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HEADER HYDROLASE 17-NOV-24 9EDJ
TITLE FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES E, UNBOUND DIMER CRYSTAL FORM 9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED HYDROLASE SAUSA300_2518;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES
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 21-JAN-26 9EDJ 0
JRNL AUTH M.FELLNER
JRNL TITL FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES E, UNBOUND DIMER CRYSTAL FORM 9
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 16814
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 831
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 46.5900 - 4.7300 0.99 2826 130 0.1688 0.2120
REMARK 3 2 4.7200 - 3.7500 1.00 2672 164 0.1587 0.2517
REMARK 3 3 3.7500 - 3.2800 1.00 2660 127 0.2013 0.3163
REMARK 3 4 3.2800 - 2.9800 1.00 2646 146 0.2258 0.3120
REMARK 3 5 2.9800 - 2.7600 1.00 2623 134 0.2444 0.3691
REMARK 3 6 2.7600 - 2.6000 0.98 2556 130 0.2482 0.3212
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.440
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 4494
REMARK 3 ANGLE : 1.002 6100
REMARK 3 CHIRALITY : 0.056 665
REMARK 3 PLANARITY : 0.009 802
REMARK 3 DIHEDRAL : 6.564 594
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 -1 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8468 -23.6615 1.3682
REMARK 3 T TENSOR
REMARK 3 T11: 0.3049 T22: 0.4020
REMARK 3 T33: 0.3911 T12: 0.0293
REMARK 3 T13: -0.0080 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 1.4294 L22: 3.1734
REMARK 3 L33: 4.2254 L12: -1.0278
REMARK 3 L13: -0.2969 L23: 0.2174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0878 S12: 0.0913 S13: 0.0983
REMARK 3 S21: -0.3331 S22: -0.1163 S23: 0.1411
REMARK 3 S31: -0.0549 S32: -0.0846 S33: 0.0202
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 167 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4759 -7.3009 35.9590
REMARK 3 T TENSOR
REMARK 3 T11: 0.8339 T22: 0.8084
REMARK 3 T33: 0.8312 T12: 0.0612
REMARK 3 T13: -0.0971 T23: -0.1000
REMARK 3 L TENSOR
REMARK 3 L11: 3.8429 L22: 5.2421
REMARK 3 L33: 1.9787 L12: 0.0839
REMARK 3 L13: -0.8131 L23: -0.1559
REMARK 3 S TENSOR
REMARK 3 S11: 0.3490 S12: -0.6403 S13: 0.3330
REMARK 3 S21: 0.9727 S22: -0.6362 S23: -0.3516
REMARK 3 S31: -0.5419 S32: -0.5557 S33: 0.6330
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3482 5.9374 29.4495
REMARK 3 T TENSOR
REMARK 3 T11: 0.4142 T22: 0.4067
REMARK 3 T33: 0.4287 T12: 0.0322
REMARK 3 T13: -0.0671 T23: 0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 4.6325 L22: 3.2143
REMARK 3 L33: 2.2853 L12: -2.2519
REMARK 3 L13: -1.3580 L23: 1.8060
REMARK 3 S TENSOR
REMARK 3 S11: -0.1349 S12: -0.3309 S13: 0.3486
REMARK 3 S21: 0.1557 S22: 0.2957 S23: -0.2928
REMARK 3 S31: 0.0671 S32: 0.1208 S33: -0.1292
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3041 0.6275 20.2638
REMARK 3 T TENSOR
REMARK 3 T11: 0.3592 T22: 0.3474
REMARK 3 T33: 0.3536 T12: -0.0087
REMARK 3 T13: -0.0400 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 3.7916 L22: 2.7890
REMARK 3 L33: 2.1648 L12: -1.6499
REMARK 3 L13: -0.4970 L23: 0.6359
REMARK 3 S TENSOR
REMARK 3 S11: 0.0362 S12: 0.3773 S13: -0.0775
REMARK 3 S21: -0.1840 S22: 0.0490 S23: 0.0708
REMARK 3 S31: 0.1269 S32: -0.0500 S33: -0.0744
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 167 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3412 -16.2792 10.1160
REMARK 3 T TENSOR
REMARK 3 T11: 0.6580 T22: 0.8826
REMARK 3 T33: 1.2521 T12: 0.0583
REMARK 3 T13: 0.1844 T23: -0.1034
REMARK 3 L TENSOR
REMARK 3 L11: 3.9102 L22: 1.8584
REMARK 3 L33: 3.3016 L12: -1.2526
REMARK 3 L13: -0.6032 L23: 2.3484
REMARK 3 S TENSOR
REMARK 3 S11: -0.3017 S12: 0.2725 S13: 0.4198
REMARK 3 S21: 0.1163 S22: 0.9267 S23: -0.2225
REMARK 3 S31: -1.0952 S32: 0.6898 S33: -0.8433
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 184 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1312 -29.1903 3.4345
REMARK 3 T TENSOR
REMARK 3 T11: 0.4882 T22: 0.4245
REMARK 3 T33: 0.3237 T12: 0.0237
REMARK 3 T13: 0.0279 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 3.7817 L22: 3.4427
REMARK 3 L33: 4.5881 L12: -2.2541
REMARK 3 L13: -1.3797 L23: -0.0681
REMARK 3 S TENSOR
REMARK 3 S11: -0.0849 S12: 0.0950 S13: 0.1932
REMARK 3 S21: -0.0049 S22: 0.1420 S23: -0.2919
REMARK 3 S31: 0.5469 S32: 0.3776 S33: -0.0699
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 9EDJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1000290253.
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 : 5.5
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 : 16871
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 46.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.81700
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 (%): 41.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 UL 13.9 MG/ML FPHE (10 MM HEPES PH
REMARK 280 7.6, 100 MM NACL) WERE MIXED WITH 0.15 UL OF RESERVOIR SOLUTION.
REMARK 280 SITTING DROP RESERVOIR CONTAINED 25 UL OF 200 MM POTASSIUM
REMARK 280 THIOCYANATE, 100 MM SODIUM ACETATE PH 5.5 AND 25% PEG 2000 MME.
REMARK 280 CRYSTAL WAS FROZEN IN A SOLUTION OF ~25% ETHYLENE GLYCOL, 75%
REMARK 280 RESERVOIR., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
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 49.39700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.22250
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.39700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.22250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 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 GLY B -2
REMARK 465 PRO B -1
REMARK 465 GLY B 0
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 LEU A 6 -159.26 -101.74
REMARK 500 PRO A 96 156.99 -49.39
REMARK 500 SER A 103 -130.42 55.89
REMARK 500 GLU A 127 75.99 35.86
REMARK 500 LYS A 175 -72.48 -55.76
REMARK 500 GLU A 201 -65.09 -139.44
REMARK 500 ASN A 209 75.01 -69.63
REMARK 500 SER A 230 34.72 -94.08
REMARK 500 PRO A 254 156.68 -49.71
REMARK 500 SER B 103 -137.49 56.75
REMARK 500 ASP B 182 -84.13 -91.63
REMARK 500 GLU B 201 -54.71 -121.15
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9EDJ A 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 9EDJ B 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
SEQADV 9EDJ GLY A -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EDJ PRO A -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EDJ GLY A 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EDJ GLY B -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EDJ PRO B -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 9EDJ 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
FORMUL 3 HOH *24(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 ASN A 168 1 33
HELIX 7 AA7 ALA A 170 GLN A 179 1 10
HELIX 8 AA8 THR A 183 GLU A 201 1 19
HELIX 9 AA9 GLU A 201 HIS A 207 1 7
HELIX 10 AB1 THR A 211 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 SER B 178 1 9
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 THR B 216 5 6
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 TRP B 275 1 13
SHEET 1 AA1 3 GLU A 2 GLU A 5 0
SHEET 2 AA1 3 ALA A 9 VAL A 16 -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 GLU A 5 0
SHEET 2 AA2 8 ALA A 9 VAL A 16 -1 O LEU A 11 N LEU A 4
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 PHE A 24 O VAL A 49
SHEET 5 AA2 8 VAL A 97 SER A 102 1 O TYR A 98 N ILE A 23
SHEET 6 AA2 8 VAL A 120 HIS A 126 1 O HIS A 126 N GLY A 101
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 GLY B 101 O HIS B 126
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 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 THR A 223
SHEET 4 AA4 8 VAL B 97 SER B 102 1 N GLY B 101 O HIS B 126
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 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
CRYST1 52.315 98.794 102.445 90.00 90.00 90.00 P 2 21 21 8
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 0.019115 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010122 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009761 0.00000
TER 2201 GLY A 276
TER 4391 GLY B 276
MASTER 331 0 0 27 27 0 0 6 4413 2 0 44
END |