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HEADER HYDROLASE 17-JUL-24 9COM
TITLE FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES E, UNBOUND DIMER CRYSTAL FORM 5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FPHE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: N-TERMINAL GPG FROM EXPRESSION TAG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS USA300;
SOURCE 3 ORGANISM_TAXID: 367830;
SOURCE 4 GENE: SAUSA300_2518;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS FPHE, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 06-AUG-25 9COM 0
JRNL AUTH M.FELLNER
JRNL TITL FPHE, STAPHYLOCOCCUS AUREUS, S. AUREUS,
JRNL TITL 2 FLUOROPHOSPHONATE-BINDING, SERINE HYDROLASES, LIPASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.04 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) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 51365
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.730
REMARK 3 FREE R VALUE TEST SET COUNT : 2429
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 43.4000 - 5.2500 0.98 3083 143 0.1570 0.1909
REMARK 3 2 5.2500 - 4.1700 0.99 2974 120 0.1491 0.2068
REMARK 3 3 4.1700 - 3.6500 0.99 2914 136 0.1754 0.2434
REMARK 3 4 3.6400 - 3.3100 0.99 2920 138 0.1991 0.2486
REMARK 3 5 3.3100 - 3.0700 0.99 2872 158 0.2157 0.2686
REMARK 3 6 3.0700 - 2.8900 1.00 2890 129 0.2190 0.2750
REMARK 3 7 2.8900 - 2.7500 0.99 2874 161 0.2235 0.2660
REMARK 3 8 2.7500 - 2.6300 1.00 2890 131 0.2337 0.2841
REMARK 3 9 2.6300 - 2.5300 0.99 2860 171 0.2395 0.2675
REMARK 3 10 2.5300 - 2.4400 1.00 2866 130 0.2343 0.2323
REMARK 3 11 2.4400 - 2.3600 1.00 2860 148 0.2430 0.3013
REMARK 3 12 2.3600 - 2.3000 0.99 2834 137 0.2442 0.3037
REMARK 3 13 2.3000 - 2.2400 1.00 2898 134 0.2537 0.2791
REMARK 3 14 2.2400 - 2.1800 1.00 2855 146 0.2614 0.3259
REMARK 3 15 2.1800 - 2.1300 1.00 2857 156 0.2886 0.3125
REMARK 3 16 2.1300 - 2.0900 1.00 2837 159 0.2972 0.3455
REMARK 3 17 2.0900 - 2.0400 0.93 2652 132 0.3314 0.3133
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.300
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 : 0.008 6751
REMARK 3 ANGLE : 0.912 9163
REMARK 3 CHIRALITY : 0.055 998
REMARK 3 PLANARITY : 0.008 1205
REMARK 3 DIHEDRAL : 6.715 893
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6785 53.1606 33.5522
REMARK 3 T TENSOR
REMARK 3 T11: 0.2668 T22: 0.3467
REMARK 3 T33: 0.3027 T12: 0.0044
REMARK 3 T13: 0.0268 T23: 0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 3.8760 L22: 2.7448
REMARK 3 L33: 2.5098 L12: -0.1616
REMARK 3 L13: 0.2674 L23: -0.2689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: -0.4222 S13: -0.2283
REMARK 3 S21: 0.0721 S22: -0.0219 S23: -0.0234
REMARK 3 S31: 0.1728 S32: -0.0700 S33: 0.0028
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3931 30.1822 10.1029
REMARK 3 T TENSOR
REMARK 3 T11: 0.8176 T22: 0.6507
REMARK 3 T33: 0.7348 T12: 0.0156
REMARK 3 T13: -0.0148 T23: -0.0479
REMARK 3 L TENSOR
REMARK 3 L11: -0.0064 L22: 3.9550
REMARK 3 L33: 0.5560 L12: -0.4505
REMARK 3 L13: -0.2643 L23: 1.5290
REMARK 3 S TENSOR
REMARK 3 S11: -0.0364 S12: 0.0423 S13: -0.6231
REMARK 3 S21: -0.8401 S22: -0.1304 S23: 0.5608
REMARK 3 S31: 0.0981 S32: 0.1497 S33: 0.1311
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8303 7.6055 15.2096
REMARK 3 T TENSOR
REMARK 3 T11: 0.3421 T22: 0.3183
REMARK 3 T33: 0.2545 T12: -0.0204
REMARK 3 T13: -0.0209 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 3.8511 L22: 5.2963
REMARK 3 L33: 2.3591 L12: -0.9364
REMARK 3 L13: -0.8948 L23: 0.9281
REMARK 3 S TENSOR
REMARK 3 S11: 0.0815 S12: 0.2265 S13: -0.1657
REMARK 3 S21: -0.4912 S22: -0.1556 S23: -0.0135
REMARK 3 S31: 0.0756 S32: -0.1137 S33: 0.0600
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9118 8.8034 26.8937
REMARK 3 T TENSOR
REMARK 3 T11: 0.2644 T22: 0.3401
REMARK 3 T33: 0.3326 T12: 0.0026
REMARK 3 T13: -0.0016 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 3.7301 L22: 3.0984
REMARK 3 L33: 2.1702 L12: -0.4005
REMARK 3 L13: 0.1415 L23: 0.3037
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: -0.2763 S13: 0.0032
REMARK 3 S21: 0.1173 S22: -0.0454 S23: 0.2074
REMARK 3 S31: 0.0099 S32: -0.2963 S33: 0.0756
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5061 37.5001 11.3699
REMARK 3 T TENSOR
REMARK 3 T11: 0.6587 T22: 0.5749
REMARK 3 T33: 0.6355 T12: 0.0615
REMARK 3 T13: 0.1332 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 1.2229 L22: 6.5125
REMARK 3 L33: 0.0277 L12: -2.3515
REMARK 3 L13: -0.1267 L23: 0.7298
REMARK 3 S TENSOR
REMARK 3 S11: 0.2129 S12: 0.1349 S13: 0.3098
REMARK 3 S21: -1.2959 S22: -0.3503 S23: -0.7273
REMARK 3 S31: -0.1089 S32: -0.2417 S33: 0.1941
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 185 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7631 58.0497 22.3980
REMARK 3 T TENSOR
REMARK 3 T11: 0.3320 T22: 0.3216
REMARK 3 T33: 0.2550 T12: 0.0208
REMARK 3 T13: -0.0018 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 3.3285 L22: 5.3659
REMARK 3 L33: 2.7996 L12: 0.9061
REMARK 3 L13: 0.3393 L23: -0.8947
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.0156 S13: 0.0167
REMARK 3 S21: -0.4557 S22: 0.0673 S23: 0.0785
REMARK 3 S31: 0.0903 S32: -0.1240 S33: -0.0507
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3617 21.6672 -2.8544
REMARK 3 T TENSOR
REMARK 3 T11: 0.2947 T22: 0.3650
REMARK 3 T33: 0.4656 T12: -0.0007
REMARK 3 T13: 0.1138 T23: 0.1009
REMARK 3 L TENSOR
REMARK 3 L11: 3.7719 L22: 6.1437
REMARK 3 L33: 3.8718 L12: -1.1106
REMARK 3 L13: -0.3198 L23: 0.0388
REMARK 3 S TENSOR
REMARK 3 S11: 0.0435 S12: 0.1272 S13: 0.0533
REMARK 3 S21: -0.3525 S22: -0.3866 S23: -0.8917
REMARK 3 S31: 0.1280 S32: 0.3597 S33: 0.3079
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 137 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.5770 47.7067 -6.2625
REMARK 3 T TENSOR
REMARK 3 T11: 0.6489 T22: 0.8563
REMARK 3 T33: 0.8588 T12: 0.0195
REMARK 3 T13: -0.1619 T23: -0.0970
REMARK 3 L TENSOR
REMARK 3 L11: 0.0022 L22: 8.7523
REMARK 3 L33: 1.0346 L12: -0.2721
REMARK 3 L13: 0.0046 L23: 2.6671
REMARK 3 S TENSOR
REMARK 3 S11: -0.2561 S12: -0.1313 S13: 0.3311
REMARK 3 S21: -0.3980 S22: -0.2856 S23: 1.5065
REMARK 3 S31: -0.2132 S32: -0.2837 S33: 0.4345
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 184 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.7545 67.2216 6.6697
REMARK 3 T TENSOR
REMARK 3 T11: 0.4762 T22: 0.4624
REMARK 3 T33: 0.3448 T12: 0.0016
REMARK 3 T13: -0.0337 T23: -0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 3.6099 L22: 7.0246
REMARK 3 L33: 2.6204 L12: 0.8236
REMARK 3 L13: -0.1098 L23: -1.5271
REMARK 3 S TENSOR
REMARK 3 S11: 0.1497 S12: -0.4743 S13: 0.3237
REMARK 3 S21: 0.7489 S22: -0.2005 S23: 0.5392
REMARK 3 S31: -0.4601 S32: -0.2850 S33: 0.0615
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 9COM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-24.
REMARK 100 THE DEPOSITION ID IS D_1000286004.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 0.954
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 : 51434
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
REMARK 200 RESOLUTION RANGE LOW (A) : 48.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 1.43600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 UL 13.9 MG/ML FPHE (10MM HEPES PH
REMARK 280 7.6, 100MM NACL) WERE MIXED WITH 0.15 UL OF RESERVOIR SOLUTION.
REMARK 280 SITTING DROP RESERVOIR CONTAINED 25 UL OF 0.2 M POTASSIUM
REMARK 280 THIOCYANATE, 0.1 M TRIS PH 8.5 AND 22% W/V POLYETHYLENE GLYCOL
REMARK 280 MONOMETHYL ETHER 2,000. CRYSTAL WAS FROZEN IN A SOLUTION OF ~25%
REMARK 280 GLYCEROL, 75% RESERVOIR AFTER ~10S SOAKING IN THAT SOLUTION.,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.39850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.88200
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.39850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 68.88200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 86.79700
REMARK 350 BIOMT3 2 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 GLY B -2
REMARK 465 GLY C -2
REMARK 465 PRO C -1
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 -128.01 55.47
REMARK 500 GLU A 127 70.12 43.39
REMARK 500 GLU A 201 -54.67 -121.93
REMARK 500 SER B 103 -131.15 62.31
REMARK 500 GLU B 127 74.32 37.52
REMARK 500 GLU B 201 -54.65 -121.78
REMARK 500 SER C 103 -131.84 59.30
REMARK 500 ASP C 136 42.95 -97.27
REMARK 500 ALA C 170 153.28 -49.56
REMARK 500 TYR C 218 34.88 -99.42
REMARK 500 LYS C 244 43.47 -93.83
REMARK 500 GLU C 245 -32.81 -153.88
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 K C 301 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU C 272 O
REMARK 620 2 LEU C 272 O 0.0
REMARK 620 3 ASN C 273 O 75.3 75.3
REMARK 620 4 ASN C 273 O 75.3 75.3 0.0
REMARK 620 5 GLY C 276 OXT 76.2 76.2 151.3 151.3
REMARK 620 6 GLY C 276 OXT 76.2 76.2 151.3 151.3 0.0
REMARK 620 7 HOH C 402 O 56.6 56.6 117.7 117.7 45.6 45.6
REMARK 620 N 1 2 3 4 5 6
DBREF 9COM A 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 9COM B 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 9COM C 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
SEQADV 9COM GLY A -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9COM PRO A -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9COM GLY A 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9COM GLY B -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9COM PRO B -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9COM GLY B 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9COM GLY C -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9COM PRO C -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9COM GLY C 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
SEQRES 1 C 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 C 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 C 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 C 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 C 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 C 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 C 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 C 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 C 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 C 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 C 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 C 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 C 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 C 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 C 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 C 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 C 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 C 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 C 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 C 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 C 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 C 279 LEU LEU ASN MET TRP GLY
HET K C 301 1
HETNAM K POTASSIUM ION
FORMUL 4 K K 1+
FORMUL 5 HOH *206(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 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 ASN B 168 1 33
HELIX 21 AC3 ALA B 170 MET B 177 1 8
HELIX 22 AC4 THR B 183 GLU B 201 1 19
HELIX 23 AC5 GLU B 201 HIS B 207 1 7
HELIX 24 AC6 LEU B 212 LYS B 217 1 6
HELIX 25 AC7 TYR B 218 ASP B 220 5 3
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
HELIX 29 AD2 THR C 31 ILE C 34 5 4
HELIX 30 AD3 PHE C 35 LYS C 43 1 9
HELIX 31 AD4 PRO C 66 ASN C 71 5 6
HELIX 32 AD5 ASP C 75 SER C 93 1 19
HELIX 33 AD6 SER C 103 TYR C 116 1 14
HELIX 34 AD7 ASP C 136 LEU C 167 1 32
HELIX 35 AD8 ALA C 170 SER C 178 1 9
HELIX 36 AD9 THR C 183 GLU C 201 1 19
HELIX 37 AE1 GLU C 201 HIS C 207 1 7
HELIX 38 AE2 LEU C 212 LYS C 217 1 6
HELIX 39 AE3 TYR C 218 ILE C 222 5 5
HELIX 40 AE4 ASP C 229 ARG C 231 5 3
HELIX 41 AE5 SER C 233 GLY C 247 1 15
HELIX 42 AE6 LEU C 258 LYS C 263 1 6
HELIX 43 AE7 LYS C 263 GLY C 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 ASP A 52 -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 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 THR B 223 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 LEU B 4 O LEU B 11
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
SHEET 1 AA5 3 GLU C 2 LEU C 6 0
SHEET 2 AA5 3 ALA C 9 GLY C 17 -1 O ALA C 9 N LEU C 6
SHEET 3 AA5 3 GLU C 60 LEU C 61 -1 O GLU C 60 N LYS C 10
SHEET 1 AA6 6 GLU C 2 LEU C 6 0
SHEET 2 AA6 6 ALA C 9 GLY C 17 -1 O ALA C 9 N LEU C 6
SHEET 3 AA6 6 THR C 47 VAL C 51 -1 O VAL C 48 N VAL C 16
SHEET 4 AA6 6 VAL C 21 ILE C 25 1 N PHE C 24 O VAL C 49
SHEET 5 AA6 6 VAL C 97 SER C 102 1 O TYR C 98 N ILE C 23
SHEET 6 AA6 6 VAL C 120 HIS C 126 1 O LYS C 121 N VAL C 97
SHEET 1 AA7 2 LEU C 224 GLY C 227 0
SHEET 2 AA7 2 ILE C 250 ILE C 253 1 O VAL C 251 N LEU C 224
LINK O LEU C 272 K K C 301 1555 1555 2.79
LINK O LEU C 272 K K C 301 1555 2575 3.23
LINK O ASN C 273 K K C 301 1555 1555 2.86
LINK O ASN C 273 K K C 301 1555 2575 2.53
LINK OXT GLY C 276 K K C 301 1555 1555 2.72
LINK OXT GLY C 276 K K C 301 1555 2575 3.31
LINK K K C 301 O HOH C 402 1555 1555 3.27
CRYST1 67.399 86.797 137.764 90.00 90.00 90.00 P 2 21 21 12
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 0.014837 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011521 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007259 0.00000
TER 2201 GLY A 276
TER 4402 GLY B 276
TER 6596 GLY C 276
MASTER 409 0 1 43 38 0 0 6 6800 3 5 66
END |