HEADER CYTOKINE/SIGNALING PROTEIN 29-NOV-06 2O26
TITLE STRUCTURE OF A CLASS III RTK SIGNALING ASSEMBLY
CAVEAT 2O26 NAG L 1 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIT LIGAND;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 FRAGMENT: RESIDUES 28-166;
COMPND 5 SYNONYM: C-KIT LIGAND, STEM CELL FACTOR, SCF, MAST CELL GROWTH
COMPND 6 FACTOR, MGF, HEMATOPOIETIC GROWTH FACTOR KL, STEEL FACTOR;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MAST/STEM CELL GROWTH FACTOR RECEPTOR;
COMPND 11 CHAIN: X, Y, U, W;
COMPND 12 FRAGMENT: RESIDUES 25-314;
COMPND 13 SYNONYM: SCFR, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE KIT, C-KIT,
COMPND 14 CD117 ANTIGEN;
COMPND 15 EC: 2.7.10.1;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: KITLG, KITL, MGF, SL, SLF;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PACGP67A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: KIT, SL;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS STEM CELL FACTOR, RECEPTOR TYROSINE KINASE, CLASS III, RECEPTOR-
KEYWDS 2 LIGAND COMPLEX, GROWTH FACTOR, CYTOKINE, 4-HELIX BUNDLE, CYTOKINE-
KEYWDS 3 SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LIU,X.CHEN,P.J.FOCIA,X.HE
REVDAT 6 27-DEC-23 2O26 1 REMARK
REVDAT 5 20-OCT-21 2O26 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 2O26 1 CAVEAT COMPND REMARK SEQADV
REVDAT 4 2 1 HET HETNAM FORMUL LINK
REVDAT 4 3 1 SITE ATOM
REVDAT 3 13-JUL-11 2O26 1 VERSN
REVDAT 2 24-FEB-09 2O26 1 VERSN
REVDAT 1 13-MAR-07 2O26 0
JRNL AUTH H.LIU,X.CHEN,P.J.FOCIA,X.HE
JRNL TITL STRUCTURAL BASIS FOR STEM CELL FACTOR-KIT SIGNALING AND
JRNL TITL 2 ACTIVATION OF CLASS III RECEPTOR TYROSINE KINASES.
JRNL REF EMBO J. V. 26 891 2007
JRNL REFN ISSN 0261-4189
JRNL PMID 17255936
JRNL DOI 10.1038/SJ.EMBOJ.7601545
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2913310.310
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 82454
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) : 0.237
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4155
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12641
REMARK 3 BIN R VALUE (WORKING SET) : 0.4020
REMARK 3 BIN FREE R VALUE : 0.4170
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 648
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13066
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 308
REMARK 3 SOLVENT ATOMS : 1730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 98.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.75000
REMARK 3 B22 (A**2) : 15.28000
REMARK 3 B33 (A**2) : -16.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : 0.70
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) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.76
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.100
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.21
REMARK 3 BSOL : 46.88
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2O26 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040592.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 5ID-B
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82592
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 96.8
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.38900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, MES, PH 6.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 100.07700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X, Y, C, D, G, H
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, U, W, I, J, K, L
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 HIS A 147
REMARK 465 HIS B 142
REMARK 465 HIS B 143
REMARK 465 HIS B 144
REMARK 465 HIS B 145
REMARK 465 HIS B 146
REMARK 465 HIS B 147
REMARK 465 HIS E 142
REMARK 465 HIS E 143
REMARK 465 HIS E 144
REMARK 465 HIS E 145
REMARK 465 HIS E 146
REMARK 465 HIS E 147
REMARK 465 HIS F 142
REMARK 465 HIS F 143
REMARK 465 HIS F 144
REMARK 465 HIS F 145
REMARK 465 HIS F 146
REMARK 465 HIS F 147
REMARK 465 SER X 25
REMARK 465 GLN X 26
REMARK 465 PRO X 27
REMARK 465 SER X 28
REMARK 465 ALA X 29
REMARK 465 SER X 30
REMARK 465 PRO X 31
REMARK 465 GLY X 32
REMARK 465 GLU X 33
REMARK 465 PRO X 34
REMARK 465 SER X 35
REMARK 465 VAL X 311
REMARK 465 GLU X 312
REMARK 465 LYS X 313
REMARK 465 GLY X 314
REMARK 465 SER Y 25
REMARK 465 GLN Y 26
REMARK 465 PRO Y 27
REMARK 465 SER Y 28
REMARK 465 ALA Y 29
REMARK 465 SER Y 30
REMARK 465 PRO Y 31
REMARK 465 GLY Y 32
REMARK 465 GLU Y 33
REMARK 465 PRO Y 34
REMARK 465 SER Y 35
REMARK 465 VAL Y 311
REMARK 465 GLU Y 312
REMARK 465 LYS Y 313
REMARK 465 GLY Y 314
REMARK 465 SER U 25
REMARK 465 GLN U 26
REMARK 465 PRO U 27
REMARK 465 SER U 28
REMARK 465 ALA U 29
REMARK 465 SER U 30
REMARK 465 PRO U 31
REMARK 465 GLY U 32
REMARK 465 GLU U 33
REMARK 465 PRO U 34
REMARK 465 SER U 35
REMARK 465 VAL U 311
REMARK 465 GLU U 312
REMARK 465 LYS U 313
REMARK 465 GLY U 314
REMARK 465 SER W 25
REMARK 465 GLN W 26
REMARK 465 PRO W 27
REMARK 465 SER W 28
REMARK 465 ALA W 29
REMARK 465 SER W 30
REMARK 465 PRO W 31
REMARK 465 GLY W 32
REMARK 465 GLU W 33
REMARK 465 PRO W 34
REMARK 465 SER W 35
REMARK 465 VAL W 311
REMARK 465 GLU W 312
REMARK 465 LYS W 313
REMARK 465 GLY W 314
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 CD LYS U 79 O HOH U 544 0.79
REMARK 500 CE LYS U 79 O HOH U 544 1.39
REMARK 500 CG LYS U 79 O HOH U 544 1.94
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 SER B 133 CA SER B 133 CB 0.117
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 PRO A 102 CA - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO X 41 CA - N - CD ANGL. DEV. = -17.6 DEGREES
REMARK 500 CYS X 152 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 CYS Y 98 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 CYS Y 152 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 PRO U 138 CA - N - CD ANGL. DEV. = -20.9 DEGREES
REMARK 500 CYS W 152 CA - CB - SG ANGL. DEV. = 6.8 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 ILE A 66 -78.07 -86.09
REMARK 500 SER A 67 -154.60 -143.91
REMARK 500 LEU A 70 96.10 -54.71
REMARK 500 LYS A 99 78.55 31.65
REMARK 500 SER A 101 54.98 -156.90
REMARK 500 PRO A 102 -86.69 -45.91
REMARK 500 LYS A 103 119.22 -176.44
REMARK 500 ARG A 104 155.50 -36.90
REMARK 500 CYS A 138 52.64 -102.09
REMARK 500 HIS A 142 56.95 -90.36
REMARK 500 HIS A 144 26.50 -78.40
REMARK 500 HIS A 145 117.00 71.16
REMARK 500 ILE B 66 -78.58 -86.39
REMARK 500 SER B 67 -155.12 -143.42
REMARK 500 LEU B 70 94.62 -54.09
REMARK 500 LYS B 99 77.51 32.26
REMARK 500 SER B 101 44.16 -159.35
REMARK 500 PRO B 102 -94.70 -32.79
REMARK 500 LYS B 103 119.92 -172.62
REMARK 500 ARG B 104 154.65 -34.53
REMARK 500 SER B 136 103.07 -49.27
REMARK 500 VAL B 139 -159.02 -112.74
REMARK 500 ILE E 66 -78.59 -85.63
REMARK 500 SER E 67 -154.86 -143.00
REMARK 500 LEU E 70 95.46 -54.41
REMARK 500 LYS E 99 77.90 31.81
REMARK 500 SER E 101 44.16 -159.65
REMARK 500 PRO E 102 -94.24 -32.90
REMARK 500 LYS E 103 120.90 -172.67
REMARK 500 ARG E 104 155.99 -36.98
REMARK 500 SER E 136 -153.89 -141.37
REMARK 500 ILE F 66 -78.48 -86.48
REMARK 500 SER F 67 -154.47 -143.48
REMARK 500 LEU F 70 95.16 -54.08
REMARK 500 LYS F 99 78.27 32.04
REMARK 500 SER F 101 44.10 -159.62
REMARK 500 PRO F 102 -94.53 -32.99
REMARK 500 LYS F 103 119.91 -172.33
REMARK 500 ARG F 104 152.55 -33.82
REMARK 500 CYS F 138 30.74 -88.10
REMARK 500 LEU F 140 108.33 -54.57
REMARK 500 PRO X 41 84.94 -56.85
REMARK 500 VAL X 64 -70.99 -120.04
REMARK 500 ASN X 73 86.04 -43.55
REMARK 500 SER X 131 -161.91 -123.65
REMARK 500 ARG X 136 85.40 -66.20
REMARK 500 ALA X 169 -48.73 -133.18
REMARK 500 ASN X 175 79.36 42.11
REMARK 500 PRO X 218 -70.41 -48.26
REMARK 500 ASN X 251 -65.16 -124.13
REMARK 500
REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O27 RELATED DB: PDB
REMARK 900 STRUCTURE OF A CLASS III RTK SIGNALING ASSEMBLY
DBREF 2O26 A 3 141 UNP P20826 SCF_MOUSE 28 166
DBREF 2O26 B 3 141 UNP P20826 SCF_MOUSE 28 166
DBREF 2O26 E 3 141 UNP P20826 SCF_MOUSE 28 166
DBREF 2O26 F 3 141 UNP P20826 SCF_MOUSE 28 166
DBREF 2O26 U 25 314 UNP P05532 KIT_MOUSE 25 314
DBREF 2O26 W 25 314 UNP P05532 KIT_MOUSE 25 314
DBREF 2O26 X 25 314 UNP P05532 KIT_MOUSE 25 314
DBREF 2O26 Y 25 314 UNP P05532 KIT_MOUSE 25 314
SEQADV 2O26 HIS A 142 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS A 143 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS A 144 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS A 145 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS A 146 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS A 147 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS B 142 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS B 143 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS B 144 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS B 145 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS B 146 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS B 147 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS E 142 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS E 143 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS E 144 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS E 145 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS E 146 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS E 147 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS F 142 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS F 143 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS F 144 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS F 145 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS F 146 UNP P20826 EXPRESSION TAG
SEQADV 2O26 HIS F 147 UNP P20826 EXPRESSION TAG
SEQADV 2O26 GLN U 146 UNP P05532 ASN 146 ENGINEERED MUTATION
SEQADV 2O26 GLN W 146 UNP P05532 ASN 146 ENGINEERED MUTATION
SEQADV 2O26 GLN X 146 UNP P05532 ASN 146 ENGINEERED MUTATION
SEQADV 2O26 GLN Y 146 UNP P05532 ASN 146 ENGINEERED MUTATION
SEQRES 1 A 145 ILE CYS GLY ASN PRO VAL THR ASP ASN VAL LYS ASP ILE
SEQRES 2 A 145 THR LYS LEU VAL ALA ASN LEU PRO ASN ASP TYR MET ILE
SEQRES 3 A 145 THR LEU ASN TYR VAL ALA GLY MET ASP VAL LEU PRO SER
SEQRES 4 A 145 HIS CYS TRP LEU ARG ASP MET VAL ILE GLN LEU SER LEU
SEQRES 5 A 145 SER LEU THR THR LEU LEU ASP LYS PHE SER ASN ILE SER
SEQRES 6 A 145 GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS LEU GLY
SEQRES 7 A 145 LYS ILE VAL ASP ASP LEU VAL LEU CYS MET GLU GLU ASN
SEQRES 8 A 145 ALA PRO LYS ASN ILE LYS GLU SER PRO LYS ARG PRO GLU
SEQRES 9 A 145 THR ARG SER PHE THR PRO GLU GLU PHE PHE SER ILE PHE
SEQRES 10 A 145 ASN ARG SER ILE ASP ALA PHE LYS ASP PHE MET VAL ALA
SEQRES 11 A 145 SER ASP THR SER ASP CYS VAL LEU SER HIS HIS HIS HIS
SEQRES 12 A 145 HIS HIS
SEQRES 1 B 145 ILE CYS GLY ASN PRO VAL THR ASP ASN VAL LYS ASP ILE
SEQRES 2 B 145 THR LYS LEU VAL ALA ASN LEU PRO ASN ASP TYR MET ILE
SEQRES 3 B 145 THR LEU ASN TYR VAL ALA GLY MET ASP VAL LEU PRO SER
SEQRES 4 B 145 HIS CYS TRP LEU ARG ASP MET VAL ILE GLN LEU SER LEU
SEQRES 5 B 145 SER LEU THR THR LEU LEU ASP LYS PHE SER ASN ILE SER
SEQRES 6 B 145 GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS LEU GLY
SEQRES 7 B 145 LYS ILE VAL ASP ASP LEU VAL LEU CYS MET GLU GLU ASN
SEQRES 8 B 145 ALA PRO LYS ASN ILE LYS GLU SER PRO LYS ARG PRO GLU
SEQRES 9 B 145 THR ARG SER PHE THR PRO GLU GLU PHE PHE SER ILE PHE
SEQRES 10 B 145 ASN ARG SER ILE ASP ALA PHE LYS ASP PHE MET VAL ALA
SEQRES 11 B 145 SER ASP THR SER ASP CYS VAL LEU SER HIS HIS HIS HIS
SEQRES 12 B 145 HIS HIS
SEQRES 1 E 145 ILE CYS GLY ASN PRO VAL THR ASP ASN VAL LYS ASP ILE
SEQRES 2 E 145 THR LYS LEU VAL ALA ASN LEU PRO ASN ASP TYR MET ILE
SEQRES 3 E 145 THR LEU ASN TYR VAL ALA GLY MET ASP VAL LEU PRO SER
SEQRES 4 E 145 HIS CYS TRP LEU ARG ASP MET VAL ILE GLN LEU SER LEU
SEQRES 5 E 145 SER LEU THR THR LEU LEU ASP LYS PHE SER ASN ILE SER
SEQRES 6 E 145 GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS LEU GLY
SEQRES 7 E 145 LYS ILE VAL ASP ASP LEU VAL LEU CYS MET GLU GLU ASN
SEQRES 8 E 145 ALA PRO LYS ASN ILE LYS GLU SER PRO LYS ARG PRO GLU
SEQRES 9 E 145 THR ARG SER PHE THR PRO GLU GLU PHE PHE SER ILE PHE
SEQRES 10 E 145 ASN ARG SER ILE ASP ALA PHE LYS ASP PHE MET VAL ALA
SEQRES 11 E 145 SER ASP THR SER ASP CYS VAL LEU SER HIS HIS HIS HIS
SEQRES 12 E 145 HIS HIS
SEQRES 1 F 145 ILE CYS GLY ASN PRO VAL THR ASP ASN VAL LYS ASP ILE
SEQRES 2 F 145 THR LYS LEU VAL ALA ASN LEU PRO ASN ASP TYR MET ILE
SEQRES 3 F 145 THR LEU ASN TYR VAL ALA GLY MET ASP VAL LEU PRO SER
SEQRES 4 F 145 HIS CYS TRP LEU ARG ASP MET VAL ILE GLN LEU SER LEU
SEQRES 5 F 145 SER LEU THR THR LEU LEU ASP LYS PHE SER ASN ILE SER
SEQRES 6 F 145 GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS LEU GLY
SEQRES 7 F 145 LYS ILE VAL ASP ASP LEU VAL LEU CYS MET GLU GLU ASN
SEQRES 8 F 145 ALA PRO LYS ASN ILE LYS GLU SER PRO LYS ARG PRO GLU
SEQRES 9 F 145 THR ARG SER PHE THR PRO GLU GLU PHE PHE SER ILE PHE
SEQRES 10 F 145 ASN ARG SER ILE ASP ALA PHE LYS ASP PHE MET VAL ALA
SEQRES 11 F 145 SER ASP THR SER ASP CYS VAL LEU SER HIS HIS HIS HIS
SEQRES 12 F 145 HIS HIS
SEQRES 1 X 290 SER GLN PRO SER ALA SER PRO GLY GLU PRO SER PRO PRO
SEQRES 2 X 290 SER ILE HIS PRO ALA GLN SER GLU LEU ILE VAL GLU ALA
SEQRES 3 X 290 GLY ASP THR LEU SER LEU THR CYS ILE ASP PRO ASP PHE
SEQRES 4 X 290 VAL ARG TRP THR PHE LYS THR TYR PHE ASN GLU MET VAL
SEQRES 5 X 290 GLU ASN LYS LYS ASN GLU TRP ILE GLN GLU LYS ALA GLU
SEQRES 6 X 290 ALA THR ARG THR GLY THR TYR THR CYS SER ASN SER ASN
SEQRES 7 X 290 GLY LEU THR SER SER ILE TYR VAL PHE VAL ARG ASP PRO
SEQRES 8 X 290 ALA LYS LEU PHE LEU VAL GLY LEU PRO LEU PHE GLY LYS
SEQRES 9 X 290 GLU ASP SER ASP ALA LEU VAL ARG CYS PRO LEU THR ASP
SEQRES 10 X 290 PRO GLN VAL SER GLN TYR SER LEU ILE GLU CYS ASP GLY
SEQRES 11 X 290 LYS SER LEU PRO THR ASP LEU THR PHE VAL PRO ASN PRO
SEQRES 12 X 290 LYS ALA GLY ILE THR ILE LYS ASN VAL LYS ARG ALA TYR
SEQRES 13 X 290 HIS ARG LEU CYS VAL ARG CYS ALA ALA GLN ARG ASP GLY
SEQRES 14 X 290 THR TRP LEU HIS SER ASP LYS PHE THR LEU LYS VAL ARG
SEQRES 15 X 290 GLU ALA ILE LYS ALA ILE PRO VAL VAL SER VAL PRO GLU
SEQRES 16 X 290 THR SER HIS LEU LEU LYS LYS GLY ASP THR PHE THR VAL
SEQRES 17 X 290 VAL CYS THR ILE LYS ASP VAL SER THR SER VAL ASN SER
SEQRES 18 X 290 MET TRP LEU LYS MET ASN PRO GLN PRO GLN HIS ILE ALA
SEQRES 19 X 290 GLN VAL LYS HIS ASN SER TRP HIS ARG GLY ASP PHE ASN
SEQRES 20 X 290 TYR GLU ARG GLN GLU THR LEU THR ILE SER SER ALA ARG
SEQRES 21 X 290 VAL ASP ASP SER GLY VAL PHE MET CYS TYR ALA ASN ASN
SEQRES 22 X 290 THR PHE GLY SER ALA ASN VAL THR THR THR LEU LYS VAL
SEQRES 23 X 290 VAL GLU LYS GLY
SEQRES 1 Y 290 SER GLN PRO SER ALA SER PRO GLY GLU PRO SER PRO PRO
SEQRES 2 Y 290 SER ILE HIS PRO ALA GLN SER GLU LEU ILE VAL GLU ALA
SEQRES 3 Y 290 GLY ASP THR LEU SER LEU THR CYS ILE ASP PRO ASP PHE
SEQRES 4 Y 290 VAL ARG TRP THR PHE LYS THR TYR PHE ASN GLU MET VAL
SEQRES 5 Y 290 GLU ASN LYS LYS ASN GLU TRP ILE GLN GLU LYS ALA GLU
SEQRES 6 Y 290 ALA THR ARG THR GLY THR TYR THR CYS SER ASN SER ASN
SEQRES 7 Y 290 GLY LEU THR SER SER ILE TYR VAL PHE VAL ARG ASP PRO
SEQRES 8 Y 290 ALA LYS LEU PHE LEU VAL GLY LEU PRO LEU PHE GLY LYS
SEQRES 9 Y 290 GLU ASP SER ASP ALA LEU VAL ARG CYS PRO LEU THR ASP
SEQRES 10 Y 290 PRO GLN VAL SER GLN TYR SER LEU ILE GLU CYS ASP GLY
SEQRES 11 Y 290 LYS SER LEU PRO THR ASP LEU THR PHE VAL PRO ASN PRO
SEQRES 12 Y 290 LYS ALA GLY ILE THR ILE LYS ASN VAL LYS ARG ALA TYR
SEQRES 13 Y 290 HIS ARG LEU CYS VAL ARG CYS ALA ALA GLN ARG ASP GLY
SEQRES 14 Y 290 THR TRP LEU HIS SER ASP LYS PHE THR LEU LYS VAL ARG
SEQRES 15 Y 290 GLU ALA ILE LYS ALA ILE PRO VAL VAL SER VAL PRO GLU
SEQRES 16 Y 290 THR SER HIS LEU LEU LYS LYS GLY ASP THR PHE THR VAL
SEQRES 17 Y 290 VAL CYS THR ILE LYS ASP VAL SER THR SER VAL ASN SER
SEQRES 18 Y 290 MET TRP LEU LYS MET ASN PRO GLN PRO GLN HIS ILE ALA
SEQRES 19 Y 290 GLN VAL LYS HIS ASN SER TRP HIS ARG GLY ASP PHE ASN
SEQRES 20 Y 290 TYR GLU ARG GLN GLU THR LEU THR ILE SER SER ALA ARG
SEQRES 21 Y 290 VAL ASP ASP SER GLY VAL PHE MET CYS TYR ALA ASN ASN
SEQRES 22 Y 290 THR PHE GLY SER ALA ASN VAL THR THR THR LEU LYS VAL
SEQRES 23 Y 290 VAL GLU LYS GLY
SEQRES 1 U 290 SER GLN PRO SER ALA SER PRO GLY GLU PRO SER PRO PRO
SEQRES 2 U 290 SER ILE HIS PRO ALA GLN SER GLU LEU ILE VAL GLU ALA
SEQRES 3 U 290 GLY ASP THR LEU SER LEU THR CYS ILE ASP PRO ASP PHE
SEQRES 4 U 290 VAL ARG TRP THR PHE LYS THR TYR PHE ASN GLU MET VAL
SEQRES 5 U 290 GLU ASN LYS LYS ASN GLU TRP ILE GLN GLU LYS ALA GLU
SEQRES 6 U 290 ALA THR ARG THR GLY THR TYR THR CYS SER ASN SER ASN
SEQRES 7 U 290 GLY LEU THR SER SER ILE TYR VAL PHE VAL ARG ASP PRO
SEQRES 8 U 290 ALA LYS LEU PHE LEU VAL GLY LEU PRO LEU PHE GLY LYS
SEQRES 9 U 290 GLU ASP SER ASP ALA LEU VAL ARG CYS PRO LEU THR ASP
SEQRES 10 U 290 PRO GLN VAL SER GLN TYR SER LEU ILE GLU CYS ASP GLY
SEQRES 11 U 290 LYS SER LEU PRO THR ASP LEU THR PHE VAL PRO ASN PRO
SEQRES 12 U 290 LYS ALA GLY ILE THR ILE LYS ASN VAL LYS ARG ALA TYR
SEQRES 13 U 290 HIS ARG LEU CYS VAL ARG CYS ALA ALA GLN ARG ASP GLY
SEQRES 14 U 290 THR TRP LEU HIS SER ASP LYS PHE THR LEU LYS VAL ARG
SEQRES 15 U 290 GLU ALA ILE LYS ALA ILE PRO VAL VAL SER VAL PRO GLU
SEQRES 16 U 290 THR SER HIS LEU LEU LYS LYS GLY ASP THR PHE THR VAL
SEQRES 17 U 290 VAL CYS THR ILE LYS ASP VAL SER THR SER VAL ASN SER
SEQRES 18 U 290 MET TRP LEU LYS MET ASN PRO GLN PRO GLN HIS ILE ALA
SEQRES 19 U 290 GLN VAL LYS HIS ASN SER TRP HIS ARG GLY ASP PHE ASN
SEQRES 20 U 290 TYR GLU ARG GLN GLU THR LEU THR ILE SER SER ALA ARG
SEQRES 21 U 290 VAL ASP ASP SER GLY VAL PHE MET CYS TYR ALA ASN ASN
SEQRES 22 U 290 THR PHE GLY SER ALA ASN VAL THR THR THR LEU LYS VAL
SEQRES 23 U 290 VAL GLU LYS GLY
SEQRES 1 W 290 SER GLN PRO SER ALA SER PRO GLY GLU PRO SER PRO PRO
SEQRES 2 W 290 SER ILE HIS PRO ALA GLN SER GLU LEU ILE VAL GLU ALA
SEQRES 3 W 290 GLY ASP THR LEU SER LEU THR CYS ILE ASP PRO ASP PHE
SEQRES 4 W 290 VAL ARG TRP THR PHE LYS THR TYR PHE ASN GLU MET VAL
SEQRES 5 W 290 GLU ASN LYS LYS ASN GLU TRP ILE GLN GLU LYS ALA GLU
SEQRES 6 W 290 ALA THR ARG THR GLY THR TYR THR CYS SER ASN SER ASN
SEQRES 7 W 290 GLY LEU THR SER SER ILE TYR VAL PHE VAL ARG ASP PRO
SEQRES 8 W 290 ALA LYS LEU PHE LEU VAL GLY LEU PRO LEU PHE GLY LYS
SEQRES 9 W 290 GLU ASP SER ASP ALA LEU VAL ARG CYS PRO LEU THR ASP
SEQRES 10 W 290 PRO GLN VAL SER GLN TYR SER LEU ILE GLU CYS ASP GLY
SEQRES 11 W 290 LYS SER LEU PRO THR ASP LEU THR PHE VAL PRO ASN PRO
SEQRES 12 W 290 LYS ALA GLY ILE THR ILE LYS ASN VAL LYS ARG ALA TYR
SEQRES 13 W 290 HIS ARG LEU CYS VAL ARG CYS ALA ALA GLN ARG ASP GLY
SEQRES 14 W 290 THR TRP LEU HIS SER ASP LYS PHE THR LEU LYS VAL ARG
SEQRES 15 W 290 GLU ALA ILE LYS ALA ILE PRO VAL VAL SER VAL PRO GLU
SEQRES 16 W 290 THR SER HIS LEU LEU LYS LYS GLY ASP THR PHE THR VAL
SEQRES 17 W 290 VAL CYS THR ILE LYS ASP VAL SER THR SER VAL ASN SER
SEQRES 18 W 290 MET TRP LEU LYS MET ASN PRO GLN PRO GLN HIS ILE ALA
SEQRES 19 W 290 GLN VAL LYS HIS ASN SER TRP HIS ARG GLY ASP PHE ASN
SEQRES 20 W 290 TYR GLU ARG GLN GLU THR LEU THR ILE SER SER ALA ARG
SEQRES 21 W 290 VAL ASP ASP SER GLY VAL PHE MET CYS TYR ALA ASN ASN
SEQRES 22 W 290 THR PHE GLY SER ALA ASN VAL THR THR THR LEU LYS VAL
SEQRES 23 W 290 VAL GLU LYS GLY
MODRES 2O26 ASN X 296 ASN GLYCOSYLATION SITE
MODRES 2O26 ASN X 303 ASN GLYCOSYLATION SITE
MODRES 2O26 ASN Y 296 ASN GLYCOSYLATION SITE
MODRES 2O26 ASN Y 303 ASN GLYCOSYLATION SITE
MODRES 2O26 ASN U 296 ASN GLYCOSYLATION SITE
MODRES 2O26 ASN U 303 ASN GLYCOSYLATION SITE
MODRES 2O26 ASN W 296 ASN GLYCOSYLATION SITE
MODRES 2O26 ASN W 303 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET FUL C 3 10
HET NAG D 1 14
HET NAG D 2 14
HET MAN D 3 11
HET NAG G 1 14
HET NAG G 2 14
HET FUL G 3 10
HET NAG H 1 14
HET NAG H 2 14
HET MAN H 3 11
HET NAG I 1 14
HET NAG I 2 14
HET FUL I 3 10
HET NAG J 1 14
HET NAG J 2 14
HET MAN J 3 11
HET NAG K 1 14
HET NAG K 2 14
HET FUL K 3 10
HET NAG L 1 14
HET NAG L 2 14
HET MAN L 3 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
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 FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUL FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 9 NAG 16(C8 H15 N O6)
FORMUL 9 FUL 4(C6 H12 O5)
FORMUL 10 MAN 4(C6 H12 O6)
FORMUL 17 HOH *1730(H2 O)
HELIX 1 1 THR A 9 LYS A 13 5 5
HELIX 2 2 ASP A 14 ASN A 21 1 8
HELIX 3 3 PRO A 40 LYS A 62 1 23
HELIX 4 4 SER A 71 MET A 90 1 20
HELIX 5 5 THR A 111 ASP A 128 1 18
HELIX 6 6 THR B 9 LYS B 13 5 5
HELIX 7 7 ASP B 14 ASN B 21 1 8
HELIX 8 8 PRO B 40 LYS B 62 1 23
HELIX 9 9 SER B 71 MET B 90 1 20
HELIX 10 10 THR B 111 ASP B 128 1 18
HELIX 11 11 THR E 9 LYS E 13 5 5
HELIX 12 12 ASP E 14 ASN E 21 1 8
HELIX 13 13 PRO E 40 LYS E 62 1 23
HELIX 14 14 SER E 71 MET E 90 1 20
HELIX 15 15 THR E 111 ASP E 128 1 18
HELIX 16 16 THR F 9 LYS F 13 5 5
HELIX 17 17 ASP F 14 ASN F 21 1 8
HELIX 18 18 PRO F 40 LYS F 62 1 23
HELIX 19 19 SER F 71 MET F 90 1 20
HELIX 20 20 THR F 111 ASP F 128 1 18
HELIX 21 21 GLU X 89 THR X 93 5 5
HELIX 22 22 LYS X 177 HIS X 181 5 5
HELIX 23 23 GLU Y 89 THR Y 93 5 5
HELIX 24 24 LYS Y 177 HIS Y 181 5 5
HELIX 25 25 GLU U 89 THR U 93 5 5
HELIX 26 26 LYS U 177 HIS U 181 5 5
HELIX 27 27 GLU W 89 THR W 93 5 5
HELIX 28 28 LYS W 177 HIS W 181 5 5
SHEET 1 A 2 ILE A 28 TYR A 32 0
SHEET 2 A 2 GLU A 106 PHE A 110 -1 O PHE A 110 N ILE A 28
SHEET 1 B 2 ILE B 28 TYR B 32 0
SHEET 2 B 2 GLU B 106 PHE B 110 -1 O PHE B 110 N ILE B 28
SHEET 1 C 2 ILE E 28 TYR E 32 0
SHEET 2 C 2 GLU E 106 PHE E 110 -1 O PHE E 110 N ILE E 28
SHEET 1 D 2 ILE F 28 TYR F 32 0
SHEET 2 D 2 GLU F 106 PHE F 110 -1 O PHE F 110 N ILE F 28
SHEET 1 E 3 SER X 38 ILE X 39 0
SHEET 2 E 3 LEU X 54 ILE X 59 -1 O ILE X 59 N SER X 38
SHEET 3 E 3 GLU X 82 GLN X 85 -1 O TRP X 83 N LEU X 56
SHEET 1 F 5 GLU X 45 GLU X 49 0
SHEET 2 F 5 THR X 105 ARG X 113 1 O PHE X 111 N LEU X 46
SHEET 3 F 5 GLY X 94 ASN X 100 -1 N GLY X 94 O VAL X 110
SHEET 4 F 5 PHE X 63 LYS X 69 -1 N THR X 67 O THR X 97
SHEET 5 F 5 MET X 75 ASN X 78 -1 O ASN X 78 N TRP X 66
SHEET 1 G 4 LEU X 125 LYS X 128 0
SHEET 2 G 4 PHE X 201 ARG X 206 1 O ARG X 206 N GLY X 127
SHEET 3 G 4 CYS X 184 ARG X 191 -1 N VAL X 185 O PHE X 201
SHEET 4 G 4 SER X 145 GLU X 151 -1 N SER X 145 O GLN X 190
SHEET 1 H 4 LEU X 125 LYS X 128 0
SHEET 2 H 4 PHE X 201 ARG X 206 1 O ARG X 206 N GLY X 127
SHEET 3 H 4 CYS X 184 ARG X 191 -1 N VAL X 185 O PHE X 201
SHEET 4 H 4 THR X 194 HIS X 197 -1 O THR X 194 N ARG X 191
SHEET 1 I 3 ALA X 133 VAL X 135 0
SHEET 2 I 3 GLY X 170 LYS X 174 -1 O ILE X 171 N VAL X 135
SHEET 3 I 3 THR X 162 ASN X 166 -1 N THR X 162 O LYS X 174
SHEET 1 J 4 VAL X 214 SER X 216 0
SHEET 2 J 4 PHE X 230 ASP X 238 -1 O THR X 235 N SER X 216
SHEET 3 J 4 ASN X 271 ILE X 280 -1 O GLU X 276 N CYS X 234
SHEET 4 J 4 VAL X 260 LYS X 261 -1 N LYS X 261 O THR X 277
SHEET 1 K 4 VAL X 214 SER X 216 0
SHEET 2 K 4 PHE X 230 ASP X 238 -1 O THR X 235 N SER X 216
SHEET 3 K 4 ASN X 271 ILE X 280 -1 O GLU X 276 N CYS X 234
SHEET 4 K 4 SER X 264 GLY X 268 -1 N TRP X 265 O GLU X 273
SHEET 1 L 4 PRO X 254 HIS X 256 0
SHEET 2 L 4 ASN X 244 MET X 250 -1 N LYS X 249 O GLN X 255
SHEET 3 L 4 GLY X 289 ASN X 296 -1 O MET X 292 N LEU X 248
SHEET 4 L 4 SER X 301 LEU X 308 -1 O THR X 306 N PHE X 291
SHEET 1 M 3 SER Y 38 ILE Y 39 0
SHEET 2 M 3 LEU Y 54 ILE Y 59 -1 O ILE Y 59 N SER Y 38
SHEET 3 M 3 GLU Y 82 GLN Y 85 -1 O TRP Y 83 N LEU Y 56
SHEET 1 N 5 GLU Y 45 GLU Y 49 0
SHEET 2 N 5 THR Y 105 ARG Y 113 1 O PHE Y 111 N LEU Y 46
SHEET 3 N 5 GLY Y 94 ASN Y 100 -1 N GLY Y 94 O VAL Y 110
SHEET 4 N 5 PHE Y 63 LYS Y 69 -1 N THR Y 67 O THR Y 97
SHEET 5 N 5 MET Y 75 ASN Y 78 -1 O ASN Y 78 N TRP Y 66
SHEET 1 O 4 LEU Y 125 LYS Y 128 0
SHEET 2 O 4 PHE Y 201 ARG Y 206 1 O LYS Y 204 N LEU Y 125
SHEET 3 O 4 CYS Y 184 ARG Y 191 -1 N VAL Y 185 O PHE Y 201
SHEET 4 O 4 SER Y 145 GLU Y 151 -1 N SER Y 145 O GLN Y 190
SHEET 1 P 4 LEU Y 125 LYS Y 128 0
SHEET 2 P 4 PHE Y 201 ARG Y 206 1 O LYS Y 204 N LEU Y 125
SHEET 3 P 4 CYS Y 184 ARG Y 191 -1 N VAL Y 185 O PHE Y 201
SHEET 4 P 4 THR Y 194 HIS Y 197 -1 O THR Y 194 N ARG Y 191
SHEET 1 Q 3 ALA Y 133 VAL Y 135 0
SHEET 2 Q 3 GLY Y 170 LYS Y 174 -1 O ILE Y 171 N VAL Y 135
SHEET 3 Q 3 THR Y 162 ASN Y 166 -1 N THR Y 162 O LYS Y 174
SHEET 1 R 4 VAL Y 214 SER Y 216 0
SHEET 2 R 4 PHE Y 230 ASP Y 238 -1 O THR Y 235 N SER Y 216
SHEET 3 R 4 ASN Y 271 ILE Y 280 -1 O GLU Y 276 N CYS Y 234
SHEET 4 R 4 VAL Y 260 LYS Y 261 -1 N LYS Y 261 O THR Y 277
SHEET 1 S 4 VAL Y 214 SER Y 216 0
SHEET 2 S 4 PHE Y 230 ASP Y 238 -1 O THR Y 235 N SER Y 216
SHEET 3 S 4 ASN Y 271 ILE Y 280 -1 O GLU Y 276 N CYS Y 234
SHEET 4 S 4 SER Y 264 GLY Y 268 -1 N TRP Y 265 O GLU Y 273
SHEET 1 T 5 SER Y 221 HIS Y 222 0
SHEET 2 T 5 SER Y 301 LEU Y 308 1 O THR Y 307 N HIS Y 222
SHEET 3 T 5 GLY Y 289 ASN Y 296 -1 N PHE Y 291 O THR Y 306
SHEET 4 T 5 ASN Y 244 MET Y 250 -1 N LEU Y 248 O MET Y 292
SHEET 5 T 5 PRO Y 254 HIS Y 256 -1 O GLN Y 255 N LYS Y 249
SHEET 1 U 3 SER U 38 ILE U 39 0
SHEET 2 U 3 LEU U 54 ILE U 59 -1 O ILE U 59 N SER U 38
SHEET 3 U 3 GLU U 82 GLN U 85 -1 O TRP U 83 N LEU U 56
SHEET 1 V 5 GLU U 45 GLU U 49 0
SHEET 2 V 5 THR U 105 ARG U 113 1 O PHE U 111 N LEU U 46
SHEET 3 V 5 GLY U 94 ASN U 100 -1 N GLY U 94 O VAL U 110
SHEET 4 V 5 PHE U 63 LYS U 69 -1 N THR U 67 O THR U 97
SHEET 5 V 5 MET U 75 ASN U 78 -1 O ASN U 78 N TRP U 66
SHEET 1 W 4 LEU U 125 LYS U 128 0
SHEET 2 W 4 PHE U 201 ARG U 206 1 O LYS U 204 N LEU U 125
SHEET 3 W 4 CYS U 184 ARG U 191 -1 N VAL U 185 O PHE U 201
SHEET 4 W 4 SER U 145 GLU U 151 -1 N SER U 148 O ALA U 188
SHEET 1 X 4 LEU U 125 LYS U 128 0
SHEET 2 X 4 PHE U 201 ARG U 206 1 O LYS U 204 N LEU U 125
SHEET 3 X 4 CYS U 184 ARG U 191 -1 N VAL U 185 O PHE U 201
SHEET 4 X 4 THR U 194 HIS U 197 -1 O THR U 194 N ARG U 191
SHEET 1 Y 3 ALA U 133 VAL U 135 0
SHEET 2 Y 3 ILE U 171 LYS U 174 -1 O ILE U 171 N VAL U 135
SHEET 3 Y 3 THR U 162 VAL U 164 -1 N THR U 162 O LYS U 174
SHEET 1 Z 4 VAL U 214 SER U 216 0
SHEET 2 Z 4 PHE U 230 ASP U 238 -1 O THR U 235 N SER U 216
SHEET 3 Z 4 ASN U 271 ILE U 280 -1 O TYR U 272 N ASP U 238
SHEET 4 Z 4 VAL U 260 LYS U 261 -1 N LYS U 261 O THR U 277
SHEET 1 AA 4 VAL U 214 SER U 216 0
SHEET 2 AA 4 PHE U 230 ASP U 238 -1 O THR U 235 N SER U 216
SHEET 3 AA 4 ASN U 271 ILE U 280 -1 O TYR U 272 N ASP U 238
SHEET 4 AA 4 SER U 264 GLY U 268 -1 N TRP U 265 O GLU U 273
SHEET 1 AB 4 PRO U 254 HIS U 256 0
SHEET 2 AB 4 ASN U 244 MET U 250 -1 N LYS U 249 O GLN U 255
SHEET 3 AB 4 GLY U 289 ASN U 296 -1 O MET U 292 N LEU U 248
SHEET 4 AB 4 SER U 301 LEU U 308 -1 O LEU U 308 N GLY U 289
SHEET 1 AC 3 SER W 38 ILE W 39 0
SHEET 2 AC 3 LEU W 54 ILE W 59 -1 O ILE W 59 N SER W 38
SHEET 3 AC 3 GLU W 82 GLN W 85 -1 O TRP W 83 N LEU W 56
SHEET 1 AD 5 GLU W 45 GLU W 49 0
SHEET 2 AD 5 THR W 105 ARG W 113 1 O PHE W 111 N LEU W 46
SHEET 3 AD 5 GLY W 94 ASN W 100 -1 N GLY W 94 O VAL W 110
SHEET 4 AD 5 PHE W 63 LYS W 69 -1 N THR W 67 O THR W 97
SHEET 5 AD 5 MET W 75 ASN W 78 -1 O ASN W 78 N TRP W 66
SHEET 1 AE 4 LEU W 125 LYS W 128 0
SHEET 2 AE 4 PHE W 201 ARG W 206 1 O LYS W 204 N LEU W 125
SHEET 3 AE 4 CYS W 184 ARG W 191 -1 N VAL W 185 O PHE W 201
SHEET 4 AE 4 SER W 145 GLU W 151 -1 N SER W 145 O GLN W 190
SHEET 1 AF 4 LEU W 125 LYS W 128 0
SHEET 2 AF 4 PHE W 201 ARG W 206 1 O LYS W 204 N LEU W 125
SHEET 3 AF 4 CYS W 184 ARG W 191 -1 N VAL W 185 O PHE W 201
SHEET 4 AF 4 THR W 194 HIS W 197 -1 O THR W 194 N ARG W 191
SHEET 1 AG 3 ALA W 133 VAL W 135 0
SHEET 2 AG 3 GLY W 170 LYS W 174 -1 O ILE W 171 N VAL W 135
SHEET 3 AG 3 THR W 162 ASN W 166 -1 N THR W 162 O LYS W 174
SHEET 1 AH 4 VAL W 214 SER W 216 0
SHEET 2 AH 4 PHE W 230 ASP W 238 -1 O LYS W 237 N VAL W 214
SHEET 3 AH 4 ASN W 271 ILE W 280 -1 O GLU W 276 N CYS W 234
SHEET 4 AH 4 VAL W 260 LYS W 261 -1 N LYS W 261 O THR W 277
SHEET 1 AI 4 VAL W 214 SER W 216 0
SHEET 2 AI 4 PHE W 230 ASP W 238 -1 O LYS W 237 N VAL W 214
SHEET 3 AI 4 ASN W 271 ILE W 280 -1 O GLU W 276 N CYS W 234
SHEET 4 AI 4 SER W 264 GLY W 268 -1 N TRP W 265 O GLU W 273
SHEET 1 AJ 4 PRO W 254 HIS W 256 0
SHEET 2 AJ 4 ASN W 244 MET W 250 -1 N LYS W 249 O GLN W 255
SHEET 3 AJ 4 GLY W 289 ASN W 296 -1 O MET W 292 N LEU W 248
SHEET 4 AJ 4 SER W 301 LEU W 308 -1 O THR W 306 N PHE W 291
SSBOND 1 CYS A 4 CYS A 89 1555 1555 2.04
SSBOND 2 CYS A 43 CYS A 138 1555 1555 2.01
SSBOND 3 CYS B 4 CYS B 89 1555 1555 2.03
SSBOND 4 CYS B 43 CYS B 138 1555 1555 2.04
SSBOND 5 CYS E 4 CYS E 89 1555 1555 2.04
SSBOND 6 CYS E 43 CYS E 138 1555 1555 2.04
SSBOND 7 CYS F 4 CYS F 89 1555 1555 2.04
SSBOND 8 CYS F 43 CYS F 138 1555 1555 2.04
SSBOND 9 CYS X 58 CYS X 98 1555 1555 2.03
SSBOND 10 CYS X 137 CYS X 187 1555 1555 2.03
SSBOND 11 CYS X 152 CYS X 184 1555 1555 2.03
SSBOND 12 CYS X 234 CYS X 293 1555 1555 2.04
SSBOND 13 CYS Y 58 CYS Y 98 1555 1555 2.03
SSBOND 14 CYS Y 137 CYS Y 187 1555 1555 2.03
SSBOND 15 CYS Y 152 CYS Y 184 1555 1555 2.03
SSBOND 16 CYS Y 234 CYS Y 293 1555 1555 2.03
SSBOND 17 CYS U 58 CYS U 98 1555 1555 2.04
SSBOND 18 CYS U 137 CYS U 187 1555 1555 1.99
SSBOND 19 CYS U 152 CYS U 184 1555 1555 2.03
SSBOND 20 CYS U 234 CYS U 293 1555 1555 2.03
SSBOND 21 CYS W 58 CYS W 98 1555 1555 2.03
SSBOND 22 CYS W 137 CYS W 187 1555 1555 2.03
SSBOND 23 CYS W 152 CYS W 184 1555 1555 2.03
SSBOND 24 CYS W 234 CYS W 293 1555 1555 2.03
LINK ND2 ASN X 296 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN X 303 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN Y 296 C1 NAG G 1 1555 1555 1.46
LINK ND2 ASN Y 303 C1 NAG H 1 1555 1555 1.46
LINK ND2 ASN U 296 C1 NAG I 1 1555 1555 1.45
LINK ND2 ASN U 303 C1 NAG J 1 1555 1555 1.46
LINK ND2 ASN W 296 C1 NAG K 1 1555 1555 1.45
LINK ND2 ASN W 303 C1 NAG L 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O6 NAG C 1 C1 FUL C 3 1555 1555 1.40
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.39
LINK O4 NAG D 2 C1 MAN D 3 1555 1555 1.39
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.40
LINK O6 NAG G 1 C1 FUL G 3 1555 1555 1.41
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.40
LINK O4 NAG H 2 C1 MAN H 3 1555 1555 1.39
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.40
LINK O6 NAG I 1 C1 FUL I 3 1555 1555 1.40
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.40
LINK O4 NAG J 2 C1 MAN J 3 1555 1555 1.39
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.39
LINK O6 NAG K 1 C1 FUL K 3 1555 1555 1.40
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.40
LINK O4 NAG L 2 C1 MAN L 3 1555 1555 1.39
CRYST1 76.849 200.154 82.023 90.00 91.42 90.00 P 1 21 1 8
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 0.013013 0.000000 0.000323 0.00000
SCALE2 0.000000 0.004996 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012195 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
