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HEADER HYDROLASE 14-OCT-16 5TNR
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED 16,17-EPDPE HYDROLYSIS INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 3 CHAIN: C, D, A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN UCBPP-PA14);
SOURCE 3 ORGANISM_TAXID: 208963;
SOURCE 4 STRAIN: UCBPP-PA14;
SOURCE 5 GENE: PA14_26090;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10
KEYWDS EPOXIDE HYDROLASE, HYDROXYALKYL-ENZYME INTERMEDIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.HVORECNY,D.R.MADDEN
REVDAT 1 18-OCT-17 5TNR 0
JRNL AUTH K.L.HVORECNY,D.R.MADDEN
JRNL TITL CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY
JRNL TITL 2 FACTOR CIF CONTAINING THE ADDUCTED 16,17-EPDPE HYDROLYSIS
JRNL TITL 3 INTERMEDIATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 115459
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 5759
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 46.7588 - 5.5899 0.99 3756 288 0.1638 0.1865
REMARK 3 2 5.5899 - 4.4380 1.00 3951 0 0.1306 0.0000
REMARK 3 3 4.4380 - 3.8773 1.00 3638 288 0.1307 0.1334
REMARK 3 4 3.8773 - 3.5229 1.00 3601 288 0.1393 0.1496
REMARK 3 5 3.5229 - 3.2705 1.00 3873 0 0.1418 0.0000
REMARK 3 6 3.2705 - 3.0777 1.00 3591 288 0.1567 0.1795
REMARK 3 7 3.0777 - 2.9236 1.00 3590 288 0.1652 0.1802
REMARK 3 8 2.9236 - 2.7964 1.00 3841 0 0.1575 0.0000
REMARK 3 9 2.7964 - 2.6887 1.00 3566 288 0.1565 0.1935
REMARK 3 10 2.6887 - 2.5960 1.00 3571 288 0.1618 0.1895
REMARK 3 11 2.5960 - 2.5148 1.00 3870 0 0.1553 0.0000
REMARK 3 12 2.5148 - 2.4429 0.99 3507 288 0.1595 0.1913
REMARK 3 13 2.4429 - 2.3786 1.00 3558 288 0.1619 0.1938
REMARK 3 14 2.3786 - 2.3206 1.00 3842 0 0.1563 0.0000
REMARK 3 15 2.3206 - 2.2678 1.00 3541 288 0.1612 0.1793
REMARK 3 16 2.2678 - 2.2196 1.00 3542 288 0.1572 0.1915
REMARK 3 17 2.2196 - 2.1752 1.00 3838 0 0.1672 0.0000
REMARK 3 18 2.1752 - 2.1341 1.00 3523 288 0.1627 0.2254
REMARK 3 19 2.1341 - 2.0960 1.00 3524 288 0.1650 0.2075
REMARK 3 20 2.0960 - 2.0605 0.99 3841 0 0.1764 0.0000
REMARK 3 21 2.0605 - 2.0272 0.99 3520 288 0.1809 0.2211
REMARK 3 22 2.0272 - 1.9960 1.00 3483 288 0.1865 0.2238
REMARK 3 23 1.9960 - 1.9667 1.00 3813 0 0.1860 0.0000
REMARK 3 24 1.9667 - 1.9390 1.00 3556 288 0.1950 0.2240
REMARK 3 25 1.9390 - 1.9128 1.00 3519 287 0.1932 0.2376
REMARK 3 26 1.9128 - 1.8879 1.00 3811 0 0.2070 0.0000
REMARK 3 27 1.8879 - 1.8643 1.00 3558 288 0.2133 0.2507
REMARK 3 28 1.8643 - 1.8419 1.00 3512 288 0.2209 0.2430
REMARK 3 29 1.8419 - 1.8205 1.00 3782 0 0.2260 0.0000
REMARK 3 30 1.8205 - 1.8000 1.00 3582 288 0.2486 0.2825
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.300
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 : 0.007 9853
REMARK 3 ANGLE : 0.856 13373
REMARK 3 CHIRALITY : 0.054 1370
REMARK 3 PLANARITY : 0.006 1773
REMARK 3 DIHEDRAL : 16.088 5803
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN C AND RESID 25:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0845 -5.9703 -27.0516
REMARK 3 T TENSOR
REMARK 3 T11: 0.0806 T22: 0.0836
REMARK 3 T33: 0.1022 T12: 0.0012
REMARK 3 T13: -0.0160 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.8333 L22: 0.8478
REMARK 3 L33: 0.7371 L12: 0.0076
REMARK 3 L13: 0.0613 L23: -0.0413
REMARK 3 S TENSOR
REMARK 3 S11: -0.0191 S12: 0.0447 S13: -0.0931
REMARK 3 S21: -0.0781 S22: 0.0249 S23: 0.1383
REMARK 3 S31: 0.0555 S32: -0.0997 S33: -0.0045
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN D AND RESID 25:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8969 -14.9980 -15.6400
REMARK 3 T TENSOR
REMARK 3 T11: 0.0827 T22: 0.0842
REMARK 3 T33: 0.0618 T12: 0.0218
REMARK 3 T13: -0.0049 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.7214 L22: 0.9625
REMARK 3 L33: 0.4032 L12: -0.2209
REMARK 3 L13: 0.0499 L23: -0.0698
REMARK 3 S TENSOR
REMARK 3 S11: -0.0122 S12: -0.0066 S13: -0.0531
REMARK 3 S21: 0.0365 S22: 0.0052 S23: -0.0586
REMARK 3 S31: -0.0019 S32: 0.0477 S33: 0.0082
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 25:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2749 21.9881 -27.3300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0849 T22: 0.0865
REMARK 3 T33: 0.0655 T12: 0.0003
REMARK 3 T13: 0.0156 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.6926 L22: 0.8363
REMARK 3 L33: 0.6800 L12: 0.0114
REMARK 3 L13: 0.0104 L23: 0.1584
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: 0.0830 S13: 0.0546
REMARK 3 S21: -0.1161 S22: 0.0172 S23: -0.0887
REMARK 3 S31: -0.0500 S32: 0.0988 S33: -0.0046
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND RESID 25:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.9907 30.8803 -15.6512
REMARK 3 T TENSOR
REMARK 3 T11: 0.0727 T22: 0.0877
REMARK 3 T33: 0.1046 T12: 0.0141
REMARK 3 T13: 0.0054 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 1.1611 L22: 1.1781
REMARK 3 L33: 0.5864 L12: -0.4043
REMARK 3 L13: -0.1289 L23: -0.0105
REMARK 3 S TENSOR
REMARK 3 S11: 0.0253 S12: -0.0147 S13: 0.0191
REMARK 3 S21: 0.0082 S22: -0.0232 S23: 0.1778
REMARK 3 S31: -0.0180 S32: -0.0944 S33: -0.0013
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 5TNR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000223249.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS MAY 1, 2016
REMARK 200 DATA SCALING SOFTWARE : XDS MAY 1, 2016
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115528
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.743
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.750
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.83
REMARK 200 R MERGE FOR SHELL (I) : 0.59700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.980
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.6.0
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PH5 CALCIUM CHLORIDE
REMARK 280 PEG 8000, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 88.21200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.21200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.92300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.45600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.92300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.45600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 88.21200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.92300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 84.45600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 88.21200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.92300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 84.45600
REMARK 290 SMTRY3 8 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: 2800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 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: 2800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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 501 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 801 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 831 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 GLY C 318
REMARK 465 ARG C 319
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 GLY D 318
REMARK 465 ARG D 319
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
REMARK 465 GLY A 318
REMARK 465 ARG A 319
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 GLY B 318
REMARK 465 ARG B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
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 D 509 O HOH D 772 1.81
REMARK 500 O HOH D 635 O HOH D 724 1.85
REMARK 500 O HOH D 713 O HOH D 768 1.89
REMARK 500 O HOH C 700 O HOH C 726 1.92
REMARK 500 O HOH D 621 O HOH D 777 2.00
REMARK 500 OE1 GLU A 172 O HOH A 501 2.02
REMARK 500 O HOH A 540 O HOH A 771 2.02
REMARK 500 O HOH C 756 O HOH C 760 2.03
REMARK 500 O HOH C 508 O HOH C 515 2.04
REMARK 500 O HOH A 748 O HOH A 776 2.04
REMARK 500 O HOH C 676 O HOH C 756 2.06
REMARK 500 O HOH A 676 O HOH A 756 2.07
REMARK 500 O HOH B 605 O HOH B 736 2.07
REMARK 500 O HOH A 570 O HOH A 655 2.09
REMARK 500 O HOH B 736 O HOH B 771 2.12
REMARK 500 O HOH A 508 O HOH A 765 2.13
REMARK 500 O HOH B 521 O HOH B 609 2.13
REMARK 500 O HOH C 647 O HOH C 769 2.14
REMARK 500 O HOH D 519 O HOH D 676 2.15
REMARK 500 O HOH D 756 O HOH D 810 2.16
REMARK 500 O HOH A 681 O HOH A 723 2.16
REMARK 500 O HOH B 717 O HOH B 743 2.16
REMARK 500 O HOH C 510 O HOH C 746 2.17
REMARK 500 O HOH D 700 O HOH D 789 2.18
REMARK 500 O HOH C 565 O HOH C 724 2.19
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 D 743 O HOH B 694 5545 2.10
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 ASP C 129 -131.30 60.46
REMARK 500 CYS C 303 57.93 -142.25
REMARK 500 THR D 99 -64.01 -97.14
REMARK 500 ASP D 129 -130.19 56.93
REMARK 500 ALA D 154 146.25 -171.32
REMARK 500 ASP D 184 -159.57 -84.90
REMARK 500 ASP A 129 -131.79 60.90
REMARK 500 CYS A 303 58.10 -140.43
REMARK 500 THR B 99 -62.93 -93.65
REMARK 500 ASP B 129 -132.04 57.89
REMARK 500 ALA B 154 142.83 -173.35
REMARK 500 CYS B 303 51.71 -141.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 795 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH D 829 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH D 830 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH D 831 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH D 832 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH D 833 DISTANCE = 6.75 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7EZ C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7EZ A 401 and ASP A
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7EZ B 401 and ASP B
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7EZ D 401 and ASP D
REMARK 800 129
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TNF RELATED DB: PDB
REMARK 900 RELATED ID: 5TNG RELATED DB: PDB
REMARK 900 RELATED ID: 5TNH RELATED DB: PDB
REMARK 900 RELATED ID: 5TNL RELATED DB: PDB
REMARK 900 RELATED ID: 5TNM RELATED DB: PDB
REMARK 900 RELATED ID: 5TNN RELATED DB: PDB
REMARK 900 RELATED ID: 5TNS RELATED DB: PDB
DBREF1 5TNR C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNR C A0A0M3KL26 1 301
DBREF1 5TNR D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNR D A0A0M3KL26 1 301
DBREF1 5TNR A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNR A A0A0M3KL26 1 301
DBREF1 5TNR B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNR B A0A0M3KL26 1 301
SEQADV 5TNR GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNR GLN D 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNR GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNR GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
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 ASP 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 GLN 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 ASP 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 GLN 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
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 ASP 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 GLN 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 ASP 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 GLN 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
HET 7EZ C 401 25
HET 7EZ D 401 25
HET 7EZ A 401 25
HET 7EZ B 401 25
HETNAM 7EZ (4Z,7Z,10Z,13Z,16R,17R,19Z)-16,17-DIHYDROXYDOCOSA-4,7,
HETNAM 2 7EZ 10,13,19-PENTAENOIC ACID
FORMUL 5 7EZ 4(C22 H34 O4)
FORMUL 9 HOH *1226(H2 O)
HELIX 1 AA1 THR C 66 HIS C 71 5 6
HELIX 2 AA2 GLN C 72 ALA C 78 1 7
HELIX 3 AA3 SER C 102 SER C 118 1 17
HELIX 4 AA4 ASP C 129 ASN C 134 1 6
HELIX 5 AA5 THR C 135 ASN C 142 1 8
HELIX 6 AA6 ASP C 158 ARG C 163 5 6
HELIX 7 AA7 TRP C 176 ALA C 183 1 8
HELIX 8 AA8 ARG C 186 ALA C 193 1 8
HELIX 9 AA9 LYS C 195 HIS C 207 1 13
HELIX 10 AB1 ASN C 210 PHE C 214 5 5
HELIX 11 AB2 SER C 215 ALA C 227 1 13
HELIX 12 AB3 LYS C 228 ALA C 241 1 14
HELIX 13 AB4 ALA C 241 ALA C 253 1 13
HELIX 14 AB5 THR C 274 ALA C 284 1 11
HELIX 15 AB6 TRP C 298 CYS C 303 1 6
HELIX 16 AB7 CYS C 303 SER C 316 1 14
HELIX 17 AB8 THR D 66 HIS D 71 5 6
HELIX 18 AB9 GLN D 72 ALA D 78 1 7
HELIX 19 AC1 SER D 102 SER D 118 1 17
HELIX 20 AC2 ASP D 129 ASN D 134 1 6
HELIX 21 AC3 THR D 135 ASN D 142 1 8
HELIX 22 AC4 ASP D 158 PHE D 164 5 7
HELIX 23 AC5 TRP D 176 ALA D 183 1 8
HELIX 24 AC6 ARG D 186 ALA D 193 1 8
HELIX 25 AC7 LYS D 195 HIS D 207 1 13
HELIX 26 AC8 ASN D 210 PHE D 214 5 5
HELIX 27 AC9 SER D 215 ALA D 227 1 13
HELIX 28 AD1 LYS D 228 ALA D 241 1 14
HELIX 29 AD2 ALA D 241 ALA D 253 1 13
HELIX 30 AD3 THR D 274 ALA D 284 1 11
HELIX 31 AD4 TRP D 298 CYS D 303 1 6
HELIX 32 AD5 CYS D 303 ARG D 317 1 15
HELIX 33 AD6 THR A 66 HIS A 71 5 6
HELIX 34 AD7 LEU A 73 ALA A 78 1 6
HELIX 35 AD8 SER A 102 SER A 118 1 17
HELIX 36 AD9 ASP A 129 ASN A 134 1 6
HELIX 37 AE1 THR A 135 ASN A 142 1 8
HELIX 38 AE2 ASP A 158 ARG A 163 5 6
HELIX 39 AE3 TRP A 176 ALA A 183 1 8
HELIX 40 AE4 ARG A 186 ALA A 193 1 8
HELIX 41 AE5 LYS A 195 HIS A 207 1 13
HELIX 42 AE6 ASN A 210 PHE A 214 5 5
HELIX 43 AE7 SER A 215 ALA A 227 1 13
HELIX 44 AE8 LYS A 228 ALA A 241 1 14
HELIX 45 AE9 ALA A 241 ALA A 253 1 13
HELIX 46 AF1 THR A 274 ALA A 282 1 9
HELIX 47 AF2 TRP A 298 CYS A 303 1 6
HELIX 48 AF3 CYS A 303 SER A 316 1 14
HELIX 49 AF4 THR B 66 HIS B 71 5 6
HELIX 50 AF5 GLN B 72 ALA B 78 1 7
HELIX 51 AF6 SER B 102 SER B 118 1 17
HELIX 52 AF7 ASP B 129 ASN B 134 1 6
HELIX 53 AF8 THR B 135 ASN B 142 1 8
HELIX 54 AF9 ASP B 158 PHE B 164 5 7
HELIX 55 AG1 TRP B 176 ALA B 183 1 8
HELIX 56 AG2 ARG B 186 ALA B 193 1 8
HELIX 57 AG3 LYS B 195 HIS B 207 1 13
HELIX 58 AG4 ASN B 210 PHE B 214 5 5
HELIX 59 AG5 SER B 215 ALA B 227 1 13
HELIX 60 AG6 LYS B 228 ALA B 241 1 14
HELIX 61 AG7 ALA B 241 ALA B 253 1 13
HELIX 62 AG8 THR B 274 ALA B 284 1 11
HELIX 63 AG9 TRP B 298 CYS B 303 1 6
HELIX 64 AH1 CYS B 303 ARG B 317 1 15
SHEET 1 AA1 8 GLU C 35 VAL C 41 0
SHEET 2 AA1 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 AA1 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA1 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA1 8 PHE C 123 HIS C 128 1 O VAL C 126 N VAL C 60
SHEET 6 AA1 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
SHEET 7 AA1 8 THR C 261 GLY C 266 1 O MET C 262 N LEU C 149
SHEET 8 AA1 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA2 8 GLU D 35 VAL D 41 0
SHEET 2 AA2 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA2 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA2 8 LEU D 56 VAL D 60 1 N LEU D 59 O ILE D 84
SHEET 5 AA2 8 PHE D 123 HIS D 128 1 O VAL D 126 N VAL D 60
SHEET 6 AA2 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA2 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA2 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA3 2 PHE D 167 THR D 168 0
SHEET 2 AA3 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SHEET 1 AA4 8 GLU A 35 VAL A 41 0
SHEET 2 AA4 8 VAL A 44 GLY A 52 -1 O VAL A 44 N VAL A 41
SHEET 3 AA4 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 AA4 8 LEU A 56 VAL A 60 1 N VAL A 57 O THR A 82
SHEET 5 AA4 8 PHE A 123 HIS A 128 1 O VAL A 126 N VAL A 60
SHEET 6 AA4 8 ILE A 146 MET A 152 1 O ALA A 147 N PHE A 123
SHEET 7 AA4 8 THR A 261 GLY A 266 1 O MET A 262 N TYR A 151
SHEET 8 AA4 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 AA5 8 PHE B 34 VAL B 41 0
SHEET 2 AA5 8 VAL B 44 GLY B 52 -1 O VAL B 44 N VAL B 41
SHEET 3 AA5 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 AA5 8 LEU B 56 VAL B 60 1 N VAL B 57 O THR B 82
SHEET 5 AA5 8 PHE B 123 HIS B 128 1 O ASP B 124 N MET B 58
SHEET 6 AA5 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 AA5 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 AA5 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 AA6 2 PHE B 167 THR B 168 0
SHEET 2 AA6 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SSBOND 1 CYS C 295 CYS C 303 1555 1555 2.00
SSBOND 2 CYS D 295 CYS D 303 1555 1555 1.98
SSBOND 3 CYS A 295 CYS A 303 1555 1555 2.00
SSBOND 4 CYS B 295 CYS B 303 1555 1555 2.00
LINK OD1 ASP C 129 C6 7EZ C 401 1555 1555 1.42
LINK OD1 ASP D 129 C6 7EZ D 401 1555 1555 1.42
LINK OD1 ASP A 129 C6 7EZ A 401 1555 1555 1.43
LINK OD1 ASP B 129 C6 7EZ B 401 1555 1555 1.42
SITE 1 AC1 11 ASP C 129 GLN C 153 PHE C 164 PRO C 165
SITE 2 AC1 11 HIS C 177 PHE C 178 HIS C 207 TYR C 239
SITE 3 AC1 11 MET C 272 HIS C 297 HOH C 535
SITE 1 AC2 15 PHE A 63 HIS A 128 ILE A 130 GLY A 131
SITE 2 AC2 15 ILE A 132 MET A 152 GLN A 153 ALA A 154
SITE 3 AC2 15 PHE A 164 HIS A 177 TYR A 239 MET A 272
SITE 4 AC2 15 HIS A 297 HOH A 652 HOH A 782
SITE 1 AC3 20 PHE B 63 HIS B 128 ILE B 130 GLY B 131
SITE 2 AC3 20 ILE B 132 MET B 152 GLN B 153 ALA B 154
SITE 3 AC3 20 VAL B 175 HIS B 177 PHE B 178 HIS B 207
SITE 4 AC3 20 TYR B 239 GLY B 270 MET B 272 HIS B 297
SITE 5 AC3 20 HOH B 550 HOH B 577 HOH B 594 HOH B 680
SITE 1 AC4 19 PHE D 63 HIS D 128 ILE D 130 GLY D 131
SITE 2 AC4 19 ILE D 132 MET D 152 GLN D 153 ALA D 154
SITE 3 AC4 19 VAL D 175 HIS D 177 PHE D 178 HIS D 207
SITE 4 AC4 19 TYR D 239 GLY D 270 MET D 272 HIS D 297
SITE 5 AC4 19 HOH D 564 HOH D 648 HOH D 702
CRYST1 83.846 168.912 176.424 90.00 90.00 90.00 C 2 2 21 32
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 0.011927 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005920 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005668 0.00000
TER 2371 ARG C 317
TER 4741 ARG D 317
TER 7094 ARG A 317
TER 9456 ARG B 317
MASTER 487 0 4 64 36 0 17 610678 4 112 96
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