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HEADER HYDROLASE 25-APR-12 4EUS
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF BOUND TO 1,2-
TITLE 2 HEXANEDIOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: 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 4EUS 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. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 149955
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 7520
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 46.4679 - 5.1247 0.99 4760 376 0.1858 0.1888
REMARK 3 2 5.1247 - 4.0684 1.00 5062 0 0.1263 0.0000
REMARK 3 3 4.0684 - 3.5544 1.00 4654 376 0.1509 0.1746
REMARK 3 4 3.5544 - 3.2295 1.00 4639 376 0.1567 0.1882
REMARK 3 5 3.2295 - 2.9980 1.00 5020 0 0.1718 0.0000
REMARK 3 6 2.9980 - 2.8213 1.00 4637 376 0.1712 0.1913
REMARK 3 7 2.8213 - 2.6800 1.00 4644 376 0.1655 0.1833
REMARK 3 8 2.6800 - 2.5634 1.00 4985 0 0.1638 0.0000
REMARK 3 9 2.5634 - 2.4647 1.00 4636 376 0.1653 0.1879
REMARK 3 10 2.4647 - 2.3797 1.00 4619 376 0.1672 0.1901
REMARK 3 11 2.3797 - 2.3052 1.00 4979 0 0.1615 0.0000
REMARK 3 12 2.3052 - 2.2394 1.00 4643 376 0.1733 0.2146
REMARK 3 13 2.2394 - 2.1804 1.00 4626 376 0.1654 0.2013
REMARK 3 14 2.1804 - 2.1272 1.00 5004 0 0.1618 0.0000
REMARK 3 15 2.1272 - 2.0788 1.00 4596 376 0.1638 0.1844
REMARK 3 16 2.0788 - 2.0346 1.00 4610 376 0.1643 0.1965
REMARK 3 17 2.0346 - 1.9939 1.00 4977 0 0.1639 0.0000
REMARK 3 18 1.9939 - 1.9563 1.00 4581 376 0.1654 0.1938
REMARK 3 19 1.9563 - 1.9213 1.00 4631 376 0.1638 0.1919
REMARK 3 20 1.9213 - 1.8888 1.00 4992 0 0.1748 0.0000
REMARK 3 21 1.8888 - 1.8583 1.00 4569 376 0.1864 0.2222
REMARK 3 22 1.8583 - 1.8297 1.00 4646 376 0.1909 0.2288
REMARK 3 23 1.8297 - 1.8028 1.00 4977 0 0.1863 0.0000
REMARK 3 24 1.8028 - 1.7774 1.00 4617 376 0.2026 0.2234
REMARK 3 25 1.7774 - 1.7534 1.00 4541 376 0.2020 0.2272
REMARK 3 26 1.7534 - 1.7306 1.00 4986 0 0.2138 0.0000
REMARK 3 27 1.7306 - 1.7090 1.00 4616 376 0.2247 0.2446
REMARK 3 28 1.7090 - 1.6884 1.00 4552 376 0.2343 0.2659
REMARK 3 29 1.6884 - 1.6688 1.00 5003 0 0.2347 0.0000
REMARK 3 30 1.6688 - 1.6500 1.00 4633 376 0.2458 0.2828
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 33.49
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.020
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) : -0.85060
REMARK 3 B22 (A**2) : -1.36040
REMARK 3 B33 (A**2) : 2.21090
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.40120
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 9776
REMARK 3 ANGLE : 1.061 13278
REMARK 3 CHIRALITY : 0.077 1371
REMARK 3 PLANARITY : 0.005 1750
REMARK 3 DIHEDRAL : 13.441 3570
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 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9278 12.3684 -27.4424
REMARK 3 T TENSOR
REMARK 3 T11: 0.0800 T22: 0.0814
REMARK 3 T33: 0.0608 T12: 0.0012
REMARK 3 T13: 0.0118 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.5993 L22: 0.6217
REMARK 3 L33: 0.6191 L12: 0.0434
REMARK 3 L13: 0.0725 L23: -0.0366
REMARK 3 S TENSOR
REMARK 3 S11: 0.0030 S12: 0.0631 S13: -0.0529
REMARK 3 S21: -0.0484 S22: -0.0191 S23: -0.0628
REMARK 3 S31: 0.0766 S32: 0.0604 S33: 0.0100
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain B and resid 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0711 51.3549 -15.8003
REMARK 3 T TENSOR
REMARK 3 T11: 0.0708 T22: 0.0618
REMARK 3 T33: 0.0862 T12: -0.0137
REMARK 3 T13: -0.0177 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.8047 L22: 0.7015
REMARK 3 L33: 0.3728 L12: 0.2526
REMARK 3 L13: -0.0256 L23: 0.0485
REMARK 3 S TENSOR
REMARK 3 S11: -0.0185 S12: 0.0213 S13: 0.1201
REMARK 3 S21: 0.0361 S22: 0.0063 S23: -0.0315
REMARK 3 S31: -0.0619 S32: -0.0026 S33: 0.0057
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain C and resid 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6619 44.3894 -27.2750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0629 T22: 0.0543
REMARK 3 T33: 0.0717 T12: -0.0019
REMARK 3 T13: 0.0038 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.5488 L22: 0.7523
REMARK 3 L33: 0.7013 L12: -0.0164
REMARK 3 L13: 0.0400 L23: -0.0926
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: 0.0143 S13: 0.0844
REMARK 3 S21: -0.0155 S22: -0.0145 S23: 0.0923
REMARK 3 S31: -0.0840 S32: -0.0528 S33: 0.0105
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain D and resid 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7063 5.4248 -15.7749
REMARK 3 T TENSOR
REMARK 3 T11: 0.0532 T22: 0.0642
REMARK 3 T33: 0.0466 T12: -0.0237
REMARK 3 T13: 0.0071 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.7399 L22: 0.5389
REMARK 3 L33: 0.3630 L12: 0.0786
REMARK 3 L13: -0.0360 L23: -0.1175
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: 0.0066 S13: -0.0444
REMARK 3 S21: -0.0076 S22: -0.0014 S23: 0.0740
REMARK 3 S31: 0.0223 S32: -0.0070 S33: -0.0093
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 4EUS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-12
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) : 1.0000
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 : 149966
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 46.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 FOR THE DATA SET : 15.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37700
REMARK 200 FOR SHELL : 3.590
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 (%): 46.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 0.125M CALCIUM CHLORIDE,
REMARK 280 0.1M SODIUM ACETATE, 0.02M 1,2-HEXANEDIOL, VAPOR DIFFUSION,
REMARK 280 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 84.88400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.12450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.88400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.12450
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: 2760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 2780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20630 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 D 589 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 712 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 635 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 646 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 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 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 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 -132.27 60.70
REMARK 500 CYS A 303 54.87 -144.11
REMARK 500 THR B 99 -69.67 -93.04
REMARK 500 ASP B 129 -132.64 60.13
REMARK 500 ALA B 154 148.25 -175.96
REMARK 500 ASP B 185 19.57 55.54
REMARK 500 ASP C 129 -131.30 60.24
REMARK 500 CYS C 303 56.01 -143.33
REMARK 500 THR D 99 -67.69 -93.07
REMARK 500 ASP D 129 -133.49 59.39
REMARK 500 ALA D 154 148.41 -176.69
REMARK 500 CYS D 303 55.94 -144.01
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 0RE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0RE D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 SAME PROTEIN, BUT THE APO-STRUCTURE
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 4EUS A 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4EUS B 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4EUS C 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4EUS D 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
SEQADV 4EUS HIS A 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS A 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS A 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS A 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS A 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS A 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS B 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS B 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS B 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS B 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS B 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS B 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS C 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS C 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS C 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS C 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS C 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS C 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS D 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS D 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS D 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS D 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS HIS D 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4EUS 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 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 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 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 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 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 0RE B 401 8
HET 0RE D 401 8
HETNAM 0RE (2S)-HEXANE-1,2-DIOL
FORMUL 5 0RE 2(C6 H14 O2)
FORMUL 7 HOH *1334(H2 O)
HELIX 1 1 THR A 66 HIS A 71 5 6
HELIX 2 2 LEU A 73 ALA A 78 1 6
HELIX 3 3 SER A 102 SER A 118 1 17
HELIX 4 4 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 LYS B 281 1 8
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 LYS C 281 1 8
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 ALA D 227 1 13
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 LYS D 281 1 8
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 VAL A 44 N VAL A 41
SHEET 3 A 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 A 8 LEU A 56 VAL A 60 1 N 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 PHE B 34 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 ILE B 84
SHEET 5 C 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 C 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 C 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 C 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 D 2 PHE B 167 THR B 168 0
SHEET 2 D 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 E 8 GLU C 35 VAL C 41 0
SHEET 2 E 8 VAL C 44 GLY C 52 -1 O LEU C 46 N ARG C 39
SHEET 3 E 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 E 8 LEU C 56 VAL C 60 1 N LEU C 59 O ILE C 84
SHEET 5 E 8 PHE C 123 HIS C 128 1 O VAL C 126 N VAL C 60
SHEET 6 E 8 ILE C 146 MET C 152 1 O 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 PHE D 34 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 VAL D 126 N VAL D 60
SHEET 6 G 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 G 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 G 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 H 2 PHE D 167 THR D 168 0
SHEET 2 H 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SSBOND 1 CYS A 295 CYS A 303 1555 1555 2.01
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 2.00
SITE 1 AC1 13 ASP B 129 ILE B 130 TRP B 133 GLU B 153
SITE 2 AC1 13 PRO B 155 HIS B 177 PHE B 178 TYR B 239
SITE 3 AC1 13 MET B 272 HIS B 297 HOH B 579 HOH B 629
SITE 4 AC1 13 HOH B 685
SITE 1 AC2 10 ASP D 129 TRP D 133 PRO D 155 HIS D 177
SITE 2 AC2 10 PHE D 178 TYR D 239 MET D 272 HIS D 297
SITE 3 AC2 10 HOH D 538 HOH D 664
CRYST1 169.768 84.249 90.132 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 0.005890 0.000000 0.001071 0.00000
SCALE2 0.000000 0.011870 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011277 0.00000
TER 2392 ARG A 317
TER 4735 ARG B 317
TER 7128 ARG C 317
TER 9467 ARG D 317
MASTER 396 0 2 64 40 0 7 610702 4 24 96
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