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HEADER HYDROLASE 25-OCT-01 1K8Q
TITLE CRYSTAL STRUCTURE OF DOG GASTRIC LIPASE IN COMPLEX WITH A
TITLE 2 PHOSPHONATE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE, GASTRIC;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS FAMILIARIS;
SOURCE 3 GENE: LIPF;
SOURCE 4 EXPRESSION_SYSTEM: ZEA MAYS;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: HI-II MAIZE GERMPLASM;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PUC18
KEYWDS APHA BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROUSSEL,N.MILED,L.BERTI-DUPUIS,M.RIVIERE,S.SPINELLI,
AUTHOR 2 P.BERNA,V.GRUBER,R.VERGER,C.CAMBILLAU
REVDAT 1 06-MAR-02 1K8Q 0
JRNL AUTH A.ROUSSEL,N.MILED,L.BERTI-DUPUIS,M.RIVIERE,
JRNL AUTH 2 S.SPINELLI,P.BERNA,V.GRUBER,R.VERGER,C.CAMBILLAU
JRNL TITL CRYSTAL STRUCTURE OF THE OPEN FORM OF DOG GASTRIC
JRNL TITL 2 LIPASE IN COMPLEX WITH A PHOSPHONATE INHIBITOR
JRNL REF J.BIOL.CHEM. V. 277 2266 2002
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 24389
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1174
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6064
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 188
REMARK 3 SOLVENT ATOMS : 382
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K8Q COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-2001.
REMARK 100 THE RCSB ID CODE IS RCSB014700.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24343
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21500
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1HLG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % PEGMME 2000, 0.1 M SODIUM
REMARK 280 ACETATE AND 0.2 M AMMONIUM SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 1/2+X,1/2-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 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 88.57800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.57800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.60450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.24900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.60450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.24900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 88.57800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.60450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.24900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 88.57800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.60450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.24900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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
REMARK 500 O HOH 1 O HOH 296 2.15
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 249 CE MET A 249 SD 0.077
REMARK 500 MET B 249 CE MET B 249 SD 0.076
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 37 N - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 ILE A 45 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 ASP A 93 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 GLU A 230 N - CA - C ANGL. DEV. = 11.3 DEGREES
REMARK 500 CYS A 244 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP A 247 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 LEU A 260 CA - CB - CG ANGL. DEV. = -9.4 DEGREES
REMARK 500 ALA A 327 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 TRP A 358 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 GLY B 37 N - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 ILE B 45 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 ASP B 93 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 GLU B 230 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 CYS B 244 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 PHE B 246 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP B 247 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 LEU B 260 CA - CB - CG ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP B 288 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 ALA B 327 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 TRP B 358 N - CA - C ANGL. DEV. = 8.6 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 153 -119.87 64.36
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 80 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH 123 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH 189 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH 210 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH 244 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH 299 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH 304 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH 314 DISTANCE = 5.73 ANGSTROMS
REMARK 525 HOH 350 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH 370 DISTANCE = 5.76 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HLG RELATED DB: PDB
REMARK 900 1HLG CONTAINS HUMAN GASTRIC LIPASE WITHOUT INHIBITOR
DBREF 1K8Q A 1 377 SWS P80035 LIPG_CANFA 20 396
DBREF 1K8Q B 1 377 SWS P80035 LIPG_CANFA 20 396
SEQADV 1K8Q ALA A 1 SWS P80035 LEU 20 CONFLICT
SEQADV 1K8Q ILE A 192 SWS P80035 LEU 211 CONFLICT
SEQADV 1K8Q ALA B 1 SWS P80035 LEU 20 CONFLICT
SEQADV 1K8Q ILE B 192 SWS P80035 LEU 211 CONFLICT
SEQRES 1 A 377 ALA PHE GLY LYS LEU HIS PRO THR ASN PRO GLU VAL THR
SEQRES 2 A 377 MET ASN ILE SER GLN MET ILE THR TYR TRP GLY TYR PRO
SEQRES 3 A 377 ALA GLU GLU TYR GLU VAL VAL THR GLU ASP GLY TYR ILE
SEQRES 4 A 377 LEU GLY ILE ASP ARG ILE PRO TYR GLY ARG LYS ASN SER
SEQRES 5 A 377 GLU ASN ILE GLY ARG ARG PRO VAL ALA PHE LEU GLN HIS
SEQRES 6 A 377 GLY LEU LEU ALA SER ALA THR ASN TRP ILE SER ASN LEU
SEQRES 7 A 377 PRO ASN ASN SER LEU ALA PHE ILE LEU ALA ASP ALA GLY
SEQRES 8 A 377 TYR ASP VAL TRP LEU GLY ASN SER ARG GLY ASN THR TRP
SEQRES 9 A 377 ALA ARG ARG ASN LEU TYR TYR SER PRO ASP SER VAL GLU
SEQRES 10 A 377 PHE TRP ALA PHE SER PHE ASP GLU MET ALA LYS TYR ASP
SEQRES 11 A 377 LEU PRO ALA THR ILE ASP PHE ILE LEU LYS LYS THR GLY
SEQRES 12 A 377 GLN ASP LYS LEU HIS TYR VAL GLY HIS SER GLN GLY THR
SEQRES 13 A 377 THR ILE GLY PHE ILE ALA PHE SER THR ASN PRO LYS LEU
SEQRES 14 A 377 ALA LYS ARG ILE LYS THR PHE TYR ALA LEU ALA PRO VAL
SEQRES 15 A 377 ALA THR VAL LYS TYR THR GLU THR LEU ILE ASN LYS LEU
SEQRES 16 A 377 MET LEU VAL PRO SER PHE LEU PHE LYS LEU ILE PHE GLY
SEQRES 17 A 377 ASN LYS ILE PHE TYR PRO HIS HIS PHE PHE ASP GLN PHE
SEQRES 18 A 377 LEU ALA THR GLU VAL CYS SER ARG GLU THR VAL ASP LEU
SEQRES 19 A 377 LEU CYS SER ASN ALA LEU PHE ILE ILE CYS GLY PHE ASP
SEQRES 20 A 377 THR MET ASN LEU ASN MET SER ARG LEU ASP VAL TYR LEU
SEQRES 21 A 377 SER HIS ASN PRO ALA GLY THR SER VAL GLN ASN VAL LEU
SEQRES 22 A 377 HIS TRP SER GLN ALA VAL LYS SER GLY LYS PHE GLN ALA
SEQRES 23 A 377 PHE ASP TRP GLY SER PRO VAL GLN ASN MET MET HIS TYR
SEQRES 24 A 377 HIS GLN SER MET PRO PRO TYR TYR ASN LEU THR ASP MET
SEQRES 25 A 377 HIS VAL PRO ILE ALA VAL TRP ASN GLY GLY ASN ASP LEU
SEQRES 26 A 377 LEU ALA ASP PRO HIS ASP VAL ASP LEU LEU LEU SER LYS
SEQRES 27 A 377 LEU PRO ASN LEU ILE TYR HIS ARG LYS ILE PRO PRO TYR
SEQRES 28 A 377 ASN HIS LEU ASP PHE ILE TRP ALA MET ASP ALA PRO GLN
SEQRES 29 A 377 ALA VAL TYR ASN GLU ILE VAL SER MET MET GLY THR ASP
SEQRES 1 B 377 ALA PHE GLY LYS LEU HIS PRO THR ASN PRO GLU VAL THR
SEQRES 2 B 377 MET ASN ILE SER GLN MET ILE THR TYR TRP GLY TYR PRO
SEQRES 3 B 377 ALA GLU GLU TYR GLU VAL VAL THR GLU ASP GLY TYR ILE
SEQRES 4 B 377 LEU GLY ILE ASP ARG ILE PRO TYR GLY ARG LYS ASN SER
SEQRES 5 B 377 GLU ASN ILE GLY ARG ARG PRO VAL ALA PHE LEU GLN HIS
SEQRES 6 B 377 GLY LEU LEU ALA SER ALA THR ASN TRP ILE SER ASN LEU
SEQRES 7 B 377 PRO ASN ASN SER LEU ALA PHE ILE LEU ALA ASP ALA GLY
SEQRES 8 B 377 TYR ASP VAL TRP LEU GLY ASN SER ARG GLY ASN THR TRP
SEQRES 9 B 377 ALA ARG ARG ASN LEU TYR TYR SER PRO ASP SER VAL GLU
SEQRES 10 B 377 PHE TRP ALA PHE SER PHE ASP GLU MET ALA LYS TYR ASP
SEQRES 11 B 377 LEU PRO ALA THR ILE ASP PHE ILE LEU LYS LYS THR GLY
SEQRES 12 B 377 GLN ASP LYS LEU HIS TYR VAL GLY HIS SER GLN GLY THR
SEQRES 13 B 377 THR ILE GLY PHE ILE ALA PHE SER THR ASN PRO LYS LEU
SEQRES 14 B 377 ALA LYS ARG ILE LYS THR PHE TYR ALA LEU ALA PRO VAL
SEQRES 15 B 377 ALA THR VAL LYS TYR THR GLU THR LEU ILE ASN LYS LEU
SEQRES 16 B 377 MET LEU VAL PRO SER PHE LEU PHE LYS LEU ILE PHE GLY
SEQRES 17 B 377 ASN LYS ILE PHE TYR PRO HIS HIS PHE PHE ASP GLN PHE
SEQRES 18 B 377 LEU ALA THR GLU VAL CYS SER ARG GLU THR VAL ASP LEU
SEQRES 19 B 377 LEU CYS SER ASN ALA LEU PHE ILE ILE CYS GLY PHE ASP
SEQRES 20 B 377 THR MET ASN LEU ASN MET SER ARG LEU ASP VAL TYR LEU
SEQRES 21 B 377 SER HIS ASN PRO ALA GLY THR SER VAL GLN ASN VAL LEU
SEQRES 22 B 377 HIS TRP SER GLN ALA VAL LYS SER GLY LYS PHE GLN ALA
SEQRES 23 B 377 PHE ASP TRP GLY SER PRO VAL GLN ASN MET MET HIS TYR
SEQRES 24 B 377 HIS GLN SER MET PRO PRO TYR TYR ASN LEU THR ASP MET
SEQRES 25 B 377 HIS VAL PRO ILE ALA VAL TRP ASN GLY GLY ASN ASP LEU
SEQRES 26 B 377 LEU ALA ASP PRO HIS ASP VAL ASP LEU LEU LEU SER LYS
SEQRES 27 B 377 LEU PRO ASN LEU ILE TYR HIS ARG LYS ILE PRO PRO TYR
SEQRES 28 B 377 ASN HIS LEU ASP PHE ILE TRP ALA MET ASP ALA PRO GLN
SEQRES 29 B 377 ALA VAL TYR ASN GLU ILE VAL SER MET MET GLY THR ASP
MODRES 1K8Q ASN A 15 ASN GLYCOSYLATION SITE
MODRES 1K8Q ASN A 80 ASN GLYCOSYLATION SITE
MODRES 1K8Q ASN A 252 ASN GLYCOSYLATION SITE
MODRES 1K8Q ASN A 308 ASN GLYCOSYLATION SITE
MODRES 1K8Q ASN B 15 ASN GLYCOSYLATION SITE
MODRES 1K8Q ASN B 80 ASN GLYCOSYLATION SITE
MODRES 1K8Q ASN B 252 ASN GLYCOSYLATION SITE
MODRES 1K8Q ASN B 308 ASN GLYCOSYLATION SITE
HET NAG A1001 14
HET NAG A1002 14
HET NAG A1003 14
HET NAG A1005 14
HET NAG B1001 14
HET NAG B1002 14
HET NAG B1003 14
HET NAG B1005 14
HET BOG 1002 20
HET BOG 2002 20
HET C11 1001 18
HET C11 2001 18
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BOG B-OCTYLGLUCOSIDE
HETNAM C11 UNDECYL-PHOSPHINIC ACID BUTYL ESTER
HETSYN NAG NAG
FORMUL 3 NAG 8(C8 H15 N1 O6)
FORMUL 11 BOG 2(C14 H28 O6)
FORMUL 13 C11 2(C15 H33 O2 P1)
FORMUL 15 HOH *382(H2 O1)
HELIX 1 1 ASN A 9 MET A 14 5 6
HELIX 2 2 ASN A 15 TRP A 23 1 9
HELIX 3 3 SER A 70 ILE A 75 5 6
HELIX 4 4 SER A 82 ALA A 90 1 9
HELIX 5 5 SER A 122 TYR A 129 1 8
HELIX 6 6 TYR A 129 GLY A 143 1 15
HELIX 7 7 SER A 153 ASN A 166 1 14
HELIX 8 8 ASN A 166 LYS A 171 1 6
HELIX 9 9 THR A 190 LEU A 197 5 8
HELIX 10 10 PRO A 199 PHE A 207 1 9
HELIX 11 11 HIS A 216 VAL A 226 1 11
HELIX 12 12 VAL A 232 GLY A 245 1 14
HELIX 13 13 ASP A 247 LEU A 251 5 5
HELIX 14 14 ASN A 252 SER A 254 5 3
HELIX 15 15 ARG A 255 SER A 261 1 7
HELIX 16 16 VAL A 269 GLY A 282 1 14
HELIX 17 17 SER A 291 HIS A 300 1 10
HELIX 18 18 ASN A 308 MET A 312 5 5
HELIX 19 19 ASP A 328 SER A 337 1 10
HELIX 20 20 LEU A 354 ALA A 359 1 6
HELIX 21 21 ASP A 361 VAL A 366 1 6
HELIX 22 22 VAL A 366 THR A 376 1 11
HELIX 23 23 ASN B 9 MET B 14 5 6
HELIX 24 24 ASN B 15 TRP B 23 1 9
HELIX 25 25 SER B 70 ILE B 75 5 6
HELIX 26 26 SER B 82 ALA B 90 1 9
HELIX 27 27 SER B 122 TYR B 129 1 8
HELIX 28 28 TYR B 129 GLY B 143 1 15
HELIX 29 29 SER B 153 SER B 164 1 12
HELIX 30 30 ASN B 166 LYS B 171 1 6
HELIX 31 31 THR B 190 LEU B 197 5 8
HELIX 32 32 PRO B 199 PHE B 207 1 9
HELIX 33 33 HIS B 216 VAL B 226 1 11
HELIX 34 34 VAL B 232 GLY B 245 1 14
HELIX 35 35 ASP B 247 LEU B 251 5 5
HELIX 36 36 ASN B 252 SER B 254 5 3
HELIX 37 37 ARG B 255 SER B 261 1 7
HELIX 38 38 VAL B 269 GLY B 282 1 14
HELIX 39 39 SER B 291 HIS B 300 1 10
HELIX 40 40 ASN B 308 MET B 312 5 5
HELIX 41 41 ASP B 328 SER B 337 1 10
HELIX 42 42 LEU B 354 ALA B 359 1 6
HELIX 43 43 ASP B 361 VAL B 366 1 6
HELIX 44 44 VAL B 366 THR B 376 1 11
SHEET 1 A 8 GLU A 28 VAL A 33 0
SHEET 2 A 8 TYR A 38 ILE A 45 -1 O LEU A 40 N VAL A 32
SHEET 3 A 8 ASP A 93 LEU A 96 -1 O LEU A 96 N ASP A 43
SHEET 4 A 8 VAL A 60 GLN A 64 1 N ALA A 61 O TRP A 95
SHEET 5 A 8 LEU A 147 HIS A 152 1 O HIS A 148 N PHE A 62
SHEET 6 A 8 ILE A 173 LEU A 179 1 O TYR A 177 N TYR A 149
SHEET 7 A 8 ILE A 316 GLY A 321 1 O ALA A 317 N PHE A 176
SHEET 8 A 8 LEU A 342 ILE A 348 1 O TYR A 344 N VAL A 318
SHEET 1 B 3 GLU A 28 VAL A 33 0
SHEET 2 B 3 TYR A 38 ILE A 45 -1 O LEU A 40 N VAL A 32
SHEET 3 B 3 ARG A 107 ASN A 108 -1 O ARG A 107 N ILE A 39
SHEET 1 C 2 ILE A 211 PHE A 212 0
SHEET 2 C 2 THR A 267 SER A 268 -1 O THR A 267 N PHE A 212
SHEET 1 D 8 GLU B 28 VAL B 33 0
SHEET 2 D 8 TYR B 38 ILE B 45 -1 O LEU B 40 N VAL B 32
SHEET 3 D 8 ASP B 93 LEU B 96 -1 O LEU B 96 N ASP B 43
SHEET 4 D 8 VAL B 60 GLN B 64 1 N ALA B 61 O TRP B 95
SHEET 5 D 8 LEU B 147 HIS B 152 1 O VAL B 150 N GLN B 64
SHEET 6 D 8 ILE B 173 LEU B 179 1 O TYR B 177 N TYR B 149
SHEET 7 D 8 ILE B 316 GLY B 321 1 O ALA B 317 N PHE B 176
SHEET 8 D 8 LEU B 342 ILE B 348 1 O ILE B 343 N ILE B 316
SHEET 1 E 3 GLU B 28 VAL B 33 0
SHEET 2 E 3 TYR B 38 ILE B 45 -1 O LEU B 40 N VAL B 32
SHEET 3 E 3 ARG B 107 ASN B 108 -1 O ARG B 107 N ILE B 39
SHEET 1 F 2 ILE B 211 PHE B 212 0
SHEET 2 F 2 THR B 267 SER B 268 -1 O THR B 267 N PHE B 212
SSBOND 1 CYS A 227 CYS A 236
SSBOND 2 CYS B 227 CYS B 236
LINK ND2 ASN A 15 C1 NAG A1001
LINK ND2 ASN A 80 C1 NAG A1002
LINK ND2 ASN A 252 C1 NAG A1003
LINK ND2 ASN A 308 C1 NAG A1005
LINK ND2 ASN B 15 C1 NAG B1001
LINK ND2 ASN B 80 C1 NAG B1002
LINK ND2 ASN B 252 C1 NAG B1003
LINK ND2 ASN B 308 C1 NAG B1005
CISPEP 1 ASN A 263 PRO A 264 0 -0.21
CISPEP 2 ASN B 263 PRO B 264 0 0.66
CRYST1 61.209 164.498 177.156 90.00 90.00 90.00 C 2 2 21 16
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 0.016337 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006079 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005645 0.00000
END |