
REMARK 3 T13: -0.0081 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.3835 L22: 1.1622
REMARK 3 L33: 2.2910 L12: -0.1065
REMARK 3 L13: -0.2950 L23: 0.5023
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: 0.0542 S13: 0.0521
REMARK 3 S21: -0.0606 S22: 0.0163 S23: -0.0903
REMARK 3 S31: -0.0680 S32: 0.2111 S33: -0.0161
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 153 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1478 -15.9164 16.1935
REMARK 3 T TENSOR
REMARK 3 T11: 0.1525 T22: 0.1536
REMARK 3 T33: 0.1522 T12: -0.0111
REMARK 3 T13: 0.0196 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.9580 L22: 1.3350
REMARK 3 L33: 2.5851 L12: 0.2330
REMARK 3 L13: 0.2987 L23: 0.4351
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: -0.1887 S13: 0.1001
REMARK 3 S21: 0.1304 S22: -0.0523 S23: 0.1098
REMARK 3 S31: -0.0456 S32: -0.2287 S33: 0.0164
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 8SBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1000273484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
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
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81242
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 46.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : 0.14400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 8.60
REMARK 200 R MERGE FOR SHELL (I) : 1.19000
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 (%): 40.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20UL 25.0 MG/ML FPHE (10MM HEPES PH
REMARK 280 7.5, 100MM NACL) WERE MIXED WITH 3UL FLUOROPHOSPHONATE MOLECULE
REMARK 280 (10MM IN DMSO) AND INCUBATED AT 4C OVERNIGHT. 0.2 UL 21.7 MG/ML
REMARK 280 FPHE-FLUOROPHOSPHONATE WERE MIXED WITH 0.2 UL OF RESERVOIR
REMARK 280 SOLUTION. SITTING DROP RESERVOIR CONTAINED 25 UL OF 180MM
REMARK 280 MAGNESIUM CHLORIDE HEXAHYDRATE, 100MM TRIS PH 8.0, 22.5% PEG
REMARK 280 2000 MME. CRYSTAL APPEARED WITHIN A DAY AT 16C AND GREW UNTIL
REMARK 280 DAY 3. IT WAS FROZEN IN A SOLUTION OF ~25% GLYCEROL, 75%
REMARK 280 RESERVOIR., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 37.28700
REMARK 290 SMTRY3 2 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: 13640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 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 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 B -2
REMARK 465 PRO B -1
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 473 O HOH A 649 2.12
REMARK 500 O HOH A 553 O HOH A 649 2.12
REMARK 500 O HOH B 555 O HOH B 647 2.18
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 103 -132.44 60.29
REMARK 500 SER A 103 -131.77 60.29
REMARK 500 GLU A 201 -51.89 -126.72
REMARK 500 SER B 103 -132.65 60.26
REMARK 500 SER B 103 -131.72 60.26
REMARK 500 GLU B 201 -51.88 -125.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 654 DISTANCE = 6.23 ANGSTROMS
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 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 136 OD2
REMARK 620 2 HOH A 410 O 92.4
REMARK 620 3 HOH A 456 O 107.4 159.4
REMARK 620 4 HOH A 470 O 103.3 80.8 88.9
REMARK 620 5 HOH A 580 O 177.1 89.9 70.2 75.3
REMARK 620 6 HOH A 620 O 100.5 79.4 101.9 149.4 81.6
REMARK 620 N 1 2 3 4 5
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 ASN A 273 OD1
REMARK 620 2 HOH A 534 O 86.5
REMARK 620 3 HOH A 600 O 99.0 100.8
REMARK 620 4 HOH B 472 O 91.0 175.2 83.7
REMARK 620 5 HOH B 521 O 178.1 94.3 79.1 88.3
REMARK 620 6 HOH B 576 O 93.6 85.1 166.3 90.9 88.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 432 O
REMARK 620 2 HOH A 560 O 89.2
REMARK 620 3 HOH B 446 O 176.1 88.8
REMARK 620 4 HOH B 449 O 86.9 84.5 96.2
REMARK 620 5 HOH B 596 O 90.5 89.8 86.2 173.8
REMARK 620 N 1 2 3 4
DBREF 8SBQ A 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 8SBQ B 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
SEQADV 8SBQ GLY A -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8SBQ PRO A -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8SBQ GLY A 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8SBQ GLY B -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8SBQ PRO B -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8SBQ GLY B 0 UNP Q2FDS6 EXPRESSION TAG
SEQRES 1 A 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 A 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 A 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 A 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 A 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 A 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 A 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 A 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 A 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 A 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 A 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 A 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 A 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 A 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 A 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 A 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 A 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 A 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 A 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 A 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 A 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 A 279 LEU LEU ASN MET TRP GLY
SEQRES 1 B 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 B 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 B 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 B 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 B 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 B 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 B 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 B 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 B 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 B 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 B 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 B 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 B 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 B 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 B 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 B 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 B 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 B 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 B 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 B 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 B 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 B 279 LEU LEU ASN MET TRP GLY
HET ZUV A 301 23
HET MG A 302 1
HET MG A 303 1
HET ZUV B 301 23
HET MG B 302 1
HETNAM ZUV ETHYL (R)-(10-{[(BUT-3-YN-1-YL)CARBAMOYL]OXY}DECYL)
HETNAM 2 ZUV PHOSPHONOFLUORIDATE
HETNAM MG MAGNESIUM ION
FORMUL 3 ZUV 2(C17 H31 F N O4 P)
FORMUL 4 MG 3(MG 2+)
FORMUL 8 HOH *534(H2 O)
HELIX 1 AA1 THR A 31 ILE A 34 5 4
HELIX 2 AA2 PHE A 35 LYS A 43 1 9
HELIX 3 AA3 PRO A 66 ASN A 71 5 6
HELIX 4 AA4 ASP A 75 SER A 93 1 19
HELIX 5 AA5 SER A 103 TYR A 116 1 14
HELIX 6 AA6 ASP A 136 LEU A 167 1 32
HELIX 7 AA7 ALA A 170 GLN A 179 1 10
HELIX 8 AA8 THR A 183 GLU A 201 1 19
HELIX 9 AA9 GLU A 201 HIS A 207 1 7
HELIX 10 AB1 THR A 211 LYS A 217 1 7
HELIX 11 AB2 TYR A 218 ASP A 220 5 3
HELIX 12 AB3 SER A 233 GLY A 247 1 15
HELIX 13 AB4 LEU A 258 LYS A 263 1 6
HELIX 14 AB5 LYS A 263 GLY A 276 1 14
HELIX 15 AB6 THR B 31 ILE B 34 5 4
HELIX 16 AB7 PHE B 35 LYS B 43 1 9
HELIX 17 AB8 PRO B 66 ASN B 71 5 6
HELIX 18 AB9 ASP B 75 SER B 93 1 19
HELIX 19 AC1 SER B 103 TYR B 116 1 14
HELIX 20 AC2 ASP B 136 THR B 153 1 18
HELIX 21 AC3 THR B 153 LEU B 167 1 15
HELIX 22 AC4 ALA B 170 GLN B 179 1 10
HELIX 23 AC5 THR B 183 GLU B 201 1 19
HELIX 24 AC6 GLU B 201 HIS B 207 1 7
HELIX 25 AC7 THR B 211 LYS B 217 1 7
HELIX 26 AC8 TYR B 218 ASP B 220 5 3
HELIX 27 AC9 SER B 233 GLY B 247 1 15
HELIX 28 AD1 LEU B 258 LYS B 263 1 6
HELIX 29 AD2 LYS B 263 GLY B 276 1 14
SHEET 1 AA1 3 GLU A 2 LEU A 6 0
SHEET 2 AA1 3 ALA A 9 GLY A 17 -1 O LEU A 11 N LEU A 4
SHEET 3 AA1 3 GLU A 60 LEU A 61 -1 O GLU A 60 N LYS A 10
SHEET 1 AA2 8 GLU A 2 LEU A 6 0
SHEET 2 AA2 8 ALA A 9 GLY A 17 -1 O LEU A 11 N LEU A 4
SHEET 3 AA2 8 THR A 47 VAL A 51 -1 O VAL A 48 N VAL A 16
SHEET 4 AA2 8 VAL A 21 ILE A 25 1 N PHE A 24 O VAL A 49
SHEET 5 AA2 8 VAL A 97 SER A 102 1 O TYR A 98 N ILE A 23
SHEET 6 AA2 8 VAL A 120 HIS A 126 1 O LYS A 121 N VAL A 97
SHEET 7 AA2 8 ILE B 222 GLY B 227 1 O LEU B 225 N PHE A 125
SHEET 8 AA2 8 ILE B 250 ILE B 253 1 O VAL B 251 N LEU B 224
SHEET 1 AA3 8 ILE A 250 ILE A 253 0
SHEET 2 AA3 8 ILE A 222 GLY A 227 1 N LEU A 224 O VAL A 251
SHEET 3 AA3 8 VAL B 120 HIS B 126 1 O PHE B 125 N LEU A 225
SHEET 4 AA3 8 VAL B 97 SER B 102 1 N VAL B 97 O LYS B 121
SHEET 5 AA3 8 VAL B 21 ILE B 25 1 N ILE B 23 O TYR B 98
SHEET 6 AA3 8 THR B 47 ASP B 52 1 O VAL B 49 N PHE B 24
SHEET 7 AA3 8 ALA B 9 GLY B 17 -1 N VAL B 16 O VAL B 48
SHEET 8 AA3 8 GLU B 2 LEU B 6 -1 N GLU B 2 O TYR B 13
SHEET 1 AA4 8 ILE A 250 ILE A 253 0
SHEET 2 AA4 8 ILE A 222 GLY A 227 1 N LEU A 224 O VAL A 251
SHEET 3 AA4 8 VAL B 120 HIS B 126 1 O PHE B 125 N LEU A 225
SHEET 4 AA4 8 VAL B 97 SER B 102 1 N VAL B 97 O LYS B 121
SHEET 5 AA4 8 VAL B 21 ILE B 25 1 N ILE B 23 O TYR B 98
SHEET 6 AA4 8 THR B 47 ASP B 52 1 O VAL B 49 N PHE B 24
SHEET 7 AA4 8 ALA B 9 GLY B 17 -1 N VAL B 16 O VAL B 48
SHEET 8 AA4 8 GLU B 60 LEU B 61 -1 O GLU B 60 N LYS B 10
LINK OG SER A 103 P4 ZUV A 301 1555 1555 1.58
LINK OG SER B 103 P4 ZUV B 301 1555 1555 1.59
LINK OD2 ASP A 136 MG MG A 303 1555 1555 2.34
LINK OD1 ASN A 273 MG MG A 302 1555 1555 2.13
LINK MG MG A 302 O HOH A 534 1555 1555 2.18
LINK MG MG A 302 O HOH A 600 1555 1555 2.00
LINK MG MG A 302 O HOH B 472 1555 1454 2.24
LINK MG MG A 302 O HOH B 521 1555 1454 2.35
LINK MG MG A 302 O HOH B 576 1555 1454 2.11
LINK MG MG A 303 O HOH A 410 1555 2445 2.12
LINK MG MG A 303 O HOH A 456 1555 2445 2.17
LINK MG MG A 303 O HOH A 470 1555 2445 2.33
LINK MG MG A 303 O HOH A 580 1555 2445 2.12
LINK MG MG A 303 O HOH A 620 1555 1555 2.16
LINK O HOH A 432 MG MG B 302 1455 1555 2.22
LINK O HOH A 560 MG MG B 302 1455 1555 2.06
LINK MG MG B 302 O HOH B 446 1555 1555 2.11
LINK MG MG B 302 O HOH B 449 1555 1555 2.12
LINK MG MG B 302 O HOH B 596 1555 1555 2.04
CRYST1 46.936 74.574 73.862 90.00 91.53 90.00 P 1 21 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 0.021306 0.000000 0.000569 0.00000
SCALE2 0.000000 0.013409 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013544 0.00000
TER 2261 GLY A 276
TER 4494 GLY B 276
MASTER 374 0 5 29 27 0 0 6 4969 2 59 44
END |