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HEADER HYDROLASE 28-NOV-11 3UUF
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 3UUF 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. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 10455
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 531
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 741
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 22
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2187
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.93000
REMARK 3 B22 (A**2) : -0.93000
REMARK 3 B33 (A**2) : 1.87000
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): 0.611
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.292
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.219
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.379
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2287 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3105 ; 1.840 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 277 ; 8.047 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 109 ;33.505 ;24.404
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 361 ;17.631 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;18.855 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 331 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1768 ; 0.009 ; 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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3UUF 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 RCSB069221.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.5
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 : 11015
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 18.952
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11400
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.50200
REMARK 200 R SYM FOR SHELL (I) : 0.50200
REMARK 200 FOR SHELL : 1.500
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: 3NGM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 20% PEGMME 5000,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 29.88650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.82975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.94325
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 OG1 THR A 32 C2 MAN A 504 2.12
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 TRP A 116 CE2 TRP A 116 CD2 0.077
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 33 146.54 -38.29
REMARK 500 GLU A 61 90.25 -54.08
REMARK 500 ASP A 68 5.25 -67.63
REMARK 500 GLU A 77 1.53 -163.31
REMARK 500 LEU A 110 0.11 -64.70
REMARK 500 SER A 171 -130.22 62.29
REMARK 500 PRO A 231 1.72 -62.27
REMARK 500 PRO A 243 -171.15 -60.62
REMARK 500 ASP A 245 131.10 76.02
REMARK 500 ASN A 253 -3.42 74.17
REMARK 500 PHE A 276 45.28 -109.94
REMARK 500 ASP A 279 -72.17 -68.46
REMARK 500 PHE A 286 69.47 38.17
REMARK 500 ALA A 292 -146.08 75.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 60 GLU A 61 147.42
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 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES A 501-502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UUE RELATED DB: PDB
DBREF 3UUF A 27 304 UNP A8PUY1 A8PUY1_MALGO 27 304
SEQRES 1 A 278 ARG GLY GLY SER SER THR ASP GLN PRO VAL ALA ASN PRO
SEQRES 2 A 278 TYR ASN THR LYS GLU ILE SER LEU ALA ALA GLY LEU VAL
SEQRES 3 A 278 GLN GLN THR TYR CYS ASP SER THR GLU ASN GLY LEU LYS
SEQRES 4 A 278 ILE GLY ASP SER GLU LEU LEU TYR THR MET GLY GLU GLY
SEQRES 5 A 278 TYR ALA ARG GLN ARG VAL ASN ILE TYR HIS SER PRO SER
SEQRES 6 A 278 LEU GLY ILE ALA VAL ALA ILE GLU GLY THR ASN LEU PHE
SEQRES 7 A 278 SER LEU ASN SER ASP LEU HIS ASP ALA LYS PHE TRP GLN
SEQRES 8 A 278 GLU ASP PRO ASN GLU ARG TYR ILE GLN TYR TYR PRO LYS
SEQRES 9 A 278 GLY THR LYS LEU MET HIS GLY PHE GLN GLN ALA TYR ASN
SEQRES 10 A 278 ASP LEU MET ASP ASP ILE PHE THR ALA VAL LYS LYS TYR
SEQRES 11 A 278 LYS LYS GLU LYS ASN GLU LYS ARG VAL THR VAL ILE GLY
SEQRES 12 A 278 HIS SER LEU GLY ALA ALA MET GLY LEU LEU CYS ALA MET
SEQRES 13 A 278 ASP ILE GLU LEU ARG MET ASP GLY GLY LEU TYR LYS THR
SEQRES 14 A 278 TYR LEU PHE GLY LEU PRO ARG LEU GLY ASN PRO THR PHE
SEQRES 15 A 278 ALA SER PHE VAL ASP GLN LYS ILE GLY ASP LYS PHE HIS
SEQRES 16 A 278 SER ILE ILE ASN GLY ARG ASP TRP VAL PRO THR VAL PRO
SEQRES 17 A 278 PRO ARG ALA LEU GLY TYR GLN HIS PRO SER ASP TYR VAL
SEQRES 18 A 278 TRP ILE TYR PRO GLY ASN SER THR SER ALA LYS LEU TYR
SEQRES 19 A 278 PRO GLY GLN GLU ASN VAL HIS GLY ILE LEU THR VAL ALA
SEQRES 20 A 278 ARG GLU PHE ASN PHE ASP ASP HIS GLN GLY ILE TYR PHE
SEQRES 21 A 278 HIS THR GLN ILE GLY ALA VAL MET GLY GLU CYS PRO ALA
SEQRES 22 A 278 GLN VAL GLY ALA HIS
MODRES 3UUF ASN A 253 ASN GLYCOSYLATION SITE
MODRES 3UUF THR A 32 THR GLYCOSYLATION SITE
HET NAG A 501 14
HET NAG A 502 14
HET MAN A 504 11
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 3 MAN C6 H12 O6
FORMUL 4 HOH *12(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 ASP A 144 1 9
HELIX 6 6 LEU A 145 ASN A 161 1 17
HELIX 7 7 SER A 171 MET A 188 1 18
HELIX 8 8 ASN A 205 GLY A 217 1 13
HELIX 9 9 TRP A 229 VAL A 233 5 5
HELIX 10 10 PRO A 235 GLY A 239 5 5
HELIX 11 11 GLY A 268 VAL A 272 5 5
HELIX 12 12 ASP A 279 GLN A 282 5 4
HELIX 13 13 GLY A 291 GLY A 295 5 5
SHEET 1 A10 VAL A 36 ALA A 37 0
SHEET 2 A10 ALA A 257 GLN A 263 -1 O LEU A 259 N VAL A 36
SHEET 3 A10 SER A 244 ILE A 249 -1 N TYR A 246 O TYR A 260
SHEET 4 A10 PHE A 220 ASN A 225 1 N ILE A 224 O ILE A 249
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 ILE A 168
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 2.02
LINK ND2 ASN A 253 C1 NAG A 501 1555 1555 1.44
LINK O4 NAG A 501 C1 NAG A 502 1555 1555 1.46
LINK OG1 THR A 32 C1 MAN A 504 1555 1555 1.47
CISPEP 1 VAL A 233 PRO A 234 0 -6.13
CISPEP 2 TYR A 250 PRO A 251 0 -1.86
CISPEP 3 CYS A 297 PRO A 298 0 -0.35
SITE 1 AC1 2 THR A 32 ASP A 33
SITE 1 AC2 6 ASN A 253 ASP A 279 ASP A 280 GLN A 282
SITE 2 AC2 6 GLY A 283 GLN A 289
CRYST1 77.507 77.507 59.773 90.00 90.00 90.00 P 43 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 0.012902 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012902 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016730 0.00000
TER 2188 HIS A 304
MASTER 314 0 3 13 14 0 3 6 2238 1 43 22
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