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HEADER HYDROLASE 02-APR-12 4EHB
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE D129S
TITLE 2 MUTATION BOUND TO EPOXYHEXANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CIF;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208963;
SOURCE 4 STRAIN: PA14;
SOURCE 5 GENE: PA14_26090;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMQ70
KEYWDS ALPHA BETA HYDROLASE, EPOXIDE HYDROLASE, SECRETED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.HVORECNY,C.D.BAHL,D.R.MADDEN
REVDAT 1 07-AUG-13 4EHB 0
JRNL AUTH C.D.BAHL,K.L.HVORECNY,D.R.MADDEN
JRNL TITL CIF EPOXIDE HYDROLASE ENZYME ACTIVITY IS REQUIRED FOR CFTR
JRNL TITL 2 INHIBITORY ACTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 99957
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4990
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 43.4416 - 5.7442 0.97 3221 246 0.2258 0.2064
REMARK 3 2 5.7442 - 4.5609 0.98 3398 0 0.1524 10000000.0000
REMARK 3 3 4.5609 - 3.9849 0.98 3146 251 0.1420 0.1484
REMARK 3 4 3.9849 - 3.6207 0.98 3129 256 0.1682 0.1881
REMARK 3 5 3.6207 - 3.3613 0.98 3383 0 0.1693 10000000.0000
REMARK 3 6 3.3613 - 3.1632 0.97 3105 248 0.1698 0.1871
REMARK 3 7 3.1632 - 3.0048 0.98 3148 250 0.1741 0.2100
REMARK 3 8 3.0048 - 2.8740 0.98 3344 0 0.1763 10000000.0000
REMARK 3 9 2.8740 - 2.7634 0.97 3105 248 0.1731 0.2129
REMARK 3 10 2.7634 - 2.6681 0.97 3086 249 0.1729 0.2099
REMARK 3 11 2.6681 - 2.5847 0.97 3379 0 0.1741 10000000.0000
REMARK 3 12 2.5847 - 2.5108 0.97 3088 251 0.1707 0.2212
REMARK 3 13 2.5108 - 2.4447 0.97 3069 249 0.1773 0.2305
REMARK 3 14 2.4447 - 2.3851 0.97 3335 0 0.1757 10000000.0000
REMARK 3 15 2.3851 - 2.3308 0.97 3048 248 0.1830 0.2410
REMARK 3 16 2.3308 - 2.2812 0.97 3057 250 0.1720 0.2369
REMARK 3 17 2.2812 - 2.2356 0.97 3345 0 0.1803 10000000.0000
REMARK 3 18 2.2356 - 2.1934 0.97 3065 253 0.1773 0.2558
REMARK 3 19 2.1934 - 2.1543 0.97 3056 252 0.1741 0.2186
REMARK 3 20 2.1543 - 2.1177 0.96 3325 0 0.1737 10000000.0000
REMARK 3 21 2.1177 - 2.0836 0.96 3036 251 0.1743 0.2249
REMARK 3 22 2.0836 - 2.0515 0.97 3071 248 0.1807 0.2257
REMARK 3 23 2.0515 - 2.0214 0.96 3280 0 0.1862 10000000.0000
REMARK 3 24 2.0214 - 1.9929 0.97 3041 252 0.1850 0.2561
REMARK 3 25 1.9929 - 1.9659 0.96 3057 247 0.1936 0.2582
REMARK 3 26 1.9659 - 1.9404 0.96 3264 0 0.1927 10000000.0000
REMARK 3 27 1.9404 - 1.9162 0.96 3065 244 0.2115 0.2669
REMARK 3 28 1.9162 - 1.8931 0.96 3053 248 0.2282 0.3008
REMARK 3 29 1.8931 - 1.8711 0.96 3250 0 0.2340 10000000.0000
REMARK 3 30 1.8711 - 1.8500 0.96 3018 249 0.2377 0.2971
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 38.40
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.820
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) : -5.81840
REMARK 3 B22 (A**2) : -2.36180
REMARK 3 B33 (A**2) : 8.18020
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.24770
REMARK 3 B23 (A**2) : 0.00000
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 : 0.006 10002
REMARK 3 ANGLE : 1.036 13600
REMARK 3 CHIRALITY : 0.075 1397
REMARK 3 PLANARITY : 0.005 1794
REMARK 3 DIHEDRAL : 16.263 3710
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 25:319)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9805 12.1571 -27.0419
REMARK 3 T TENSOR
REMARK 3 T11: 0.0502 T22: 0.0493
REMARK 3 T33: 0.0291 T12: -0.0075
REMARK 3 T13: -0.0028 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.1867 L22: 0.1354
REMARK 3 L33: 0.1715 L12: -0.0235
REMARK 3 L13: 0.0748 L23: -0.0205
REMARK 3 S TENSOR
REMARK 3 S11: 0.0177 S12: 0.0229 S13: -0.0405
REMARK 3 S21: -0.0028 S22: -0.0211 S23: -0.0143
REMARK 3 S31: 0.0320 S32: 0.0317 S33: 0.0016
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain B and resid 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7884 51.8044 -15.4811
REMARK 3 T TENSOR
REMARK 3 T11: 0.0561 T22: 0.0544
REMARK 3 T33: 0.0680 T12: -0.0530
REMARK 3 T13: -0.0185 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.0401 L22: 0.0623
REMARK 3 L33: 0.0397 L12: 0.0216
REMARK 3 L13: -0.0034 L23: 0.0144
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: -0.0079 S13: 0.0450
REMARK 3 S21: 0.0050 S22: 0.0065 S23: -0.0137
REMARK 3 S31: -0.0155 S32: 0.0046 S33: 0.0061
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain C and resid 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8606 44.8752 -27.0292
REMARK 3 T TENSOR
REMARK 3 T11: 0.0460 T22: 0.0396
REMARK 3 T33: 0.0441 T12: -0.0096
REMARK 3 T13: 0.0117 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.1058 L22: 0.1500
REMARK 3 L33: 0.1282 L12: 0.0132
REMARK 3 L13: 0.0171 L23: 0.0106
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: 0.0106 S13: 0.0479
REMARK 3 S21: -0.0040 S22: -0.0282 S23: 0.0333
REMARK 3 S31: -0.0222 S32: -0.0084 S33: 0.0064
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain D and resid 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7774 5.3269 -15.5223
REMARK 3 T TENSOR
REMARK 3 T11: 0.0570 T22: 0.0537
REMARK 3 T33: 0.0314 T12: -0.0478
REMARK 3 T13: 0.0079 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.0723 L22: 0.0870
REMARK 3 L33: 0.0248 L12: 0.0271
REMARK 3 L13: -0.0279 L23: -0.0240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: -0.0079 S13: -0.0067
REMARK 3 S21: 0.0034 S22: 0.0104 S23: 0.0319
REMARK 3 S31: 0.0091 S32: 0.0003 S33: 0.0309
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 4EHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT MONOCHROMATOR
REMARK 200 OPTICS : TOROIDAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS-PACKAGE
REMARK 200 DATA SCALING SOFTWARE : XDS-PACKAGE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99966
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 43.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39200
REMARK 200 FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PDB ENTRY 3KD2 CHAIN A
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 8000, 0.125M CALCIUM CHLORIDE,
REMARK 280 0.1M SODIUM ACETATE, 0.02M EPOXYHEXANE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 83.71500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.96000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.71500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.96000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D 691 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 594 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 612 LIES ON A SPECIAL POSITION.
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 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
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 129 -135.28 59.52
REMARK 500 GLU A 153 60.09 60.24
REMARK 500 ALA A 154 145.07 174.90
REMARK 500 THR B 99 -65.41 -91.14
REMARK 500 SER B 129 -137.45 56.31
REMARK 500 ALA B 154 141.98 175.47
REMARK 500 CYS B 303 56.16 -142.27
REMARK 500 HIS B 320 109.12 175.27
REMARK 500 THR C 99 -67.23 -90.42
REMARK 500 SER C 129 -135.07 58.08
REMARK 500 ALA C 154 147.01 179.63
REMARK 500 CYS C 303 54.38 -141.36
REMARK 500 THR D 99 -65.86 -98.37
REMARK 500 SER D 129 -135.57 57.06
REMARK 500 ALA D 154 145.31 169.14
REMARK 500 TRP D 298 59.31 -94.07
REMARK 500 CYS D 303 59.54 -142.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0PZ A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0PZ B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0PZ C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0PZ D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 SAME PROTEIN, BUT WITH THE WILD TYPE SEQUENCE
REMARK 900 RELATED ID: 3KDA RELATED DB: PDB
REMARK 900 RELATED ID: 3PI6 RELATED DB: PDB
REMARK 900 RELATED ID: 4DLN RELATED DB: PDB
REMARK 900 RELATED ID: 4DM7 RELATED DB: PDB
REMARK 900 RELATED ID: 4DMC RELATED DB: PDB
REMARK 900 RELATED ID: 4DMF RELATED DB: PDB
REMARK 900 RELATED ID: 4DMH RELATED DB: PDB
REMARK 900 RELATED ID: 4DNF RELATED DB: PDB
REMARK 900 RELATED ID: 4DNO RELATED DB: PDB
DBREF 4EHB A 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4EHB B 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4EHB C 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4EHB D 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
SEQADV 4EHB SER A 129 UNP Q02P97 ASP 129 ENGINEERED MUTATION
SEQADV 4EHB HIS A 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS A 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS A 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS A 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS A 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS A 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB SER B 129 UNP Q02P97 ASP 129 ENGINEERED MUTATION
SEQADV 4EHB HIS B 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS B 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS B 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS B 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS B 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS B 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB SER C 129 UNP Q02P97 ASP 129 ENGINEERED MUTATION
SEQADV 4EHB HIS C 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS C 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS C 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS C 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS C 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS C 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB SER D 129 UNP Q02P97 ASP 129 ENGINEERED MUTATION
SEQADV 4EHB HIS D 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS D 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS D 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS D 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS D 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4EHB HIS D 325 UNP Q02P97 EXPRESSION TAG
SEQRES 1 A 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 A 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 A 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 A 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 A 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 A 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 A 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 A 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 A 301 SER ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 A 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 A 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 A 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 A 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 A 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 A 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 A 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 A 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 A 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 A 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 A 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 A 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 A 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 A 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 A 301 HIS HIS
SEQRES 1 B 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 B 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 B 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 B 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 B 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 B 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 B 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 B 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 B 301 SER ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 B 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 B 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 B 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 B 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 B 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 B 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 B 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 B 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 B 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 B 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 B 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 B 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 B 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 B 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 B 301 HIS HIS
SEQRES 1 C 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 C 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 C 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 C 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 C 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 C 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 C 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 C 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 C 301 SER ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 C 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 C 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 C 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 C 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 C 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 C 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 C 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 C 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 C 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 C 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 C 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 C 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 C 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 C 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 C 301 HIS HIS
SEQRES 1 D 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 D 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 D 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 D 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 D 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 D 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 D 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 D 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 D 301 SER ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 D 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 D 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 D 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 D 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 D 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 D 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 D 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 D 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 D 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 D 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 D 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 D 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 D 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 D 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 D 301 HIS HIS
HET 0PZ A 401 7
HET 0PZ B 401 7
HET 0PZ C 401 7
HET 0PZ D 401 7
HETNAM 0PZ (2R)-2-BUTYLOXIRANE
FORMUL 5 0PZ 4(C6 H12 O)
FORMUL 9 HOH *1059(H2 O)
HELIX 1 1 THR A 66 HIS A 71 5 6
HELIX 2 2 LEU A 73 ALA A 78 1 6
HELIX 3 3 SER A 102 SER A 118 1 17
HELIX 4 4 SER A 129 ASN A 134 1 6
HELIX 5 5 THR A 135 ASN A 142 1 8
HELIX 6 6 ASP A 158 PHE A 164 5 7
HELIX 7 7 TRP A 176 ALA A 183 1 8
HELIX 8 8 ARG A 186 ALA A 193 1 8
HELIX 9 9 LYS A 195 HIS A 207 1 13
HELIX 10 10 ASN A 210 PHE A 214 5 5
HELIX 11 11 SER A 215 ALA A 227 1 13
HELIX 12 12 LYS A 228 ALA A 241 1 14
HELIX 13 13 ALA A 241 ALA A 253 1 13
HELIX 14 14 THR A 274 ALA A 284 1 11
HELIX 15 15 TRP A 298 CYS A 303 1 6
HELIX 16 16 CYS A 303 SER A 316 1 14
HELIX 17 17 THR B 66 HIS B 71 5 6
HELIX 18 18 GLN B 72 ALA B 78 1 7
HELIX 19 19 SER B 102 SER B 118 1 17
HELIX 20 20 SER B 129 ASN B 134 1 6
HELIX 21 21 THR B 135 ASN B 142 1 8
HELIX 22 22 ASP B 158 PHE B 164 5 7
HELIX 23 23 TRP B 176 ALA B 183 1 8
HELIX 24 24 ARG B 186 ALA B 193 1 8
HELIX 25 25 LYS B 195 HIS B 207 1 13
HELIX 26 26 SER B 215 LYS B 228 1 14
HELIX 27 27 LYS B 228 ALA B 241 1 14
HELIX 28 28 ALA B 241 ALA B 253 1 13
HELIX 29 29 THR B 274 ALA B 284 1 11
HELIX 30 30 TRP B 298 CYS B 303 1 6
HELIX 31 31 CYS B 303 SER B 316 1 14
HELIX 32 32 THR C 66 HIS C 71 5 6
HELIX 33 33 GLN C 72 ALA C 78 1 7
HELIX 34 34 SER C 102 SER C 118 1 17
HELIX 35 35 SER C 129 ASN C 134 1 6
HELIX 36 36 THR C 135 ASN C 142 1 8
HELIX 37 37 ASP C 158 PHE C 164 5 7
HELIX 38 38 TRP C 176 ALA C 183 1 8
HELIX 39 39 ARG C 186 ALA C 193 1 8
HELIX 40 40 LYS C 195 HIS C 207 1 13
HELIX 41 41 ASN C 210 PHE C 214 5 5
HELIX 42 42 SER C 215 ALA C 227 1 13
HELIX 43 43 LYS C 228 ALA C 241 1 14
HELIX 44 44 ALA C 241 ALA C 253 1 13
HELIX 45 45 THR C 274 LYS C 281 1 8
HELIX 46 46 TRP C 298 CYS C 303 1 6
HELIX 47 47 CYS C 303 SER C 316 1 14
HELIX 48 48 THR D 66 HIS D 71 5 6
HELIX 49 49 GLN D 72 ALA D 78 1 7
HELIX 50 50 SER D 102 SER D 118 1 17
HELIX 51 51 SER D 129 ASN D 134 1 6
HELIX 52 52 THR D 135 ASN D 142 1 8
HELIX 53 53 ASP D 158 PHE D 164 5 7
HELIX 54 54 TRP D 176 ALA D 183 1 8
HELIX 55 55 ARG D 186 ALA D 193 1 8
HELIX 56 56 LYS D 195 HIS D 207 1 13
HELIX 57 57 SER D 215 ALA D 227 1 13
HELIX 58 58 LYS D 228 ALA D 241 1 14
HELIX 59 59 ALA D 241 ALA D 253 1 13
HELIX 60 60 THR D 274 ALA D 282 1 9
HELIX 61 61 TRP D 298 CYS D 303 1 6
HELIX 62 62 CYS D 303 ARG D 317 1 15
SHEET 1 A 8 GLU A 35 VAL A 41 0
SHEET 2 A 8 VAL A 44 GLY A 52 -1 O VAL A 44 N VAL A 41
SHEET 3 A 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 A 8 LEU A 56 VAL A 60 1 N VAL A 57 O THR A 82
SHEET 5 A 8 PHE A 123 HIS A 128 1 O VAL A 126 N VAL A 60
SHEET 6 A 8 ILE A 146 MET A 152 1 O ALA A 147 N PHE A 123
SHEET 7 A 8 THR A 261 GLY A 266 1 O MET A 262 N TYR A 151
SHEET 8 A 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 B 2 PHE A 167 THR A 168 0
SHEET 2 B 2 GLY A 171 GLU A 172 -1 O GLY A 171 N THR A 168
SHEET 1 C 8 GLU B 35 VAL B 41 0
SHEET 2 C 8 VAL B 44 GLY B 51 -1 O TYR B 48 N ALA B 37
SHEET 3 C 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 C 8 LEU B 56 VAL B 60 1 N LEU B 59 O ILE B 84
SHEET 5 C 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 C 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 C 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 C 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 D 2 PHE B 167 THR B 168 0
SHEET 2 D 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 E 8 GLU C 35 VAL C 41 0
SHEET 2 E 8 VAL C 44 GLY C 52 -1 O LEU C 46 N ARG C 39
SHEET 3 E 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 E 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 E 8 PHE C 123 HIS C 128 1 O VAL C 126 N VAL C 60
SHEET 6 E 8 ILE C 146 MET C 152 1 O ALA C 147 N PHE C 123
SHEET 7 E 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 E 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 F 2 PHE C 167 THR C 168 0
SHEET 2 F 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SHEET 1 G 8 PHE D 34 VAL D 41 0
SHEET 2 G 8 VAL D 44 GLY D 52 -1 O LYS D 50 N GLU D 35
SHEET 3 G 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 G 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 G 8 PHE D 123 HIS D 128 1 O VAL D 126 N VAL D 60
SHEET 6 G 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 G 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 G 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 H 2 PHE D 167 THR D 168 0
SHEET 2 H 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SSBOND 1 CYS A 295 CYS A 303 1555 1555 2.02
SSBOND 2 CYS B 295 CYS B 303 1555 1555 2.01
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.02
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.01
SITE 1 AC1 8 SER A 129 TRP A 133 HIS A 177 PHE A 178
SITE 2 AC1 8 HIS A 207 TYR A 239 HIS A 297 HOH A 544
SITE 1 AC2 4 SER B 129 HIS B 177 PHE B 178 TYR B 239
SITE 1 AC3 5 SER C 129 HIS C 177 HIS C 207 TYR C 239
SITE 2 AC3 5 HIS C 297
SITE 1 AC4 7 SER D 129 ALA D 154 HIS D 177 PHE D 178
SITE 2 AC4 7 TYR D 239 MET D 272 HIS D 297
CRYST1 167.430 83.920 88.740 90.00 100.31 90.00 C 1 2 1 16
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 0.005973 0.000000 0.001087 0.00000
SCALE2 0.000000 0.011916 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011454 0.00000
TER 2403 ARG A 319
TER 4787 HIS B 321
TER 7208 HIS C 321
TER 9655 HIS D 321
MASTER 394 0 4 62 40 0 7 610551 4 36 96
END |