HEADER HYDROLASE 27-JUL-10 3O4I
TITLE STRUCTURE AND CATALYSIS OF ACYLAMINOACYL PEPTIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-PEPTIDASE;
COMPND 5 EC: 3.4.19.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_TAXID: 56636;
SOURCE 4 GENE: APE_1547.1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA/BETA HYDROLASE FOLD, BETA PROPELLER, HYDROLASE, OLIGOPEPTIDASE,
KEYWDS 2 SIZE SELECTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR V.HARMAT,K.DOMOKOS,D.K.MENYHARD,A.PALLO,Z.SZELTNER,I.SZAMOSI,T.BEKE-
AUTHOR 2 SOMFAI,G.NARAY-SZABO,L.POLGAR
REVDAT 5 06-SEP-23 3O4I 1 REMARK
REVDAT 4 06-OCT-21 3O4I 1 REMARK SEQADV
REVDAT 3 09-FEB-11 3O4I 1 JRNL
REVDAT 2 05-JAN-11 3O4I 1 JRNL
REVDAT 1 17-NOV-10 3O4I 0
JRNL AUTH V.HARMAT,K.DOMOKOS,D.K.MENYHARD,A.PALLO,Z.SZELTNER,
JRNL AUTH 2 I.SZAMOSI,T.BEKE-SOMFAI,G.NARAY-SZABO,L.POLGAR
JRNL TITL STRUCTURE AND CATALYSIS OF ACYLAMINOACYL PEPTIDASE: CLOSED
JRNL TITL 2 AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE.
JRNL REF J.BIOL.CHEM. V. 286 1987 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21084296
JRNL DOI 10.1074/JBC.M110.169862
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 58407
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3091
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4216
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.4270
REMARK 3 BIN FREE R VALUE SET COUNT : 234
REMARK 3 BIN FREE R VALUE : 0.4650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8568
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 335
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : -0.10000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.271
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.051
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8807 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6011 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11956 ; 1.734 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14559 ; 1.240 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1155 ; 6.414 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 351 ;34.464 ;22.564
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1358 ;16.576 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;21.663 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1342 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9981 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1850 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5698 ; 0.637 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2378 ; 0.267 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9087 ; 1.123 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3109 ; 1.938 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2866 ; 3.065 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 6 A 17 2
REMARK 3 1 B 6 B 17 2
REMARK 3 2 A 19 A 21 2
REMARK 3 2 B 19 B 21 2
REMARK 3 3 A 322 A 323 2
REMARK 3 3 B 322 B 323 2
REMARK 3 4 A 325 A 326 2
REMARK 3 4 B 325 B 326 2
REMARK 3 5 A 328 A 580 2
REMARK 3 5 B 328 B 580 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1584 ; 0.070 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1704 ; 0.130 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 1584 ; 0.130 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1704 ; 0.140 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 25 A 187 2
REMARK 3 1 B 25 B 187 2
REMARK 3 2 A 189 A 317 4
REMARK 3 2 B 189 B 317 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 942 ; 0.240 ; 0.050
REMARK 3 MEDIUM POSITIONAL 2 A (A): 2663 ; 0.330 ; 0.500
REMARK 3 TIGHT THERMAL 2 A (A**2): 942 ; 0.790 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 2663 ; 0.850 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 23
REMARK 3 RESIDUE RANGE : A 319 A 582
REMARK 3 ORIGIN FOR THE GROUP (A): -39.6674 -34.3629 -19.0840
REMARK 3 T TENSOR
REMARK 3 T11: 0.4757 T22: 0.2154
REMARK 3 T33: 0.2210 T12: -0.0711
REMARK 3 T13: -0.1246 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 1.2007 L22: 5.9298
REMARK 3 L33: 2.4795 L12: 1.0536
REMARK 3 L13: 0.2321 L23: -0.5961
REMARK 3 S TENSOR
REMARK 3 S11: -0.1332 S12: 0.2368 S13: -0.1692
REMARK 3 S21: -1.6142 S22: 0.2305 S23: 0.3010
REMARK 3 S31: 0.2264 S32: -0.0654 S33: -0.0973
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 6 B 23
REMARK 3 RESIDUE RANGE : B 319 B 581
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5639 -4.6978 -28.9728
REMARK 3 T TENSOR
REMARK 3 T11: 0.3946 T22: 0.2897
REMARK 3 T33: 0.1565 T12: 0.0100
REMARK 3 T13: 0.0940 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 1.5478 L22: 5.2485
REMARK 3 L33: 2.9747 L12: 0.3200
REMARK 3 L13: -0.5378 L23: -0.5842
REMARK 3 S TENSOR
REMARK 3 S11: -0.1384 S12: 0.2341 S13: -0.1073
REMARK 3 S21: -0.8912 S22: -0.0314 S23: -0.5168
REMARK 3 S31: 0.6460 S32: 0.2630 S33: 0.1698
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 24 A 318
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0460 -47.1211 5.5902
REMARK 3 T TENSOR
REMARK 3 T11: 0.0455 T22: 0.1805
REMARK 3 T33: 0.2601 T12: 0.0490
REMARK 3 T13: 0.0560 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 2.7364 L22: 5.2858
REMARK 3 L33: 1.4433 L12: -0.2942
REMARK 3 L13: 0.2339 L23: -0.1910
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: 0.0613 S13: -0.2787
REMARK 3 S21: -0.0878 S22: 0.0557 S23: -0.6452
REMARK 3 S31: 0.1998 S32: 0.2325 S33: -0.0338
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 24 B 318
REMARK 3 ORIGIN FOR THE GROUP (A): -47.3152 17.6243 -29.9567
REMARK 3 T TENSOR
REMARK 3 T11: 0.2179 T22: 0.1862
REMARK 3 T33: 0.1997 T12: -0.0485
REMARK 3 T13: -0.1895 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 2.0831 L22: 2.6182
REMARK 3 L33: 2.9800 L12: 0.1045
REMARK 3 L13: 1.2949 L23: 0.0473
REMARK 3 S TENSOR
REMARK 3 S11: -0.0635 S12: -0.0225 S13: -0.0331
REMARK 3 S21: -0.6209 S22: -0.0417 S23: 0.5489
REMARK 3 S31: 0.0069 S32: -0.3152 S33: 0.1052
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3O4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060654.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61532
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.940
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.26
REMARK 200 R MERGE FOR SHELL (I) : 0.52700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: HYDROLASE AND PROPELLER DOMAINS OF PDB ENTRY 2HU5.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 78MM SODIUM ACETATE, 0.44MM EDTA,
REMARK 280 6.7MM DITHIOTHREITOL, 2.0% PEG 4000 , PH 4.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.96000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 102.96000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 51.81500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 104.94500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 51.81500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 104.94500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 102.96000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 51.81500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 104.94500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 102.96000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 51.81500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 104.94500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS HOMODIMER. THE ASYMMETRIC UNIT
REMARK 300 CONTAINS ONE DIMER (CHAINS A AND B).
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: 3920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 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 MET A 1
REMARK 465 ARG A 2
REMARK 465 ILE A 3
REMARK 465 ILE A 4
REMARK 465 MET A 5
REMARK 465 GLY A 141
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 ILE B 3
REMARK 465 ILE B 4
REMARK 465 MET B 5
REMARK 465 ARG B 582
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 11 CD NE CZ NH1 NH2
REMARK 470 VAL A 83 CG1 CG2
REMARK 470 SER A 84 OG
REMARK 470 LYS A 85 CE NZ
REMARK 470 GLU A 88 CG CD OE1 OE2
REMARK 470 LYS A 110 CE NZ
REMARK 470 GLU A 131 CB CG CD OE1 OE2
REMARK 470 ARG A 133 CZ NH1 NH2
REMARK 470 ARG A 149 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 174 CD NE CZ NH1 NH2
REMARK 470 LYS A 207 NZ
REMARK 470 ARG A 216 CZ NH1 NH2
REMARK 470 ARG A 226 CZ NH1 NH2
REMARK 470 ARG A 244 NE CZ NH1 NH2
REMARK 470 ARG A 328 CZ NH1 NH2
REMARK 470 GLU A 352 CG CD OE1 OE2
REMARK 470 GLU A 475 CG CD OE1 OE2
REMARK 470 GLU A 479 CG CD OE1 OE2
REMARK 470 LEU A 480 CG CD1 CD2
REMARK 470 ARG A 486 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 490 CG CD OE1 OE2
REMARK 470 THR A 493 OG1 CG2
REMARK 470 ARG A 497 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 498 CG CD OE1 OE2
REMARK 470 ILE A 499 CG1 CG2 CD1
REMARK 470 ARG A 501 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 510 CG OD1 OD2
REMARK 470 ARG A 511 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 513 CG CD CE NZ
REMARK 470 LYS A 530 CE NZ
REMARK 470 LYS A 544 CD CE NZ
REMARK 470 HIS A 556 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 581 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 582 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 55 CD OE1 OE2
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 GLU B 88 CG CD OE1 OE2
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 LYS B 207 NZ
REMARK 470 ARG B 226 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 428 CZ NH1 NH2
REMARK 470 TYR B 478 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 479 CG CD OE1 OE2
REMARK 470 GLU B 490 CG CD OE1 OE2
REMARK 470 ARG B 497 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 498 CG CD OE1 OE2
REMARK 470 ILE B 499 CG1 CG2 CD1
REMARK 470 ARG B 501 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 513 NZ
REMARK 470 LYS B 530 CG CD CE NZ
REMARK 470 GLU B 538 CG CD OE1 OE2
REMARK 470 HIS B 556 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 581 CG CD NE CZ NH1 NH2
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 OD1 ASP B 82 O ALA B 87 2.09
REMARK 500 NH2 ARG A 334 O HOH A 621 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL A 13 CB VAL A 13 CG1 -0.198
REMARK 500 VAL A 13 CB VAL A 13 CG2 -0.176
REMARK 500 PHE A 41 CZ PHE A 41 CE2 0.160
REMARK 500 VAL B 13 CB VAL B 13 CG1 -0.138
REMARK 500 VAL B 13 CB VAL B 13 CG2 -0.189
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 325 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 GLN A 522 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ARG B 244 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP B 325 CB - CG - OD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG B 328 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLN B 522 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
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 32 -135.42 53.18
REMARK 500 ARG A 61 -86.99 -97.94
REMARK 500 SER A 66 -169.38 -171.05
REMARK 500 SER A 116 159.54 177.12
REMARK 500 ARG A 145 138.89 -170.14
REMARK 500 ARG A 216 -73.21 -131.41
REMARK 500 ASP A 274 46.37 38.20
REMARK 500 ASP A 414 50.45 -154.76
REMARK 500 SER A 445 -130.42 54.29
REMARK 500 VAL A 472 -57.77 -121.54
REMARK 500 ASN A 523 44.62 -142.59
REMARK 500 ASP B 32 -140.98 64.41
REMARK 500 ASP B 52 33.23 -147.61
REMARK 500 ARG B 61 -93.56 -103.84
REMARK 500 SER B 66 -169.93 -167.38
REMARK 500 GLU B 88 48.82 -93.57
REMARK 500 SER B 116 156.52 176.30
REMARK 500 ASP B 140 -165.09 -128.08
REMARK 500 ALA B 148 136.92 -170.71
REMARK 500 PRO B 151 30.70 -77.73
REMARK 500 ARG B 160 114.61 -163.88
REMARK 500 MET B 206 36.67 71.91
REMARK 500 THR B 214 -169.75 -128.25
REMARK 500 ARG B 216 -83.77 -138.63
REMARK 500 ASP B 414 50.29 -154.43
REMARK 500 SER B 445 -129.70 59.22
REMARK 500 VAL B 472 -51.99 -122.64
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 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 586
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 587
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O4G RELATED DB: PDB
REMARK 900 RELATED ID: 3O4H RELATED DB: PDB
REMARK 900 RELATED ID: 3O4J RELATED DB: PDB
DBREF 3O4I A 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4I B 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
SEQADV 3O4I ALA A 524 UNP Q9YBQ2 ASP 524 ENGINEERED MUTATION
SEQADV 3O4I ALA B 524 UNP Q9YBQ2 ASP 524 ENGINEERED MUTATION
SEQRES 1 A 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 A 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 A 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 A 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 A 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 A 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 A 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 A 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 A 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 A 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 A 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 A 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 A 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 A 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 A 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 A 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 A 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 A 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 A 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 A 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 A 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 A 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 A 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 A 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 A 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 A 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 A 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 A 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 A 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 A 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 A 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 A 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 A 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 A 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 A 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 A 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 A 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 A 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 A 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 A 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 A 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 A 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 A 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 A 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 A 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 B 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 B 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 B 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 B 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 B 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 B 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 B 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 B 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 B 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 B 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 B 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 B 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 B 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 B 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 B 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 B 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 B 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 B 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 B 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 B 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 B 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 B 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 B 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 B 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 B 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 B 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 B 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 B 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 B 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 B 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 B 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 B 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 B 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 B 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 B 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 B 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 B 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 B 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 B 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 B 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 B 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 B 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 B 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 B 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 B 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
HET GOL A 583 6
HET CL A 584 1
HET GOL B 583 6
HET GOL B 584 6
HET GOL B 585 6
HET GOL B 586 6
HET GOL B 587 6
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 6(C3 H8 O3)
FORMUL 4 CL CL 1-
FORMUL 10 HOH *335(H2 O)
HELIX 1 1 GLU A 8 VAL A 22 1 15
HELIX 2 2 LYS A 238 ARG A 244 1 7
HELIX 3 3 PRO A 323 SER A 329 1 7
HELIX 4 4 ASP A 379 ALA A 388 1 10
HELIX 5 5 GLY A 404 LYS A 410 1 7
HELIX 6 6 GLY A 417 SER A 433 1 17
HELIX 7 7 SER A 445 LYS A 458 1 14
HELIX 8 8 ASP A 473 LEU A 480 1 8
HELIX 9 9 ASP A 482 THR A 493 1 12
HELIX 10 10 SER A 496 ARG A 503 1 8
HELIX 11 11 SER A 504 ILE A 512 5 9
HELIX 12 12 PRO A 528 ARG A 542 1 15
HELIX 13 13 THR A 560 LEU A 568 1 9
HELIX 14 14 LEU A 568 GLU A 580 1 13
HELIX 15 15 GLU B 8 VAL B 22 1 15
HELIX 16 16 LYS B 238 ARG B 244 1 7
HELIX 17 17 PRO B 323 SER B 329 1 7
HELIX 18 18 ASP B 379 ALA B 388 1 10
HELIX 19 19 GLY B 404 LYS B 410 1 7
HELIX 20 20 GLY B 417 SER B 433 1 17
HELIX 21 21 SER B 445 LYS B 458 1 14
HELIX 22 22 ASP B 473 LEU B 480 1 8
HELIX 23 23 ASP B 482 THR B 493 1 12
HELIX 24 24 SER B 496 ARG B 503 1 8
HELIX 25 25 SER B 504 ILE B 512 5 9
HELIX 26 26 PRO B 528 ARG B 542 1 15
HELIX 27 27 THR B 560 LEU B 568 1 9
HELIX 28 28 LEU B 568 ARG B 579 1 12
SHEET 1 A 4 LYS A 24 VAL A 31 0
SHEET 2 A 4 LYS A 35 SER A 42 -1 O PHE A 41 N LYS A 24
SHEET 3 A 4 SER A 45 ASP A 52 -1 O TYR A 49 N VAL A 38
SHEET 4 A 4 GLU A 55 LYS A 58 -1 O VAL A 57 N LEU A 50
SHEET 1 B 4 SER A 66 VAL A 67 0
SHEET 2 B 4 ARG A 76 ASP A 82 -1 O VAL A 80 N SER A 66
SHEET 3 B 4 HIS A 90 ASN A 96 -1 O ALA A 91 N ARG A 81
SHEET 4 B 4 GLN A 104 ARG A 105 -1 O GLN A 104 N LYS A 94
SHEET 1 C 5 ASP A 69 PRO A 70 0
SHEET 2 C 5 ARG A 113 ASP A 119 1 O ASP A 119 N ASP A 69
SHEET 3 C 5 VAL A 124 THR A 130 -1 O THR A 127 N LEU A 115
SHEET 4 C 5 ARG A 133 LEU A 139 -1 O ARG A 133 N THR A 130
SHEET 5 C 5 GLU A 146 LEU A 150 -1 O LEU A 147 N LEU A 136
SHEET 1 D 4 GLY A 154 ARG A 160 0
SHEET 2 D 4 LEU A 163 GLY A 168 -1 O ALA A 165 N ASP A 158
SHEET 3 D 4 SER A 176 ASN A 181 -1 O PHE A 178 N GLY A 166
SHEET 4 D 4 ARG A 188 PHE A 190 -1 O PHE A 190 N LEU A 177
SHEET 1 E 3 SER A 196 PHE A 197 0
SHEET 2 E 3 VAL A 208 GLU A 213 -1 O GLU A 213 N SER A 196
SHEET 3 E 3 SER A 201 ILE A 202 -1 N SER A 201 O THR A 209
SHEET 1 F 4 SER A 196 PHE A 197 0
SHEET 2 F 4 VAL A 208 GLU A 213 -1 O GLU A 213 N SER A 196
SHEET 3 F 4 ARG A 219 VAL A 223 -1 O ARG A 219 N LEU A 212
SHEET 4 F 4 VAL A 230 ASP A 232 -1 O GLU A 231 N THR A 222
SHEET 1 G 4 ALA A 247 TYR A 253 0
SHEET 2 G 4 LEU A 259 ARG A 265 -1 O VAL A 262 N TRP A 250
SHEET 3 G 4 ARG A 268 ILE A 273 -1 O PHE A 272 N VAL A 261
SHEET 4 G 4 GLU A 276 VAL A 278 -1 O GLU A 276 N ILE A 273
SHEET 1 H 4 ASN A 284 TRP A 291 0
SHEET 2 H 4 LYS A 294 SER A 301 -1 O LYS A 294 N TRP A 291
SHEET 3 H 4 THR A 304 LEU A 311 -1 O LEU A 311 N LEU A 295
SHEET 4 H 4 PRO A 316 LEU A 318 -1 O LEU A 317 N ILE A 308
SHEET 1 I16 ILE A 330 GLU A 339 0
SHEET 2 I16 ARG A 345 SER A 353 -1 O GLU A 352 N GLY A 332
SHEET 3 I16 HIS A 391 PRO A 395 -1 O VAL A 392 N LEU A 351
SHEET 4 I16 GLY A 360 VAL A 366 1 N VAL A 363 O VAL A 393
SHEET 5 I16 ALA A 436 TYR A 444 1 O TYR A 440 N VAL A 364
SHEET 6 I16 GLY A 465 GLY A 468 1 O GLY A 468 N GLY A 443
SHEET 7 I16 LEU A 516 PRO A 521 1 O ALA A 517 N ALA A 467
SHEET 8 I16 PHE A 546 ILE A 551 1 O GLU A 547 N LEU A 518
SHEET 9 I16 PHE B 546 ILE B 551 -1 O ILE B 550 N ALA A 548
SHEET 10 I16 LEU B 516 PRO B 521 1 N LEU B 518 O GLU B 547
SHEET 11 I16 GLY B 465 GLY B 468 1 N ALA B 467 O ALA B 517
SHEET 12 I16 ALA B 436 TYR B 444 1 N GLY B 443 O GLY B 468
SHEET 13 I16 GLY B 360 VAL B 366 1 N VAL B 364 O TYR B 440
SHEET 14 I16 HIS B 391 PRO B 395 1 O HIS B 391 N VAL B 363
SHEET 15 I16 ARG B 345 SER B 353 -1 N TYR B 349 O MET B 394
SHEET 16 I16 ILE B 330 GLU B 339 -1 N VAL B 338 O VAL B 346
SHEET 1 J 4 LYS B 24 VAL B 31 0
SHEET 2 J 4 LYS B 35 SER B 42 -1 O LEU B 37 N GLY B 29
SHEET 3 J 4 SER B 45 TYR B 51 -1 O TYR B 49 N VAL B 38
SHEET 4 J 4 THR B 56 LYS B 58 -1 O VAL B 57 N LEU B 50
SHEET 1 K 4 SER B 66 VAL B 67 0
SHEET 2 K 4 ARG B 76 ASP B 82 -1 O VAL B 80 N SER B 66
SHEET 3 K 4 HIS B 90 ASN B 96 -1 O PHE B 93 N LEU B 79
SHEET 4 K 4 GLN B 104 ARG B 105 -1 O GLN B 104 N LYS B 94
SHEET 1 L 5 ASP B 69 PRO B 70 0
SHEET 2 L 5 ARG B 113 ASP B 119 1 O ASP B 119 N ASP B 69
SHEET 3 L 5 VAL B 124 ALA B 129 -1 O VAL B 125 N VAL B 118
SHEET 4 L 5 VAL B 134 ASP B 140 -1 O TYR B 137 N PHE B 126
SHEET 5 L 5 GLY B 143 LEU B 150 -1 O ALA B 148 N LEU B 136
SHEET 1 M 4 GLY B 154 ARG B 160 0
SHEET 2 M 4 LEU B 163 GLY B 168 -1 O LEU B 167 N PHE B 155
SHEET 3 M 4 SER B 176 ASN B 181 -1 O SER B 176 N GLY B 168
SHEET 4 M 4 GLY B 185 PHE B 190 -1 O PHE B 190 N LEU B 177
SHEET 1 N 4 SER B 196 ILE B 202 0
SHEET 2 N 4 VAL B 208 GLU B 213 -1 O THR B 209 N SER B 201
SHEET 3 N 4 ARG B 219 VAL B 223 -1 O VAL B 221 N ALA B 210
SHEET 4 N 4 VAL B 230 ASP B 232 -1 O GLU B 231 N THR B 222
SHEET 1 O 4 ALA B 247 TYR B 253 0
SHEET 2 O 4 LEU B 259 ARG B 265 -1 O ALA B 260 N GLY B 252
SHEET 3 O 4 ARG B 268 ILE B 273 -1 O ARG B 268 N ARG B 265
SHEET 4 O 4 GLU B 276 VAL B 278 -1 O GLU B 276 N ILE B 273
SHEET 1 P 4 ASN B 284 TRP B 291 0
SHEET 2 P 4 LYS B 294 SER B 301 -1 O LYS B 294 N TRP B 291
SHEET 3 P 4 THR B 304 SER B 310 -1 O ARG B 307 N HIS B 299
SHEET 4 P 4 PRO B 316 LEU B 318 -1 O LEU B 318 N ILE B 308
CISPEP 1 LEU A 311 PRO A 312 0 13.35
CISPEP 2 THR A 358 PRO A 359 0 0.09
CISPEP 3 GLY A 369 PRO A 370 0 13.97
CISPEP 4 LEU B 311 PRO B 312 0 5.50
CISPEP 5 THR B 358 PRO B 359 0 5.59
CISPEP 6 GLY B 369 PRO B 370 0 10.30
SITE 1 AC1 3 SER A 66 ILE A 114 HOH A 601
SITE 1 AC2 5 ALA B 148 ARG B 149 PHE B 170 VAL B 189
SITE 2 AC2 5 HOH B 598
SITE 1 AC3 3 GLY B 369 SER B 445 PHE B 485
SITE 1 AC4 2 ARG B 11 ALA B 388
SITE 1 AC5 1 HOH B 714
CRYST1 103.630 209.890 205.920 90.00 90.00 90.00 C 2 2 21 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 0.009650 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004856 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
