| content |
HEADER HYDROLASE 22-JUN-23 8T87
TITLE FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES E, UNBOUND DIMER CRYSTAL FORM 1
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_PLASMID: F1010
KEYWDS FPHE, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 06-MAR-24 8T87 0
JRNL AUTH J.JO,T.UPADHYAY,E.C.WOODS,K.W.PARK,N.J.PEDOWITZ,
JRNL AUTH 2 J.JAWOREK-KORJAKOWSKA,S.WANG,T.A.VALDEZ,M.FELLNER,M.BOGYO
JRNL TITL DEVELOPMENT OF OXADIAZOLONE ACTIVITY-BASED PROBES TARGETING
JRNL TITL 2 FPHE FOR SPECIFIC DETECTION OF STAPHYLOCOCCUS AUREUS
JRNL TITL 3 INFECTIONS.
JRNL REF J.AM.CHEM.SOC. 2024
JRNL REFN ESSN 1520-5126
JRNL PMID 38411555
JRNL DOI 10.1021/JACS.3C13974
REMARK 2
REMARK 2 RESOLUTION. 1.62 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) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 60354
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 2954
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 38.7300 - 4.4800 0.98 2799 153 0.1641 0.1779
REMARK 3 2 4.4800 - 3.5600 0.99 2811 122 0.1415 0.1648
REMARK 3 3 3.5600 - 3.1100 0.99 2738 167 0.1704 0.2256
REMARK 3 4 3.1100 - 2.8200 0.99 2784 154 0.1831 0.2000
REMARK 3 5 2.8200 - 2.6200 0.99 2776 138 0.1907 0.2275
REMARK 3 6 2.6200 - 2.4700 0.99 2753 135 0.1847 0.2227
REMARK 3 7 2.4700 - 2.3400 0.99 2787 113 0.1860 0.2121
REMARK 3 8 2.3400 - 2.2400 0.99 2732 172 0.1817 0.2240
REMARK 3 9 2.2400 - 2.1500 0.99 2749 151 0.1918 0.2196
REMARK 3 10 2.1500 - 2.0800 0.99 2745 153 0.2021 0.2443
REMARK 3 11 2.0800 - 2.0100 0.99 2739 131 0.2056 0.2521
REMARK 3 12 2.0100 - 1.9600 0.99 2713 171 0.2038 0.2354
REMARK 3 13 1.9600 - 1.9100 0.98 2762 118 0.2108 0.2641
REMARK 3 14 1.9100 - 1.8600 0.98 2749 122 0.2245 0.2571
REMARK 3 15 1.8600 - 1.8200 0.99 2788 110 0.2552 0.3068
REMARK 3 16 1.8200 - 1.7800 0.98 2655 176 0.2863 0.3451
REMARK 3 17 1.7800 - 1.7400 0.99 2747 136 0.3144 0.3383
REMARK 3 18 1.7400 - 1.7100 0.97 2711 120 0.3418 0.3721
REMARK 3 19 1.7100 - 1.6800 0.99 2729 149 0.3436 0.3984
REMARK 3 20 1.6800 - 1.6500 0.97 2671 151 0.3695 0.3729
REMARK 3 21 1.6500 - 1.6200 0.89 2462 112 0.3902 0.4317
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.720
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 : 0.011 4525
REMARK 3 ANGLE : 1.135 6148
REMARK 3 CHIRALITY : 0.065 669
REMARK 3 PLANARITY : 0.011 811
REMARK 3 DIHEDRAL : 6.424 602
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0494 -9.5036 9.0098
REMARK 3 T TENSOR
REMARK 3 T11: 0.2619 T22: 0.2213
REMARK 3 T33: 0.2716 T12: -0.0073
REMARK 3 T13: -0.0048 T23: 0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 0.8837 L22: 2.0225
REMARK 3 L33: 2.1090 L12: 0.0209
REMARK 3 L13: 0.4012 L23: -0.3545
REMARK 3 S TENSOR
REMARK 3 S11: -0.0639 S12: 0.0566 S13: 0.1686
REMARK 3 S21: 0.0874 S22: -0.0198 S23: -0.0788
REMARK 3 S31: -0.3541 S32: 0.0090 S33: 0.0831
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 153 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1976 -25.3263 -13.9386
REMARK 3 T TENSOR
REMARK 3 T11: 0.6511 T22: 0.4702
REMARK 3 T33: 0.7490 T12: 0.1436
REMARK 3 T13: -0.0688 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 2.2329 L22: 1.3039
REMARK 3 L33: 2.5789 L12: 0.3798
REMARK 3 L13: 2.4511 L23: 0.2505
REMARK 3 S TENSOR
REMARK 3 S11: 0.2179 S12: 0.1179 S13: -0.6123
REMARK 3 S21: -0.3231 S22: -0.3341 S23: 0.0672
REMARK 3 S31: 0.8339 S32: 0.3406 S33: 0.0318
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3415 -13.3817 -24.3570
REMARK 3 T TENSOR
REMARK 3 T11: 0.2158 T22: 0.2006
REMARK 3 T33: 0.3233 T12: 0.0343
REMARK 3 T13: 0.0002 T23: -0.0781
REMARK 3 L TENSOR
REMARK 3 L11: 2.6782 L22: 1.5204
REMARK 3 L33: 3.1324 L12: -0.0387
REMARK 3 L13: 0.0378 L23: 0.5287
REMARK 3 S TENSOR
REMARK 3 S11: 0.0216 S12: 0.0785 S13: -0.3959
REMARK 3 S21: 0.0571 S22: 0.1565 S23: -0.3369
REMARK 3 S31: 0.3634 S32: 0.2041 S33: -0.0813
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7017 -5.9289 -26.0543
REMARK 3 T TENSOR
REMARK 3 T11: 0.1945 T22: 0.3617
REMARK 3 T33: 0.4276 T12: 0.0254
REMARK 3 T13: 0.0184 T23: -0.1684
REMARK 3 L TENSOR
REMARK 3 L11: 2.1620 L22: 1.7210
REMARK 3 L33: 2.0320 L12: 0.0553
REMARK 3 L13: -0.2790 L23: 0.7790
REMARK 3 S TENSOR
REMARK 3 S11: 0.0467 S12: 0.0971 S13: -0.0718
REMARK 3 S21: -0.0863 S22: 0.3255 S23: -0.5350
REMARK 3 S31: 0.0356 S32: 0.6081 S33: -0.2700
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.3831 -15.8639 5.9478
REMARK 3 T TENSOR
REMARK 3 T11: 0.3212 T22: 0.4720
REMARK 3 T33: 0.3949 T12: 0.0503
REMARK 3 T13: 0.0299 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 4.1625 L22: 1.0378
REMARK 3 L33: 4.3513 L12: -2.2608
REMARK 3 L13: 4.8949 L23: -2.5437
REMARK 3 S TENSOR
REMARK 3 S11: 0.2627 S12: -0.2711 S13: -0.0749
REMARK 3 S21: -0.2330 S22: -0.0078 S23: -0.0097
REMARK 3 S31: 0.4539 S32: -0.0969 S33: -0.1996
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 184 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5551 -15.7175 16.9836
REMARK 3 T TENSOR
REMARK 3 T11: 0.2340 T22: 0.2215
REMARK 3 T33: 0.2290 T12: 0.0099
REMARK 3 T13: 0.0185 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.3711 L22: 2.4082
REMARK 3 L33: 2.8480 L12: 0.2733
REMARK 3 L13: 1.1246 L23: -0.2597
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: -0.1703 S13: 0.0088
REMARK 3 S21: 0.3329 S22: 0.0322 S23: -0.0405
REMARK 3 S31: -0.1332 S32: -0.2332 S33: -0.0065
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 8T87 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1000275462.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-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 : 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 : 60409
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 46.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 1.18000
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 (%): 37.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL 15.2 MG/ML FPHE (9 MM HEPES PH
REMARK 280 7.5, 87 MM NACL, 13% DMSO) MIXED WITH 0.2 UL OF RESERVOIR
REMARK 280 SOLUTION. SITTING DROP RESERVOIR CONTAINED 25 UL OF 0.18 M
REMARK 280 MAGNESIUM CHLORIDE, 0.1 M TRIS PH 7.5, 22.5 % W/V POLYETHYLENE
REMARK 280 GLYCOL MONOMETHYL ETHER 2000. CRYSTAL WAS FROZEN IN A SOLUTION
REMARK 280 OF ~25% GLYCEROL, 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 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 37.04100
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 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 B 494 O HOH B 505 2.13
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 476 O HOH B 508 1455 2.13
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 -129.43 60.86
REMARK 500 GLU A 127 71.33 42.87
REMARK 500 GLU A 201 -54.00 -127.20
REMARK 500 TRP A 275 -46.79 -133.07
REMARK 500 SER B 103 -129.47 57.32
REMARK 500 GLU B 127 70.48 47.39
REMARK 500 THR B 153 -50.22 -132.97
REMARK 500 GLU B 201 -51.76 -131.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 231 0.16 SIDE CHAIN
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 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 7 OE1
REMARK 620 2 HOH A 483 O 93.1
REMARK 620 3 HOH A 485 O 84.8 111.2
REMARK 620 4 HOH A 486 O 100.7 163.4 61.4
REMARK 620 5 HOH A 498 O 171.9 79.8 94.2 85.8
REMARK 620 N 1 2 3 4
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 MET A 274 O
REMARK 620 2 MET B 274 O 49.3
REMARK 620 3 HOH B 448 O 47.6 1.9
REMARK 620 4 HOH B 456 O 49.2 1.1 2.5
REMARK 620 5 HOH B 461 O 49.0 0.9 1.4 2.0
REMARK 620 6 HOH B 476 O 47.8 2.0 2.1 1.4 2.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 402 O
REMARK 620 2 HOH A 436 O 155.0
REMARK 620 3 HOH A 466 O 56.7 124.3
REMARK 620 4 ASN B 273 OD1 73.6 105.2 129.1
REMARK 620 5 HOH B 443 O 83.0 122.0 76.2 88.3
REMARK 620 6 HOH B 473 O 73.0 82.0 91.4 83.7 155.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 305 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 433 O
REMARK 620 2 HOH A 508 O 86.7
REMARK 620 3 HOH A 510 O 91.1 108.9
REMARK 620 4 HOH B 415 O 169.7 93.0 98.7
REMARK 620 5 HOH B 499 O 81.0 154.6 93.6 95.2
REMARK 620 6 HOH B 503 O 86.2 80.7 169.9 83.6 76.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 437 O
REMARK 620 2 HOH A 497 O 76.2
REMARK 620 3 HOH B 401 O 163.4 87.3
REMARK 620 4 HOH B 446 O 84.7 75.2 93.3
REMARK 620 5 HOH B 490 O 97.8 82.0 77.4 155.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 237 OD2
REMARK 620 2 HOH B 464 O 93.8
REMARK 620 3 HOH B 465 O 87.1 168.1
REMARK 620 4 HOH B 479 O 171.9 92.4 85.8
REMARK 620 5 HOH B 493 O 95.3 101.3 90.4 88.6
REMARK 620 6 HOH B 498 O 87.1 81.9 86.3 88.7 175.8
REMARK 620 N 1 2 3 4 5
DBREF 8T87 A 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 8T87 B 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
SEQADV 8T87 GLY A -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T87 PRO A -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T87 GLY A 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T87 GLY B -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T87 PRO B -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8T87 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 MG A 301 1
HET MG B 301 1
HET MG B 302 1
HET MG B 303 1
HET MG B 304 1
HET MG B 305 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 6(MG 2+)
FORMUL 9 HOH *219(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 SER A 178 1 9
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 TRP A 275 1 13
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 SER B 178 1 9
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 SER B 233 GLY B 247 1 15
HELIX 27 AC9 LEU B 258 LYS B 263 1 6
HELIX 28 AD1 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 VAL A 21
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 LEU B 22
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 LEU B 22
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 OE1 GLN A 7 MG MG A 301 1555 1555 2.13
LINK O MET A 274 MG MG B 302 1555 1454 2.19
LINK MG MG A 301 O HOH A 483 1555 1555 1.98
LINK MG MG A 301 O HOH A 485 1555 1555 2.33
LINK MG MG A 301 O HOH A 486 1555 1655 1.95
LINK MG MG A 301 O HOH A 498 1555 1655 2.23
LINK O HOH A 402 MG MG B 303 1656 1555 2.59
LINK O HOH A 433 MG MG B 305 1555 1555 1.96
LINK O HOH A 436 MG MG B 303 1656 1555 2.12
LINK O HOH A 437 MG MG B 301 1455 1555 2.37
LINK O HOH A 466 MG MG B 303 1656 1555 2.31
LINK O HOH A 497 MG MG B 301 1455 1555 2.01
LINK O HOH A 508 MG MG B 305 1555 1555 1.92
LINK O HOH A 510 MG MG B 305 2545 1555 2.03
LINK OD2 ASP B 237 MG MG B 304 1555 1555 2.14
LINK OD1 ASN B 273 MG MG B 303 1555 1555 2.08
LINK O MET B 274 MG MG B 302 1555 1555 1.91
LINK MG MG B 301 O HOH B 401 1555 1555 2.31
LINK MG MG B 301 O HOH B 446 1555 1555 2.26
LINK MG MG B 301 O HOH B 490 1555 1555 2.10
LINK MG MG B 302 O HOH B 448 1555 1555 2.03
LINK MG MG B 302 O HOH B 456 1555 1555 2.15
LINK MG MG B 302 O HOH B 461 1555 1555 2.06
LINK MG MG B 302 O HOH B 476 1555 1555 2.14
LINK MG MG B 303 O HOH B 443 1555 1555 1.84
LINK MG MG B 303 O HOH B 473 1555 1555 2.29
LINK MG MG B 304 O HOH B 464 1555 1555 2.04
LINK MG MG B 304 O HOH B 465 1555 1555 2.01
LINK MG MG B 304 O HOH B 479 1555 2445 2.18
LINK MG MG B 304 O HOH B 493 1555 1555 2.18
LINK MG MG B 304 O HOH B 498 1555 1555 2.49
LINK MG MG B 305 O HOH B 415 1555 1555 2.02
LINK MG MG B 305 O HOH B 499 1555 1555 2.10
LINK MG MG B 305 O HOH B 503 1555 1555 2.08
CRYST1 46.787 74.082 71.424 90.00 91.28 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 0.021373 0.000000 0.000478 0.00000
SCALE2 0.000000 0.013499 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014004 0.00000
TER 4368 GLY A 276
TER 8720 GLY B 276
MASTER 443 0 6 28 27 0 0 6 4611 2 33 44
END |