HEADER HYDROLASE 16-JAN-01 1HXK
TITLE GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH DEOXYMANNOJIRIMICIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-MANNOSIDASE II;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GOLGI ALPHA-MANNOSIDASE II;
COMPND 5 EC: 3.2.1.114;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 8 EXPRESSION_SYSTEM_CELL: S2
KEYWDS N-TERMINAL ALPHA-BETA DOMAIN, THREE HELIX BUNDLE, 2 C-TERMINAL BETA
KEYWDS 2 BARRELS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.H.VAN DEN ELSEN,D.A.KUNTZ,D.R.ROSE
REVDAT 6 09-AUG-23 1HXK 1 HETSYN
REVDAT 5 29-JUL-20 1HXK 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 13-JUL-11 1HXK 1 VERSN
REVDAT 3 24-FEB-09 1HXK 1 VERSN
REVDAT 2 01-APR-03 1HXK 1 JRNL
REVDAT 1 16-JAN-02 1HXK 0
JRNL AUTH J.M.VAN DEN ELSEN,D.A.KUNTZ,D.R.ROSE
JRNL TITL STRUCTURE OF GOLGI ALPHA-MANNOSIDASE II: A TARGET FOR
JRNL TITL 2 INHIBITION OF GROWTH AND METASTASIS OF CANCER CELLS.
JRNL REF EMBO J. V. 20 3008 2001
JRNL REFN ISSN 0261-4189
JRNL PMID 11406577
JRNL DOI 10.1093/EMBOJ/20.12.3008
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 145650
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 SET) : 0.197
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 6888
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.57
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10341
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 364
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8181
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 983
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.24000
REMARK 3 B33 (A**2) : -0.29000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : 0.11
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.19
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.801
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 : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 40.88
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012661.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : BEND CYLINDRICAL GE(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : BENT CYLINDRICAL SI-MIRROR (RH
REMARK 200 COATING) BEND CYLINDRICAL GE(111)
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 148337
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 85.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.33100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1HTY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, MPD, TRIS, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 34.40700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.14050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.80800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.14050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.80800
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: MONOMERIC
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 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 SER A 1045
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 56 78.15 -100.50
REMARK 500 TRP A 95 -85.78 -170.67
REMARK 500 ASP A 106 -62.26 -128.62
REMARK 500 THR A 162 -64.99 72.35
REMARK 500 GLN A 227 -50.24 -135.72
REMARK 500 ARG A 289 58.16 -98.92
REMARK 500 LYS A 300 -3.20 77.82
REMARK 500 SER A 411 -123.87 39.78
REMARK 500 ILE A 549 -47.97 -139.61
REMARK 500 LEU A 550 115.60 -165.05
REMARK 500 PRO A 562 37.94 -79.83
REMARK 500 ARG A 653 161.11 173.60
REMARK 500 ASN A 732 56.13 -95.60
REMARK 500 SER A 762 -7.20 75.23
REMARK 500 SER A 833 -12.15 -152.41
REMARK 500 GLU A 991 89.46 46.63
REMARK 500 GLU A 992 -146.38 -122.38
REMARK 500 HIS A 993 86.42 19.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 90 NE2
REMARK 620 2 ASP A 92 OD1 90.7
REMARK 620 3 ASP A 204 OD1 94.4 171.9
REMARK 620 4 HIS A 471 NE2 105.4 90.6 94.1
REMARK 620 5 DMJ A1103 O2 88.4 99.3 74.6 163.0
REMARK 620 6 DMJ A1103 O3 157.6 82.2 90.8 96.0 71.9
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HTY RELATED DB: PDB
REMARK 900 1HTY IS GOLGI ALPHA-MANNOSIDASE II
REMARK 900 RELATED ID: 1HWW RELATED DB: PDB
REMARK 900 1HWW IS GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE
DBREF 1HXK A 31 1045 UNP Q24451 MAN2_DROME 94 1108
SEQRES 1 A 1015 CYS GLN ASP VAL VAL GLN ASP VAL PRO ASN VAL ASP VAL
SEQRES 2 A 1015 GLN MET LEU GLU LEU TYR ASP ARG MET SER PHE LYS ASP
SEQRES 3 A 1015 ILE ASP GLY GLY VAL TRP LYS GLN GLY TRP ASN ILE LYS
SEQRES 4 A 1015 TYR ASP PRO LEU LYS TYR ASN ALA HIS HIS LYS LEU LYS
SEQRES 5 A 1015 VAL PHE VAL VAL PRO HIS SER HIS ASN ASP PRO GLY TRP
SEQRES 6 A 1015 ILE GLN THR PHE GLU GLU TYR TYR GLN HIS ASP THR LYS
SEQRES 7 A 1015 HIS ILE LEU SER ASN ALA LEU ARG HIS LEU HIS ASP ASN
SEQRES 8 A 1015 PRO GLU MET LYS PHE ILE TRP ALA GLU ILE SER TYR PHE
SEQRES 9 A 1015 ALA ARG PHE TYR HIS ASP LEU GLY GLU ASN LYS LYS LEU
SEQRES 10 A 1015 GLN MET LYS SER ILE VAL LYS ASN GLY GLN LEU GLU PHE
SEQRES 11 A 1015 VAL THR GLY GLY TRP VAL MET PRO ASP GLU ALA ASN SER
SEQRES 12 A 1015 HIS TRP ARG ASN VAL LEU LEU GLN LEU THR GLU GLY GLN
SEQRES 13 A 1015 THR TRP LEU LYS GLN PHE MET ASN VAL THR PRO THR ALA
SEQRES 14 A 1015 SER TRP ALA ILE ASP PRO PHE GLY HIS SER PRO THR MET
SEQRES 15 A 1015 PRO TYR ILE LEU GLN LYS SER GLY PHE LYS ASN MET LEU
SEQRES 16 A 1015 ILE GLN ARG THR HIS TYR SER VAL LYS LYS GLU LEU ALA
SEQRES 17 A 1015 GLN GLN ARG GLN LEU GLU PHE LEU TRP ARG GLN ILE TRP
SEQRES 18 A 1015 ASP ASN LYS GLY ASP THR ALA LEU PHE THR HIS MET MET
SEQRES 19 A 1015 PRO PHE TYR SER TYR ASP ILE PRO HIS THR CYS GLY PRO
SEQRES 20 A 1015 ASP PRO LYS VAL CYS CYS GLN PHE ASP PHE LYS ARG MET
SEQRES 21 A 1015 GLY SER PHE GLY LEU SER CYS PRO TRP LYS VAL PRO PRO
SEQRES 22 A 1015 ARG THR ILE SER ASP GLN ASN VAL ALA ALA ARG SER ASP
SEQRES 23 A 1015 LEU LEU VAL ASP GLN TRP LYS LYS LYS ALA GLU LEU TYR
SEQRES 24 A 1015 ARG THR ASN VAL LEU LEU ILE PRO LEU GLY ASP ASP PHE
SEQRES 25 A 1015 ARG PHE LYS GLN ASN THR GLU TRP ASP VAL GLN ARG VAL
SEQRES 26 A 1015 ASN TYR GLU ARG LEU PHE GLU HIS ILE ASN SER GLN ALA
SEQRES 27 A 1015 HIS PHE ASN VAL GLN ALA GLN PHE GLY THR LEU GLN GLU
SEQRES 28 A 1015 TYR PHE ASP ALA VAL HIS GLN ALA GLU ARG ALA GLY GLN
SEQRES 29 A 1015 ALA GLU PHE PRO THR LEU SER GLY ASP PHE PHE THR TYR
SEQRES 30 A 1015 ALA ASP ARG SER ASP ASN TYR TRP SER GLY TYR TYR THR
SEQRES 31 A 1015 SER ARG PRO TYR HIS LYS ARG MET ASP ARG VAL LEU MET
SEQRES 32 A 1015 HIS TYR VAL ARG ALA ALA GLU MET LEU SER ALA TRP HIS
SEQRES 33 A 1015 SER TRP ASP GLY MET ALA ARG ILE GLU GLU ARG LEU GLU
SEQRES 34 A 1015 GLN ALA ARG ARG GLU LEU SER LEU PHE GLN HIS HIS ASP
SEQRES 35 A 1015 GLY ILE THR GLY THR ALA LYS THR HIS VAL VAL VAL ASP
SEQRES 36 A 1015 TYR GLU GLN ARG MET GLN GLU ALA LEU LYS ALA CYS GLN
SEQRES 37 A 1015 MET VAL MET GLN GLN SER VAL TYR ARG LEU LEU THR LYS
SEQRES 38 A 1015 PRO SER ILE TYR SER PRO ASP PHE SER PHE SER TYR PHE
SEQRES 39 A 1015 THR LEU ASP ASP SER ARG TRP PRO GLY SER GLY VAL GLU
SEQRES 40 A 1015 ASP SER ARG THR THR ILE ILE LEU GLY GLU ASP ILE LEU
SEQRES 41 A 1015 PRO SER LYS HIS VAL VAL MET HIS ASN THR LEU PRO HIS
SEQRES 42 A 1015 TRP ARG GLU GLN LEU VAL ASP PHE TYR VAL SER SER PRO
SEQRES 43 A 1015 PHE VAL SER VAL THR ASP LEU ALA ASN ASN PRO VAL GLU
SEQRES 44 A 1015 ALA GLN VAL SER PRO VAL TRP SER TRP HIS HIS ASP THR
SEQRES 45 A 1015 LEU THR LYS THR ILE HIS PRO GLN GLY SER THR THR LYS
SEQRES 46 A 1015 TYR ARG ILE ILE PHE LYS ALA ARG VAL PRO PRO MET GLY
SEQRES 47 A 1015 LEU ALA THR TYR VAL LEU THR ILE SER ASP SER LYS PRO
SEQRES 48 A 1015 GLU HIS THR SER TYR ALA SER ASN LEU LEU LEU ARG LYS
SEQRES 49 A 1015 ASN PRO THR SER LEU PRO LEU GLY GLN TYR PRO GLU ASP
SEQRES 50 A 1015 VAL LYS PHE GLY ASP PRO ARG GLU ILE SER LEU ARG VAL
SEQRES 51 A 1015 GLY ASN GLY PRO THR LEU ALA PHE SER GLU GLN GLY LEU
SEQRES 52 A 1015 LEU LYS SER ILE GLN LEU THR GLN ASP SER PRO HIS VAL
SEQRES 53 A 1015 PRO VAL HIS PHE LYS PHE LEU LYS TYR GLY VAL ARG SER
SEQRES 54 A 1015 HIS GLY ASP ARG SER GLY ALA TYR LEU PHE LEU PRO ASN
SEQRES 55 A 1015 GLY PRO ALA SER PRO VAL GLU LEU GLY GLN PRO VAL VAL
SEQRES 56 A 1015 LEU VAL THR LYS GLY LYS LEU GLU SER SER VAL SER VAL
SEQRES 57 A 1015 GLY LEU PRO SER VAL VAL HIS GLN THR ILE MET ARG GLY
SEQRES 58 A 1015 GLY ALA PRO GLU ILE ARG ASN LEU VAL ASP ILE GLY SER
SEQRES 59 A 1015 LEU ASP ASN THR GLU ILE VAL MET ARG LEU GLU THR HIS
SEQRES 60 A 1015 ILE ASP SER GLY ASP ILE PHE TYR THR ASP LEU ASN GLY
SEQRES 61 A 1015 LEU GLN PHE ILE LYS ARG ARG ARG LEU ASP LYS LEU PRO
SEQRES 62 A 1015 LEU GLN ALA ASN TYR TYR PRO ILE PRO SER GLY MET PHE
SEQRES 63 A 1015 ILE GLU ASP ALA ASN THR ARG LEU THR LEU LEU THR GLY
SEQRES 64 A 1015 GLN PRO LEU GLY GLY SER SER LEU ALA SER GLY GLU LEU
SEQRES 65 A 1015 GLU ILE MET GLN ASP ARG ARG LEU ALA SER ASP ASP GLU
SEQRES 66 A 1015 ARG GLY LEU GLY GLN GLY VAL LEU ASP ASN LYS PRO VAL
SEQRES 67 A 1015 LEU HIS ILE TYR ARG LEU VAL LEU GLU LYS VAL ASN ASN
SEQRES 68 A 1015 CYS VAL ARG PRO SER LYS LEU HIS PRO ALA GLY TYR LEU
SEQRES 69 A 1015 THR SER ALA ALA HIS LYS ALA SER GLN SER LEU LEU ASP
SEQRES 70 A 1015 PRO LEU ASP LYS PHE ILE PHE ALA GLU ASN GLU TRP ILE
SEQRES 71 A 1015 GLY ALA GLN GLY GLN PHE GLY GLY ASP HIS PRO SER ALA
SEQRES 72 A 1015 ARG GLU ASP LEU ASP VAL SER VAL MET ARG ARG LEU THR
SEQRES 73 A 1015 LYS SER SER ALA LYS THR GLN ARG VAL GLY TYR VAL LEU
SEQRES 74 A 1015 HIS ARG THR ASN LEU MET GLN CYS GLY THR PRO GLU GLU
SEQRES 75 A 1015 HIS THR GLN LYS LEU ASP VAL CYS HIS LEU LEU PRO ASN
SEQRES 76 A 1015 VAL ALA ARG CYS GLU ARG THR THR LEU THR PHE LEU GLN
SEQRES 77 A 1015 ASN LEU GLU HIS LEU ASP GLY MET VAL ALA PRO GLU VAL
SEQRES 78 A 1015 CYS PRO MET GLU THR ALA ALA TYR VAL SER SER HIS SER
SEQRES 79 A 1015 SER
MODRES 1HXK ASN A 194 ASN GLYCOSYLATION SITE
HET NAG A1101 14
HET ZN A1102 1
HET DMJ A1103 11
HET MRD A1104 8
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM DMJ 1-DEOXYMANNOJIRIMYCIN
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
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
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 ZN ZN 2+
FORMUL 4 DMJ C6 H13 N O4
FORMUL 5 MRD C6 H14 O2
FORMUL 6 HOH *983(H2 O)
HELIX 1 1 MET A 45 MET A 52 1 8
HELIX 2 2 ASP A 71 TYR A 75 5 5
HELIX 3 3 THR A 98 ASP A 106 1 9
HELIX 4 4 ASP A 106 ASN A 121 1 16
HELIX 5 5 GLU A 130 HIS A 139 1 10
HELIX 6 6 GLY A 142 ASN A 155 1 14
HELIX 7 7 HIS A 174 ASN A 194 1 21
HELIX 8 8 PRO A 210 LYS A 218 1 9
HELIX 9 9 HIS A 230 GLN A 240 1 11
HELIX 10 10 ASP A 270 THR A 274 5 5
HELIX 11 11 ASP A 278 CYS A 283 1 6
HELIX 12 12 GLN A 284 ASP A 286 5 3
HELIX 13 13 ASN A 310 GLU A 327 1 18
HELIX 14 14 GLN A 346 GLN A 367 1 22
HELIX 15 15 ALA A 368 PHE A 370 5 3
HELIX 16 16 THR A 378 ALA A 392 1 15
HELIX 17 17 SER A 416 THR A 420 5 5
HELIX 18 18 ARG A 422 TRP A 445 1 24
HELIX 19 19 ASP A 449 ALA A 452 5 4
HELIX 20 20 ARG A 453 GLN A 469 1 17
HELIX 21 21 LYS A 479 LEU A 509 1 31
HELIX 22 22 PRO A 823 TYR A 828 5 6
HELIX 23 23 THR A 915 ASP A 927 1 13
HELIX 24 24 ASP A 998 LEU A 1002 5 5
HELIX 25 25 ASP A 1024 VAL A 1027 5 4
SHEET 1 A 6 VAL A 43 GLN A 44 0
SHEET 2 A 6 THR A 399 SER A 401 1 O THR A 399 N VAL A 43
SHEET 3 A 6 GLU A 244 TRP A 247 1 O LEU A 246 N LEU A 400
SHEET 4 A 6 LEU A 259 MET A 263 -1 O LEU A 259 N TRP A 247
SHEET 5 A 6 ASN A 223 ILE A 226 1 O MET A 224 N HIS A 262
SHEET 6 A 6 ALA A 199 ALA A 202 1 N SER A 200 O ASN A 223
SHEET 1 B 3 VAL A 333 ASP A 341 0
SHEET 2 B 3 LEU A 81 HIS A 90 1 O LYS A 82 N LEU A 334
SHEET 3 B 3 VAL A 372 PHE A 376 1 O GLN A 373 N VAL A 83
SHEET 1 C 2 PHE A 126 TRP A 128 0
SHEET 2 C 2 LEU A 158 PHE A 160 1 N GLU A 159 O PHE A 126
SHEET 1 D 6 PHE A 524 ASP A 527 0
SHEET 2 D 6 ASP A 930 PHE A 934 -1 O LYS A 931 N ASP A 527
SHEET 3 D 6 SER A 552 ASN A 559 -1 O HIS A 554 N PHE A 934
SHEET 4 D 6 GLY A 628 ILE A 636 -1 O GLY A 628 N ASN A 559
SHEET 5 D 6 VAL A 578 ASP A 582 -1 N SER A 579 O THR A 635
SHEET 6 D 6 PRO A 587 VAL A 588 -1 N VAL A 588 O VAL A 580
SHEET 1 E 5 PHE A 524 ASP A 527 0
SHEET 2 E 5 ASP A 930 PHE A 934 -1 O LYS A 931 N ASP A 527
SHEET 3 E 5 SER A 552 ASN A 559 -1 O HIS A 554 N PHE A 934
SHEET 4 E 5 GLY A 628 ILE A 636 -1 O GLY A 628 N ASN A 559
SHEET 5 E 5 GLN A 945 PHE A 946 -1 N PHE A 946 O LEU A 629
SHEET 1 F 5 THR A 542 ILE A 543 0
SHEET 2 F 5 ARG A 565 VAL A 573 1 O TYR A 572 N ILE A 543
SHEET 3 F 5 THR A 606 VAL A 624 -1 O TYR A 616 N VAL A 573
SHEET 4 F 5 ALA A 590 ASP A 601 -1 O GLN A 591 N ILE A 619
SHEET 5 F 5 THR A 644 TYR A 646 1 O SER A 645 N VAL A 592
SHEET 1 G12 LYS A 669 GLY A 671 0
SHEET 2 G12 SER A 648 LEU A 652 1 O ASN A 649 N LYS A 669
SHEET 3 G12 VAL A 745 LYS A 749 -1 O VAL A 745 N LEU A 652
SHEET 4 G12 SER A 754 LEU A 760 -1 N SER A 755 O THR A 748
SHEET 5 G12 VAL A 763 MET A 769 -1 O VAL A 763 N LEU A 760
SHEET 6 G12 GLU A 775 VAL A 780 -1 O GLU A 775 N ILE A 768
SHEET 7 G12 VAL A 888 LYS A 898 -1 O VAL A 888 N VAL A 780
SHEET 8 G12 THR A 842 THR A 848 -1 O ARG A 843 N GLU A 897
SHEET 9 G12 GLY A 834 GLU A 838 -1 O MET A 835 N LEU A 846
SHEET 10 G12 ILE A 803 LEU A 808 -1 N TYR A 805 O PHE A 836
SHEET 11 G12 GLN A 812 ARG A 817 -1 O GLN A 812 N LEU A 808
SHEET 12 G12 ALA A 911 GLY A 912 -1 N GLY A 912 O PHE A 813
SHEET 1 H 8 TYR A 829 ILE A 831 0
SHEET 2 H 8 LEU A 852 SER A 855 -1 O LEU A 852 N ILE A 831
SHEET 3 H 8 GLU A 861 ARG A 869 -1 N GLU A 863 O SER A 855
SHEET 4 H 8 THR A 788 THR A 796 -1 O THR A 788 N ARG A 869
SHEET 5 H 8 VAL A 706 TYR A 715 -1 N HIS A 709 O GLU A 795
SHEET 6 H 8 LEU A 694 GLN A 698 -1 O LEU A 694 N PHE A 710
SHEET 7 H 8 THR A 685 PHE A 688 -1 N THR A 685 O GLN A 698
SHEET 8 H 8 ILE A 676 ARG A 679 -1 O ILE A 676 N PHE A 688
SHEET 1 I 6 TYR A 829 ILE A 831 0
SHEET 2 I 6 LEU A 852 SER A 855 -1 O LEU A 852 N ILE A 831
SHEET 3 I 6 GLU A 861 ARG A 869 -1 N GLU A 863 O SER A 855
SHEET 4 I 6 THR A 788 THR A 796 -1 O THR A 788 N ARG A 869
SHEET 5 I 6 VAL A 706 TYR A 715 -1 N HIS A 709 O GLU A 795
SHEET 6 I 6 SER A 736 PRO A 737 -1 O SER A 736 N LYS A 714
SHEET 1 J 5 LEU A 957 ARG A 964 0
SHEET 2 J 5 GLN A 973 ARG A 981 -1 N GLY A 976 O ARG A 963
SHEET 3 J 5 THR A1036 HIS A1043 -1 O ALA A1037 N LEU A 979
SHEET 4 J 5 VAL A1006 THR A1012 -1 N ALA A1007 O SER A1042
SHEET 5 J 5 ASN A1019 HIS A1022 -1 N LEU A1020 O ARG A1011
SSBOND 1 CYS A 31 CYS A 1032 1555 1555 2.03
SSBOND 2 CYS A 275 CYS A 282 1555 1555 2.03
SSBOND 3 CYS A 283 CYS A 297 1555 1555 2.04
SSBOND 4 CYS A 902 CYS A 987 1555 1555 2.03
SSBOND 5 CYS A 1000 CYS A 1009 1555 1555 2.02
LINK ND2 ASN A 194 C1 NAG A1101 1555 1555 1.45
LINK NE2 HIS A 90 ZN ZN A1102 1555 1555 2.11
LINK OD1 ASP A 92 ZN ZN A1102 1555 1555 2.08
LINK OD1 ASP A 204 ZN ZN A1102 1555 1555 2.11
LINK NE2 HIS A 471 ZN ZN A1102 1555 1555 2.15
LINK ZN ZN A1102 O2 DMJ A1103 1555 1555 2.41
LINK ZN ZN A1102 O3 DMJ A1103 1555 1555 2.33
CISPEP 1 PHE A 405 THR A 406 0 -0.04
CISPEP 2 TRP A 531 PRO A 532 0 -0.22
CRYST1 68.814 109.616 138.281 90.00 90.00 90.00 P 21 21 21 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 0.014532 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009123 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007232 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
