HEADER SIGNALING PROTEIN 02-APR-04 1SYT
TITLE CRYSTAL STRUCTURE OF SIGNALLING PROTEIN FROM GOAT SPG-40 IN THE
TITLE 2 PRESENSE OF N,N',N''-TRIACETYL-CHITOTRIOSE AT 2.6A RESOLUTION
CAVEAT 1SYT NAG B 1 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BP40;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SPG-40
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAPRA HIRCUS;
SOURCE 3 ORGANISM_COMMON: GOAT;
SOURCE 4 ORGANISM_TAXID: 9925
KEYWDS SIGNALLING PROTEIN, GOAT SPG-40, 2.6A RESOLUTION, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KUMAR,R.PREM KUMAR,D.B.SRIVASTAVA,S.SHARMA,T.P.SINGH
REVDAT 5 25-OCT-23 1SYT 1 HETSYN
REVDAT 4 29-JUL-20 1SYT 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 13-JUL-11 1SYT 1 VERSN
REVDAT 2 24-FEB-09 1SYT 1 VERSN
REVDAT 1 20-APR-04 1SYT 0
JRNL AUTH J.KUMAR,R.PREM KUMAR,D.B.SRIVASTAVA,S.SHARMA,T.P.SINGH
JRNL TITL CRYSTAL STRUCTURE OF SIGNALLING PROTEIN FROM GOAT SPG-40 IN
JRNL TITL 2 THE PRESENSE OF N,N',N''-TRIACETYL-CHITOTRIOSE AT 2.6A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
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) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 12892
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 671
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) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 926
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2874
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.30000
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): 1.313
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.288
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.304
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.361
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2992 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2649 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4056 ; 1.725 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6126 ; 1.256 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 359 ; 2.605 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 496 ;19.652 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 437 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3318 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 671 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 697 ; 0.252 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2635 ; 0.243 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1 ; 0.157 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 202 ; 0.143 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 3 ; 0.177 ; 0.500
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): 3 ; 0.121 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 26 ; 0.260 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.115 ; 0.500
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): 1791 ; 1.353 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2869 ; 2.538 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1201 ; 2.971 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1187 ; 4.850 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1SYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022101.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JAN-04
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5414
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13563
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
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) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 1QZO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM TRIS-HCL, 50MM NACL, 19% ETHANOL,
REMARK 280 PH 7.8, VAPOR 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 31.55550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.81300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.01800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.81300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.55550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.01800
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 300 REMARK: THE BIOLOGICAL UNIT IS MONOMER
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, 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 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 ASP A 112 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 178 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 280 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 LEU A 320 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH2 ANGL. DEV. = -3.9 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 PHE A 37 103.93 78.44
REMARK 500 TRP A 48 -63.89 -126.48
REMARK 500 ALA A 117 50.50 -111.58
REMARK 500 TRP A 118 95.50 -66.04
REMARK 500 TYR A 120 99.16 77.32
REMARK 500 ASP A 169 71.13 -104.60
REMARK 500 TYR A 185 23.20 -157.85
REMARK 500 ALA A 190 -4.62 -53.47
REMARK 500 GLN A 193 56.90 -53.29
REMARK 500 ASN A 205 73.01 -61.36
REMARK 500 SER A 206 10.29 -167.73
REMARK 500 ASP A 207 104.08 -178.22
REMARK 500 SER A 210 45.96 76.56
REMARK 500 SER A 214 51.19 -94.77
REMARK 500 ALA A 332 107.37 72.23
REMARK 500 GLN A 345 122.50 -21.26
REMARK 500 ASN A 346 13.73 -65.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QZO RELATED DB: PDB
DBREF 1SYT A 1 362 GB 19526603 AAL87007 22 383
SEQADV 1SYT VAL A 33 GB 19526603 ILE 54 SEE REMARK 999
SEQADV 1SYT ALA A 131 GB 19526603 GLY 152 SEE REMARK 999
SEQADV 1SYT ASN A 205 GB 19526603 GLN 226 SEE REMARK 999
SEQADV 1SYT SER A 206 GB 19526603 GLU 227 SEE REMARK 999
SEQADV 1SYT A GB 19526603 ASP 232 SEE REMARK 999
SEQADV 1SYT GLY A 253 GB 19526603 VAL 274 SEE REMARK 999
SEQADV 1SYT ARG A 361 GB 19526603 GLU 382 SEE REMARK 999
SEQRES 1 A 361 TYR LYS LEU ILE CYS TYR TYR THR SER TRP SER GLN TYR
SEQRES 2 A 361 ARG GLU GLY ASP GLY SER CYS PHE PRO ASP ALA ILE ASP
SEQRES 3 A 361 PRO PHE LEU CYS THR HIS VAL ILE TYR SER PHE ALA ASN
SEQRES 4 A 361 ILE SER ASN ASN GLU ILE ASP THR TRP GLU TRP ASN ASP
SEQRES 5 A 361 VAL THR LEU TYR ASP THR LEU ASN THR LEU LYS ASN ARG
SEQRES 6 A 361 ASN PRO LYS LEU LYS THR LEU LEU SER VAL GLY GLY TRP
SEQRES 7 A 361 ASN PHE GLY PRO GLU ARG PHE SER LYS ILE ALA SER LYS
SEQRES 8 A 361 THR GLN SER ARG ARG THR PHE ILE LYS SER VAL PRO PRO
SEQRES 9 A 361 PHE LEU ARG THR HIS GLY PHE ASP GLY LEU ASP LEU ALA
SEQRES 10 A 361 TRP LEU TYR PRO GLY ARG ARG ASP LYS ARG HIS LEU THR
SEQRES 11 A 361 ALA LEU VAL LYS GLU MET LYS ALA GLU PHE ALA ARG GLU
SEQRES 12 A 361 ALA GLN ALA GLY THR GLU ARG LEU LEU LEU SER ALA ALA
SEQRES 13 A 361 VAL SER ALA GLY LYS ILE ALA ILE ASP ARG GLY TYR ASP
SEQRES 14 A 361 ILE ALA GLN ILE SER ARG HIS LEU ASP PHE ILE SER LEU
SEQRES 15 A 361 LEU THR TYR ASP PHE HIS GLY ALA TRP ARG GLN THR VAL
SEQRES 16 A 361 GLY HIS HIS SER PRO LEU PHE ARG GLY ASN SER ASP ALA
SEQRES 17 A 361 SER SER ARG PHE SER ASN ALA ASP TYR ALA VAL SER TYR
SEQRES 18 A 361 MET LEU ARG LEU GLY ALA PRO ALA ASN LYS LEU VAL MET
SEQRES 19 A 361 GLY ILE PRO THR PHE GLY ARG SER PHE THR LEU ALA SER
SEQRES 20 A 361 SER LYS THR ASP GLY GLY ALA PRO ILE SER GLY PRO GLY
SEQRES 21 A 361 ILE PRO GLY ARG PHE THR LYS GLU LYS GLY ILE LEU ALA
SEQRES 22 A 361 TYR TYR GLU ILE CYS ASP PHE LEU HIS GLY ALA THR THR
SEQRES 23 A 361 HIS ARG PHE ARG ASP GLN GLN VAL PRO TYR ALA THR LYS
SEQRES 24 A 361 GLY ASN GLN TRP VAL ALA TYR ASP ASP GLN GLU SER VAL
SEQRES 25 A 361 LYS ASN LYS ALA ARG TYR LEU LYS ASN ARG GLN LEU ALA
SEQRES 26 A 361 GLY ALA MET VAL TRP ALA LEU ASP LEU ASP ASP PHE ARG
SEQRES 27 A 361 GLY THR PHE CYS GLY GLN ASN LEU THR PHE PRO LEU THR
SEQRES 28 A 361 SER ALA VAL LYS ASP VAL LEU ALA ARG VAL
MODRES 1SYT ASN A 39 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET MAN B 3 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
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
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 MAN C6 H12 O6
FORMUL 3 HOH *204(H2 O)
HELIX 1 1 TRP A 10 ARG A 14 5 5
HELIX 2 2 GLU A 15 SER A 19 5 5
HELIX 3 3 PHE A 21 ILE A 25 5 5
HELIX 4 4 ASN A 51 THR A 61 1 11
HELIX 5 5 THR A 61 ASN A 66 1 6
HELIX 6 6 GLY A 81 LYS A 91 1 11
HELIX 7 7 LYS A 91 GLY A 110 1 20
HELIX 8 8 ASP A 125 ALA A 144 1 20
HELIX 9 9 GLN A 145 GLY A 147 5 3
HELIX 10 10 GLY A 160 TYR A 168 1 9
HELIX 11 11 ASP A 169 ARG A 175 1 7
HELIX 12 12 ASN A 215 LEU A 226 1 12
HELIX 13 13 PRO A 229 ASN A 231 5 3
HELIX 14 14 TYR A 275 LEU A 282 1 8
HELIX 15 15 ASP A 309 ARG A 323 1 15
HELIX 16 16 PHE A 349 ARG A 361 1 13
SHEET 1 A10 GLU A 44 ASP A 46 0
SHEET 2 A10 HIS A 32 SER A 41 -1 N SER A 41 O GLU A 44
SHEET 3 A10 LYS A 70 GLY A 76 1 O LEU A 72 N TYR A 35
SHEET 4 A10 GLY A 113 ALA A 117 1 O ASP A 115 N LEU A 73
SHEET 5 A10 LEU A 152 VAL A 157 1 O LEU A 152 N LEU A 114
SHEET 6 A10 PHE A 179 LEU A 182 1 O SER A 181 N VAL A 157
SHEET 7 A10 LEU A 233 PRO A 238 1 O VAL A 234 N LEU A 182
SHEET 8 A10 GLY A 327 TRP A 331 1 O MET A 329 N ILE A 237
SHEET 9 A10 LYS A 2 THR A 8 1 N ILE A 4 O VAL A 330
SHEET 10 A10 HIS A 32 SER A 41 1 O SER A 36 N TYR A 7
SHEET 1 B 3 ILE A 257 PRO A 260 0
SHEET 2 B 3 PHE A 240 LEU A 246 -1 N THR A 245 O GLY A 259
SHEET 3 B 3 ILE A 272 ALA A 274 -1 O LEU A 273 N GLY A 241
SHEET 1 C 5 ILE A 257 PRO A 260 0
SHEET 2 C 5 PHE A 240 LEU A 246 -1 N THR A 245 O GLY A 259
SHEET 3 C 5 GLN A 303 ALA A 306 -1 O ALA A 306 N ARG A 242
SHEET 4 C 5 VAL A 295 LYS A 300 -1 N ALA A 298 O VAL A 305
SHEET 5 C 5 THR A 286 PHE A 290 -1 N HIS A 288 O TYR A 297
SSBOND 1 CYS A 5 CYS A 30 1555 1555 2.01
SSBOND 2 CYS A 279 CYS A 343 1555 1555 2.04
LINK ND2 ASN A 39 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 2.00
LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.47
CRYST1 63.111 66.036 107.626 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 0.015845 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015143 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009291 0.00000
(ATOM LINES ARE NOT SHOWN.)
END