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HEADER HYDROLASE 20-SEP-22 8B48
TITLE STRUCTURE OF LENTITHECIUM FLUVIATILE CARBOHYDRATE ESTERASE FROM THE
TITLE 2 CE15 FAMILY (LFCE15C)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE ESTERASE FAMILY 15 PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LENTITHECIUM FLUVIATILE;
SOURCE 3 ORGANISM_TAXID: 690899;
SOURCE 4 GENE: K458DRAFT_349146;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SMD1168H
KEYWDS LIGNOCELLULOSE DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SCHOLZEN,S.MAZURKEWICH,J.C.N.POULSEN,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 07-JUN-23 8B48 0
JRNL AUTH S.MAZURKEWICH,K.C.SCHOLZEN,R.H.BRUSCH,J.C.N.POULSEN,
JRNL AUTH 2 Y.THEIBICH,S.HUTTNER,L.OLSSON,J.LARSBRINK,L.LO LEGGIO
JRNL TITL STRUCTURAL AND FUNCTIONAL INVESTIGATION OF A FUNGAL MEMBER
JRNL TITL 2 OF CARBOHYDRATE ESTERASE FAMILY 15 WITH POTENTIAL
JRNL TITL 3 SPECIFICITY FOR RARE XYLANS.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 79 545 2023
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 37227091
JRNL DOI 10.1107/S205979832300325X
REMARK 2
REMARK 2 RESOLUTION. 2.65 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 47781
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.801
REMARK 3 FREE R VALUE TEST SET COUNT : 2294
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3350
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.4550
REMARK 3 BIN FREE R VALUE SET COUNT : 182
REMARK 3 BIN FREE R VALUE : 0.4840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11382
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 250
REMARK 3 SOLVENT ATOMS : 303
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.93800
REMARK 3 B22 (A**2) : -2.86800
REMARK 3 B33 (A**2) : -0.62300
REMARK 3 B12 (A**2) : -2.67600
REMARK 3 B13 (A**2) : 5.12400
REMARK 3 B23 (A**2) : -2.90900
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): 0.415
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.509
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.729
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12005 ; 0.006 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 11023 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16324 ; 1.448 ; 1.674
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25502 ; 1.183 ; 1.604
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1485 ; 7.225 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 566 ;34.509 ;22.208
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1844 ;17.730 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;18.085 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1626 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15318 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2738 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2371 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 93 ; 0.280 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5701 ; 0.164 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 338 ; 0.169 ; 0.200
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): 5922 ; 4.419 ; 6.155
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5923 ; 4.418 ; 6.155
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7398 ; 6.859 ; 9.224
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7399 ; 6.858 ; 9.226
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6083 ; 4.583 ; 6.565
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6079 ; 4.583 ; 6.565
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8921 ; 7.042 ; 9.702
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8922 ; 7.041 ; 9.702
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 : 6
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
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 20 A 389 NULL
REMARK 3 2 B 20 B 389 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 3 A 20 A 389 NULL
REMARK 3 4 C 20 C 389 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 5 A 21 A 388 NULL
REMARK 3 6 D 21 D 388 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 7 B 20 B 389 NULL
REMARK 3 8 C 20 C 389 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 9 B 21 B 388 NULL
REMARK 3 10 D 21 D 388 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 11 C 21 C 388 NULL
REMARK 3 12 D 21 D 388 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8B48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1292124715.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX IV
REMARK 200 BEAMLINE : BIOMAX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980779
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47781
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 47.254
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.000
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: 3PIC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN STOCK: 13.7 MG/ML IN 20 MM
REMARK 280 TRIS PH 8.0 RESERVOIR: 0.2 M AMMONIUM FORMATE PH 6.6, 20 %W/V
REMARK 280 PEG 3350 DROP: 3:1 PROTEIN TO RESERVOIR RATIO, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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 GLN A 17
REMARK 465 ALA A 18
REMARK 465 PRO A 19
REMARK 465 GLU A 390
REMARK 465 GLN A 391
REMARK 465 LYS A 392
REMARK 465 LEU A 393
REMARK 465 ILE A 394
REMARK 465 SER A 395
REMARK 465 GLU A 396
REMARK 465 GLU A 397
REMARK 465 ASP A 398
REMARK 465 LEU A 399
REMARK 465 ASN A 400
REMARK 465 SER A 401
REMARK 465 ALA A 402
REMARK 465 VAL A 403
REMARK 465 ASP A 404
REMARK 465 HIS A 405
REMARK 465 HIS A 406
REMARK 465 HIS A 407
REMARK 465 HIS A 408
REMARK 465 HIS A 409
REMARK 465 HIS A 410
REMARK 465 GLN B 17
REMARK 465 ALA B 18
REMARK 465 PRO B 19
REMARK 465 GLU B 390
REMARK 465 GLN B 391
REMARK 465 LYS B 392
REMARK 465 LEU B 393
REMARK 465 ILE B 394
REMARK 465 SER B 395
REMARK 465 GLU B 396
REMARK 465 GLU B 397
REMARK 465 ASP B 398
REMARK 465 LEU B 399
REMARK 465 ASN B 400
REMARK 465 SER B 401
REMARK 465 ALA B 402
REMARK 465 VAL B 403
REMARK 465 ASP B 404
REMARK 465 HIS B 405
REMARK 465 HIS B 406
REMARK 465 HIS B 407
REMARK 465 HIS B 408
REMARK 465 HIS B 409
REMARK 465 HIS B 410
REMARK 465 GLN C 17
REMARK 465 ALA C 18
REMARK 465 PRO C 19
REMARK 465 GLU C 390
REMARK 465 GLN C 391
REMARK 465 LYS C 392
REMARK 465 LEU C 393
REMARK 465 ILE C 394
REMARK 465 SER C 395
REMARK 465 GLU C 396
REMARK 465 GLU C 397
REMARK 465 ASP C 398
REMARK 465 LEU C 399
REMARK 465 ASN C 400
REMARK 465 SER C 401
REMARK 465 ALA C 402
REMARK 465 VAL C 403
REMARK 465 ASP C 404
REMARK 465 HIS C 405
REMARK 465 HIS C 406
REMARK 465 HIS C 407
REMARK 465 HIS C 408
REMARK 465 HIS C 409
REMARK 465 HIS C 410
REMARK 465 GLN D 17
REMARK 465 ALA D 18
REMARK 465 PRO D 19
REMARK 465 SER D 20
REMARK 465 GLU D 390
REMARK 465 GLN D 391
REMARK 465 LYS D 392
REMARK 465 LEU D 393
REMARK 465 ILE D 394
REMARK 465 SER D 395
REMARK 465 GLU D 396
REMARK 465 GLU D 397
REMARK 465 ASP D 398
REMARK 465 LEU D 399
REMARK 465 ASN D 400
REMARK 465 SER D 401
REMARK 465 ALA D 402
REMARK 465 VAL D 403
REMARK 465 ASP D 404
REMARK 465 HIS D 405
REMARK 465 HIS D 406
REMARK 465 HIS D 407
REMARK 465 HIS D 408
REMARK 465 HIS D 409
REMARK 465 HIS D 410
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 O6 BMA F 3 O5 MAN F 5 1.81
REMARK 500 O GLN B 66 O TYR B 70 2.07
REMARK 500 O PRO B 273 O HOH B 501 2.11
REMARK 500 O4 NAG F 2 O5 BMA F 3 2.14
REMARK 500 C6 BMA G 3 C1 MAN G 4 2.19
REMARK 500 ND2 ASN D 241 O5 NAG H 1 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 ALA A 32 123.18 -34.04
REMARK 500 SER A 69 -52.18 -128.33
REMARK 500 ALA A 83 112.83 -167.03
REMARK 500 LYS A 188 28.45 83.69
REMARK 500 SER A 200 -124.00 60.24
REMARK 500 SER A 227 -30.24 84.45
REMARK 500 ALA A 228 -86.35 -105.14
REMARK 500 PRO A 273 37.56 -77.60
REMARK 500 CYS A 337 2.62 82.78
REMARK 500 CYS A 337 2.35 83.07
REMARK 500 THR A 362 38.95 -142.65
REMARK 500 PRO B 25 151.30 -45.05
REMARK 500 ALA B 32 123.41 -32.99
REMARK 500 SER B 69 -84.69 -120.18
REMARK 500 ALA B 83 111.93 -167.56
REMARK 500 SER B 85 85.83 -151.85
REMARK 500 LYS B 188 28.63 83.32
REMARK 500 SER B 200 -121.77 66.80
REMARK 500 SER B 227 -29.82 84.17
REMARK 500 ALA B 228 -86.80 -105.07
REMARK 500 PRO B 273 38.30 -77.98
REMARK 500 CYS B 337 2.37 80.92
REMARK 500 THR B 362 36.59 -145.43
REMARK 500 ALA C 32 122.25 -32.28
REMARK 500 SER C 69 -51.65 -127.82
REMARK 500 ALA C 83 110.11 -165.15
REMARK 500 SER C 85 85.20 -151.36
REMARK 500 LYS C 188 28.37 83.69
REMARK 500 SER C 200 -123.61 58.24
REMARK 500 SER C 227 -29.85 84.34
REMARK 500 ALA C 228 -86.28 -105.91
REMARK 500 PRO C 273 38.08 -78.34
REMARK 500 CYS C 337 1.42 82.49
REMARK 500 THR C 362 37.13 -142.75
REMARK 500 PRO D 25 150.14 -43.35
REMARK 500 ALA D 32 122.01 -32.30
REMARK 500 SER D 69 -52.27 -129.63
REMARK 500 ALA D 83 111.75 -167.29
REMARK 500 SER D 85 85.92 -150.92
REMARK 500 LYS D 188 28.08 83.38
REMARK 500 SER D 200 -124.20 58.04
REMARK 500 SER D 227 -29.73 83.59
REMARK 500 ALA D 228 -86.89 -105.40
REMARK 500 PRO D 273 39.52 -79.03
REMARK 500 CYS D 337 2.32 82.56
REMARK 500 THR D 362 37.70 -141.46
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 C 573 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH C 574 DISTANCE = 7.38 ANGSTROMS
REMARK 525 HOH C 575 DISTANCE = 9.24 ANGSTROMS
REMARK 525 HOH D 666 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH D 667 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH D 668 DISTANCE = 9.92 ANGSTROMS
REMARK 525 HOH D 669 DISTANCE = 12.53 ANGSTROMS
DBREF1 8B48 A 17 387 UNP A0A6G1IIU9_9PLEO
DBREF2 8B48 A A0A6G1IIU9 17 387
DBREF1 8B48 B 17 387 UNP A0A6G1IIU9_9PLEO
DBREF2 8B48 B A0A6G1IIU9 17 387
DBREF1 8B48 C 17 387 UNP A0A6G1IIU9_9PLEO
DBREF2 8B48 C A0A6G1IIU9 17 387
DBREF1 8B48 D 17 387 UNP A0A6G1IIU9_9PLEO
DBREF2 8B48 D A0A6G1IIU9 17 387
SEQADV 8B48 GLY A 388 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU A 389 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU A 390 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLN A 391 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LYS A 392 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU A 393 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ILE A 394 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 SER A 395 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU A 396 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU A 397 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASP A 398 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU A 399 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASN A 400 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 SER A 401 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ALA A 402 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 VAL A 403 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASP A 404 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS A 405 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS A 406 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS A 407 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS A 408 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS A 409 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS A 410 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLY B 388 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU B 389 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU B 390 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLN B 391 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LYS B 392 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU B 393 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ILE B 394 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 SER B 395 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU B 396 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU B 397 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASP B 398 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU B 399 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASN B 400 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 SER B 401 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ALA B 402 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 VAL B 403 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASP B 404 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS B 405 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS B 406 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS B 407 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS B 408 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS B 409 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS B 410 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLY C 388 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU C 389 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU C 390 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLN C 391 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LYS C 392 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU C 393 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ILE C 394 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 SER C 395 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU C 396 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU C 397 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASP C 398 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU C 399 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASN C 400 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 SER C 401 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ALA C 402 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 VAL C 403 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASP C 404 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS C 405 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS C 406 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS C 407 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS C 408 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS C 409 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS C 410 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLY D 388 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU D 389 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU D 390 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLN D 391 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LYS D 392 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU D 393 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ILE D 394 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 SER D 395 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU D 396 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 GLU D 397 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASP D 398 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 LEU D 399 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASN D 400 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 SER D 401 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ALA D 402 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 VAL D 403 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 ASP D 404 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS D 405 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS D 406 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS D 407 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS D 408 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS D 409 UNP A0A6G1IIU EXPRESSION TAG
SEQADV 8B48 HIS D 410 UNP A0A6G1IIU EXPRESSION TAG
SEQRES 1 A 394 GLN ALA PRO SER CYS PRO ASN LEU PRO ALA SER ILE ASN
SEQRES 2 A 394 TYR ALA ALA ASN PRO LYS LEU PRO ASP PRO PHE LEU ALA
SEQRES 3 A 394 LEU SER GLY THR ARG LEU SER LYS LYS ASP GLN TRP PRO
SEQRES 4 A 394 CYS ARG LYS GLU GLU ILE ARG GLN LEU PHE GLN ARG TYR
SEQRES 5 A 394 SER TYR GLY THR PHE PRO PRO ARG PRO GLU SER VAL THR
SEQRES 6 A 394 ALA ALA MET SER GLY ASN ALA LEU LYS ILE THR VAL SER
SEQRES 7 A 394 GLU GLY SER LYS SER MET SER PHE SER VAL ASN ILE LYS
SEQRES 8 A 394 LEU PRO SER SER GLY ALA ALA PRO TYR PRO ALA ILE ILE
SEQRES 9 A 394 ALA TYR GLY SER ALA SER LEU PRO ILE PRO ASN THR VAL
SEQRES 10 A 394 ALA THR ILE THR TYR GLN ASN PHE GLU MET ALA ALA ASP
SEQRES 11 A 394 ASN GLY ARG GLY LYS GLY LYS PHE TYR GLU PHE TYR GLY
SEQRES 12 A 394 SER ASN HIS ASN ALA GLY GLY MET ILE ALA ALA ALA TRP
SEQRES 13 A 394 GLY VAL ASP ARG ILE ILE ASP ALA LEU GLU MET THR PRO
SEQRES 14 A 394 ALA ALA LYS ILE ASP PRO LYS ARG VAL GLY VAL THR GLY
SEQRES 15 A 394 CYS SER ARG ASN GLY LYS GLY SER MET ILE ALA GLY ALA
SEQRES 16 A 394 PHE VAL ASP ARG ILE ALA LEU ALA LEU PRO GLN GLU GLY
SEQRES 17 A 394 GLY GLN SER ALA ALA GLY CYS TRP ARG ILE ALA ASP GLU
SEQRES 18 A 394 ILE GLN LYS ASN GLY THR LYS VAL GLU THR ALA HIS GLN
SEQRES 19 A 394 ILE VAL ASN GLY ASP SER TRP PHE SER THR ASP PHE SER
SEQRES 20 A 394 LYS TYR VAL ASP THR VAL PRO THR LEU PRO TRP ASP ASN
SEQRES 21 A 394 HIS MET LEU HIS ALA LEU TYR ALA TYR PRO PRO ARG GLY
SEQRES 22 A 394 LEU LEU ILE ILE GLU ASN THR ALA ILE ASP TYR LEU GLY
SEQRES 23 A 394 PRO THR SER ASN TYR HIS CYS ALA THR ALA GLY ARG LYS
SEQRES 24 A 394 VAL HIS GLU ALA LEU GLY VAL LYS ASP TYR PHE GLY PHE
SEQRES 25 A 394 SER GLN ASN SER HIS SER ASP HIS CYS GLY PHE PRO LYS
SEQRES 26 A 394 ALA GLN GLN PRO GLU LEU THR ALA PHE ILE GLU ARG PHE
SEQRES 27 A 394 LEU LEU ALA LYS ASP THR LYS THR ASP VAL TRP LYS THR
SEQRES 28 A 394 ASP GLY LYS PHE THR ILE ASP GLU ARG ARG TRP ILE ASP
SEQRES 29 A 394 TRP ALA VAL PRO SER LEU SER GLY LEU GLU GLN LYS LEU
SEQRES 30 A 394 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 31 A 394 HIS HIS HIS HIS
SEQRES 1 B 394 GLN ALA PRO SER CYS PRO ASN LEU PRO ALA SER ILE ASN
SEQRES 2 B 394 TYR ALA ALA ASN PRO LYS LEU PRO ASP PRO PHE LEU ALA
SEQRES 3 B 394 LEU SER GLY THR ARG LEU SER LYS LYS ASP GLN TRP PRO
SEQRES 4 B 394 CYS ARG LYS GLU GLU ILE ARG GLN LEU PHE GLN ARG TYR
SEQRES 5 B 394 SER TYR GLY THR PHE PRO PRO ARG PRO GLU SER VAL THR
SEQRES 6 B 394 ALA ALA MET SER GLY ASN ALA LEU LYS ILE THR VAL SER
SEQRES 7 B 394 GLU GLY SER LYS SER MET SER PHE SER VAL ASN ILE LYS
SEQRES 8 B 394 LEU PRO SER SER GLY ALA ALA PRO TYR PRO ALA ILE ILE
SEQRES 9 B 394 ALA TYR GLY SER ALA SER LEU PRO ILE PRO ASN THR VAL
SEQRES 10 B 394 ALA THR ILE THR TYR GLN ASN PHE GLU MET ALA ALA ASP
SEQRES 11 B 394 ASN GLY ARG GLY LYS GLY LYS PHE TYR GLU PHE TYR GLY
SEQRES 12 B 394 SER ASN HIS ASN ALA GLY GLY MET ILE ALA ALA ALA TRP
SEQRES 13 B 394 GLY VAL ASP ARG ILE ILE ASP ALA LEU GLU MET THR PRO
SEQRES 14 B 394 ALA ALA LYS ILE ASP PRO LYS ARG VAL GLY VAL THR GLY
SEQRES 15 B 394 CYS SER ARG ASN GLY LYS GLY SER MET ILE ALA GLY ALA
SEQRES 16 B 394 PHE VAL ASP ARG ILE ALA LEU ALA LEU PRO GLN GLU GLY
SEQRES 17 B 394 GLY GLN SER ALA ALA GLY CYS TRP ARG ILE ALA ASP GLU
SEQRES 18 B 394 ILE GLN LYS ASN GLY THR LYS VAL GLU THR ALA HIS GLN
SEQRES 19 B 394 ILE VAL ASN GLY ASP SER TRP PHE SER THR ASP PHE SER
SEQRES 20 B 394 LYS TYR VAL ASP THR VAL PRO THR LEU PRO TRP ASP ASN
SEQRES 21 B 394 HIS MET LEU HIS ALA LEU TYR ALA TYR PRO PRO ARG GLY
SEQRES 22 B 394 LEU LEU ILE ILE GLU ASN THR ALA ILE ASP TYR LEU GLY
SEQRES 23 B 394 PRO THR SER ASN TYR HIS CYS ALA THR ALA GLY ARG LYS
SEQRES 24 B 394 VAL HIS GLU ALA LEU GLY VAL LYS ASP TYR PHE GLY PHE
SEQRES 25 B 394 SER GLN ASN SER HIS SER ASP HIS CYS GLY PHE PRO LYS
SEQRES 26 B 394 ALA GLN GLN PRO GLU LEU THR ALA PHE ILE GLU ARG PHE
SEQRES 27 B 394 LEU LEU ALA LYS ASP THR LYS THR ASP VAL TRP LYS THR
SEQRES 28 B 394 ASP GLY LYS PHE THR ILE ASP GLU ARG ARG TRP ILE ASP
SEQRES 29 B 394 TRP ALA VAL PRO SER LEU SER GLY LEU GLU GLN LYS LEU
SEQRES 30 B 394 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 31 B 394 HIS HIS HIS HIS
SEQRES 1 C 394 GLN ALA PRO SER CYS PRO ASN LEU PRO ALA SER ILE ASN
SEQRES 2 C 394 TYR ALA ALA ASN PRO LYS LEU PRO ASP PRO PHE LEU ALA
SEQRES 3 C 394 LEU SER GLY THR ARG LEU SER LYS LYS ASP GLN TRP PRO
SEQRES 4 C 394 CYS ARG LYS GLU GLU ILE ARG GLN LEU PHE GLN ARG TYR
SEQRES 5 C 394 SER TYR GLY THR PHE PRO PRO ARG PRO GLU SER VAL THR
SEQRES 6 C 394 ALA ALA MET SER GLY ASN ALA LEU LYS ILE THR VAL SER
SEQRES 7 C 394 GLU GLY SER LYS SER MET SER PHE SER VAL ASN ILE LYS
SEQRES 8 C 394 LEU PRO SER SER GLY ALA ALA PRO TYR PRO ALA ILE ILE
SEQRES 9 C 394 ALA TYR GLY SER ALA SER LEU PRO ILE PRO ASN THR VAL
SEQRES 10 C 394 ALA THR ILE THR TYR GLN ASN PHE GLU MET ALA ALA ASP
SEQRES 11 C 394 ASN GLY ARG GLY LYS GLY LYS PHE TYR GLU PHE TYR GLY
SEQRES 12 C 394 SER ASN HIS ASN ALA GLY GLY MET ILE ALA ALA ALA TRP
SEQRES 13 C 394 GLY VAL ASP ARG ILE ILE ASP ALA LEU GLU MET THR PRO
SEQRES 14 C 394 ALA ALA LYS ILE ASP PRO LYS ARG VAL GLY VAL THR GLY
SEQRES 15 C 394 CYS SER ARG ASN GLY LYS GLY SER MET ILE ALA GLY ALA
SEQRES 16 C 394 PHE VAL ASP ARG ILE ALA LEU ALA LEU PRO GLN GLU GLY
SEQRES 17 C 394 GLY GLN SER ALA ALA GLY CYS TRP ARG ILE ALA ASP GLU
SEQRES 18 C 394 ILE GLN LYS ASN GLY THR LYS VAL GLU THR ALA HIS GLN
SEQRES 19 C 394 ILE VAL ASN GLY ASP SER TRP PHE SER THR ASP PHE SER
SEQRES 20 C 394 LYS TYR VAL ASP THR VAL PRO THR LEU PRO TRP ASP ASN
SEQRES 21 C 394 HIS MET LEU HIS ALA LEU TYR ALA TYR PRO PRO ARG GLY
SEQRES 22 C 394 LEU LEU ILE ILE GLU ASN THR ALA ILE ASP TYR LEU GLY
SEQRES 23 C 394 PRO THR SER ASN TYR HIS CYS ALA THR ALA GLY ARG LYS
SEQRES 24 C 394 VAL HIS GLU ALA LEU GLY VAL LYS ASP TYR PHE GLY PHE
SEQRES 25 C 394 SER GLN ASN SER HIS SER ASP HIS CYS GLY PHE PRO LYS
SEQRES 26 C 394 ALA GLN GLN PRO GLU LEU THR ALA PHE ILE GLU ARG PHE
SEQRES 27 C 394 LEU LEU ALA LYS ASP THR LYS THR ASP VAL TRP LYS THR
SEQRES 28 C 394 ASP GLY LYS PHE THR ILE ASP GLU ARG ARG TRP ILE ASP
SEQRES 29 C 394 TRP ALA VAL PRO SER LEU SER GLY LEU GLU GLN LYS LEU
SEQRES 30 C 394 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 31 C 394 HIS HIS HIS HIS
SEQRES 1 D 394 GLN ALA PRO SER CYS PRO ASN LEU PRO ALA SER ILE ASN
SEQRES 2 D 394 TYR ALA ALA ASN PRO LYS LEU PRO ASP PRO PHE LEU ALA
SEQRES 3 D 394 LEU SER GLY THR ARG LEU SER LYS LYS ASP GLN TRP PRO
SEQRES 4 D 394 CYS ARG LYS GLU GLU ILE ARG GLN LEU PHE GLN ARG TYR
SEQRES 5 D 394 SER TYR GLY THR PHE PRO PRO ARG PRO GLU SER VAL THR
SEQRES 6 D 394 ALA ALA MET SER GLY ASN ALA LEU LYS ILE THR VAL SER
SEQRES 7 D 394 GLU GLY SER LYS SER MET SER PHE SER VAL ASN ILE LYS
SEQRES 8 D 394 LEU PRO SER SER GLY ALA ALA PRO TYR PRO ALA ILE ILE
SEQRES 9 D 394 ALA TYR GLY SER ALA SER LEU PRO ILE PRO ASN THR VAL
SEQRES 10 D 394 ALA THR ILE THR TYR GLN ASN PHE GLU MET ALA ALA ASP
SEQRES 11 D 394 ASN GLY ARG GLY LYS GLY LYS PHE TYR GLU PHE TYR GLY
SEQRES 12 D 394 SER ASN HIS ASN ALA GLY GLY MET ILE ALA ALA ALA TRP
SEQRES 13 D 394 GLY VAL ASP ARG ILE ILE ASP ALA LEU GLU MET THR PRO
SEQRES 14 D 394 ALA ALA LYS ILE ASP PRO LYS ARG VAL GLY VAL THR GLY
SEQRES 15 D 394 CYS SER ARG ASN GLY LYS GLY SER MET ILE ALA GLY ALA
SEQRES 16 D 394 PHE VAL ASP ARG ILE ALA LEU ALA LEU PRO GLN GLU GLY
SEQRES 17 D 394 GLY GLN SER ALA ALA GLY CYS TRP ARG ILE ALA ASP GLU
SEQRES 18 D 394 ILE GLN LYS ASN GLY THR LYS VAL GLU THR ALA HIS GLN
SEQRES 19 D 394 ILE VAL ASN GLY ASP SER TRP PHE SER THR ASP PHE SER
SEQRES 20 D 394 LYS TYR VAL ASP THR VAL PRO THR LEU PRO TRP ASP ASN
SEQRES 21 D 394 HIS MET LEU HIS ALA LEU TYR ALA TYR PRO PRO ARG GLY
SEQRES 22 D 394 LEU LEU ILE ILE GLU ASN THR ALA ILE ASP TYR LEU GLY
SEQRES 23 D 394 PRO THR SER ASN TYR HIS CYS ALA THR ALA GLY ARG LYS
SEQRES 24 D 394 VAL HIS GLU ALA LEU GLY VAL LYS ASP TYR PHE GLY PHE
SEQRES 25 D 394 SER GLN ASN SER HIS SER ASP HIS CYS GLY PHE PRO LYS
SEQRES 26 D 394 ALA GLN GLN PRO GLU LEU THR ALA PHE ILE GLU ARG PHE
SEQRES 27 D 394 LEU LEU ALA LYS ASP THR LYS THR ASP VAL TRP LYS THR
SEQRES 28 D 394 ASP GLY LYS PHE THR ILE ASP GLU ARG ARG TRP ILE ASP
SEQRES 29 D 394 TRP ALA VAL PRO SER LEU SER GLY LEU GLU GLN LYS LEU
SEQRES 30 D 394 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 31 D 394 HIS HIS HIS HIS
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET MAN F 4 11
HET MAN F 5 11
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET MAN G 4 11
HET MAN G 5 11
HET MAN G 6 11
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET MAN H 4 11
HET MAN H 5 11
HET FMT A 501 3
HET FMT D 501 3
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FMT FORMIC ACID
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
FORMUL 5 NAG 8(C8 H15 N O6)
FORMUL 5 BMA 4(C6 H12 O6)
FORMUL 5 MAN 8(C6 H12 O6)
FORMUL 9 FMT 2(C H2 O2)
FORMUL 11 HOH *303(H2 O)
HELIX 1 AA1 LYS A 50 ASP A 52 5 3
HELIX 2 AA2 GLN A 53 SER A 69 1 17
HELIX 3 AA3 GLN A 139 ALA A 144 1 6
HELIX 4 AA4 GLY A 152 GLY A 159 1 8
HELIX 5 AA5 GLY A 165 THR A 184 1 20
HELIX 6 AA6 PRO A 185 ALA A 187 5 3
HELIX 7 AA7 SER A 200 VAL A 213 1 14
HELIX 8 AA8 CYS A 231 ASN A 241 1 11
HELIX 9 AA9 THR A 247 VAL A 252 1 6
HELIX 10 AB1 SER A 259 TYR A 265 5 7
HELIX 11 AB2 THR A 268 LEU A 272 5 5
HELIX 12 AB3 ASN A 276 LEU A 282 1 7
HELIX 13 AB4 TYR A 283 TYR A 285 5 3
HELIX 14 AB5 ILE A 298 LEU A 301 5 4
HELIX 15 AB6 GLY A 302 LEU A 320 1 19
HELIX 16 AB7 VAL A 322 ASP A 324 5 3
HELIX 17 AB8 PRO A 340 ALA A 342 5 3
HELIX 18 AB9 GLN A 343 LEU A 355 1 13
HELIX 19 AC1 LYS B 50 ASP B 52 5 3
HELIX 20 AC2 GLN B 53 SER B 69 1 17
HELIX 21 AC3 GLN B 139 ALA B 144 1 6
HELIX 22 AC4 GLY B 152 GLY B 159 1 8
HELIX 23 AC5 GLY B 165 THR B 184 1 20
HELIX 24 AC6 PRO B 185 ALA B 187 5 3
HELIX 25 AC7 SER B 200 VAL B 213 1 14
HELIX 26 AC8 CYS B 231 ASN B 241 1 11
HELIX 27 AC9 THR B 247 VAL B 252 1 6
HELIX 28 AD1 SER B 259 TYR B 265 5 7
HELIX 29 AD2 THR B 268 LEU B 272 5 5
HELIX 30 AD3 ASN B 276 LEU B 282 1 7
HELIX 31 AD4 TYR B 283 TYR B 285 5 3
HELIX 32 AD5 ILE B 298 LEU B 301 5 4
HELIX 33 AD6 GLY B 302 LEU B 320 1 19
HELIX 34 AD7 VAL B 322 ASP B 324 5 3
HELIX 35 AD8 PRO B 340 ALA B 342 5 3
HELIX 36 AD9 GLN B 343 LEU B 355 1 13
HELIX 37 AE1 LYS C 50 ASP C 52 5 3
HELIX 38 AE2 GLN C 53 SER C 69 1 17
HELIX 39 AE3 GLN C 139 ALA C 144 1 6
HELIX 40 AE4 GLY C 152 GLY C 159 1 8
HELIX 41 AE5 GLY C 165 THR C 184 1 20
HELIX 42 AE6 PRO C 185 ALA C 187 5 3
HELIX 43 AE7 SER C 200 VAL C 213 1 14
HELIX 44 AE8 CYS C 231 ASN C 241 1 11
HELIX 45 AE9 THR C 247 VAL C 252 1 6
HELIX 46 AF1 SER C 259 TYR C 265 5 7
HELIX 47 AF2 THR C 268 LEU C 272 5 5
HELIX 48 AF3 ASN C 276 LEU C 282 1 7
HELIX 49 AF4 TYR C 283 TYR C 285 5 3
HELIX 50 AF5 ILE C 298 LEU C 301 5 4
HELIX 51 AF6 GLY C 302 LEU C 320 1 19
HELIX 52 AF7 VAL C 322 ASP C 324 5 3
HELIX 53 AF8 PRO C 340 ALA C 342 5 3
HELIX 54 AF9 GLN C 343 LEU C 355 1 13
HELIX 55 AG1 LYS D 50 ASP D 52 5 3
HELIX 56 AG2 GLN D 53 SER D 69 1 17
HELIX 57 AG3 GLN D 139 ALA D 144 1 6
HELIX 58 AG4 GLY D 152 GLY D 159 1 8
HELIX 59 AG5 GLY D 165 THR D 184 1 20
HELIX 60 AG6 PRO D 185 ALA D 187 5 3
HELIX 61 AG7 SER D 200 VAL D 213 1 14
HELIX 62 AG8 CYS D 231 ASN D 241 1 11
HELIX 63 AG9 THR D 247 VAL D 252 1 6
HELIX 64 AH1 SER D 259 TYR D 265 5 7
HELIX 65 AH2 THR D 268 LEU D 272 5 5
HELIX 66 AH3 ASN D 276 LEU D 282 1 7
HELIX 67 AH4 TYR D 283 TYR D 285 5 3
HELIX 68 AH5 ILE D 298 LEU D 301 5 4
HELIX 69 AH6 GLY D 302 LEU D 320 1 19
HELIX 70 AH7 VAL D 322 ASP D 324 5 3
HELIX 71 AH8 PRO D 340 ALA D 342 5 3
HELIX 72 AH9 GLN D 343 LEU D 355 1 13
SHEET 1 AA110 SER A 79 SER A 85 0
SHEET 2 AA110 ALA A 88 GLU A 95 -1 O THR A 92 N THR A 81
SHEET 3 AA110 LYS A 98 LYS A 107 -1 O PHE A 102 N ILE A 91
SHEET 4 AA110 ALA A 134 TYR A 138 -1 O THR A 137 N ASN A 105
SHEET 5 AA110 TYR A 116 TYR A 122 1 N ALA A 121 O ILE A 136
SHEET 6 AA110 ILE A 189 CYS A 199 1 O GLY A 195 N ALA A 118
SHEET 7 AA110 LEU A 218 GLN A 222 1 O LEU A 220 N VAL A 196
SHEET 8 AA110 GLY A 289 ASN A 295 1 O ILE A 293 N PRO A 221
SHEET 9 AA110 PHE A 326 ASN A 331 1 O GLY A 327 N LEU A 290
SHEET 10 AA110 TRP A 365 THR A 367 1 O LYS A 366 N PHE A 328
SHEET 1 AA210 SER B 79 SER B 85 0
SHEET 2 AA210 ALA B 88 GLU B 95 -1 O THR B 92 N THR B 81
SHEET 3 AA210 LYS B 98 LYS B 107 -1 O PHE B 102 N ILE B 91
SHEET 4 AA210 ALA B 134 TYR B 138 -1 O THR B 137 N ASN B 105
SHEET 5 AA210 TYR B 116 TYR B 122 1 N ALA B 121 O ILE B 136
SHEET 6 AA210 ILE B 189 CYS B 199 1 O GLY B 195 N ALA B 118
SHEET 7 AA210 LEU B 218 GLN B 222 1 O LEU B 220 N VAL B 196
SHEET 8 AA210 GLY B 289 GLU B 294 1 O ILE B 293 N PRO B 221
SHEET 9 AA210 PHE B 326 GLN B 330 1 O GLY B 327 N LEU B 290
SHEET 10 AA210 TRP B 365 THR B 367 1 O LYS B 366 N PHE B 328
SHEET 1 AA310 SER C 79 SER C 85 0
SHEET 2 AA310 ALA C 88 GLU C 95 -1 O THR C 92 N THR C 81
SHEET 3 AA310 LYS C 98 LYS C 107 -1 O PHE C 102 N ILE C 91
SHEET 4 AA310 ALA C 134 TYR C 138 -1 O THR C 137 N ASN C 105
SHEET 5 AA310 TYR C 116 TYR C 122 1 N ALA C 121 O ILE C 136
SHEET 6 AA310 ILE C 189 CYS C 199 1 O GLY C 195 N ALA C 118
SHEET 7 AA310 LEU C 218 GLN C 222 1 O LEU C 220 N VAL C 196
SHEET 8 AA310 GLY C 289 GLU C 294 1 O ILE C 293 N PRO C 221
SHEET 9 AA310 PHE C 326 GLN C 330 1 O GLY C 327 N LEU C 290
SHEET 10 AA310 TRP C 365 THR C 367 1 O LYS C 366 N PHE C 328
SHEET 1 AA410 SER D 79 SER D 85 0
SHEET 2 AA410 ALA D 88 GLU D 95 -1 O THR D 92 N THR D 81
SHEET 3 AA410 LYS D 98 LYS D 107 -1 O PHE D 102 N ILE D 91
SHEET 4 AA410 ALA D 134 TYR D 138 -1 O THR D 137 N ASN D 105
SHEET 5 AA410 TYR D 116 TYR D 122 1 N ALA D 121 O ILE D 136
SHEET 6 AA410 ILE D 189 CYS D 199 1 O GLY D 195 N ALA D 118
SHEET 7 AA410 LEU D 218 GLN D 222 1 O LEU D 220 N VAL D 196
SHEET 8 AA410 GLY D 289 GLU D 294 1 O ILE D 293 N PRO D 221
SHEET 9 AA410 PHE D 326 GLN D 330 1 O GLY D 327 N LEU D 290
SHEET 10 AA410 TRP D 365 THR D 367 1 O LYS D 366 N PHE D 328
SSBOND 1 CYS A 21 CYS A 56 1555 1555 2.08
SSBOND 2 CYS A 199 CYS A 337 1555 1555 2.04
SSBOND 3 CYS A 231 CYS A 309 1555 1555 2.06
SSBOND 4 CYS B 21 CYS B 56 1555 1555 2.09
SSBOND 5 CYS B 199 CYS B 337 1555 1555 2.05
SSBOND 6 CYS B 231 CYS B 309 1555 1555 2.05
SSBOND 7 CYS C 21 CYS C 56 1555 1555 2.08
SSBOND 8 CYS C 199 CYS C 337 1555 1555 2.05
SSBOND 9 CYS C 231 CYS C 309 1555 1555 2.08
SSBOND 10 CYS D 21 CYS D 56 1555 1555 2.07
SSBOND 11 CYS D 199 CYS D 337 1555 1555 2.04
SSBOND 12 CYS D 231 CYS D 309 1555 1555 2.07
LINK ND2 ASN A 241 C1 NAG E 1 1555 1555 1.42
LINK ND2 ASN B 241 C1 NAG F 1 1555 1555 1.43
LINK ND2 ASN C 241 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN D 241 C1 NAG H 1 1555 1555 1.41
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.35
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.33
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.43
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.36
LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.34
LINK O6 BMA F 3 C1 MAN F 5 1555 1555 1.33
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.43
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.34
LINK O6 BMA G 3 C1 MAN G 4 1555 1555 1.34
LINK O3 BMA G 3 C1 MAN G 6 1555 1555 1.34
LINK O3 MAN G 4 C1 MAN G 5 1555 1555 1.34
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.42
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.35
LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.33
LINK O6 BMA H 3 C1 MAN H 5 1555 1555 1.34
CISPEP 1 ALA A 114 PRO A 115 0 -10.22
CISPEP 2 TYR A 285 PRO A 286 0 -7.45
CISPEP 3 ALA B 114 PRO B 115 0 -11.19
CISPEP 4 TYR B 285 PRO B 286 0 -6.95
CISPEP 5 ALA C 114 PRO C 115 0 -9.71
CISPEP 6 TYR C 285 PRO C 286 0 -7.08
CISPEP 7 ALA D 114 PRO D 115 0 -11.63
CISPEP 8 TYR D 285 PRO D 286 0 -6.40
CRYST1 70.740 79.570 86.010 113.32 98.53 94.44 P 1 4
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 0.014136 0.001098 0.002827 0.00000
SCALE2 0.000000 0.012605 0.005719 0.00000
SCALE3 0.000000 0.000000 0.012910 0.00000
TER 2854 LEU A 389
TER 5721 LEU B 389
TER 8569 LEU C 389
TER 11411 LEU D 389
MASTER 494 0 22 72 40 0 0 611935 4 278 124
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