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HEADER HYDROLASE 07-FEB-12 4DMK
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE Y239F
TITLE 2 MUTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CIF (UNP RESIDUES 25-319);
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: 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;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMQ70
KEYWDS ALPHA BETA HYDROLASE, EPOXIDE HYDROLASE, SECRETED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.BAHL,D.R.MADDEN
REVDAT 1 07-AUG-13 4DMK 0
JRNL AUTH C.D.BAHL,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. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 190239
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 9495
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 46.2074 - 4.6593 0.99 6144 480 0.1586 0.1395
REMARK 3 2 4.6593 - 3.6987 0.99 6520 0 0.1335 10000000.0000
REMARK 3 3 3.6987 - 3.2313 0.99 6001 489 0.1445 0.1595
REMARK 3 4 3.2313 - 2.9359 0.99 5989 489 0.1627 0.1868
REMARK 3 5 2.9359 - 2.7255 0.99 6478 0 0.1594 10000000.0000
REMARK 3 6 2.7255 - 2.5648 0.98 5934 475 0.1618 0.1755
REMARK 3 7 2.5648 - 2.4364 0.98 5942 483 0.1592 0.1779
REMARK 3 8 2.4364 - 2.3304 0.98 6414 0 0.1559 10000000.0000
REMARK 3 9 2.3304 - 2.2406 0.98 5877 476 0.1495 0.1694
REMARK 3 10 2.2406 - 2.1633 0.98 5933 476 0.1520 0.1725
REMARK 3 11 2.1633 - 2.0957 0.98 6358 0 0.1491 10000000.0000
REMARK 3 12 2.0957 - 2.0358 0.98 5913 475 0.1541 0.1799
REMARK 3 13 2.0358 - 1.9822 0.97 5880 477 0.1540 0.1808
REMARK 3 14 1.9822 - 1.9338 0.97 6300 0 0.1546 10000000.0000
REMARK 3 15 1.9338 - 1.8899 0.97 5852 476 0.1552 0.1767
REMARK 3 16 1.8899 - 1.8496 0.97 5843 472 0.1564 0.1850
REMARK 3 17 1.8496 - 1.8126 0.97 6341 0 0.1550 10000000.0000
REMARK 3 18 1.8126 - 1.7784 0.97 5794 473 0.1526 0.1937
REMARK 3 19 1.7784 - 1.7467 0.97 5798 479 0.1607 0.2020
REMARK 3 20 1.7467 - 1.7171 0.97 6319 0 0.1586 10000000.0000
REMARK 3 21 1.7171 - 1.6894 0.96 5819 470 0.1558 0.1804
REMARK 3 22 1.6894 - 1.6634 0.96 5783 473 0.1502 0.1808
REMARK 3 23 1.6634 - 1.6389 0.97 6285 0 0.1560 10000000.0000
REMARK 3 24 1.6389 - 1.6158 0.97 5773 456 0.1591 0.1849
REMARK 3 25 1.6158 - 1.5940 0.96 5758 467 0.1612 0.2011
REMARK 3 26 1.5940 - 1.5733 0.96 6233 0 0.1650 10000000.0000
REMARK 3 27 1.5733 - 1.5536 0.96 5786 466 0.1697 0.1975
REMARK 3 28 1.5536 - 1.5349 0.96 5748 474 0.1766 0.2093
REMARK 3 29 1.5349 - 1.5170 0.96 6197 0 0.1817 10000000.0000
REMARK 3 30 1.5170 - 1.5000 0.96 5732 469 0.1894 0.2212
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 : 0.35
REMARK 3 B_SOL : 33.64
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.280
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) : -1.05150
REMARK 3 B22 (A**2) : -0.74060
REMARK 3 B33 (A**2) : 1.79210
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.05110
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 9897
REMARK 3 ANGLE : 1.069 13436
REMARK 3 CHIRALITY : 0.078 1378
REMARK 3 PLANARITY : 0.005 1770
REMARK 3 DIHEDRAL : 12.756 3632
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): 5.7138 29.9198 26.9823
REMARK 3 T TENSOR
REMARK 3 T11: 0.0344 T22: 0.0302
REMARK 3 T33: 0.0441 T12: 0.0050
REMARK 3 T13: -0.0022 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.3200 L22: 0.4569
REMARK 3 L33: 0.3883 L12: 0.0156
REMARK 3 L13: 0.0379 L23: 0.0130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: -0.0221 S13: 0.0533
REMARK 3 S21: 0.0334 S22: -0.0088 S23: -0.0560
REMARK 3 S31: -0.0499 S32: 0.0057 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain B and resid 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7027 -9.7387 15.6766
REMARK 3 T TENSOR
REMARK 3 T11: 0.0370 T22: 0.0410
REMARK 3 T33: 0.0246 T12: 0.0169
REMARK 3 T13: 0.0049 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.5841 L22: 0.4971
REMARK 3 L33: 0.2522 L12: -0.1250
REMARK 3 L13: 0.0194 L23: 0.1265
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: 0.0151 S13: -0.0295
REMARK 3 S21: -0.0098 S22: -0.0022 S23: -0.0633
REMARK 3 S31: 0.0258 S32: 0.0102 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain C and resid 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9860 -2.9665 27.2378
REMARK 3 T TENSOR
REMARK 3 T11: 0.0361 T22: 0.0375
REMARK 3 T33: 0.0176 T12: 0.0034
REMARK 3 T13: 0.0101 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.3954 L22: 0.3607
REMARK 3 L33: 0.3863 L12: -0.0021
REMARK 3 L13: 0.0452 L23: 0.0885
REMARK 3 S TENSOR
REMARK 3 S11: -0.0041 S12: -0.0535 S13: -0.0380
REMARK 3 S21: 0.0425 S22: -0.0102 S23: 0.0367
REMARK 3 S31: 0.0572 S32: -0.0176 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain D and resid 25:320)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0606 36.6377 15.7294
REMARK 3 T TENSOR
REMARK 3 T11: 0.0316 T22: 0.0254
REMARK 3 T33: 0.0494 T12: 0.0124
REMARK 3 T13: -0.0158 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.5987 L22: 0.5250
REMARK 3 L33: 0.2289 L12: -0.1914
REMARK 3 L13: -0.0340 L23: -0.0891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.0095 S13: 0.1003
REMARK 3 S21: -0.0285 S22: 0.0029 S23: 0.0056
REMARK 3 S31: -0.0326 S32: -0.0083 S33: 0.0000
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 4DMK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-09
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) : 0.9770
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 : 190252
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 46.186
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30200
REMARK 200 FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: CHAIN A OF PDB ENTRY 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15.5% PEG 8000, 0.125M CALCIUM
REMARK 280 CHLORIDE, 0.1M SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 84.33900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.01600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.33900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.01600
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: 3330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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: 3350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20780 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 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 B 698 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 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 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 319 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG B 319 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG C 319 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG D 319 CB CG CD NE CZ NH1 NH2
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 -131.10 61.35
REMARK 500 ALA A 154 148.16 178.03
REMARK 500 CYS A 303 55.45 -141.34
REMARK 500 THR B 99 -67.26 -90.49
REMARK 500 ASP B 129 -137.49 60.86
REMARK 500 ALA B 154 145.07 -179.12
REMARK 500 ASP B 185 18.84 58.90
REMARK 500 CYS B 303 54.65 -142.36
REMARK 500 ASP C 129 -129.88 61.67
REMARK 500 ALA C 154 148.55 175.10
REMARK 500 CYS C 303 55.83 -142.19
REMARK 500 THR D 99 -69.04 -91.16
REMARK 500 ASP D 129 -134.82 58.38
REMARK 500 ALA D 154 144.98 -179.96
REMARK 500 ASP D 185 18.89 59.64
REMARK 500 CYS D 303 54.60 -140.32
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 GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL 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 4DMK A 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DMK B 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DMK C 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DMK D 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
SEQADV 4DMK PHE A 239 UNP Q02P97 TYR 239 ENGINEERED MUTATION
SEQADV 4DMK HIS A 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS A 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS A 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS A 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS A 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS A 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK PHE B 239 UNP Q02P97 TYR 239 ENGINEERED MUTATION
SEQADV 4DMK HIS B 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS B 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS B 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS B 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS B 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS B 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK PHE C 239 UNP Q02P97 TYR 239 ENGINEERED MUTATION
SEQADV 4DMK HIS C 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS C 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS C 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS C 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS C 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS C 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK PHE D 239 UNP Q02P97 TYR 239 ENGINEERED MUTATION
SEQADV 4DMK HIS D 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS D 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS D 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS D 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK HIS D 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DMK 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 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 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 PHE 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 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 PHE 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 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 PHE 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 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 PHE 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 GOL A 401 6
HET GOL B 401 6
HET GOL C 401 6
HET GOL D 401 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *1250(H2 O)
HELIX 1 1 THR A 66 HIS A 71 5 6
HELIX 2 2 GLN A 72 ALA A 78 1 7
HELIX 3 3 SER A 102 SER A 118 1 17
HELIX 4 4 ASP 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 ASP 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 ASN B 210 PHE B 214 5 5
HELIX 27 27 SER B 215 ALA B 227 1 13
HELIX 28 28 LYS B 228 ALA B 241 1 14
HELIX 29 29 ALA B 241 ALA B 253 1 13
HELIX 30 30 THR B 274 ALA B 284 1 11
HELIX 31 31 TRP B 298 CYS B 303 1 6
HELIX 32 32 CYS B 303 ARG B 317 1 15
HELIX 33 33 THR C 66 HIS C 71 5 6
HELIX 34 34 LEU C 73 ALA C 78 1 6
HELIX 35 35 SER C 102 SER C 118 1 17
HELIX 36 36 ASP C 129 ASN C 134 1 6
HELIX 37 37 THR C 135 ASN C 142 1 8
HELIX 38 38 ASP C 158 PHE C 164 5 7
HELIX 39 39 TRP C 176 ALA C 183 1 8
HELIX 40 40 ARG C 186 ALA C 193 1 8
HELIX 41 41 LYS C 195 HIS C 207 1 13
HELIX 42 42 ASN C 210 PHE C 214 5 5
HELIX 43 43 SER C 215 ALA C 227 1 13
HELIX 44 44 LYS C 228 ALA C 241 1 14
HELIX 45 45 ALA C 241 ALA C 253 1 13
HELIX 46 46 THR C 274 ALA C 284 1 11
HELIX 47 47 TRP C 298 CYS C 303 1 6
HELIX 48 48 CYS C 303 SER C 316 1 14
HELIX 49 49 THR D 66 HIS D 71 5 6
HELIX 50 50 GLN D 72 ALA D 78 1 7
HELIX 51 51 SER D 102 SER D 118 1 17
HELIX 52 52 ASP D 129 ASN D 134 1 6
HELIX 53 53 THR D 135 ASN D 142 1 8
HELIX 54 54 ASP D 158 PHE D 164 5 7
HELIX 55 55 TRP D 176 ALA D 183 1 8
HELIX 56 56 ARG D 186 ALA D 193 1 8
HELIX 57 57 LYS D 195 HIS D 207 1 13
HELIX 58 58 ASN D 210 PHE D 214 5 5
HELIX 59 59 SER D 215 LYS D 228 1 14
HELIX 60 60 LYS D 228 ALA D 241 1 14
HELIX 61 61 ALA D 241 ALA D 253 1 13
HELIX 62 62 THR D 274 ALA D 284 1 11
HELIX 63 63 TRP D 298 CYS D 303 1 6
HELIX 64 64 CYS D 303 SER D 316 1 14
SHEET 1 A 8 GLU A 35 VAL A 41 0
SHEET 2 A 8 VAL A 44 GLY A 52 -1 O LEU A 46 N ARG A 39
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 LEU A 59 O ILE A 84
SHEET 5 A 8 PHE A 123 HIS A 128 1 O ASP A 124 N LEU A 56
SHEET 6 A 8 ILE A 146 MET A 152 1 O VAL A 150 N LEU A 125
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 52 -1 O LEU B 46 N ARG B 39
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 VAL B 57 O THR B 82
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 LYS C 50 N GLU C 35
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 ASP C 124 N LEU C 56
SHEET 6 E 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
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 GLU D 35 VAL D 41 0
SHEET 2 G 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
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 ASP D 124 N LEU D 56
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 2.01
SSBOND 2 CYS B 295 CYS B 303 1555 1555 2.01
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.01
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.01
SITE 1 AC1 11 ASP A 129 GLU A 153 ALA A 154 PRO A 155
SITE 2 AC1 11 VAL A 175 PHE A 178 HIS A 207 HIS A 297
SITE 3 AC1 11 HOH A 529 HOH A 653 HOH A 682
SITE 1 AC2 10 ASP B 129 GLU B 153 ALA B 154 HIS B 177
SITE 2 AC2 10 PHE B 178 PHE B 239 HIS B 297 HOH B 608
SITE 3 AC2 10 HOH B 792 HOH B 795
SITE 1 AC3 10 ASP C 129 GLU C 153 ALA C 154 PRO C 155
SITE 2 AC3 10 VAL C 175 HIS C 207 HIS C 297 HOH C 531
SITE 3 AC3 10 HOH C 646 HOH C 677
SITE 1 AC4 8 ASP D 129 GLU D 153 PRO D 155 HIS D 207
SITE 2 AC4 8 HIS D 297 HOH D 567 HOH D 664 HOH D 783
CRYST1 168.678 84.032 89.278 90.00 100.50 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 0.005928 0.000000 0.001099 0.00000
SCALE2 0.000000 0.011900 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011392 0.00000
TER 2408 HIS A 320
TER 4787 HIS B 321
TER 7195 HIS C 321
TER 9570 HIS D 320
MASTER 402 0 4 64 40 0 11 610742 4 32 96
END |