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HEADER HYDROLASE 28-NOV-11 3UUE
TITLE CRYSTAL STRUCTURE OF MONO- AND DIACYLGLYCEROL LIPASE FROM MALASSEZIA
TITLE 2 GLOBOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIP1, SECRETORY LIPASE (FAMILY 3);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 26-304;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MALASSEZIA GLOBOSA;
SOURCE 3 ORGANISM_COMMON: DANDRUFF-ASSOCIATED FUNGUS;
SOURCE 4 ORGANISM_TAXID: 425265;
SOURCE 5 STRAIN: ATCC MYA-4612 / CBS 7966;
SOURCE 6 GENE: MGL_0797;
SOURCE 7 EXPRESSION_SYSTEM: KOMAGATAELLA PHAFFII;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 460519
KEYWDS LID-DOMAIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.XU,J.XU,S.HOU,J.LIU
REVDAT 1 25-APR-12 3UUE 0
JRNL AUTH T.XU,L.LIU,S.HOU,J.XU,B.YANG,Y.WANG,J.LIU
JRNL TITL CRYSTAL STRUCTURE OF A MONO- AND DIACYLGLYCEROL LIPASE FROM
JRNL TITL 2 MALASSEZIA GLOBOSA REVEALS A NOVEL LID CONFORMATION AND
JRNL TITL 3 INSIGHTS INTO THE SUBSTRATE SPECIFICITY.
JRNL REF J.STRUCT.BIOL. 2012
JRNL REFN ESSN 1095-8657
JRNL PMID 22484238
JRNL DOI 10.1016/J.JSB.2012.03.006
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 49385
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2635
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2605
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2191
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 97
REMARK 3 SOLVENT ATOMS : 282
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.14000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.062
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.064
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.036
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.908
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2387 ; 0.018 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3248 ; 1.875 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 290 ; 6.785 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 111 ;31.156 ;24.414
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 370 ;11.057 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;16.654 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 357 ; 0.131 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1812 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : NULL
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
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: U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3UUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-11.
REMARK 100 THE RCSB ID CODE IS RCSB069220.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52050
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.31700
REMARK 200 R SYM FOR SHELL (I) : 0.31700
REMARK 200 FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX MR_ROSSETA
REMARK 200 STARTING MODEL: 3UUF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 1000, 10% PEG 8000, PH 8.0,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 44.37200
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 O HOH A 815 O HOH A 821 1.94
REMARK 500 OG SER A 105 OD1 ASN A 107 2.11
REMARK 500 OD2 ASP A 218 O HOH A 871 2.14
REMARK 500 O HOH A 843 O HOH A 859 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O2 GOL A 510 O HOH A 717 1655 2.06
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 HIS A 304 CG HIS A 304 CD2 0.056
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. = 4.3 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH2 ANGL. DEV. = -4.0 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 SER A 171 -128.33 58.79
REMARK 500 ASP A 245 138.26 84.68
REMARK 500 ASN A 253 -0.18 71.95
REMARK 500 PHE A 276 53.80 -118.50
REMARK 500 GLN A 282 40.60 -109.56
REMARK 500 ILE A 290 73.31 -110.65
REMARK 500 ALA A 292 -143.78 65.04
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 MAN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES A 501-505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UUF RELATED DB: PDB
DBREF 3UUE A 26 304 UNP A8PUY1 A8PUY1_MALGO 26 304
SEQRES 1 A 279 GLY ARG GLY GLY SER SER THR ASP GLN PRO VAL ALA ASN
SEQRES 2 A 279 PRO TYR ASN THR LYS GLU ILE SER LEU ALA ALA GLY LEU
SEQRES 3 A 279 VAL GLN GLN THR TYR CYS ASP SER THR GLU ASN GLY LEU
SEQRES 4 A 279 LYS ILE GLY ASP SER GLU LEU LEU TYR THR MET GLY GLU
SEQRES 5 A 279 GLY TYR ALA ARG GLN ARG VAL ASN ILE TYR HIS SER PRO
SEQRES 6 A 279 SER LEU GLY ILE ALA VAL ALA ILE GLU GLY THR ASN LEU
SEQRES 7 A 279 PHE SER LEU ASN SER ASP LEU HIS ASP ALA LYS PHE TRP
SEQRES 8 A 279 GLN GLU ASP PRO ASN GLU ARG TYR ILE GLN TYR TYR PRO
SEQRES 9 A 279 LYS GLY THR LYS LEU MET HIS GLY PHE GLN GLN ALA TYR
SEQRES 10 A 279 ASN ASP LEU MET ASP ASP ILE PHE THR ALA VAL LYS LYS
SEQRES 11 A 279 TYR LYS LYS GLU LYS ASN GLU LYS ARG VAL THR VAL ILE
SEQRES 12 A 279 GLY HIS SER LEU GLY ALA ALA MET GLY LEU LEU CYS ALA
SEQRES 13 A 279 MET ASP ILE GLU LEU ARG MET ASP GLY GLY LEU TYR LYS
SEQRES 14 A 279 THR TYR LEU PHE GLY LEU PRO ARG LEU GLY ASN PRO THR
SEQRES 15 A 279 PHE ALA SER PHE VAL ASP GLN LYS ILE GLY ASP LYS PHE
SEQRES 16 A 279 HIS SER ILE ILE ASN GLY ARG ASP TRP VAL PRO THR VAL
SEQRES 17 A 279 PRO PRO ARG ALA LEU GLY TYR GLN HIS PRO SER ASP TYR
SEQRES 18 A 279 VAL TRP ILE TYR PRO GLY ASN SER THR SER ALA LYS LEU
SEQRES 19 A 279 TYR PRO GLY GLN GLU ASN VAL HIS GLY ILE LEU THR VAL
SEQRES 20 A 279 ALA ARG GLU PHE ASN PHE ASP ASP HIS GLN GLY ILE TYR
SEQRES 21 A 279 PHE HIS THR GLN ILE GLY ALA VAL MET GLY GLU CYS PRO
SEQRES 22 A 279 ALA GLN VAL GLY ALA HIS
MODRES 3UUE THR A 32 THR GLYCOSYLATION SITE
MODRES 3UUE ASN A 253 ASN GLYCOSYLATION SITE
HET NAG A 501 14
HET NAG A 502 14
HET BMA A 503 11
HET MAN A 504 11
HET MAN A 505 11
HET MAN A 506 11
HET CL A 507 1
HET GOL A 508 6
HET GOL A 509 6
HET GOL A 510 6
HET GOL A 511 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 2 MAN 3(C6 H12 O6)
FORMUL 4 CL CL 1-
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *282(H2 O)
HELIX 1 1 ASN A 41 GLN A 54 1 14
HELIX 2 2 THR A 55 CYS A 57 5 3
HELIX 3 3 ASP A 112 PHE A 115 5 4
HELIX 4 4 TYR A 124 TYR A 128 5 5
HELIX 5 5 HIS A 136 ASN A 161 1 26
HELIX 6 6 SER A 171 MET A 188 1 18
HELIX 7 7 ASN A 205 GLY A 217 1 13
HELIX 8 8 TRP A 229 VAL A 233 5 5
HELIX 9 9 PRO A 235 GLY A 239 5 5
HELIX 10 10 GLY A 268 VAL A 272 5 5
HELIX 11 11 GLY A 291 GLY A 295 5 5
SHEET 1 A10 VAL A 36 ALA A 37 0
SHEET 2 A10 ALA A 257 TYR A 260 -1 O LEU A 259 N VAL A 36
SHEET 3 A10 TYR A 246 ILE A 249 -1 N TYR A 246 O TYR A 260
SHEET 4 A10 PHE A 220 ASN A 225 1 N SER A 222 O VAL A 247
SHEET 5 A10 LYS A 194 PHE A 198 1 N LEU A 197 O ILE A 223
SHEET 6 A10 VAL A 165 HIS A 170 1 N GLY A 169 O PHE A 198
SHEET 7 A10 GLY A 93 ILE A 98 1 N VAL A 96 O THR A 166
SHEET 8 A10 VAL A 84 SER A 89 -1 N ASN A 85 O ALA A 97
SHEET 9 A10 SER A 69 MET A 75 -1 N LEU A 72 O ILE A 86
SHEET 10 A10 LYS A 65 ILE A 66 -1 N ILE A 66 O SER A 69
SHEET 1 B 2 GLN A 117 GLU A 118 0
SHEET 2 B 2 LEU A 134 MET A 135 -1 O LEU A 134 N GLU A 118
SHEET 1 C 2 ILE A 284 TYR A 285 0
SHEET 2 C 2 THR A 288 GLN A 289 -1 O THR A 288 N TYR A 285
SSBOND 1 CYS A 57 CYS A 297 1555 1555 2.05
LINK O4 NAG A 502 C1 BMA A 503 1555 1555 1.38
LINK O4 NAG A 501 C1 NAG A 502 1555 1555 1.43
LINK O6 BMA A 503 C1 MAN A 504 1555 1555 1.43
LINK O3 MAN A 504 C1 MAN A 505 1555 1555 1.43
LINK OG1 THR A 32 C1 MAN A 506 1555 1555 1.44
LINK ND2 ASN A 253 C1 NAG A 501 1555 1555 1.44
CISPEP 1 VAL A 233 PRO A 234 0 -12.50
CISPEP 2 TYR A 250 PRO A 251 0 2.45
CISPEP 3 CYS A 297 PRO A 298 0 2.88
SITE 1 AC1 8 THR A 32 ASP A 33 HIS A 111 ASP A 112
SITE 2 AC1 8 TRP A 116 HOH A 728 HOH A 735 HOH A 774
SITE 1 AC2 5 GLU A 77 GLY A 78 TYR A 79 ALA A 80
SITE 2 AC2 5 ARG A 81
SITE 1 AC3 5 TRP A 248 TYR A 250 TYR A 260 HOH A 630
SITE 2 AC3 5 HOH A 880
SITE 1 AC4 4 GLY A 26 GLY A 29 GLY A 262 GLN A 263
SITE 1 AC5 10 GLN A 34 VAL A 36 PHE A 104 SER A 105
SITE 2 AC5 10 SER A 108 ASP A 109 ASP A 112 LYS A 114
SITE 3 AC5 10 PHE A 115 HOH A 717
SITE 1 AC6 2 TRP A 116 GLN A 117
SITE 1 AC7 22 GLU A 122 ARG A 123 ASN A 143 ASP A 144
SITE 2 AC7 22 LEU A 145 MET A 146 ASP A 147 ASP A 148
SITE 3 AC7 22 ASN A 253 ASP A 279 ASP A 280 GLN A 282
SITE 4 AC7 22 GLY A 283 GLN A 289 GLY A 291 MET A 294
SITE 5 AC7 22 HOH A 609 HOH A 631 HOH A 759 HOH A 823
SITE 6 AC7 22 HOH A 826 HOH A 830
CRYST1 39.807 88.744 45.132 90.00 106.04 90.00 P 1 21 1 2
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 0.025121 0.000000 0.007222 0.00000
SCALE2 0.000000 0.011268 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023055 0.00000
TER 2225 HIS A 304
MASTER 348 0 11 11 14 0 17 6 2570 1 100 22
END |