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HEADER HYDROLASE/HYDROLASE INHIBITOR 14-OCT-16 5TNS
TITLE CRYSTAL STRUCTURE OF THE D129S MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING 1,2-EPOXYCYCLOHEXANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 3 CHAIN: A, B, C, D;
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-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.HVORECNY,D.R.MADDEN
REVDAT 1 11-OCT-17 5TNS 0
JRNL AUTH K.L.HVORECNY,C.D.BAHL,S.KITAMURA,K.S.S.LEE,B.D.HAMMOCK,
JRNL AUTH 2 C.MORISSEAU,D.R.MADDEN
JRNL TITL ACTIVE-SITE FLEXIBILITY AND SUBSTRATE SPECIFICITY IN A
JRNL TITL 2 BACTERIAL VIRULENCE FACTOR: CRYSTALLOGRAPHIC SNAPSHOTS OF AN
JRNL TITL 3 EPOXIDE HYDROLASE.
JRNL REF STRUCTURE V. 25 697 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28392259
JRNL DOI 10.1016/J.STR.2017.03.002
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 118202
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5930
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 39.2429 - 5.4330 0.98 3838 301 0.1575 0.1758
REMARK 3 2 5.4330 - 4.3141 0.98 4038 0 0.1235 0.0000
REMARK 3 3 4.3141 - 3.7693 0.98 3734 296 0.1314 0.1502
REMARK 3 4 3.7693 - 3.4249 0.98 3722 302 0.1376 0.1601
REMARK 3 5 3.4249 - 3.1795 0.98 4003 0 0.1453 0.0000
REMARK 3 6 3.1795 - 2.9921 0.98 3680 298 0.1555 0.1795
REMARK 3 7 2.9921 - 2.8423 0.97 3678 297 0.1605 0.1857
REMARK 3 8 2.8423 - 2.7186 0.97 3988 0 0.1504 0.0000
REMARK 3 9 2.7186 - 2.6140 0.97 3654 298 0.1527 0.1757
REMARK 3 10 2.6140 - 2.5238 0.97 3660 297 0.1566 0.1833
REMARK 3 11 2.5238 - 2.4449 0.97 3982 0 0.1571 0.0000
REMARK 3 12 2.4449 - 2.3750 0.97 3631 296 0.1560 0.1887
REMARK 3 13 2.3750 - 2.3125 0.97 3655 296 0.1538 0.1975
REMARK 3 14 2.3125 - 2.2561 0.97 3936 0 0.1484 0.0000
REMARK 3 15 2.2561 - 2.2048 0.97 3628 301 0.1512 0.1795
REMARK 3 16 2.2048 - 2.1579 0.97 3627 296 0.1542 0.1932
REMARK 3 17 2.1579 - 2.1147 0.96 3926 0 0.1504 0.0000
REMARK 3 18 2.1147 - 2.0748 0.96 3588 292 0.1548 0.2065
REMARK 3 19 2.0748 - 2.0378 0.96 3598 296 0.1604 0.1888
REMARK 3 20 2.0378 - 2.0032 0.96 3958 0 0.1588 0.0000
REMARK 3 21 2.0032 - 1.9709 0.96 3620 293 0.1553 0.1884
REMARK 3 22 1.9709 - 1.9406 0.96 3574 292 0.1564 0.2100
REMARK 3 23 1.9406 - 1.9121 0.96 3867 0 0.1545 0.0000
REMARK 3 24 1.9121 - 1.8851 0.96 3628 291 0.1634 0.1749
REMARK 3 25 1.8851 - 1.8596 0.96 3568 296 0.1713 0.2371
REMARK 3 26 1.8596 - 1.8355 0.96 3910 0 0.1773 0.0000
REMARK 3 27 1.8355 - 1.8126 0.95 3603 296 0.1829 0.2541
REMARK 3 28 1.8126 - 1.7907 0.95 3551 298 0.1747 0.2251
REMARK 3 29 1.7907 - 1.7699 0.95 3801 0 0.1837 0.0000
REMARK 3 30 1.7699 - 1.7500 0.95 3626 298 0.1831 0.2102
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.970
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 : 0.006 9902
REMARK 3 ANGLE : 0.811 13476
REMARK 3 CHIRALITY : 0.052 1390
REMARK 3 PLANARITY : 0.006 1774
REMARK 3 DIHEDRAL : 15.009 5882
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 25:321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8763 12.1064 -27.3289
REMARK 3 T TENSOR
REMARK 3 T11: 0.0917 T22: 0.1069
REMARK 3 T33: 0.0685 T12: -0.0063
REMARK 3 T13: 0.0022 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.5831 L22: 0.6451
REMARK 3 L33: 0.7362 L12: -0.0680
REMARK 3 L13: 0.0626 L23: -0.0737
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: 0.0857 S13: -0.0651
REMARK 3 S21: -0.0666 S22: -0.0389 S23: -0.0306
REMARK 3 S31: 0.0914 S32: 0.0717 S33: 0.0245
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN B AND RESID 25:321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9378 51.8388 -15.5645
REMARK 3 T TENSOR
REMARK 3 T11: 0.0992 T22: 0.0889
REMARK 3 T33: 0.1206 T12: -0.0251
REMARK 3 T13: -0.0274 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.1095 L22: 1.0813
REMARK 3 L33: 0.4722 L12: 0.4046
REMARK 3 L13: -0.0462 L23: 0.1235
REMARK 3 S TENSOR
REMARK 3 S11: -0.0216 S12: -0.0070 S13: 0.1680
REMARK 3 S21: 0.0241 S22: 0.0216 S23: -0.0301
REMARK 3 S31: -0.0712 S32: 0.0242 S33: 0.0009
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN C AND RESID 25:318 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0155 44.9655 -26.9559
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.0897
REMARK 3 T33: 0.1070 T12: -0.0114
REMARK 3 T13: 0.0026 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.4947 L22: 0.8992
REMARK 3 L33: 0.6888 L12: -0.0402
REMARK 3 L13: 0.0691 L23: -0.0411
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: 0.0142 S13: 0.0882
REMARK 3 S21: -0.0364 S22: -0.0398 S23: 0.0856
REMARK 3 S31: -0.0842 S32: -0.0291 S33: 0.0228
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN D AND RESID 25:321 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8015 5.4861 -15.6309
REMARK 3 T TENSOR
REMARK 3 T11: 0.0926 T22: 0.0898
REMARK 3 T33: 0.0626 T12: -0.0274
REMARK 3 T13: 0.0041 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.9812 L22: 0.8152
REMARK 3 L33: 0.4811 L12: 0.2649
REMARK 3 L13: -0.0257 L23: -0.1464
REMARK 3 S TENSOR
REMARK 3 S11: 0.0228 S12: -0.0292 S13: -0.0508
REMARK 3 S21: 0.0123 S22: -0.0001 S23: 0.0868
REMARK 3 S31: 0.0379 S32: -0.0067 S33: -0.0202
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 5TNS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000223435.
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 : 5.0
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS DEC 6, 2010
REMARK 200 DATA SCALING SOFTWARE : XDS DEC 6, 2010
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120855
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 46.158
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.750
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.79
REMARK 200 R MERGE FOR SHELL (I) : 0.45600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.240
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.10_2155: ???
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
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 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 83.97200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.84500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.97200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.84500
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: 2750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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: 20800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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 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 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 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: 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 C 451 O HOH C 491 1.84
REMARK 500 O HOH B 600 O HOH B 604 1.89
REMARK 500 O HOH B 520 O HOH B 601 2.02
REMARK 500 OE2 GLU C 189 O HOH C 401 2.14
REMARK 500 O HOH C 636 O HOH C 642 2.18
REMARK 500 OE2 GLU B 35 O HOH B 401 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 129 -136.58 62.90
REMARK 500 ALA A 154 146.63 -179.99
REMARK 500 TRP A 298 65.77 -100.14
REMARK 500 CYS A 303 55.50 -141.26
REMARK 500 THR B 99 -67.25 -92.86
REMARK 500 SER B 129 -136.53 57.72
REMARK 500 ALA B 154 146.06 -178.90
REMARK 500 ASP B 185 18.64 57.16
REMARK 500 SER C 129 -137.21 61.58
REMARK 500 ALA C 154 149.43 179.55
REMARK 500 TRP C 298 66.79 -100.03
REMARK 500 CYS C 303 55.17 -142.05
REMARK 500 THR D 99 -68.10 -92.16
REMARK 500 SER D 129 -138.25 58.69
REMARK 500 ALA D 154 147.18 -179.92
REMARK 500 CYS D 303 51.17 -141.41
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 7EX D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 RELATED ID: 4DMC RELATED DB: PDB
REMARK 900 RELATED ID: 5TNJ RELATED DB: PDB
DBREF1 5TNS A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNS A A0A0M3KL26 1 301
DBREF1 5TNS B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNS B A0A0M3KL26 1 301
DBREF1 5TNS C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNS C A0A0M3KL26 1 301
DBREF1 5TNS D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNS D A0A0M3KL26 1 301
SEQADV 5TNS SER A 129 UNP A0A0M3KL2 ASP 105 ENGINEERED MUTATION
SEQADV 5TNS SER B 129 UNP A0A0M3KL2 ASP 105 ENGINEERED MUTATION
SEQADV 5TNS SER C 129 UNP A0A0M3KL2 ASP 105 ENGINEERED MUTATION
SEQADV 5TNS SER D 129 UNP A0A0M3KL2 ASP 105 ENGINEERED MUTATION
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 7EX D 401 7
HETNAM 7EX (1R,6S)-7-OXABICYCLO[4.1.0]HEPTANE
FORMUL 5 7EX C6 H10 O
FORMUL 6 HOH *1083(H2 O)
HELIX 1 AA1 THR A 66 HIS A 71 5 6
HELIX 2 AA2 LEU A 73 ALA A 78 1 6
HELIX 3 AA3 SER A 102 SER A 118 1 17
HELIX 4 AA4 SER A 129 ASN A 134 1 6
HELIX 5 AA5 THR A 135 ASN A 142 1 8
HELIX 6 AA6 ASP A 158 PHE A 164 5 7
HELIX 7 AA7 TRP A 176 ALA A 183 1 8
HELIX 8 AA8 ARG A 186 ALA A 193 1 8
HELIX 9 AA9 LYS A 195 HIS A 207 1 13
HELIX 10 AB1 ASN A 210 PHE A 214 5 5
HELIX 11 AB2 SER A 215 ALA A 227 1 13
HELIX 12 AB3 LYS A 228 ALA A 241 1 14
HELIX 13 AB4 ALA A 241 ALA A 253 1 13
HELIX 14 AB5 THR A 274 ALA A 284 1 11
HELIX 15 AB6 TRP A 298 CYS A 303 1 6
HELIX 16 AB7 CYS A 303 SER A 316 1 14
HELIX 17 AB8 THR B 66 HIS B 71 5 6
HELIX 18 AB9 GLN B 72 ALA B 78 1 7
HELIX 19 AC1 SER B 102 SER B 118 1 17
HELIX 20 AC2 SER B 129 ASN B 134 1 6
HELIX 21 AC3 THR B 135 ASN B 142 1 8
HELIX 22 AC4 ASP B 158 PHE B 164 5 7
HELIX 23 AC5 TRP B 176 ALA B 183 1 8
HELIX 24 AC6 ARG B 186 ALA B 193 1 8
HELIX 25 AC7 LYS B 195 HIS B 207 1 13
HELIX 26 AC8 SER B 215 LYS B 228 1 14
HELIX 27 AC9 LYS B 228 ALA B 241 1 14
HELIX 28 AD1 ALA B 241 ALA B 253 1 13
HELIX 29 AD2 THR B 274 ALA B 282 1 9
HELIX 30 AD3 TRP B 298 CYS B 303 1 6
HELIX 31 AD4 CYS B 303 ARG B 317 1 15
HELIX 32 AD5 THR C 66 HIS C 71 5 6
HELIX 33 AD6 LEU C 73 ALA C 78 1 6
HELIX 34 AD7 SER C 102 SER C 118 1 17
HELIX 35 AD8 SER C 129 ASN C 134 1 6
HELIX 36 AD9 THR C 135 ASN C 142 1 8
HELIX 37 AE1 ASP C 158 PHE C 164 5 7
HELIX 38 AE2 VAL C 175 ALA C 183 1 9
HELIX 39 AE3 ARG C 186 ALA C 193 1 8
HELIX 40 AE4 LYS C 195 HIS C 207 1 13
HELIX 41 AE5 ASN C 210 PHE C 214 5 5
HELIX 42 AE6 SER C 215 ALA C 227 1 13
HELIX 43 AE7 LYS C 228 ALA C 241 1 14
HELIX 44 AE8 ALA C 241 ALA C 253 1 13
HELIX 45 AE9 THR C 274 ALA C 282 1 9
HELIX 46 AF1 TRP C 298 CYS C 303 1 6
HELIX 47 AF2 CYS C 303 SER C 316 1 14
HELIX 48 AF3 THR D 66 HIS D 71 5 6
HELIX 49 AF4 GLN D 72 ALA D 78 1 7
HELIX 50 AF5 SER D 102 SER D 118 1 17
HELIX 51 AF6 SER D 129 ASN D 134 1 6
HELIX 52 AF7 THR D 135 ASN D 142 1 8
HELIX 53 AF8 ASP D 158 PHE D 164 5 7
HELIX 54 AF9 TRP D 176 ALA D 183 1 8
HELIX 55 AG1 ARG D 186 ALA D 193 1 8
HELIX 56 AG2 LYS D 195 HIS D 207 1 13
HELIX 57 AG3 ASN D 210 PHE D 214 5 5
HELIX 58 AG4 SER D 215 ALA D 227 1 13
HELIX 59 AG5 LYS D 228 ALA D 241 1 14
HELIX 60 AG6 ALA D 241 ALA D 253 1 13
HELIX 61 AG7 THR D 274 ALA D 284 1 11
HELIX 62 AG8 TRP D 298 CYS D 303 1 6
HELIX 63 AG9 CYS D 303 ARG D 317 1 15
SHEET 1 AA1 8 GLU A 35 VAL A 41 0
SHEET 2 AA1 8 VAL A 44 GLY A 52 -1 O VAL A 44 N VAL A 41
SHEET 3 AA1 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 AA1 8 LEU A 56 VAL A 60 1 N VAL A 57 O THR A 82
SHEET 5 AA1 8 PHE A 123 HIS A 128 1 O VAL A 126 N VAL A 60
SHEET 6 AA1 8 ILE A 146 MET A 152 1 O VAL A 150 N LEU A 125
SHEET 7 AA1 8 THR A 261 GLY A 266 1 O MET A 262 N TYR A 151
SHEET 8 AA1 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 AA2 2 PHE A 167 THR A 168 0
SHEET 2 AA2 2 GLY A 171 GLU A 172 -1 O GLY A 171 N THR A 168
SHEET 1 AA3 8 GLU B 35 VAL B 41 0
SHEET 2 AA3 8 VAL B 44 GLY B 52 -1 O LEU B 46 N ARG B 39
SHEET 3 AA3 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 AA3 8 LEU B 56 VAL B 60 1 N VAL B 57 O THR B 82
SHEET 5 AA3 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 AA3 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 AA3 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 AA3 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 AA4 2 PHE B 167 THR B 168 0
SHEET 2 AA4 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 AA5 8 GLU C 35 VAL C 41 0
SHEET 2 AA5 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 AA5 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA5 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA5 8 PHE C 123 HIS C 128 1 O ASP C 124 N LEU C 56
SHEET 6 AA5 8 ILE C 146 MET C 152 1 O VAL C 150 N ALA C 127
SHEET 7 AA5 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA5 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA6 2 PHE C 167 THR C 168 0
SHEET 2 AA6 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SHEET 1 AA7 8 GLU D 35 VAL D 41 0
SHEET 2 AA7 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA7 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA7 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 AA7 8 PHE D 123 HIS D 128 1 O ASP D 124 N LEU D 56
SHEET 6 AA7 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA7 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA7 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA8 2 PHE D 167 THR D 168 0
SHEET 2 AA8 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 1.99
SSBOND 2 CYS B 295 CYS B 303 1555 1555 2.00
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.00
SSBOND 4 CYS D 295 CYS D 303 1555 1555 1.99
SITE 1 AC1 7 PHE D 63 SER D 129 ALA D 154 HIS D 177
SITE 2 AC1 7 PHE D 178 TYR D 239 HIS D 297
CRYST1 167.944 83.690 89.175 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 0.005954 0.000000 0.001083 0.00000
SCALE2 0.000000 0.011949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011398 0.00000
TER 2404 HIS A 321
TER 4791 HIS B 321
TER 7162 GLY C 318
TER 9581 HIS D 321
MASTER 377 0 1 63 40 0 2 610543 4 15 96
END |