| 5tnm-pdb | HEADER HYDROLASE 14-OCT-16 5TNM
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED (R)-1,2-EPOXYOCTANE HYDROLYSIS
TITLE 3 INTERMEDIATE
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
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.HVORECNY,D.R.MADDEN
REVDAT 1 11-OCT-17 5TNM 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. 1.70 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 134236
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 6720
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 19.8157 - 5.2505 1.00 4256 336 0.1528 0.1934
REMARK 3 2 5.2505 - 4.1803 1.00 4549 0 0.1216 0.0000
REMARK 3 3 4.1803 - 3.6556 1.00 4157 336 0.1297 0.1321
REMARK 3 4 3.6556 - 3.3231 1.00 4179 336 0.1339 0.1307
REMARK 3 5 3.3231 - 3.0859 1.00 4495 0 0.1458 0.0000
REMARK 3 6 3.0859 - 2.9045 1.00 4135 336 0.1582 0.1741
REMARK 3 7 2.9045 - 2.7595 1.00 4145 336 0.1546 0.1839
REMARK 3 8 2.7595 - 2.6396 1.00 4488 0 0.1508 0.0000
REMARK 3 9 2.6396 - 2.5382 1.00 4133 336 0.1557 0.1851
REMARK 3 10 2.5382 - 2.4508 1.00 4160 336 0.1597 0.1730
REMARK 3 11 2.4508 - 2.3743 1.00 4458 0 0.1508 0.0000
REMARK 3 12 2.3743 - 2.3065 1.00 4150 336 0.1456 0.1721
REMARK 3 13 2.3065 - 2.2459 1.00 4110 336 0.1499 0.1808
REMARK 3 14 2.2459 - 2.1912 1.00 4467 0 0.1495 0.0000
REMARK 3 15 2.1912 - 2.1414 1.00 4119 336 0.1506 0.1838
REMARK 3 16 2.1414 - 2.0959 1.00 4139 336 0.1406 0.1674
REMARK 3 17 2.0959 - 2.0540 1.00 4462 0 0.1429 0.0000
REMARK 3 18 2.0540 - 2.0153 1.00 4144 336 0.1462 0.1786
REMARK 3 19 2.0153 - 1.9793 1.00 4117 336 0.1457 0.1790
REMARK 3 20 1.9793 - 1.9458 1.00 4432 0 0.1429 0.0000
REMARK 3 21 1.9458 - 1.9145 1.00 4112 336 0.1382 0.1639
REMARK 3 22 1.9145 - 1.8850 1.00 4130 336 0.1529 0.1940
REMARK 3 23 1.8850 - 1.8573 1.00 4473 0 0.1600 0.0000
REMARK 3 24 1.8573 - 1.8312 1.00 4135 336 0.1517 0.1854
REMARK 3 25 1.8312 - 1.8064 1.00 4101 336 0.1569 0.2001
REMARK 3 26 1.8064 - 1.7830 1.00 4487 0 0.1577 0.0000
REMARK 3 27 1.7830 - 1.7607 1.00 4122 336 0.1618 0.2049
REMARK 3 28 1.7607 - 1.7395 1.00 4090 336 0.1671 0.2018
REMARK 3 29 1.7395 - 1.7193 1.00 4454 0 0.1737 0.0000
REMARK 3 30 1.7193 - 1.7000 1.00 4117 336 0.1851 0.2369
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.100
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 10007
REMARK 3 ANGLE : 0.808 13623
REMARK 3 CHIRALITY : 0.053 1407
REMARK 3 PLANARITY : 0.006 1794
REMARK 3 DIHEDRAL : 14.860 5938
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 25:320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9683 12.1771 27.3541
REMARK 3 T TENSOR
REMARK 3 T11: 0.0904 T22: 0.1002
REMARK 3 T33: 0.0838 T12: 0.0062
REMARK 3 T13: 0.0037 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.8766 L22: 0.8145
REMARK 3 L33: 0.8017 L12: 0.1087
REMARK 3 L13: 0.1491 L23: -0.0147
REMARK 3 S TENSOR
REMARK 3 S11: 0.0154 S12: -0.0991 S13: -0.0825
REMARK 3 S21: 0.0666 S22: -0.0253 S23: 0.0284
REMARK 3 S31: 0.0900 S32: -0.0251 S33: 0.0113
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN B AND RESID 25:320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0045 51.3258 15.5025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.0885
REMARK 3 T33: 0.1296 T12: 0.0142
REMARK 3 T13: -0.0223 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.1795 L22: 1.3755
REMARK 3 L33: 0.5877 L12: -0.4225
REMARK 3 L13: 0.0311 L23: -0.1055
REMARK 3 S TENSOR
REMARK 3 S11: -0.0231 S12: 0.0131 S13: 0.1442
REMARK 3 S21: -0.0481 S22: 0.0142 S23: 0.0693
REMARK 3 S31: -0.0812 S32: -0.0359 S33: 0.0055
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN C AND RESID 25:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7970 44.0469 27.0051
REMARK 3 T TENSOR
REMARK 3 T11: 0.0985 T22: 0.0996
REMARK 3 T33: 0.1355 T12: 0.0081
REMARK 3 T13: 0.0049 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.7415 L22: 1.0135
REMARK 3 L33: 0.7922 L12: 0.0730
REMARK 3 L13: 0.0092 L23: 0.0985
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: -0.0420 S13: 0.1190
REMARK 3 S21: 0.0451 S22: -0.0326 S23: -0.0806
REMARK 3 S31: -0.0943 S32: 0.0191 S33: 0.0143
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN D AND RESID 25:320 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7196 4.8997 15.7640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0921 T22: 0.0972
REMARK 3 T33: 0.0789 T12: 0.0239
REMARK 3 T13: 0.0074 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.0569 L22: 1.1879
REMARK 3 L33: 0.5410 L12: -0.3160
REMARK 3 L13: -0.0552 L23: 0.1487
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: 0.0576 S13: -0.0490
REMARK 3 S21: -0.0252 S22: -0.0117 S23: -0.1236
REMARK 3 S31: 0.0462 S32: 0.0234 S33: -0.0064
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 5TNM 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_1000221257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-15
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 : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.078
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS NOV 3, 2014
REMARK 200 DATA SCALING SOFTWARE : XDS NOV 3, 2014
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134244
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 19.814
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.230
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.8900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.25
REMARK 200 R MERGE FOR SHELL (I) : 0.33100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.85
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 84.14850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.02150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.14850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.02150
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: 2780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20930 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: 2770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20800 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 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 A 720 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 726 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 715 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 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 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
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 HIS D 321
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 D 640 O HOH D 706 2.17
REMARK 500 O ALA B 25 O HOH B 501 2.17
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 A 129 -132.14 62.61
REMARK 500 ALA A 154 145.61 -175.61
REMARK 500 CYS A 303 54.18 -142.05
REMARK 500 THR B 99 -69.40 -93.43
REMARK 500 ASP B 129 -131.15 58.34
REMARK 500 ALA B 154 147.20 -173.40
REMARK 500 ASP C 129 -131.80 61.77
REMARK 500 ALA C 154 147.42 -174.46
REMARK 500 CYS C 303 55.84 -141.44
REMARK 500 THR D 99 -67.16 -93.22
REMARK 500 ASP D 129 -131.02 58.98
REMARK 500 ALA D 154 143.93 -174.51
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 B 713 DISTANCE = 5.94 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7F2 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7F2 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7F2 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7F2 D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TND RELATED DB: PDB
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: 5TNK RELATED DB: PDB
REMARK 900 RELATED ID: 5TNL RELATED DB: PDB
REMARK 900 RELATED ID: 5TNN RELATED DB: PDB
REMARK 900 RELATED ID: 5TNR RELATED DB: PDB
REMARK 900 RELATED ID: 5TNS RELATED DB: PDB
DBREF1 5TNM A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNM A A0A0M3KL26 1 301
DBREF1 5TNM B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNM B A0A0M3KL26 1 301
DBREF1 5TNM C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNM C A0A0M3KL26 1 301
DBREF1 5TNM D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNM D A0A0M3KL26 1 301
SEQADV 5TNM GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNM GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNM GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNM GLN D 153 UNP A0A0M3KL2 GLU 129 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 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
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
HET 7F2 A 401 9
HET 7F2 B 401 9
HET 7F2 C 401 9
HET 7F2 D 401 9
HETNAM 7F2 (2R)-OCTANE-1,2-DIOL
FORMUL 5 7F2 4(C8 H18 O2)
FORMUL 9 HOH *972(H2 O)
HELIX 1 AA1 THR A 66 HIS A 71 5 6
HELIX 2 AA2 GLN A 72 ALA A 78 1 7
HELIX 3 AA3 SER A 102 SER A 118 1 17
HELIX 4 AA4 ASP 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 LYS A 281 1 8
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 ASP 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 ASN B 210 PHE B 214 5 5
HELIX 27 AC9 SER B 215 LYS B 228 1 14
HELIX 28 AD1 LYS B 228 ALA B 241 1 14
HELIX 29 AD2 ALA B 241 ALA B 253 1 13
HELIX 30 AD3 THR B 274 ALA B 284 1 11
HELIX 31 AD4 TRP B 298 CYS B 303 1 6
HELIX 32 AD5 CYS B 303 ARG B 317 1 15
HELIX 33 AD6 THR C 66 HIS C 71 5 6
HELIX 34 AD7 GLN C 72 ALA C 78 1 7
HELIX 35 AD8 SER C 102 SER C 118 1 17
HELIX 36 AD9 ASP C 129 ASN C 134 1 6
HELIX 37 AE1 THR C 135 ASN C 142 1 8
HELIX 38 AE2 ASP C 158 PHE C 164 5 7
HELIX 39 AE3 VAL C 175 ALA C 183 1 9
HELIX 40 AE4 ARG C 186 ALA C 193 1 8
HELIX 41 AE5 LYS C 195 HIS C 207 1 13
HELIX 42 AE6 ASN C 210 PHE C 214 5 5
HELIX 43 AE7 SER C 215 ALA C 227 1 13
HELIX 44 AE8 LYS C 228 ALA C 241 1 14
HELIX 45 AE9 ALA C 241 ALA C 253 1 13
HELIX 46 AF1 THR C 274 ALA C 284 1 11
HELIX 47 AF2 TRP C 298 CYS C 303 1 6
HELIX 48 AF3 CYS C 303 SER C 316 1 14
HELIX 49 AF4 THR D 66 HIS D 71 5 6
HELIX 50 AF5 GLN D 72 ALA D 78 1 7
HELIX 51 AF6 SER D 102 SER D 118 1 17
HELIX 52 AF7 ASP D 129 ASN D 134 1 6
HELIX 53 AF8 THR D 135 ASN D 142 1 8
HELIX 54 AF9 ASP D 158 PHE D 164 5 7
HELIX 55 AG1 TRP D 176 ALA D 183 1 8
HELIX 56 AG2 ARG D 186 ALA D 193 1 8
HELIX 57 AG3 LYS D 195 HIS D 207 1 13
HELIX 58 AG4 ASN D 210 PHE D 214 5 5
HELIX 59 AG5 SER D 215 ALA D 227 1 13
HELIX 60 AG6 LYS D 228 ALA D 241 1 14
HELIX 61 AG7 ALA D 241 ALA D 253 1 13
HELIX 62 AG8 THR D 274 ALA D 282 1 9
HELIX 63 AG9 TRP D 298 CYS D 303 1 6
HELIX 64 AH1 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 ALA A 147 N PHE A 123
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 VAL B 44 N VAL B 41
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 ASP B 124 N LEU B 56
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 VAL C 126 N VAL C 60
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 2.00
SSBOND 2 CYS B 295 CYS B 303 1555 1555 2.00
SSBOND 3 CYS C 295 CYS C 303 1555 1555 1.99
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.01
LINK OD1 ASP A 129 C 7F2 A 401 1555 1555 1.40
LINK OD1 ASP B 129 C 7F2 B 401 1555 1555 1.41
LINK OD1 ASP C 129 C 7F2 C 401 1555 1555 1.40
LINK OD1 ASP D 129 C 7F2 D 401 1555 1555 1.41
SITE 1 AC1 8 LEU A 174 HIS A 177 PHE A 178 HIS A 207
SITE 2 AC1 8 TYR A 239 GLY A 270 MET A 272 HIS A 297
SITE 1 AC2 6 LEU B 174 VAL B 175 HIS B 177 PHE B 178
SITE 2 AC2 6 TYR B 239 MET B 272
SITE 1 AC3 8 GLN C 153 VAL C 175 HIS C 177 PHE C 178
SITE 2 AC3 8 HIS C 207 TYR C 239 GLY C 270 HIS C 297
SITE 1 AC4 5 VAL D 175 HIS D 177 PHE D 178 TYR D 239
SITE 2 AC4 5 MET D 272
CRYST1 168.297 84.043 89.253 90.00 100.39 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 0.005942 0.000000 0.001089 0.00000
SCALE2 0.000000 0.011899 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011391 0.00000
TER 2451 HIS A 320
TER 4845 HIS B 320
TER 7266 ARG C 317
TER 9652 HIS D 320
MASTER 414 0 4 64 40 0 8 610435 4 48 96
END
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