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HEADER HYDROLASE 28-JUN-23 8TAV
TITLE FPHH, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES H, BORONIC ACID-BASED COMPOUND N34 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROPHOSPHONATE-BINDING SERINE HYDROLASE H;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA300-0114;
SOURCE 3 ORGANISM_TAXID: 1385527;
SOURCE 4 GENE: EST_2;
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: F1011
KEYWDS FPHH, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, BORONIC ACID, COVALENT, BORON-SERINE,
KEYWDS 3 BORON-HISTIDINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 17-JUL-24 8TAV 0
JRNL AUTH M.FELLNER
JRNL TITL FPHH, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES H, BORONIC ACID-BASED COMPOUND N34 BOUND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.39 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) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 50356
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 2494
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 47.6500 - 3.6300 1.00 2737 147 0.1577 0.1950
REMARK 3 2 3.6300 - 2.8800 1.00 2690 144 0.1555 0.1736
REMARK 3 3 2.8800 - 2.5200 1.00 2683 136 0.1614 0.1598
REMARK 3 4 2.5200 - 2.2900 1.00 2661 141 0.1469 0.1800
REMARK 3 5 2.2900 - 2.1200 1.00 2649 141 0.1373 0.1463
REMARK 3 6 2.1200 - 2.0000 1.00 2686 136 0.1459 0.1657
REMARK 3 7 2.0000 - 1.9000 1.00 2645 138 0.1420 0.1546
REMARK 3 8 1.9000 - 1.8200 1.00 2670 125 0.1462 0.1705
REMARK 3 9 1.8200 - 1.7500 1.00 2647 146 0.1490 0.1772
REMARK 3 10 1.7500 - 1.6900 1.00 2654 138 0.1670 0.2033
REMARK 3 11 1.6900 - 1.6300 1.00 2691 121 0.1572 0.1948
REMARK 3 12 1.6300 - 1.5900 1.00 2623 131 0.1721 0.1926
REMARK 3 13 1.5900 - 1.5400 1.00 2677 145 0.1802 0.1899
REMARK 3 14 1.5400 - 1.5100 1.00 2612 160 0.2084 0.2124
REMARK 3 15 1.5100 - 1.4700 1.00 2654 128 0.2113 0.2080
REMARK 3 16 1.4700 - 1.4400 1.00 2665 143 0.2363 0.2790
REMARK 3 17 1.4400 - 1.4100 1.00 2634 136 0.2512 0.2841
REMARK 3 18 1.4100 - 1.3900 0.98 2584 138 0.2946 0.3315
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.650
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 : 0.009 2084
REMARK 3 ANGLE : 1.113 2834
REMARK 3 CHIRALITY : 0.076 289
REMARK 3 PLANARITY : 0.008 372
REMARK 3 DIHEDRAL : 8.899 277
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 5:27 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.794 -2.331 6.234
REMARK 3 T TENSOR
REMARK 3 T11: 0.1549 T22: 0.1236
REMARK 3 T33: 0.1262 T12: 0.0089
REMARK 3 T13: -0.0043 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 1.5222 L22: 2.6437
REMARK 3 L33: 1.3152 L12: -0.0288
REMARK 3 L13: -0.1793 L23: -0.3313
REMARK 3 S TENSOR
REMARK 3 S11: -0.0268 S12: -0.0999 S13: 0.1041
REMARK 3 S21: 0.1545 S22: 0.0171 S23: 0.1078
REMARK 3 S31: -0.1826 S32: -0.0715 S33: 0.0121
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 28:121 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.332 -8.765 4.491
REMARK 3 T TENSOR
REMARK 3 T11: 0.1387 T22: 0.1346
REMARK 3 T33: 0.1280 T12: 0.0114
REMARK 3 T13: -0.0005 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.0097 L22: 1.2901
REMARK 3 L33: 0.9930 L12: 0.1254
REMARK 3 L13: 0.1218 L23: -0.0609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0202 S12: -0.0408 S13: 0.0477
REMARK 3 S21: 0.0697 S22: -0.0046 S23: 0.0859
REMARK 3 S31: -0.0660 S32: -0.0555 S33: 0.0212
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 122:140 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.457 -20.459 18.435
REMARK 3 T TENSOR
REMARK 3 T11: 0.2189 T22: 0.1874
REMARK 3 T33: 0.1956 T12: 0.0111
REMARK 3 T13: -0.0235 T23: 0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 2.0174 L22: 5.3722
REMARK 3 L33: 7.7926 L12: 0.5310
REMARK 3 L13: 0.8770 L23: 5.0514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: -0.0947 S13: 0.0902
REMARK 3 S21: 0.1953 S22: 0.1060 S23: -0.1427
REMARK 3 S31: -0.0336 S32: 0.2360 S33: -0.1323
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 141:158 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.610 -23.122 29.241
REMARK 3 T TENSOR
REMARK 3 T11: 0.3830 T22: 0.3413
REMARK 3 T33: 0.2736 T12: 0.0351
REMARK 3 T13: -0.0668 T23: -0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 2.2143 L22: 1.0872
REMARK 3 L33: 2.2909 L12: 0.2742
REMARK 3 L13: 1.4701 L23: 0.3727
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: -0.1562 S13: -0.1748
REMARK 3 S21: -0.2194 S22: 0.1963 S23: -0.0561
REMARK 3 S31: 0.0699 S32: -0.0636 S33: -0.1343
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 159:177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.611 -25.668 3.200
REMARK 3 T TENSOR
REMARK 3 T11: 0.2160 T22: 0.1523
REMARK 3 T33: 0.1998 T12: -0.0193
REMARK 3 T13: -0.0003 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.9582 L22: 1.3736
REMARK 3 L33: 2.0622 L12: -0.1933
REMARK 3 L13: 0.0980 L23: -0.6825
REMARK 3 S TENSOR
REMARK 3 S11: -0.0401 S12: -0.0066 S13: -0.2021
REMARK 3 S21: -0.0801 S22: 0.0409 S23: 0.0680
REMARK 3 S31: 0.7991 S32: -0.2475 S33: -0.0432
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND RESID 178:227 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.350 -15.728 -3.198
REMARK 3 T TENSOR
REMARK 3 T11: 0.1252 T22: 0.1733
REMARK 3 T33: 0.1503 T12: 0.0024
REMARK 3 T13: 0.0012 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 1.8580 L22: 1.8751
REMARK 3 L33: 1.5778 L12: 0.1935
REMARK 3 L13: -0.0137 L23: 0.3881
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.0695 S13: -0.1181
REMARK 3 S21: 0.0094 S22: 0.0487 S23: -0.1789
REMARK 3 S31: 0.0834 S32: 0.1740 S33: -0.0348
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN A AND RESID 228:245 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.218 -2.937 -5.740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1469 T22: 0.1323
REMARK 3 T33: 0.1421 T12: -0.0009
REMARK 3 T13: -0.0053 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 2.0896 L22: 3.2581
REMARK 3 L33: 3.5893 L12: -0.3231
REMARK 3 L13: 0.1506 L23: -1.5655
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: 0.2362 S13: 0.2527
REMARK 3 S21: -0.2330 S22: -0.0895 S23: -0.2030
REMARK 3 S31: -0.2122 S32: 0.1758 S33: 0.1253
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 8TAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1000275585.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-23
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
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 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20220820
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50414
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 47.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 12.90
REMARK 200 R MERGE FOR SHELL (I) : 1.80700
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 (%): 44.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13UL 10MG/ML FPHH (10MM HEPES PH 7.5,
REMARK 280 100MM NACL) WERE MIXED WITH 5UL N34 (50MM IN DMSO) AND INCUBATED
REMARK 280 AT RT FOR ~1 HOUR. 0.2UL FPHH-N34 WERE MIXED WITH 0.2UL OF
REMARK 280 RESERVOIR SOLUTION. SITTING DROP RESERVOIR CONTAINED 180MM
REMARK 280 CALCIUM ACETATE HYDRATE, 100MM TRIS PH 7.5, 9% W/V PEG 8000 AND
REMARK 280 9% W/V PEG 1000. CRYSTAL WAS FROZEN IN A SOLUTION OF ~25%
REMARK 280 ETHYLENGLYCOL, 75% RESERVOIR., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 27.73650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.60475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 13.86825
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 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 GLN A 2
REMARK 465 ILE A 3
REMARK 465 LYS A 4
REMARK 465 GLU A 246
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 HZ2 LYS A 70 O HOH A 402 1.49
REMARK 500 HZ1 LYS A 156 O HOH A 405 1.54
REMARK 500 O HOH A 443 O HOH A 562 1.98
REMARK 500 O HOH A 405 O HOH A 586 2.05
REMARK 500 O HOH A 563 O HOH A 615 2.06
REMARK 500 O HOH A 404 O HOH A 592 2.07
REMARK 500 O HOH A 402 O HOH A 404 2.11
REMARK 500 O HOH A 413 O HOH A 566 2.14
REMARK 500 O HOH A 577 O HOH A 609 2.17
REMARK 500 O HOH A 519 O HOH A 598 2.17
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 O HOH A 558 O HOH A 602 4545 2.02
REMARK 500 O HOH A 527 O HOH A 581 3454 2.14
REMARK 500 O HOH A 608 O HOH A 618 4545 2.15
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 GLU A 13 -109.42 -129.90
REMARK 500 THR A 25 -0.66 73.53
REMARK 500 SER A 63 -159.25 -106.69
REMARK 500 SER A 93 -129.39 58.47
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 CA A 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 13 OE1
REMARK 620 2 GLU A 146 OE1 29.8
REMARK 620 3 HOH A 439 O 27.3 2.5
REMARK 620 4 HOH A 464 O 25.9 4.7 2.9
REMARK 620 5 HOH A 473 O 29.8 2.5 3.5 3.9
REMARK 620 6 HOH A 512 O 27.0 2.9 0.8 2.1 3.2
REMARK 620 7 HOH A 591 O 28.3 4.4 4.1 2.7 2.3 3.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 308 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 13 OE1
REMARK 620 2 GLU A 13 OE2 54.3
REMARK 620 3 ASP A 203 OD1 37.4 22.0
REMARK 620 4 ASP A 203 OD2 40.1 19.9 2.8
REMARK 620 5 HOH A 444 O 109.3 68.6 90.4 88.5
REMARK 620 6 HOH A 474 O 123.9 83.3 90.1 87.7 81.2
REMARK 620 7 HOH A 506 O 69.8 97.6 97.9 99.6 81.5 161.0
REMARK 620 8 HOH A 577 O 77.1 84.3 68.9 69.1 136.9 62.3 136.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 306 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 82 OE1
REMARK 620 2 HOH A 406 O 92.4
REMARK 620 3 HOH A 517 O 82.5 68.5
REMARK 620 4 HOH A 525 O 90.5 76.9 144.2
REMARK 620 5 HOH A 579 O 89.6 148.1 143.2 71.3
REMARK 620 6 HOH A 590 O 88.0 144.9 76.8 138.2 66.9
REMARK 620 7 HOH A 625 O 175.1 92.3 98.1 91.7 87.0 87.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 307 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 149 OD1
REMARK 620 2 ASP A 149 OD2 51.6
REMARK 620 3 ASP A 153 OD2 100.5 83.0
REMARK 620 4 HOH A 408 O 153.5 154.5 84.9
REMARK 620 5 HOH A 476 O 69.5 120.8 103.8 83.9
REMARK 620 6 HOH A 509 O 126.1 74.6 73.0 80.3 164.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 206 O
REMARK 620 2 ASP A 206 OD1 76.9
REMARK 620 3 ASP A 208 OD1 89.1 164.9
REMARK 620 4 HOH A 491 O 70.4 90.3 79.4
REMARK 620 5 HOH A 554 O 79.5 89.6 93.5 149.0
REMARK 620 6 HOH A 594 O 130.6 88.7 96.3 62.6 148.3
REMARK 620 7 HOH A 599 O 151.4 93.2 101.9 137.3 73.6 74.9
REMARK 620 N 1 2 3 4 5 6
DBREF1 8TAV A 1 246 UNP A0A0D6HZA6_STAAU
DBREF2 8TAV A A0A0D6HZA6 1 246
SEQADV 8TAV GLY A -2 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 8TAV PRO A -1 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 8TAV GLY A 0 UNP A0A0D6HZA EXPRESSION TAG
SEQRES 1 A 249 GLY PRO GLY MET GLN ILE LYS LEU PRO LYS PRO PHE PHE
SEQRES 2 A 249 PHE GLU GLU GLY LYS ARG ALA VAL LEU LEU LEU HIS GLY
SEQRES 3 A 249 PHE THR GLY ASN SER SER ASP VAL ARG GLN LEU GLY ARG
SEQRES 4 A 249 PHE LEU GLN LYS LYS GLY TYR THR SER TYR ALA PRO GLN
SEQRES 5 A 249 TYR GLU GLY HIS ALA ALA PRO PRO ASP GLU ILE LEU LYS
SEQRES 6 A 249 SER SER PRO PHE VAL TRP PHE LYS ASP ALA LEU ASP GLY
SEQRES 7 A 249 TYR ASP TYR LEU VAL GLU GLN GLY TYR ASP GLU ILE VAL
SEQRES 8 A 249 VAL ALA GLY LEU SER LEU GLY GLY ASP PHE ALA LEU LYS
SEQRES 9 A 249 LEU SER LEU ASN ARG ASP VAL LYS GLY ILE VAL THR MET
SEQRES 10 A 249 CYS ALA PRO MET GLY GLY LYS THR GLU GLY ALA ILE TYR
SEQRES 11 A 249 GLU GLY PHE LEU GLU TYR ALA ARG ASN PHE LYS LYS TYR
SEQRES 12 A 249 GLU GLY LYS ASP GLN GLU THR ILE ASP ASN GLU MET ASP
SEQRES 13 A 249 HIS PHE LYS PRO THR GLU THR LEU LYS GLU LEU SER GLU
SEQRES 14 A 249 ALA LEU ASP THR ILE LYS GLU GLN VAL ASP GLU VAL LEU
SEQRES 15 A 249 ASP PRO ILE LEU VAL ILE GLN ALA GLU ASN ASP ASN MET
SEQRES 16 A 249 ILE ASP PRO GLN SER ALA ASN TYR ILE TYR ASP HIS VAL
SEQRES 17 A 249 ASP SER ASP ASP LYS ASN ILE LYS TRP TYR SER GLU SER
SEQRES 18 A 249 GLY HIS VAL ILE THR ILE ASP LYS GLU LYS GLU GLN VAL
SEQRES 19 A 249 PHE GLU ASP ILE TYR GLN PHE LEU GLU SER LEU ASP TRP
SEQRES 20 A 249 SER GLU
HET ZKR A 301 14
HET ZKR A 302 16
HET ZKR A 303 16
HET CA A 304 1
HET CA A 305 1
HET CA A 306 1
HET CA A 307 1
HET CA A 308 1
HETNAM ZKR [5-(TRIFLUOROMETHYL)THIOPHEN-2-YL]BORONIC ACID
HETNAM CA CALCIUM ION
FORMUL 2 ZKR 3(C5 H4 B F3 O2 S)
FORMUL 5 CA 5(CA 2+)
FORMUL 10 HOH *227(H2 O)
HELIX 1 AA1 SER A 28 LYS A 41 1 14
HELIX 2 AA2 PRO A 56 LYS A 62 1 7
HELIX 3 AA3 SER A 64 GLN A 82 1 19
HELIX 4 AA4 SER A 93 SER A 103 1 11
HELIX 5 AA5 LYS A 121 GLU A 141 1 21
HELIX 6 AA6 ASP A 144 HIS A 154 1 11
HELIX 7 AA7 THR A 158 VAL A 175 1 18
HELIX 8 AA8 ASP A 176 VAL A 178 5 3
HELIX 9 AA9 PRO A 195 VAL A 205 1 11
HELIX 10 AB1 VAL A 221 ASP A 225 5 5
HELIX 11 AB2 GLU A 227 SER A 241 1 15
SHEET 1 AA1 7 PHE A 9 PHE A 11 0
SHEET 2 AA1 7 THR A 44 ALA A 47 -1 O ALA A 47 N PHE A 9
SHEET 3 AA1 7 ALA A 17 LEU A 21 1 N LEU A 20 O TYR A 46
SHEET 4 AA1 7 ILE A 87 LEU A 92 1 O ALA A 90 N LEU A 19
SHEET 5 AA1 7 GLY A 110 MET A 114 1 O VAL A 112 N GLY A 91
SHEET 6 AA1 7 ILE A 182 ALA A 187 1 O ILE A 185 N THR A 113
SHEET 7 AA1 7 LYS A 210 TYR A 215 1 O ASN A 211 N VAL A 184
LINK OG SER A 93 B02 ZKR A 301 1555 1555 1.41
LINK NE2 HIS A 220 B02 ZKR A 301 1555 1555 1.46
LINK OE1 GLU A 13 CA CA A 305 1555 4554 2.72
LINK OE1 GLU A 13 CA CA A 308 1555 1555 2.54
LINK OE2 GLU A 13 CA CA A 308 1555 1555 2.22
LINK OE1 GLN A 82 CA CA A 306 1555 1555 2.25
LINK OE1 GLU A 146 CA CA A 305 1555 1555 2.33
LINK OD1 ASP A 149 CA CA A 307 1555 1555 2.54
LINK OD2 ASP A 149 CA CA A 307 1555 1555 2.46
LINK OD2 ASP A 153 CA CA A 307 1555 1555 2.36
LINK OD1 ASP A 203 CA CA A 308 1555 3554 2.43
LINK OD2 ASP A 203 CA CA A 308 1555 3554 2.51
LINK O ASP A 206 CA CA A 304 1555 1555 2.31
LINK OD1 ASP A 206 CA CA A 304 1555 1555 2.38
LINK OD1 ASP A 208 CA CA A 304 1555 1555 2.38
LINK CA CA A 304 O HOH A 491 1555 1555 2.54
LINK CA CA A 304 O HOH A 554 1555 1555 2.38
LINK CA CA A 304 O HOH A 594 1555 1555 2.51
LINK CA CA A 304 O HOH A 599 1555 1555 2.44
LINK CA CA A 305 O HOH A 439 1555 1555 2.41
LINK CA CA A 305 O HOH A 464 1555 1556 2.40
LINK CA CA A 305 O HOH A 473 1555 1555 2.37
LINK CA CA A 305 O HOH A 512 1555 1555 2.32
LINK CA CA A 305 O HOH A 591 1555 3555 2.27
LINK CA CA A 306 O HOH A 406 1555 1555 2.33
LINK CA CA A 306 O HOH A 517 1555 1555 2.09
LINK CA CA A 306 O HOH A 525 1555 1555 2.40
LINK CA CA A 306 O HOH A 579 1555 1555 2.54
LINK CA CA A 306 O HOH A 590 1555 1555 2.50
LINK CA CA A 306 O HOH A 625 1555 1555 2.30
LINK CA CA A 307 O HOH A 408 1555 4545 2.34
LINK CA CA A 307 O HOH A 476 1555 1555 2.29
LINK CA CA A 307 O HOH A 509 1555 1555 2.41
LINK CA CA A 308 O HOH A 444 1555 1555 2.52
LINK CA CA A 308 O HOH A 474 1555 4555 2.33
LINK CA CA A 308 O HOH A 506 1555 1555 2.40
LINK CA CA A 308 O HOH A 577 1555 4555 2.55
CRYST1 67.381 67.381 55.473 90.00 90.00 90.00 P 43 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 0.014841 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014841 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018027 0.00000
TER 3895 SER A 245
MASTER 455 0 8 11 7 0 0 6 2207 1 83 20
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