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HEADER HYDROLASE 22-SEP-22 8B57
TITLE STRUCTURE OF PROLYL ENDOPROTEASE FROM ASPERGILLUS NIGER CBS 109712
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPROTEASE FROM ASPERGILLUS NIGER CBS 109712;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: PATENT WO2015177152A1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 GENE: ATCC64974_102810, CAN33_0042530;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 5061;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CBS 109712
KEYWDS ENDOPROTEASE, PROLINE-SPECIFIC, S28 PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.PIJNING,A.VUJICIC-ZAGAR,J.M.VAN DER LAAN,R.M.DE JONG,B.W.DIJKSTRA
REVDAT 1 20-DEC-23 8B57 0
JRNL AUTH T.PIJNING,A.VUJICIC-ZAGAR,J.M.V.D.LAAN,R.M.D.JONG,
JRNL AUTH 2 C.RAMIREZ-PALACIOS,A.VENTE,L.EDENS,B.W.DIJKSTRA
JRNL TITL STRUCTURAL AND TIME-RESOLVED MECHANISTIC INVESTIGATIONS OF
JRNL TITL 2 PROTEIN HYDROLYSIS BY THE ACIDIC PROLINE-SPECIFIC
JRNL TITL 3 ENDOPROTEASE FROM ASPERGILLUS NIGER
JRNL REF PROTEIN SCI. 2023
JRNL REFN ESSN 1469-896X
JRNL DOI 10.1002/PRO.4856
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25707
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1335
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) : 2.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.48
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1856
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3845
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 301
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.292
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.209
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.159
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.700
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4294 ; 0.010 ; 0.018
REMARK 3 BOND LENGTHS OTHERS (A): 3631 ; 0.001 ; 0.019
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5858 ; 1.403 ; 1.890
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8409 ; 1.100 ; 2.678
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 484 ; 5.916 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;35.027 ;24.076
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 541 ;14.342 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;19.125 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 633 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4771 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1003 ; 0.001 ; 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): 1939 ; 1.474 ; 2.158
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1938 ; 1.474 ; 2.158
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2422 ; 2.260 ; 3.234
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2423 ; 2.260 ; 3.234
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2355 ; 3.305 ; 2.885
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2356 ; 3.305 ; 2.887
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3437 ; 4.726 ; 4.149
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4974 ; 5.761 ;28.112
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4963 ; 5.753 ;28.076
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 42 A 526
REMARK 3 ORIGIN FOR THE GROUP (A): 28.2570 60.6310 -6.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0933 T22: 0.0441
REMARK 3 T33: 0.2036 T12: 0.0512
REMARK 3 T13: -0.0709 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 2.0526 L22: 0.9749
REMARK 3 L33: 1.0897 L12: 0.5199
REMARK 3 L13: -0.8665 L23: -0.1486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: -0.0390 S13: 0.1482
REMARK 3 S21: -0.1219 S22: 0.0080 S23: 0.2681
REMARK 3 S31: 0.0729 S32: 0.0461 S33: -0.0229
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 8B57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1292123514.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9195
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27027
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 66.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 9.10
REMARK 200 R MERGE FOR SHELL (I) : 0.63600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MR-ROSETTA
REMARK 200 STARTING MODEL: COMPOSITE MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-29% (W/V) PEG 3350, 0.1 M SODIUM
REMARK 280 CITRATE PH 5.0, 0.1 M AMMONIUM TARTRATE PH 7.2, 20 MM HAC/NAAC
REMARK 280 PH 5.0, 50 MM NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 81.01500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 81.01500
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 81.01500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 81.01500
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 81.01500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 81.01500
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 81.01500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 81.01500
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 81.01500
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 81.01500
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 81.01500
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 81.01500
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 81.01500
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 81.01500
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 81.01500
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 81.01500
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 81.01500
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 81.01500
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 81.01500
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 81.01500
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 81.01500
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 81.01500
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 81.01500
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 81.01500
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 81.01500
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 81.01500
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H
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 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 O4 NAG B 1 O5 NAG B 2 1.90
REMARK 500 O2 MAN C 5 O5 MAN C 6 1.98
REMARK 500 O4 NAG H 1 O5 NAG H 2 2.02
REMARK 500 O4 NAG C 1 O5 NAG C 2 2.03
REMARK 500 O3 BMA C 3 O5 MAN C 4 2.07
REMARK 500 O6 MAN C 7 O5 MAN C 10 2.08
REMARK 500 O4 NAG G 1 O5 NAG G 2 2.08
REMARK 500 O2 MAN C 8 O5 MAN C 9 2.10
REMARK 500 O4 NAG G 2 O5 BMA G 3 2.11
REMARK 500 O6 BMA C 3 C2 MAN C 7 2.11
REMARK 500 O2 MAN C 4 O5 MAN C 5 2.12
REMARK 500 O4 NAG C 2 O5 BMA C 3 2.13
REMARK 500 O6 BMA C 3 O5 MAN C 7 2.15
REMARK 500 O3 MAN C 7 O5 MAN C 8 2.15
REMARK 500 C6 BMA C 3 C1 MAN C 7 2.19
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 THR A 43 -60.95 79.62
REMARK 500 GLU A 88 49.68 -72.50
REMARK 500 TYR A 122 -0.10 81.67
REMARK 500 ASP A 161 94.31 -167.86
REMARK 500 SER A 179 -138.05 64.23
REMARK 500 ASP A 283 -159.11 -135.31
REMARK 500 PHE A 384 -74.49 60.45
REMARK 500 TRP A 441 5.21 -69.93
REMARK 500 PHE A 490 -147.15 -113.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 804 DISTANCE = 5.82 ANGSTROMS
DBREF 8B57 A 42 526 PDB 8B57 8B57 42 526
SEQRES 1 A 485 ALA THR THR GLY GLU ALA TYR PHE GLU GLN LEU LEU ASP
SEQRES 2 A 485 HIS HIS ASN PRO GLU LYS GLY THR PHE SER GLN ARG TYR
SEQRES 3 A 485 TRP TRP SER THR GLU TYR TRP GLY GLY PRO GLY SER PRO
SEQRES 4 A 485 VAL VAL LEU PHE THR PRO GLY GLU VAL SER ALA ASP GLY
SEQRES 5 A 485 TYR GLU GLY TYR LEU THR ASN GLU THR LEU THR GLY VAL
SEQRES 6 A 485 TYR ALA GLN GLU ILE GLN GLY ALA VAL ILE LEU ILE GLU
SEQRES 7 A 485 HIS ARG TYR TRP GLY ASP SER SER PRO TYR GLU VAL LEU
SEQRES 8 A 485 ASN ALA GLU THR LEU GLN TYR LEU THR LEU ASP GLN ALA
SEQRES 9 A 485 ILE LEU ASP MET THR TYR PHE ALA GLU THR VAL LYS LEU
SEQRES 10 A 485 GLN PHE ASP ASN SER THR ARG SER ASN ALA GLN ASN ALA
SEQRES 11 A 485 PRO TRP VAL MET VAL GLY GLY SER TYR SER GLY ALA LEU
SEQRES 12 A 485 THR ALA TRP THR GLU SER VAL ALA PRO GLY THR PHE TRP
SEQRES 13 A 485 ALA TYR HIS ALA THR SER ALA PRO VAL GLU ALA ILE TYR
SEQRES 14 A 485 ASP TYR TRP GLN TYR PHE TYR PRO ILE GLN GLN GLY MET
SEQRES 15 A 485 ALA GLN ASN CYS SER LYS ASP VAL SER LEU VAL ALA GLU
SEQRES 16 A 485 TYR VAL ASP LYS ILE GLY LYS ASN GLY THR ALA LYS GLU
SEQRES 17 A 485 GLN GLN ALA LEU LYS GLU LEU PHE GLY LEU GLY ALA VAL
SEQRES 18 A 485 GLU HIS PHE ASP ASP PHE ALA ALA VAL LEU PRO ASN GLY
SEQRES 19 A 485 PRO TYR LEU TRP GLN ASP ASN ASP PHE ALA THR GLY TYR
SEQRES 20 A 485 SER SER PHE PHE GLN PHE CYS ASP ALA VAL GLU GLY VAL
SEQRES 21 A 485 GLU ALA GLY ALA ALA VAL THR PRO GLY PRO GLU GLY VAL
SEQRES 22 A 485 GLY LEU GLU LYS ALA LEU ALA ASN TYR ALA ASN TRP PHE
SEQRES 23 A 485 ASN SER THR ILE LEU PRO ASP TYR CYS ALA SER TYR GLY
SEQRES 24 A 485 TYR TRP THR ASP GLU TRP SER VAL ALA CYS PHE ASP SER
SEQRES 25 A 485 TYR ASN ALA SER SER PRO ILE TYR THR ASP THR SER VAL
SEQRES 26 A 485 GLY ASN ALA VAL ASP ARG GLN TRP GLU TRP PHE LEU CYS
SEQRES 27 A 485 ASN GLU PRO PHE PHE TYR TRP GLN ASP GLY ALA PRO GLU
SEQRES 28 A 485 GLY THR SER THR ILE VAL PRO ARG LEU VAL SER ALA SER
SEQRES 29 A 485 TYR TRP GLN ARG GLN CYS PRO LEU TYR PHE PRO GLU THR
SEQRES 30 A 485 ASN GLY TYR THR TYR GLY SER ALA LYS GLY LYS ASN ALA
SEQRES 31 A 485 ALA THR VAL ASN SER TRP THR GLY GLY TRP ASP MET THR
SEQRES 32 A 485 ARG ASN THR THR ARG LEU ILE TRP THR ASN GLY GLN TYR
SEQRES 33 A 485 ASP PRO TRP ARG ASP SER GLY VAL SER SER THR PHE ARG
SEQRES 34 A 485 PRO GLY GLY PRO LEU ALA SER THR ALA ASN GLU PRO VAL
SEQRES 35 A 485 GLN ILE ILE PRO GLY GLY PHE HIS CYS SER ASP LEU TYR
SEQRES 36 A 485 MET ALA ASP TYR TYR ALA ASN GLU GLY VAL LYS LYS VAL
SEQRES 37 A 485 VAL ASP ASN GLU VAL LYS GLN ILE LYS GLU TRP VAL GLU
SEQRES 38 A 485 GLU TYR TYR ALA
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET MAN C 5 11
HET MAN C 6 11
HET MAN C 7 11
HET MAN C 8 11
HET MAN C 9 11
HET MAN C 10 11
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET NAG H 1 14
HET NAG H 2 14
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET GOL A 604 6
HET GOL A 605 6
HET PEG A 606 7
HET PG4 A 607 13
HET 1PE A 608 16
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN 1PE PEG400
FORMUL 2 NAG 11(C8 H15 N O6)
FORMUL 3 BMA 2(C6 H12 O6)
FORMUL 3 MAN 7(C6 H12 O6)
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 11 PEG C4 H10 O3
FORMUL 12 PG4 C8 H18 O5
FORMUL 13 1PE C10 H22 O6
FORMUL 14 HOH *104(H2 O)
HELIX 1 AA1 ASN A 57 LYS A 60 5 4
HELIX 2 AA2 TYR A 94 THR A 99 5 6
HELIX 3 AA3 THR A 102 GLN A 112 1 11
HELIX 4 AA4 GLU A 135 LEU A 140 5 6
HELIX 5 AA5 THR A 141 VAL A 156 1 16
HELIX 6 AA6 SER A 163 ASN A 167 5 5
HELIX 7 AA7 SER A 179 ALA A 192 1 14
HELIX 8 AA8 TRP A 213 TYR A 215 5 3
HELIX 9 AA9 PHE A 216 MET A 223 1 8
HELIX 10 AB1 ALA A 224 GLY A 245 1 22
HELIX 11 AB2 THR A 246 PHE A 257 1 12
HELIX 12 AB3 HIS A 264 ALA A 270 1 7
HELIX 13 AB4 VAL A 271 ASN A 282 5 12
HELIX 14 AB5 SER A 289 GLY A 300 1 12
HELIX 15 AB6 GLY A 315 ILE A 331 1 17
HELIX 16 AB7 TYR A 335 GLY A 340 5 6
HELIX 17 AB8 VAL A 348 ASP A 352 5 5
HELIX 18 AB9 SER A 358 ASP A 363 1 6
HELIX 19 AC1 ASP A 371 GLU A 381 1 11
HELIX 20 AC2 SER A 403 ARG A 409 1 7
HELIX 21 AC3 GLN A 410 PHE A 415 1 6
HELIX 22 AC4 TYR A 423 GLY A 428 5 6
HELIX 23 AC5 ASN A 430 GLY A 439 1 10
HELIX 24 AC6 GLY A 440 MET A 443 5 4
HELIX 25 AC7 TRP A 460 GLY A 464 5 5
HELIX 26 AC8 TYR A 496 ASN A 503 1 8
HELIX 27 AC9 ASN A 503 ALA A 526 1 24
SHEET 1 AA1 8 THR A 44 LEU A 52 0
SHEET 2 AA1 8 THR A 62 SER A 70 -1 O GLN A 65 N PHE A 49
SHEET 3 AA1 8 ALA A 114 ILE A 118 -1 O LEU A 117 N TRP A 68
SHEET 4 AA1 8 VAL A 81 PHE A 84 1 N VAL A 82 O ILE A 116
SHEET 5 AA1 8 TRP A 173 GLY A 178 1 O VAL A 174 N VAL A 81
SHEET 6 AA1 8 ALA A 198 THR A 202 1 O THR A 202 N GLY A 177
SHEET 7 AA1 8 LEU A 450 GLY A 455 1 O ILE A 451 N TYR A 199
SHEET 8 AA1 8 VAL A 483 ILE A 486 1 O ILE A 486 N ASN A 454
SHEET 1 AA2 2 ILE A 209 ASP A 211 0
SHEET 2 AA2 2 PHE A 384 TRP A 386 1 O TYR A 385 N ILE A 209
SSBOND 1 CYS A 227 CYS A 295 1555 1555 2.12
SSBOND 2 CYS A 336 CYS A 350 1555 1555 2.12
SSBOND 3 CYS A 379 CYS A 411 1555 1555 2.05
LINK ND2 ASN A 100 C1 NAG B 1 1555 1555 1.44
LINK ND2 ASN A 162 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 226 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 244 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN A 328 C1 NAG G 1 1555 1555 1.46
LINK ND2 ASN A 355 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN A 446 C1 NAG A 603 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.02
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.02
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.02
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.02
LINK O6 BMA C 3 C1 MAN C 7 1555 1555 1.02
LINK O2 MAN C 4 C1 MAN C 5 1555 1555 1.02
LINK O2 MAN C 5 C1 MAN C 6 1555 1555 1.02
LINK O3 MAN C 7 C1 MAN C 8 1555 1555 1.02
LINK O6 MAN C 7 C1 MAN C 10 1555 1555 1.02
LINK O2 MAN C 8 C1 MAN C 9 1555 1555 1.02
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.03
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.03
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.02
CISPEP 1 GLU A 381 PRO A 382 0 -3.72
CRYST1 162.030 162.030 162.030 90.00 90.00 90.00 I 2 3 24
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 0.006172 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006172 0.00000
TER 3846 ALA A 526
MASTER 402 0 25 27 10 0 0 6 4250 1 314 38
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