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HEADER HYDROLASE 12-JUL-23 8TFW
TITLE FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES E, BORONIC ACID-BASED COMPOUND N34 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROPHOSPHONATE-BINDING SERINE HYDROLASE E;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA300-0114;
SOURCE 3 ORGANISM_TAXID: 1385527;
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, 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 24-JUL-24 8TFW 0
JRNL AUTH M.FELLNER
JRNL TITL FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES E, BORONIC ACID-BASED COMPOUND N34 BOUND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.93 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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 38663
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 1882
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 40.0100 - 4.5400 0.99 2890 176 0.1751 0.2136
REMARK 3 2 4.5300 - 3.6000 0.99 2817 152 0.1694 0.1942
REMARK 3 3 3.6000 - 3.1500 0.99 2899 103 0.1995 0.2789
REMARK 3 4 3.1400 - 2.8600 0.99 2839 165 0.2115 0.2448
REMARK 3 5 2.8600 - 2.6500 1.00 2865 140 0.2246 0.2926
REMARK 3 6 2.6500 - 2.5000 1.00 2831 157 0.2196 0.2881
REMARK 3 7 2.5000 - 2.3700 0.98 2761 166 0.2225 0.2842
REMARK 3 8 2.3700 - 2.2700 0.99 2845 135 0.2316 0.2730
REMARK 3 9 2.2700 - 2.1800 0.97 2744 167 0.2843 0.3833
REMARK 3 10 2.1800 - 2.1100 1.00 2824 155 0.2503 0.2728
REMARK 3 11 2.1100 - 2.0400 0.97 2769 105 0.3029 0.3459
REMARK 3 12 2.0400 - 1.9800 1.00 2908 138 0.2684 0.3315
REMARK 3 13 1.9800 - 1.9300 0.98 2789 123 0.3139 0.3936
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.370
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 4528
REMARK 3 ANGLE : 1.055 6151
REMARK 3 CHIRALITY : 0.060 666
REMARK 3 PLANARITY : 0.011 809
REMARK 3 DIHEDRAL : 7.704 602
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4520 -8.9048 46.5146
REMARK 3 T TENSOR
REMARK 3 T11: 0.1800 T22: 0.1998
REMARK 3 T33: 0.1948 T12: 0.0021
REMARK 3 T13: -0.0069 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 2.1189 L22: 1.7108
REMARK 3 L33: 1.9398 L12: 0.3844
REMARK 3 L13: 0.8228 L23: 0.2314
REMARK 3 S TENSOR
REMARK 3 S11: -0.0897 S12: -0.0554 S13: 0.3001
REMARK 3 S21: 0.0271 S22: -0.0236 S23: -0.0002
REMARK 3 S31: -0.2524 S32: -0.0356 S33: 0.1184
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 153 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4842 -15.6918 15.4557
REMARK 3 T TENSOR
REMARK 3 T11: 0.2005 T22: 0.1744
REMARK 3 T33: 0.2646 T12: 0.0197
REMARK 3 T13: -0.0117 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 2.0067 L22: 1.4371
REMARK 3 L33: 2.5395 L12: 0.5174
REMARK 3 L13: 0.4501 L23: 0.4777
REMARK 3 S TENSOR
REMARK 3 S11: 0.1608 S12: -0.1136 S13: -0.4936
REMARK 3 S21: 0.1531 S22: -0.0380 S23: -0.1217
REMARK 3 S31: 0.4285 S32: 0.1220 S33: -0.0552
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8968 -5.4627 10.8099
REMARK 3 T TENSOR
REMARK 3 T11: 0.1366 T22: 0.1601
REMARK 3 T33: 0.1695 T12: 0.0009
REMARK 3 T13: 0.0211 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 3.4316 L22: 1.1929
REMARK 3 L33: 1.8931 L12: -0.0069
REMARK 3 L13: 0.5641 L23: 0.2438
REMARK 3 S TENSOR
REMARK 3 S11: -0.0249 S12: 0.1580 S13: 0.0126
REMARK 3 S21: -0.1228 S22: 0.0844 S23: -0.0959
REMARK 3 S31: -0.0464 S32: 0.2133 S33: -0.0546
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0241 -15.5253 43.1269
REMARK 3 T TENSOR
REMARK 3 T11: 0.2502 T22: 0.5037
REMARK 3 T33: 0.2217 T12: -0.0146
REMARK 3 T13: 0.0617 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 4.0589 L22: 0.7079
REMARK 3 L33: 5.1680 L12: -1.6718
REMARK 3 L13: 4.7357 L23: -2.1335
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: -0.4910 S13: 0.1986
REMARK 3 S21: -0.0659 S22: 0.0034 S23: -0.0844
REMARK 3 S31: 0.2039 S32: -0.3209 S33: -0.0022
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 184 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3197 -15.3704 54.2247
REMARK 3 T TENSOR
REMARK 3 T11: 0.1638 T22: 0.3149
REMARK 3 T33: 0.1721 T12: -0.0504
REMARK 3 T13: 0.0203 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 2.1940 L22: 1.9133
REMARK 3 L33: 1.8639 L12: -0.0756
REMARK 3 L13: 0.6595 L23: -0.1219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0727 S12: -0.3805 S13: 0.2291
REMARK 3 S21: 0.1745 S22: -0.0566 S23: -0.0364
REMARK 3 S31: -0.0003 S32: -0.3393 S33: -0.0255
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 8TFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-23.
REMARK 100 THE DEPOSITION ID IS D_1000275885.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-23
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 : 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
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38831
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 46.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.13500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 1.19500
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 (%): 41.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13UL 19 MG/ML FPHE (10MM HEPES PH 7.5,
REMARK 280 100MM NACL) WERE MIXED WITH 5UL N34 (50MM IN DMSO) AND INCUBATED
REMARK 280 AT 18C OVERNIGHT. 0.15 UL FPHE-N34 SOLUTION WAS MIXED WITH 0.3
REMARK 280 UL OF RESERVOIR SOLUTION. SITTING DROP RESERVOIR CONTAINED 25 UL
REMARK 280 OF 0.18 M MAGNESIUM CHLORIDE, 0.1 M MES PH 6.5, 22.5 % W/V
REMARK 280 POLYETHYLENE GLYCOL MONOMETHYL ETHER 2000. CRYSTAL WAS FROZEN IN
REMARK 280 A SOLUTION OF ~25% GLYCEROL, 75% RESERVOIR., VAPOR DIFFUSION,
REMARK 280 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 38.20950
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 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 OG SER A 103 O01 ZKR A 301 2.14
REMARK 500 O HOH B 416 O HOH B 434 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 406 O HOH B 449 1454 2.14
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 GLN A 7 109.43 -53.44
REMARK 500 SER A 103 -127.34 62.04
REMARK 500 GLU A 127 73.66 40.46
REMARK 500 THR A 153 -35.98 -131.52
REMARK 500 PRO B 96 150.61 -49.98
REMARK 500 SER B 103 -126.30 58.21
REMARK 500 GLU B 201 -52.77 -124.53
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 A 476 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A 477 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH B 470 DISTANCE = 5.81 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 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 83 OE1
REMARK 620 2 HOH A 454 O 102.5
REMARK 620 3 HOH A 467 O 108.4 90.7
REMARK 620 4 ASP B 146 OD1 63.7 166.2 94.2
REMARK 620 5 HOH B 408 O 88.6 89.8 162.4 89.4
REMARK 620 6 HOH B 419 O 91.3 165.7 88.3 27.8 86.9
REMARK 620 N 1 2 3 4 5
DBREF 8TFW A 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 8TFW B 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
SEQADV 8TFW GLY A -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8TFW PRO A -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8TFW GLY A 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8TFW GLY B -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8TFW PRO B -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8TFW 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 ZKR A 301 11
HET MG A 302 1
HET ZKR A 303 11
HETNAM ZKR [5-(TRIFLUOROMETHYL)THIOPHEN-2-YL]BORONIC ACID
HETNAM MG MAGNESIUM ION
FORMUL 3 ZKR 2(C5 H4 B F3 O2 S)
FORMUL 4 MG MG 2+
FORMUL 6 HOH *147(H2 O)
HELIX 1 AA1 THR A 31 ILE A 34 5 4
HELIX 2 AA2 PHE A 35 GLN A 41 1 7
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 ASN A 168 1 33
HELIX 7 AA7 ALA A 170 SER A 178 1 9
HELIX 8 AA8 GLU A 184 GLU A 201 1 18
HELIX 9 AA9 GLU A 201 HIS A 207 1 7
HELIX 10 AB1 THR A 211 TYR A 218 1 8
HELIX 11 AB2 SER A 233 GLY A 247 1 15
HELIX 12 AB3 LEU A 258 LYS A 263 1 6
HELIX 13 AB4 LYS A 263 GLY A 276 1 14
HELIX 14 AB5 THR B 31 ILE B 34 5 4
HELIX 15 AB6 PHE B 35 LYS B 43 1 9
HELIX 16 AB7 PRO B 66 ASN B 71 5 6
HELIX 17 AB8 ASP B 75 SER B 93 1 19
HELIX 18 AB9 SER B 103 TYR B 116 1 14
HELIX 19 AC1 ASP B 136 LEU B 167 1 32
HELIX 20 AC2 ALA B 170 GLN B 179 1 10
HELIX 21 AC3 THR B 183 GLU B 201 1 19
HELIX 22 AC4 GLU B 201 HIS B 207 1 7
HELIX 23 AC5 THR B 211 LYS B 217 1 7
HELIX 24 AC6 TYR B 218 ASP B 220 5 3
HELIX 25 AC7 SER B 233 GLY B 247 1 15
HELIX 26 AC8 LEU B 258 LYS B 263 1 6
HELIX 27 AC9 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 VAL A 16 -1 O TYR A 13 N GLU A 2
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 VAL A 16 -1 O TYR A 13 N GLU A 2
SHEET 3 AA2 8 THR A 47 ASP A 52 -1 O ALA A 50 N HIS A 14
SHEET 4 AA2 8 VAL A 21 ILE A 25 1 N LEU A 22 O THR A 47
SHEET 5 AA2 8 VAL A 97 SER A 102 1 O LEU A 100 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 THR A 223
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 LEU B 100
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 VAL B 16 -1 N ARG B 12 O ASP B 52
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 THR A 223
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 LEU B 100
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 VAL B 16 -1 N ARG B 12 O ASP B 52
SHEET 8 AA4 8 GLU B 60 LEU B 61 -1 O GLU B 60 N LYS B 10
LINK OG SER A 103 B02 ZKR A 301 1555 1555 1.40
LINK NE2 HIS A 257 B02 ZKR A 303 1555 1555 1.44
LINK B02 ZKR A 301 NE2 HIS B 257 1555 1555 1.44
LINK B02 ZKR A 303 OG SER B 103 1555 1555 1.40
LINK OE1 GLN A 83 MG MG A 302 1555 1555 2.12
LINK MG MG A 302 O HOH A 454 1555 1555 2.41
LINK MG MG A 302 O HOH A 467 1555 1555 2.13
LINK MG MG A 302 OD1 ASP B 146 1455 1555 2.38
LINK MG MG A 302 O HOH B 408 1555 1655 2.06
LINK MG MG A 302 O HOH B 419 1555 1655 2.35
CRYST1 46.972 76.419 73.380 90.00 90.86 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 0.021289 0.000000 0.000320 0.00000
SCALE2 0.000000 0.013086 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013629 0.00000
TER 2194 GLY A 276
TER 4402 GLY B 276
MASTER 371 0 3 27 27 0 0 6 4556 2 30 44
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