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HEADER HYDROLASE 09-SEP-16 5GW8
TITLE CRYSTAL STRUCTURE OF A PUTATIVE DAG-LIKE LIPASE (MGMDL2) FROM
TITLE 2 MALASSEZIA GLOBOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL SECRETORY LIPASE (FAMILY 3);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MALASSEZIA GLOBOSA (STRAIN ATCC MYA-4612 / CBS
SOURCE 3 7966);
SOURCE 4 ORGANISM_COMMON: DANDRUFF-ASSOCIATED FUNGUS;
SOURCE 5 ORGANISM_TAXID: 425265;
SOURCE 6 STRAIN: ATCC MYA-4612 / CBS 7966;
SOURCE 7 GENE: MGL_0799;
SOURCE 8 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: X33
KEYWDS DAG-LIKE LIPASE, N-LINKED GLYCOSYLATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.XU,H.XU,J.LIU
REVDAT 1 27-SEP-17 5GW8 0
JRNL AUTH J.XU,H.XU,J.LIU
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE DAG-LIKE LIPASE (MGMDL2)
JRNL TITL 2 FROM MALASSEZIA GLOBOSA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 48369
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2470
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3505
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 188
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4491
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 179
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.12000
REMARK 3 B22 (A**2) : -1.21000
REMARK 3 B33 (A**2) : -0.91000
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): 0.156
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.380
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4749 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4383 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6452 ; 1.605 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10057 ; 1.012 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 572 ; 6.744 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 232 ;32.888 ;23.966
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 720 ;14.214 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;19.872 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 698 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5437 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1152 ; 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): 2286 ; 0.824 ; 1.686
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2287 ; 0.824 ; 1.688
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2850 ; 1.385 ; 2.514
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2851 ; 1.385 ; 2.514
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2463 ; 1.302 ; 1.940
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2460 ; 1.302 ; 1.936
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3601 ; 2.078 ; 2.852
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5403 ; 4.654 ;14.399
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5404 ; 4.653 ;14.407
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 : 2
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 21 A 304
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3951 30.0703 -33.0745
REMARK 3 T TENSOR
REMARK 3 T11: 0.2719 T22: 0.0273
REMARK 3 T33: 0.0132 T12: 0.0338
REMARK 3 T13: -0.0377 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 1.1095 L22: 2.1322
REMARK 3 L33: 2.9543 L12: 0.0446
REMARK 3 L13: -0.3641 L23: -1.0360
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: 0.0692 S13: -0.0045
REMARK 3 S21: -0.0814 S22: -0.0793 S23: -0.0634
REMARK 3 S31: -0.4300 S32: -0.0448 S33: 0.0769
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 19 B 304
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6995 11.0228 6.0082
REMARK 3 T TENSOR
REMARK 3 T11: 0.0444 T22: 0.0561
REMARK 3 T33: 0.0404 T12: -0.0007
REMARK 3 T13: -0.0160 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.8093 L22: 1.8840
REMARK 3 L33: 3.7482 L12: -0.0829
REMARK 3 L13: 0.0238 L23: -0.7622
REMARK 3 S TENSOR
REMARK 3 S11: -0.1040 S12: -0.0764 S13: -0.0604
REMARK 3 S21: 0.1194 S22: -0.0208 S23: -0.0339
REMARK 3 S31: -0.2127 S32: -0.0552 S33: 0.1248
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5GW8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1300001576.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
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 : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50908
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 67.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.68500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 3UUE
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS
REMARK 200 AND I_PLUS/MINUS COLUMNS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% (V/V) TACSIMATE (PH 6.0), 20% PEG
REMARK 280 5000, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 38.48500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.43500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.16000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.43500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.48500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.16000
REMARK 290 SMTRY3 4 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 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: 5450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 GLY A 19
REMARK 465 ALA A 20
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 NH1 ARG A 214 O HOH A 501 2.19
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 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 83 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP B 77 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG B 83 NE - CZ - NH2 ANGL. DEV. = 3.3 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 ASN A 79 -73.29 -104.84
REMARK 500 THR A 101 -159.50 -150.52
REMARK 500 ASP A 112 -118.89 53.77
REMARK 500 SER A 171 -137.03 68.35
REMARK 500 ASP A 190 -17.85 77.16
REMARK 500 ASN A 245 68.47 72.82
REMARK 500 GLU A 275 50.18 -117.96
REMARK 500 ASN B 79 -78.92 -111.53
REMARK 500 ASP B 112 -118.87 52.84
REMARK 500 SER B 171 -135.75 71.63
REMARK 500 ASP B 190 -17.97 79.39
REMARK 500 ASN B 245 73.79 69.51
REMARK 500 THR B 271 4.91 -63.54
REMARK 500 VAL B 272 14.77 -145.15
REMARK 500 LEU B 294 -54.78 -131.65
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 MLA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLA B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound
REMARK 800 to ASN A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 402 through NAG A 403 bound to ASN A 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 401 bound
REMARK 800 to ASN B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 402 through NAG B 403 bound to ASN B 253
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GW0 RELATED DB: PDB
REMARK 900 RELATED ID: 5GW1 RELATED DB: PDB
DBREF 5GW8 A 19 304 UNP A8PUY5 A8PUY5_MALGO 19 304
DBREF 5GW8 B 19 304 UNP A8PUY5 A8PUY5_MALGO 19 304
SEQRES 1 A 286 GLY ALA LEU ILE GLU HIS HIS ALA ALA SER SER THR ASP
SEQRES 2 A 286 GLN PRO VAL ASP VAL PRO TYR ASN LEU ASP MET PHE SER
SEQRES 3 A 286 GLN ALA ALA VAL LEU ALA GLN GLU THR TYR CYS GLY GLU
SEQRES 4 A 286 GLN ALA HIS ASP TYR GLY LEU LYS LEU GLY ASP ALA THR
SEQRES 5 A 286 LEU LEU TRP THR ALA GLY ASP GLY ASN VAL ARG GLN ARG
SEQRES 6 A 286 VAL ASN LEU TYR GLN SER ASP SER LEU GLY ILE ALA VAL
SEQRES 7 A 286 ALA ILE GLN GLY THR ASN THR SER SER LEU ARG SER ASP
SEQRES 8 A 286 LEU HIS ASP ALA GLN LEU ARG PRO VAL ASP PRO ASP SER
SEQRES 9 A 286 ARG TYR ARG ARG PHE LEU PRO GLN GLY THR LYS VAL MET
SEQRES 10 A 286 ASN GLY PHE GLN LYS GLY TYR THR ASP LEU VAL ASP ASP
SEQRES 11 A 286 ILE PHE ASP HIS VAL LYS LYS PHE LYS GLN GLU LYS ASN
SEQRES 12 A 286 GLU SER ARG VAL THR VAL ILE GLY HIS SER LEU GLY ALA
SEQRES 13 A 286 ALA ILE GLY LEU LEU ALA SER LEU ASP ILE ASN LEU ARG
SEQRES 14 A 286 LEU GLU ASP GLY LEU PHE LYS SER TYR LEU PHE GLY LEU
SEQRES 15 A 286 PRO ARG VAL GLY ASN PRO ILE PHE ALA ASN PHE VAL ASP
SEQRES 16 A 286 ARG LYS ILE GLY ASP LYS LEU HIS TRP VAL VAL ASN GLY
SEQRES 17 A 286 ARG ASP TRP VAL PRO THR VAL PRO PRO ARG ALA LEU GLY
SEQRES 18 A 286 TYR GLN HIS PRO SER ASN TYR VAL TRP ILE TYR PRO ALA
SEQRES 19 A 286 ASN SER THR ASN TRP LYS LEU TYR PRO GLY GLN GLU ASN
SEQRES 20 A 286 VAL HIS GLY MET LEU THR VAL ALA ARG GLU PHE ASN PHE
SEQRES 21 A 286 ASP ASP HIS GLU GLY ILE TYR PHE HIS THR GLN ILE GLY
SEQRES 22 A 286 ALA SER LEU GLY LYS CYS PRO ALA VAL LEU GLY GLY TYR
SEQRES 1 B 286 GLY ALA LEU ILE GLU HIS HIS ALA ALA SER SER THR ASP
SEQRES 2 B 286 GLN PRO VAL ASP VAL PRO TYR ASN LEU ASP MET PHE SER
SEQRES 3 B 286 GLN ALA ALA VAL LEU ALA GLN GLU THR TYR CYS GLY GLU
SEQRES 4 B 286 GLN ALA HIS ASP TYR GLY LEU LYS LEU GLY ASP ALA THR
SEQRES 5 B 286 LEU LEU TRP THR ALA GLY ASP GLY ASN VAL ARG GLN ARG
SEQRES 6 B 286 VAL ASN LEU TYR GLN SER ASP SER LEU GLY ILE ALA VAL
SEQRES 7 B 286 ALA ILE GLN GLY THR ASN THR SER SER LEU ARG SER ASP
SEQRES 8 B 286 LEU HIS ASP ALA GLN LEU ARG PRO VAL ASP PRO ASP SER
SEQRES 9 B 286 ARG TYR ARG ARG PHE LEU PRO GLN GLY THR LYS VAL MET
SEQRES 10 B 286 ASN GLY PHE GLN LYS GLY TYR THR ASP LEU VAL ASP ASP
SEQRES 11 B 286 ILE PHE ASP HIS VAL LYS LYS PHE LYS GLN GLU LYS ASN
SEQRES 12 B 286 GLU SER ARG VAL THR VAL ILE GLY HIS SER LEU GLY ALA
SEQRES 13 B 286 ALA ILE GLY LEU LEU ALA SER LEU ASP ILE ASN LEU ARG
SEQRES 14 B 286 LEU GLU ASP GLY LEU PHE LYS SER TYR LEU PHE GLY LEU
SEQRES 15 B 286 PRO ARG VAL GLY ASN PRO ILE PHE ALA ASN PHE VAL ASP
SEQRES 16 B 286 ARG LYS ILE GLY ASP LYS LEU HIS TRP VAL VAL ASN GLY
SEQRES 17 B 286 ARG ASP TRP VAL PRO THR VAL PRO PRO ARG ALA LEU GLY
SEQRES 18 B 286 TYR GLN HIS PRO SER ASN TYR VAL TRP ILE TYR PRO ALA
SEQRES 19 B 286 ASN SER THR ASN TRP LYS LEU TYR PRO GLY GLN GLU ASN
SEQRES 20 B 286 VAL HIS GLY MET LEU THR VAL ALA ARG GLU PHE ASN PHE
SEQRES 21 B 286 ASP ASP HIS GLU GLY ILE TYR PHE HIS THR GLN ILE GLY
SEQRES 22 B 286 ALA SER LEU GLY LYS CYS PRO ALA VAL LEU GLY GLY TYR
HET NAG A 401 14
HET NAG A 402 14
HET NAG A 403 14
HET MLA A 404 7
HET ACY A 405 4
HET FMT A 406 3
HET NAG B 401 14
HET NAG B 402 14
HET NAG B 403 14
HET GOL B 404 6
HET MLA B 405 7
HET ACY B 406 4
HET ACY B 407 4
HET ACY B 408 4
HET FMT B 409 3
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MLA MALONIC ACID
HETNAM ACY ACETIC ACID
HETNAM FMT FORMIC ACID
HETNAM GOL GLYCEROL
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METHANEDICARBOXYLIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 5 MLA 2(C3 H4 O4)
FORMUL 6 ACY 4(C2 H4 O2)
FORMUL 7 FMT 2(C H2 O2)
FORMUL 10 GOL C3 H8 O3
FORMUL 16 HOH *179(H2 O)
HELIX 1 AA1 ASN A 39 THR A 53 1 15
HELIX 2 AA2 ASN A 102 LEU A 110 1 9
HELIX 3 AA3 HIS A 111 LEU A 115 5 5
HELIX 4 AA4 TYR A 124 LEU A 128 5 5
HELIX 5 AA5 ASN A 136 ASP A 144 1 9
HELIX 6 AA6 LEU A 145 LYS A 160 1 16
HELIX 7 AA7 SER A 171 LEU A 188 1 18
HELIX 8 AA8 ASN A 205 GLY A 217 1 13
HELIX 9 AA9 TRP A 229 VAL A 233 5 5
HELIX 10 AB1 PRO A 235 GLY A 239 5 5
HELIX 11 AB2 GLY A 268 ALA A 273 5 6
HELIX 12 AB3 ASN B 39 THR B 53 1 15
HELIX 13 AB4 ASN B 102 LEU B 110 1 9
HELIX 14 AB5 HIS B 111 LEU B 115 5 5
HELIX 15 AB6 TYR B 124 LEU B 128 5 5
HELIX 16 AB7 ASN B 136 ASP B 144 1 9
HELIX 17 AB8 LEU B 145 ASN B 161 1 17
HELIX 18 AB9 SER B 171 LEU B 188 1 18
HELIX 19 AC1 ASN B 205 GLY B 217 1 13
HELIX 20 AC2 TRP B 229 VAL B 233 5 5
HELIX 21 AC3 PRO B 235 GLY B 239 5 5
HELIX 22 AC4 GLY B 268 ALA B 273 5 6
SHEET 1 AA1 9 LYS A 65 LEU A 66 0
SHEET 2 AA1 9 ALA A 69 ALA A 75 -1 O ALA A 69 N LEU A 66
SHEET 3 AA1 9 VAL A 84 SER A 89 -1 O LEU A 86 N LEU A 72
SHEET 4 AA1 9 GLY A 93 ILE A 98 -1 O ALA A 97 N ASN A 85
SHEET 5 AA1 9 VAL A 165 HIS A 170 1 O THR A 166 N VAL A 96
SHEET 6 AA1 9 LYS A 194 PHE A 198 1 O TYR A 196 N VAL A 167
SHEET 7 AA1 9 LEU A 220 ASN A 225 1 O HIS A 221 N LEU A 197
SHEET 8 AA1 9 TYR A 246 ILE A 249 1 O ILE A 249 N VAL A 224
SHEET 9 AA1 9 TRP A 257 TYR A 260 -1 O TYR A 260 N TYR A 246
SHEET 1 AA2 2 PRO A 117 VAL A 118 0
SHEET 2 AA2 2 VAL A 134 MET A 135 -1 O VAL A 134 N VAL A 118
SHEET 1 AA3 2 GLY A 283 TYR A 285 0
SHEET 2 AA3 2 THR A 288 ILE A 290 -1 O THR A 288 N TYR A 285
SHEET 1 AA4 9 LYS B 65 LEU B 66 0
SHEET 2 AA4 9 ALA B 69 ALA B 75 -1 O ALA B 69 N LEU B 66
SHEET 3 AA4 9 VAL B 84 SER B 89 -1 O LEU B 86 N LEU B 72
SHEET 4 AA4 9 GLY B 93 ILE B 98 -1 O ALA B 97 N ASN B 85
SHEET 5 AA4 9 VAL B 165 HIS B 170 1 O ILE B 168 N VAL B 96
SHEET 6 AA4 9 LYS B 194 PHE B 198 1 O PHE B 198 N GLY B 169
SHEET 7 AA4 9 LEU B 220 ASN B 225 1 O HIS B 221 N LEU B 197
SHEET 8 AA4 9 TYR B 246 ILE B 249 1 O VAL B 247 N TRP B 222
SHEET 9 AA4 9 TRP B 257 TYR B 260 -1 O TYR B 260 N TYR B 246
SHEET 1 AA5 2 PRO B 117 VAL B 118 0
SHEET 2 AA5 2 VAL B 134 MET B 135 -1 O VAL B 134 N VAL B 118
SHEET 1 AA6 2 GLY B 283 TYR B 285 0
SHEET 2 AA6 2 THR B 288 ILE B 290 -1 O THR B 288 N TYR B 285
SSBOND 1 CYS A 55 CYS A 297 1555 1555 2.05
SSBOND 2 CYS B 55 CYS B 297 1555 1555 2.10
LINK ND2 ASN A 102 C1 NAG A 401 1555 1555 1.45
LINK ND2 ASN A 253 C1 NAG A 402 1555 1555 1.43
LINK ND2 ASN B 102 C1 NAG B 401 1555 1555 1.45
LINK ND2 ASN B 253 C1 NAG B 402 1555 1555 1.42
LINK O4 NAG A 402 C1 NAG A 403 1555 1555 1.44
LINK O4 NAG B 402 C1 NAG B 403 1555 1555 1.43
CISPEP 1 VAL A 233 PRO A 234 0 -14.24
CISPEP 2 TYR A 250 PRO A 251 0 1.30
CISPEP 3 CYS A 297 PRO A 298 0 -7.89
CISPEP 4 VAL B 233 PRO B 234 0 -10.46
CISPEP 5 TYR B 250 PRO B 251 0 0.78
CISPEP 6 CYS B 297 PRO B 298 0 -8.47
SITE 1 AC1 7 PRO A 235 ARG A 236 ALA A 237 ARG A 274
SITE 2 AC1 7 HOH A 559 ALA B 237 MLA B 405
SITE 1 AC2 5 TYR A 38 ASN A 39 LYS A 194 HIS A 221
SITE 2 AC2 5 HOH A 527
SITE 1 AC3 2 LYS A 154 ARG A 187
SITE 1 AC4 3 ALA B 75 GLY B 76 ARG B 81
SITE 1 AC5 8 ALA A 237 MLA A 404 PRO B 235 ARG B 236
SITE 2 AC5 8 ALA B 237 ARG B 274 HOH B 520 HOH B 525
SITE 1 AC6 2 GLN B 114 GLY B 137
SITE 1 AC7 5 TYR B 38 ASN B 39 LYS B 194 HIS B 221
SITE 2 AC7 5 HOH B 522
SITE 1 AC8 2 LYS B 154 ARG B 187
SITE 1 AC9 2 HIS B 24 ASN B 205
SITE 1 AD1 1 ASN A 102
SITE 1 AD2 6 ASN A 253 ASP A 279 ASP A 280 GLU A 282
SITE 2 AD2 6 SER A 293 LEU A 294
SITE 1 AD3 3 ASN B 102 SER B 105 SER B 293
SITE 1 AD4 6 ASN B 253 ASP B 279 ASP B 280 GLU B 282
SITE 2 AD4 6 LEU B 294 HOH B 531
CRYST1 76.970 82.320 116.870 90.00 90.00 90.00 P 21 21 21 8
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 0.012992 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012148 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008557 0.00000
TER 2250 TYR A 304
TER 4506 TYR B 304
MASTER 409 0 15 22 26 0 19 6 4796 2 134 44
END |