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HEADER CELL ADHESION 10-DEC-07 3BL8
TITLE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF NEUROLIGIN-
TITLE 2 2A FROM MOUSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: ESTERASE-LIKE DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 GENE: NLGN2, KIAA1366;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GNTI;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCEP4-NL2A
KEYWDS NEUROLIGIN-2A, CELL ADHESION, GLYCOPROTEIN, MEMBRANE,
KEYWDS 2 PHOSPHOPROTEIN, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.JIN,J.KOEHNKE,L.SHAPIRO
REVDAT 1 19-FEB-08 3BL8 0
JRNL AUTH J.KOEHNKE,X.JIN,E.C.BUDRECK,S.POSY,P.SCHEIFFELE,
JRNL AUTH 2 B.HONIG,L.SHAPIRO
JRNL TITL CRYSTAL STRUCTURE OF THE EXTRACELLULAR
JRNL TITL 2 CHOLINESTERASE-LIKE DOMAIN FROM NEUROLIGIN-2.
JRNL REF PROC.NATL.ACAD.SCI.USA 2008
JRNL REFN ASTM PNASA6 US ESSN 1091-6490
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 54190
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2714
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW : 3.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3578
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.3320
REMARK 3 BIN FREE R VALUE SET COUNT : 190
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 17374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 126.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.45000
REMARK 3 B22 (A**2) : -2.62000
REMARK 3 B33 (A**2) : -1.52000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -9.25000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.513
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.467
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 61.915
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17826 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24315 ; 1.213 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2179 ; 6.050 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 851 ;36.639 ;24.101
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2691 ;19.917 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 100 ;16.001 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2632 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13892 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 8863 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 12039 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 522 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 44 ; 0.213 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.106 ; 0.200
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): 11096 ; 0.278 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17560 ; 0.510 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7612 ; 0.528 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6754 ; 0.937 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 42 A 605
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4989 46.6581 10.9178
REMARK 3 T TENSOR
REMARK 3 T11: -0.6722 T22: -0.8698
REMARK 3 T33: -0.6265 T12: -0.0323
REMARK 3 T13: 0.0460 T23: -0.0829
REMARK 3 L TENSOR
REMARK 3 L11: 3.2225 L22: 3.7692
REMARK 3 L33: 2.1452 L12: 0.0194
REMARK 3 L13: -0.5863 L23: -0.7020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0827 S12: -0.4679 S13: 0.0174
REMARK 3 S21: 0.4323 S22: 0.1417 S23: -0.2159
REMARK 3 S31: 0.0163 S32: 0.0725 S33: -0.0590
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 42 B 605
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8399 51.0350 40.7273
REMARK 3 T TENSOR
REMARK 3 T11: -0.2211 T22: -0.0598
REMARK 3 T33: -0.3587 T12: 0.0820
REMARK 3 T13: -0.0656 T23: -0.1192
REMARK 3 L TENSOR
REMARK 3 L11: 3.1231 L22: 2.2111
REMARK 3 L33: 7.2258 L12: -0.1973
REMARK 3 L13: 2.9054 L23: -0.4658
REMARK 3 S TENSOR
REMARK 3 S11: -0.3199 S12: -0.7861 S13: 0.3309
REMARK 3 S21: 0.4620 S22: 0.0780 S23: -0.3425
REMARK 3 S31: -0.9331 S32: 0.3689 S33: 0.2419
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 42 C 605
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3197 11.5225 52.7535
REMARK 3 T TENSOR
REMARK 3 T11: -0.1688 T22: -0.1707
REMARK 3 T33: -0.1770 T12: -0.0989
REMARK 3 T13: 0.0131 T23: 0.1926
REMARK 3 L TENSOR
REMARK 3 L11: 2.8765 L22: 2.4094
REMARK 3 L33: 3.8842 L12: 0.7513
REMARK 3 L13: 0.0117 L23: -1.2379
REMARK 3 S TENSOR
REMARK 3 S11: 0.2119 S12: -0.4134 S13: -0.4720
REMARK 3 S21: 0.3166 S22: -0.0303 S23: -0.0864
REMARK 3 S31: 0.2677 S32: -0.2045 S33: -0.1816
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 42 D 605
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4060 47.4783 92.7006
REMARK 3 T TENSOR
REMARK 3 T11: 0.2362 T22: 0.7312
REMARK 3 T33: -0.2204 T12: -0.0784
REMARK 3 T13: -0.2434 T23: -0.5033
REMARK 3 L TENSOR
REMARK 3 L11: 5.1357 L22: 1.6449
REMARK 3 L33: 4.7656 L12: 0.1773
REMARK 3 L13: 3.2354 L23: 0.1363
REMARK 3 S TENSOR
REMARK 3 S11: 0.2706 S12: 0.0768 S13: -0.4014
REMARK 3 S21: 0.0210 S22: 0.2845 S23: -0.0706
REMARK 3 S31: 0.3305 S32: -0.5432 S33: -0.5551
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3BL8 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB045658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SI 111
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
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54385
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.50300
REMARK 200 R SYM FOR SHELL (I) : 0.50300
REMARK 200 FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5% PEG 6000, 0.1M BICINE, PH 8.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 1/2+X,1/2+Y,Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 107.36150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.28350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.36150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.28350
REMARK 290 SMTRY3 4 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: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 2980 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 ARG A 159
REMARK 465 ASP A 160
REMARK 465 GLU A 161
REMARK 465 ALA A 162
REMARK 465 THR A 163
REMARK 465 LEU A 164
REMARK 465 ASN A 165
REMARK 465 PRO A 166
REMARK 465 PRO A 167
REMARK 465 ASP A 168
REMARK 465 THR A 169
REMARK 465 ASP A 170
REMARK 465 ILE A 171
REMARK 465 ARG A 172
REMARK 465 ASN A 610
REMARK 465 LEU A 611
REMARK 465 HIS A 612
REMARK 465 HIS A 613
REMARK 465 HIS A 614
REMARK 465 HIS A 615
REMARK 465 HIS A 616
REMARK 465 HIS A 617
REMARK 465 HIS A 618
REMARK 465 HIS A 619
REMARK 465 GLU B 151
REMARK 465 ASP B 152
REMARK 465 GLY B 153
REMARK 465 PRO B 154
REMARK 465 LEU B 155
REMARK 465 THR B 156
REMARK 465 LYS B 157
REMARK 465 LYS B 158
REMARK 465 ARG B 159
REMARK 465 ASP B 160
REMARK 465 GLU B 161
REMARK 465 ALA B 162
REMARK 465 THR B 163
REMARK 465 LEU B 164
REMARK 465 ASN B 165
REMARK 465 PRO B 166
REMARK 465 PRO B 167
REMARK 465 ASP B 168
REMARK 465 THR B 169
REMARK 465 ASP B 170
REMARK 465 ILE B 171
REMARK 465 ARG B 172
REMARK 465 ASP B 173
REMARK 465 HIS B 609
REMARK 465 ASN B 610
REMARK 465 LEU B 611
REMARK 465 HIS B 612
REMARK 465 HIS B 613
REMARK 465 HIS B 614
REMARK 465 HIS B 615
REMARK 465 HIS B 616
REMARK 465 HIS B 617
REMARK 465 HIS B 618
REMARK 465 HIS B 619
REMARK 465 GLN C 40
REMARK 465 GLU C 151
REMARK 465 ASP C 152
REMARK 465 GLY C 153
REMARK 465 PRO C 154
REMARK 465 LEU C 155
REMARK 465 THR C 156
REMARK 465 LYS C 157
REMARK 465 LYS C 158
REMARK 465 ARG C 159
REMARK 465 ASP C 160
REMARK 465 GLU C 161
REMARK 465 ALA C 162
REMARK 465 THR C 163
REMARK 465 LEU C 164
REMARK 465 ASN C 165
REMARK 465 PRO C 166
REMARK 465 PRO C 167
REMARK 465 ASP C 168
REMARK 465 THR C 169
REMARK 465 ASP C 170
REMARK 465 ILE C 171
REMARK 465 ARG C 172
REMARK 465 ASP C 173
REMARK 465 SER C 174
REMARK 465 GLY C 175
REMARK 465 LEU C 611
REMARK 465 HIS C 612
REMARK 465 HIS C 613
REMARK 465 HIS C 614
REMARK 465 HIS C 615
REMARK 465 HIS C 616
REMARK 465 HIS C 617
REMARK 465 HIS C 618
REMARK 465 HIS C 619
REMARK 465 GLN D 40
REMARK 465 GLU D 151
REMARK 465 ASP D 152
REMARK 465 GLY D 153
REMARK 465 PRO D 154
REMARK 465 LEU D 155
REMARK 465 THR D 156
REMARK 465 LYS D 157
REMARK 465 LYS D 158
REMARK 465 ARG D 159
REMARK 465 ASP D 160
REMARK 465 GLU D 161
REMARK 465 ALA D 162
REMARK 465 THR D 163
REMARK 465 LEU D 164
REMARK 465 ASN D 165
REMARK 465 PRO D 166
REMARK 465 PRO D 167
REMARK 465 ASP D 168
REMARK 465 THR D 169
REMARK 465 ASP D 170
REMARK 465 ILE D 171
REMARK 465 ARG D 172
REMARK 465 ASP D 173
REMARK 465 SER D 174
REMARK 465 ILE D 558
REMARK 465 HIS D 559
REMARK 465 THR D 560
REMARK 465 LYS D 561
REMARK 465 PRO D 562
REMARK 465 LEU D 611
REMARK 465 HIS D 612
REMARK 465 HIS D 613
REMARK 465 HIS D 614
REMARK 465 HIS D 615
REMARK 465 HIS D 616
REMARK 465 HIS D 617
REMARK 465 HIS D 618
REMARK 465 HIS D 619
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 40 CG CD OE1 NE2
REMARK 470 LYS A 158 CG CD CE NZ
REMARK 470 VAL A 210 CG1 CG2
REMARK 470 GLN B 40 CG CD OE1 NE2
REMARK 470 VAL B 210 CG1 CG2
REMARK 470 LYS C 41 CG CD CE NZ
REMARK 470 VAL C 210 CG1 CG2
REMARK 470 VAL D 210 CG1 CG2
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 ND2 ASN B 98 O5 NAG B 801 1.61
REMARK 500 O ARG A 335 OD2 ASP A 339 1.91
REMARK 500 O PRO A 421 N LYS A 424 1.97
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA A 395 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 ALA A 496 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 ALA B 345 CB - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 GLU B 396 CB - CA - C ANGL. DEV. = -19.0 DEGREES
REMARK 500 GLY D 112 N - CA - C ANGL. DEV. = 20.2 DEGREES
REMARK 500 ALA D 113 N - CA - CB ANGL. DEV. = 11.5 DEGREES
REMARK 500 HIS D 279 CB - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 HIS D 279 N - CA - C ANGL. DEV. = 24.3 DEGREES
REMARK 500 SER D 280 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 SER D 291 N - CA - C ANGL. DEV. = 18.9 DEGREES
REMARK 500 CYS D 521 CB - CA - C ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG D 564 CB - CA - C ANGL. DEV. = -14.6 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 ALA A 81 26.43 -71.80
REMARK 500 PRO A 115 43.47 -73.21
REMARK 500 CYS A 141 -3.18 -149.50
REMARK 500 GLU A 151 -166.45 -120.23
REMARK 500 ALA A 229 90.44 -170.02
REMARK 500 GLU A 281 -79.68 -135.05
REMARK 500 GLN A 285 11.94 -150.79
REMARK 500 THR A 293 149.57 -172.27
REMARK 500 SER A 297 -8.56 -57.51
REMARK 500 ASP A 341 80.77 59.61
REMARK 500 ASP A 358 -83.87 -108.07
REMARK 500 PRO A 364 -36.23 -38.99
REMARK 500 GLU A 372 55.60 -102.58
REMARK 500 GLU A 386 -74.35 -51.57
REMARK 500 GLU A 398 33.04 70.16
REMARK 500 ASP A 399 17.39 -152.79
REMARK 500 TYR A 418 -50.65 -137.58
REMARK 500 TYR A 420 16.00 -151.68
REMARK 500 GLN A 475 22.26 86.10
REMARK 500 HIS A 485 125.70 -176.57
REMARK 500 GLU A 494 42.99 -87.03
REMARK 500 THR A 516 -169.30 -112.28
REMARK 500 PHE A 519 72.52 -119.23
REMARK 500 PRO A 520 45.27 -103.94
REMARK 500 ASN A 540 -9.49 -58.99
REMARK 500 PRO A 550 -94.56 7.84
REMARK 500 HIS A 559 158.13 -46.80
REMARK 500 ASN A 592 70.81 61.45
REMARK 500 ASN A 596 -71.77 -48.25
REMARK 500 GLU A 603 -64.90 -91.74
REMARK 500 ALA B 89 151.95 -48.52
REMARK 500 HIS B 111 54.93 -107.34
REMARK 500 SER B 138 132.85 -175.18
REMARK 500 HIS B 184 -161.43 -77.51
REMARK 500 SER B 187 -166.99 -100.22
REMARK 500 THR B 192 143.65 -175.67
REMARK 500 ASN B 206 68.40 61.49
REMARK 500 PHE B 221 -6.21 -141.07
REMARK 500 ASN B 232 10.54 58.37
REMARK 500 HIS B 279 -40.53 -27.35
REMARK 500 CYS B 317 32.63 -147.44
REMARK 500 SER B 322 -73.39 -58.15
REMARK 500 ASP B 358 -66.34 -146.77
REMARK 500 GLN B 370 22.05 -78.98
REMARK 500 ASN B 375 91.59 -62.02
REMARK 500 GLU B 398 -129.23 52.02
REMARK 500 ASP B 399 -120.14 -76.81
REMARK 500 SER B 402 105.47 -47.86
REMARK 500 ALA B 403 -57.34 70.90
REMARK 500 TYR B 418 -82.91 -109.85
REMARK 500 LYS B 424 -74.26 -91.38
REMARK 500 TYR B 435 49.56 -102.37
REMARK 500 TRP B 460 -54.23 -126.60
REMARK 500 GLN B 475 -5.98 74.05
REMARK 500 TYR B 484 65.87 -107.09
REMARK 500 HIS B 485 140.81 -175.24
REMARK 500 GLN B 488 88.91 -64.86
REMARK 500 ASP B 497 -169.81 -101.88
REMARK 500 ALA B 498 104.74 -54.47
REMARK 500 ASP B 502 -1.95 -58.80
REMARK 500 ASN B 522 94.28 -69.41
REMARK 500 GLN B 549 114.13 -163.13
REMARK 500 GLN B 553 48.16 -74.39
REMARK 500 THR B 555 71.54 -64.22
REMARK 500 PRO B 562 96.57 -19.64
REMARK 500 ASN B 563 93.26 -64.27
REMARK 500 LYS B 586 76.40 -118.66
REMARK 500 ASN B 592 105.41 -160.18
REMARK 500 ARG B 594 29.12 49.47
REMARK 500 ALA C 47 1.97 -68.19
REMARK 500 PHE C 69 67.10 -107.48
REMARK 500 PRO C 77 118.50 -33.79
REMARK 500 GLU C 88 -162.48 -129.96
REMARK 500 ASN C 98 58.75 -95.43
REMARK 500 ALA C 99 49.79 -79.78
REMARK 500 LEU C 142 84.14 -68.85
REMARK 500 HIS C 184 -167.93 -75.56
REMARK 500 TYR C 188 -10.07 74.94
REMARK 500 ASP C 226 -69.96 -146.55
REMARK 500 GLN C 227 -54.74 -125.21
REMARK 500 ARG C 258 38.74 -146.27
REMARK 500 GLU C 281 -74.21 -121.22
REMARK 500 TRP C 298 38.04 -98.63
REMARK 500 ASP C 341 45.12 78.75
REMARK 500 TYR C 347 5.70 81.74
REMARK 500 ASP C 358 -79.46 -127.58
REMARK 500 VAL C 391 52.30 -111.22
REMARK 500 ASP C 393 -8.99 -54.45
REMARK 500 SER C 394 55.95 -108.82
REMARK 500 SER C 397 -52.09 -121.89
REMARK 500 GLU C 398 -65.52 69.38
REMARK 500 ASP C 399 7.71 -66.65
REMARK 500 GLU C 422 -50.78 78.42
REMARK 500 TRP C 438 -46.82 70.35
REMARK 500 ALA C 489 75.30 52.41
REMARK 500 GLU C 490 153.98 -46.22
REMARK 500 ASP C 497 72.27 46.78
REMARK 500 ALA C 498 61.14 66.98
REMARK 500 PRO C 511 -9.04 -56.77
REMARK 500 ASN C 522 97.06 -67.16
REMARK 500 THR C 560 22.65 -72.35
REMARK 500 PRO C 562 98.40 -31.52
REMARK 500 ASN C 563 93.83 -66.11
REMARK 500 ASN C 574 -166.63 -100.65
REMARK 500 LYS C 576 -71.92 -59.13
REMARK 500 GLU C 603 -62.44 -93.02
REMARK 500 LEU C 608 39.31 -88.93
REMARK 500 PRO D 42 120.60 -15.67
REMARK 500 PRO D 94 -99.81 -58.61
REMARK 500 ALA D 99 47.00 -105.38
REMARK 500 ASN D 126 40.60 -89.52
REMARK 500 HIS D 184 53.80 -102.19
REMARK 500 TYR D 188 -7.69 -58.11
REMARK 500 PRO D 256 26.08 -66.67
REMARK 500 TRP D 298 32.44 -91.94
REMARK 500 GLN D 303 77.88 -117.17
REMARK 500 GLN D 340 -36.10 -139.23
REMARK 500 PRO D 344 -164.57 -70.36
REMARK 500 ASP D 358 -72.66 -122.54
REMARK 500 PRO D 361 -74.36 -59.29
REMARK 500 ASP D 362 -155.58 -102.30
REMARK 500 PHE D 373 44.38 -77.95
REMARK 500 ALA D 395 -47.53 -133.62
REMARK 500 ASP D 415 10.96 -68.06
REMARK 500 TYR D 418 -90.85 -123.63
REMARK 500 TYR D 435 66.42 -116.85
REMARK 500 TRP D 460 -59.19 -130.81
REMARK 500 GLN D 475 95.14 -60.12
REMARK 500 ALA D 498 72.07 49.60
REMARK 500 ALA D 515 125.01 99.43
REMARK 500 SER D 524 -169.73 -116.54
REMARK 500 THR D 544 -31.59 -135.79
REMARK 500 ARG D 564 18.45 51.55
REMARK 500 PHE D 565 -8.41 -141.52
REMARK 500 LYS D 578 58.22 31.12
REMARK 500 ARG D 594 36.14 37.74
REMARK 500 GLU D 603 -73.11 -95.92
REMARK 500 HIS D 607 21.56 -73.89
REMARK 500 HIS D 609 -78.34 -139.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 418 GLY A 419 -147.54
REMARK 500 GLY A 419 TYR A 420 -149.43
REMARK 500 TYR A 420 PRO A 421 -51.12
REMARK 500 GLU A 494 TRP A 495 135.40
REMARK 500 GLN A 549 PRO A 550 -124.45
REMARK 500 PRO B 78 LEU B 79 -149.99
REMARK 500 SER B 402 ALA B 403 140.79
REMARK 500 ASP B 517 LEU B 518 -146.50
REMARK 500 LEU B 518 PHE B 519 139.89
REMARK 500 GLN C 549 PRO C 550 48.97
REMARK 500 GLY D 371 GLU D 372 137.61
REMARK 500 GLU D 396 SER D 397 148.72
REMARK 500 GLN D 549 PRO D 550 33.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 621 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH D 621 DISTANCE = 8.55 ANGSTROMS
REMARK 525 HOH D 622 DISTANCE = 12.24 ANGSTROMS
REMARK 525 HOH D 623 DISTANCE = 15.59 ANGSTROMS
REMARK 525 HOH B 816 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH B 821 DISTANCE = 5.75 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 710
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 701
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 702
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 710
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 801
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 802
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR RESIDUE B 803
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR RESIDUE B 804
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR RESIDUE B 806
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR RESIDUE B 807
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 810
DBREF 3BL8 A 42 612 UNP Q69ZK9 NLGN2_MOUSE 42 612
DBREF 3BL8 B 42 612 UNP Q69ZK9 NLGN2_MOUSE 42 612
DBREF 3BL8 C 42 612 UNP Q69ZK9 NLGN2_MOUSE 42 612
DBREF 3BL8 D 42 612 UNP Q69ZK9 NLGN2_MOUSE 42 612
SEQADV 3BL8 GLN A 40 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 LYS A 41 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS A 613 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS A 614 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS A 615 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS A 616 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS A 617 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS A 618 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS A 619 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 GLN B 40 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 LYS B 41 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS B 613 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS B 614 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS B 615 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS B 616 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS B 617 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS B 618 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS B 619 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 GLN C 40 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 LYS C 41 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS C 613 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS C 614 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS C 615 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS C 616 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS C 617 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS C 618 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS C 619 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 GLN D 40 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 LYS D 41 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS D 613 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS D 614 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS D 615 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS D 616 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS D 617 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS D 618 UNP Q69ZK9 EXPRESSION TAG
SEQADV 3BL8 HIS D 619 UNP Q69ZK9 EXPRESSION TAG
SEQRES 1 A 580 GLN LYS PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG
SEQRES 2 A 580 GLY VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO
SEQRES 3 A 580 VAL VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO
SEQRES 4 A 580 LEU GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA
SEQRES 5 A 580 SER TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO
SEQRES 6 A 580 ALA CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE
SEQRES 7 A 580 MET LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA
SEQRES 8 A 580 ALA THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR
SEQRES 9 A 580 LEU ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR
SEQRES 10 A 580 LYS LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR
SEQRES 11 A 580 ASP ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE
SEQRES 12 A 580 LEU HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET
SEQRES 13 A 580 PHE ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE
SEQRES 14 A 580 VAL VAL THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE
SEQRES 15 A 580 LEU SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY
SEQRES 16 A 580 LEU LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU
SEQRES 17 A 580 ASN ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR
SEQRES 18 A 580 ILE PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU
SEQRES 19 A 580 LEU ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS
SEQRES 20 A 580 ALA ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER
SEQRES 21 A 580 VAL ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA
SEQRES 22 A 580 ALA LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA
SEQRES 23 A 580 VAL GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL
SEQRES 24 A 580 ASP GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE
SEQRES 25 A 580 GLY PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO
SEQRES 26 A 580 GLU ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP
SEQRES 27 A 580 MET LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE
SEQRES 28 A 580 VAL GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA
SEQRES 29 A 580 SER ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN
SEQRES 30 A 580 LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU
SEQRES 31 A 580 THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP
SEQRES 32 A 580 ASN GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE
SEQRES 33 A 580 THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA
SEQRES 34 A 580 LYS LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR
SEQRES 35 A 580 THR PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU
SEQRES 36 A 580 TRP ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL
SEQRES 37 A 580 PHE GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO
SEQRES 38 A 580 CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL
SEQRES 39 A 580 VAL MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP
SEQRES 40 A 580 PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS
SEQRES 41 A 580 THR LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS
SEQRES 42 A 580 PHE ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU
SEQRES 43 A 580 LYS PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL
SEQRES 44 A 580 ALA PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU
SEQRES 45 A 580 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 580 GLN LYS PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG
SEQRES 2 B 580 GLY VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO
SEQRES 3 B 580 VAL VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO
SEQRES 4 B 580 LEU GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA
SEQRES 5 B 580 SER TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO
SEQRES 6 B 580 ALA CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE
SEQRES 7 B 580 MET LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA
SEQRES 8 B 580 ALA THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR
SEQRES 9 B 580 LEU ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR
SEQRES 10 B 580 LYS LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR
SEQRES 11 B 580 ASP ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE
SEQRES 12 B 580 LEU HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET
SEQRES 13 B 580 PHE ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE
SEQRES 14 B 580 VAL VAL THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE
SEQRES 15 B 580 LEU SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY
SEQRES 16 B 580 LEU LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU
SEQRES 17 B 580 ASN ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR
SEQRES 18 B 580 ILE PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU
SEQRES 19 B 580 LEU ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS
SEQRES 20 B 580 ALA ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER
SEQRES 21 B 580 VAL ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA
SEQRES 22 B 580 ALA LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA
SEQRES 23 B 580 VAL GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL
SEQRES 24 B 580 ASP GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE
SEQRES 25 B 580 GLY PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO
SEQRES 26 B 580 GLU ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP
SEQRES 27 B 580 MET LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE
SEQRES 28 B 580 VAL GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA
SEQRES 29 B 580 SER ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN
SEQRES 30 B 580 LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU
SEQRES 31 B 580 THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP
SEQRES 32 B 580 ASN GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE
SEQRES 33 B 580 THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA
SEQRES 34 B 580 LYS LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR
SEQRES 35 B 580 THR PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU
SEQRES 36 B 580 TRP ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL
SEQRES 37 B 580 PHE GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO
SEQRES 38 B 580 CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL
SEQRES 39 B 580 VAL MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP
SEQRES 40 B 580 PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS
SEQRES 41 B 580 THR LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS
SEQRES 42 B 580 PHE ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU
SEQRES 43 B 580 LYS PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL
SEQRES 44 B 580 ALA PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU
SEQRES 45 B 580 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 580 GLN LYS PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG
SEQRES 2 C 580 GLY VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO
SEQRES 3 C 580 VAL VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO
SEQRES 4 C 580 LEU GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA
SEQRES 5 C 580 SER TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO
SEQRES 6 C 580 ALA CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE
SEQRES 7 C 580 MET LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA
SEQRES 8 C 580 ALA THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR
SEQRES 9 C 580 LEU ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR
SEQRES 10 C 580 LYS LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR
SEQRES 11 C 580 ASP ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE
SEQRES 12 C 580 LEU HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET
SEQRES 13 C 580 PHE ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE
SEQRES 14 C 580 VAL VAL THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE
SEQRES 15 C 580 LEU SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY
SEQRES 16 C 580 LEU LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU
SEQRES 17 C 580 ASN ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR
SEQRES 18 C 580 ILE PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU
SEQRES 19 C 580 LEU ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS
SEQRES 20 C 580 ALA ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER
SEQRES 21 C 580 VAL ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA
SEQRES 22 C 580 ALA LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA
SEQRES 23 C 580 VAL GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL
SEQRES 24 C 580 ASP GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE
SEQRES 25 C 580 GLY PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO
SEQRES 26 C 580 GLU ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP
SEQRES 27 C 580 MET LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE
SEQRES 28 C 580 VAL GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA
SEQRES 29 C 580 SER ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN
SEQRES 30 C 580 LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU
SEQRES 31 C 580 THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP
SEQRES 32 C 580 ASN GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE
SEQRES 33 C 580 THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA
SEQRES 34 C 580 LYS LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR
SEQRES 35 C 580 THR PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU
SEQRES 36 C 580 TRP ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL
SEQRES 37 C 580 PHE GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO
SEQRES 38 C 580 CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL
SEQRES 39 C 580 VAL MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP
SEQRES 40 C 580 PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS
SEQRES 41 C 580 THR LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS
SEQRES 42 C 580 PHE ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU
SEQRES 43 C 580 LYS PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL
SEQRES 44 C 580 ALA PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU
SEQRES 45 C 580 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 580 GLN LYS PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG
SEQRES 2 D 580 GLY VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO
SEQRES 3 D 580 VAL VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO
SEQRES 4 D 580 LEU GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA
SEQRES 5 D 580 SER TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO
SEQRES 6 D 580 ALA CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE
SEQRES 7 D 580 MET LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA
SEQRES 8 D 580 ALA THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR
SEQRES 9 D 580 LEU ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR
SEQRES 10 D 580 LYS LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR
SEQRES 11 D 580 ASP ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE
SEQRES 12 D 580 LEU HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET
SEQRES 13 D 580 PHE ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE
SEQRES 14 D 580 VAL VAL THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE
SEQRES 15 D 580 LEU SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY
SEQRES 16 D 580 LEU LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU
SEQRES 17 D 580 ASN ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR
SEQRES 18 D 580 ILE PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU
SEQRES 19 D 580 LEU ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS
SEQRES 20 D 580 ALA ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER
SEQRES 21 D 580 VAL ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA
SEQRES 22 D 580 ALA LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA
SEQRES 23 D 580 VAL GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL
SEQRES 24 D 580 ASP GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE
SEQRES 25 D 580 GLY PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO
SEQRES 26 D 580 GLU ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP
SEQRES 27 D 580 MET LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE
SEQRES 28 D 580 VAL GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA
SEQRES 29 D 580 SER ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN
SEQRES 30 D 580 LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU
SEQRES 31 D 580 THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP
SEQRES 32 D 580 ASN GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE
SEQRES 33 D 580 THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA
SEQRES 34 D 580 LYS LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR
SEQRES 35 D 580 THR PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU
SEQRES 36 D 580 TRP ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL
SEQRES 37 D 580 PHE GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO
SEQRES 38 D 580 CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL
SEQRES 39 D 580 VAL MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP
SEQRES 40 D 580 PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS
SEQRES 41 D 580 THR LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS
SEQRES 42 D 580 PHE ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU
SEQRES 43 D 580 LYS PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL
SEQRES 44 D 580 ALA PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU
SEQRES 45 D 580 HIS HIS HIS HIS HIS HIS HIS HIS
MODRES 3BL8 ASN A 98 ASN GLYCOSYLATION SITE
MODRES 3BL8 ASN B 98 ASN GLYCOSYLATION SITE
MODRES 3BL8 ASN B 136 ASN GLYCOSYLATION SITE
HET NAG A 701 14
HET NAG A 702 14
HET MAN A 703 11
HET NAG A 710 14
HET NAG B 801 14
HET NAG B 802 14
HET BMA B 803 11
HET MAN B 804 11
HET MAN B 806 11
HET MAN B 805 11
HET MAN B 807 11
HET NAG B 810 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM BMA BETA-D-MANNOSE
HETSYN NAG NAG
FORMUL 5 NAG 6(C8 H15 N O6)
FORMUL 5 MAN 5(C6 H12 O6)
FORMUL 7 BMA C6 H12 O6
FORMUL 9 HOH *52(H2 O)
HELIX 1 1 PRO A 120 ASN A 126 1 7
HELIX 2 2 ASN A 126 THR A 132 1 7
HELIX 3 3 TYR A 133 GLN A 135 5 3
HELIX 4 4 THR A 192 PHE A 196 5 5
HELIX 5 5 GLY A 198 ASN A 206 1 9
HELIX 6 6 LEU A 216 LEU A 222 1 7
HELIX 7 7 ASN A 232 ILE A 249 1 18
HELIX 8 8 ALA A 250 PHE A 252 5 3
HELIX 9 9 GLY A 265 SER A 277 1 13
HELIX 10 10 GLN A 303 GLY A 316 1 14
HELIX 11 11 ASP A 321 ARG A 330 1 10
HELIX 12 12 SER A 333 ASP A 339 1 7
HELIX 13 13 ASP A 363 GLY A 371 1 9
HELIX 14 14 LYS A 389 ALA A 395 5 7
HELIX 15 15 SER A 402 LEU A 417 1 16
HELIX 16 16 GLY A 423 THR A 436 1 14
HELIX 17 17 ASN A 443 TRP A 460 1 18
HELIX 18 18 TRP A 460 TYR A 474 1 15
HELIX 19 19 GLU A 503 GLY A 509 1 7
HELIX 20 20 GLY A 509 GLY A 514 1 6
HELIX 21 21 SER A 524 GLY A 545 1 22
HELIX 22 22 ASN A 563 GLU A 567 5 5
HELIX 23 23 ARG A 594 GLU A 603 1 10
HELIX 24 24 VAL A 605 HIS A 609 5 5
HELIX 25 25 PRO B 120 ASN B 126 1 7
HELIX 26 26 ASN B 126 THR B 132 1 7
HELIX 27 27 GLY B 198 TYR B 204 1 7
HELIX 28 28 LEU B 216 PHE B 221 1 6
HELIX 29 29 ASN B 232 ILE B 249 1 18
HELIX 30 30 ALA B 250 PHE B 252 5 3
HELIX 31 31 GLY B 265 SER B 277 1 13
HELIX 32 32 GLN B 303 GLY B 316 1 14
HELIX 33 33 ASP B 321 ARG B 330 1 10
HELIX 34 34 SER B 333 ASP B 339 1 7
HELIX 35 35 ASP B 363 GLN B 370 1 8
HELIX 36 36 GLY B 387 ALA B 395 5 9
HELIX 37 37 PHE B 406 ASN B 416 1 11
HELIX 38 38 TYR B 420 LYS B 424 5 5
HELIX 39 39 ASP B 425 TYR B 435 1 11
HELIX 40 40 GLU B 445 TRP B 460 1 16
HELIX 41 41 TRP B 460 TYR B 474 1 15
HELIX 42 42 GLU B 503 PHE B 508 1 6
HELIX 43 43 SER B 524 GLY B 545 1 22
HELIX 44 44 ARG B 594 GLU B 603 1 10
HELIX 45 45 LEU B 604 LEU B 608 5 5
HELIX 46 46 LEU C 79 ARG C 83 5 5
HELIX 47 47 PRO C 120 ASN C 126 1 7
HELIX 48 48 ASN C 126 ALA C 131 1 6
HELIX 49 49 THR C 132 GLN C 135 5 4
HELIX 50 50 THR C 192 PHE C 196 5 5
HELIX 51 51 GLY C 198 ASN C 206 1 9
HELIX 52 52 ASN C 232 ILE C 249 1 18
HELIX 53 53 ALA C 250 PHE C 252 5 3
HELIX 54 54 GLY C 265 SER C 277 1 13
HELIX 55 55 GLN C 303 GLY C 316 1 14
HELIX 56 56 ASP C 321 ARG C 330 1 10
HELIX 57 57 SER C 333 ASP C 339 1 7
HELIX 58 58 ASP C 363 GLY C 371 1 9
HELIX 59 59 GLY C 387 GLU C 392 5 6
HELIX 60 60 SER C 402 TYR C 418 1 17
HELIX 61 61 GLU C 422 TYR C 435 1 14
HELIX 62 62 GLY C 444 TRP C 460 1 17
HELIX 63 63 TRP C 460 TYR C 474 1 15
HELIX 64 64 GLU C 503 PHE C 508 1 6
HELIX 65 65 SER C 524 GLY C 545 1 22
HELIX 66 66 ARG C 594 GLU C 603 1 10
HELIX 67 67 GLU C 603 LEU C 608 1 6
HELIX 68 68 PRO D 120 ASN D 126 1 7
HELIX 69 69 ASN D 126 VAL D 134 1 9
HELIX 70 70 THR D 192 PHE D 196 5 5
HELIX 71 71 ASP D 197 ASN D 206 1 10
HELIX 72 72 LEU D 216 GLY D 220 5 5
HELIX 73 73 ASN D 232 ILE D 249 1 18
HELIX 74 74 GLY D 265 LEU D 276 1 12
HELIX 75 75 SER D 296 VAL D 300 5 5
HELIX 76 76 GLN D 303 GLY D 316 1 14
HELIX 77 77 ASP D 321 ARG D 330 1 10
HELIX 78 78 SER D 333 ASP D 339 1 7
HELIX 79 79 ASP D 363 GLN D 370 1 8
HELIX 80 80 GLY D 387 VAL D 391 5 5
HELIX 81 81 SER D 402 TYR D 418 1 17
HELIX 82 82 GLY D 423 TYR D 435 1 13
HELIX 83 83 GLY D 444 TRP D 460 1 17
HELIX 84 84 TRP D 460 ASP D 473 1 14
HELIX 85 85 GLU D 503 GLY D 509 1 7
HELIX 86 86 SER D 524 GLY D 545 1 22
HELIX 87 87 ARG D 594 GLU D 603 1 10
HELIX 88 88 VAL D 605 HIS D 609 5 5
SHEET 1 A 2 ARG A 50 VAL A 51 0
SHEET 2 A 2 VAL A 96 ARG A 97 1 O ARG A 97 N ARG A 50
SHEET 1 B11 ARG A 55 ARG A 56 0
SHEET 2 B11 VAL A 66 PRO A 73 -1 O VAL A 66 N ARG A 56
SHEET 3 B11 TYR A 143 PRO A 149 -1 O VAL A 148 N VAL A 67
SHEET 4 B11 ILE A 208 LEU A 212 -1 O THR A 211 N ASN A 145
SHEET 5 B11 LYS A 177 LEU A 183 1 N PRO A 178 O ILE A 208
SHEET 6 B11 GLY A 254 SER A 264 1 O ASP A 255 N LYS A 177
SHEET 7 B11 LYS A 286 GLN A 290 1 O LYS A 286 N ILE A 261
SHEET 8 B11 ASP A 377 ASN A 383 1 O LEU A 379 N ALA A 289
SHEET 9 B11 VAL A 478 TYR A 484 1 O PHE A 483 N VAL A 382
SHEET 10 B11 GLN A 579 GLY A 584 1 O ILE A 583 N TYR A 484
SHEET 11 B11 VAL A 589 ASP A 591 -1 O ARG A 590 N TYR A 580
SHEET 1 C 3 VAL B 43 THR B 46 0
SHEET 2 C 3 GLY B 49 ARG B 52 -1 O VAL B 51 N VAL B 44
SHEET 3 C 3 VAL B 96 ASN B 98 1 O ARG B 97 N ARG B 50
SHEET 1 D11 VAL B 54 ARG B 56 0
SHEET 2 D11 VAL B 66 PRO B 73 -1 O GLN B 68 N VAL B 54
SHEET 3 D11 TYR B 143 PRO B 149 -1 O LEU B 146 N PHE B 69
SHEET 4 D11 ILE B 208 LEU B 212 -1 O THR B 211 N ASN B 145
SHEET 5 D11 LYS B 177 LEU B 183 1 N MET B 180 O VAL B 210
SHEET 6 D11 GLY B 254 SER B 264 1 O THR B 260 N VAL B 179
SHEET 7 D11 LYS B 286 GLN B 290 1 O GLN B 290 N GLY B 263
SHEET 8 D11 ASP B 377 ASN B 383 1 O ASP B 377 N ALA B 287
SHEET 9 D11 VAL B 478 TYR B 484 1 O TYR B 479 N MET B 378
SHEET 10 D11 TYR B 580 GLY B 584 1 O ILE B 583 N TYR B 484
SHEET 11 D11 ARG B 588 ARG B 590 -1 O ARG B 590 N TYR B 580
SHEET 1 E 2 VAL C 43 THR C 46 0
SHEET 2 E 2 GLY C 49 ARG C 52 -1 O GLY C 49 N THR C 46
SHEET 1 F 3 VAL C 54 GLU C 57 0
SHEET 2 F 3 PRO C 65 PRO C 73 -1 O GLN C 68 N VAL C 54
SHEET 3 F 3 TYR C 143 PRO C 149 -1 O LEU C 146 N PHE C 69
SHEET 1 G 8 ILE C 208 VAL C 210 0
SHEET 2 G 8 LYS C 177 LEU C 183 1 N MET C 180 O ILE C 208
SHEET 3 G 8 GLY C 254 SER C 264 1 O THR C 260 N VAL C 179
SHEET 4 G 8 LYS C 286 GLN C 290 1 O GLN C 290 N GLY C 263
SHEET 5 G 8 ASP C 377 ASN C 383 1 O ASP C 377 N ALA C 287
SHEET 6 G 8 VAL C 478 PHE C 483 1 O PHE C 483 N VAL C 382
SHEET 7 G 8 TYR C 580 ILE C 583 1 O LEU C 581 N PHE C 480
SHEET 8 G 8 ARG C 588 ARG C 590 -1 O ARG C 588 N HIS C 582
SHEET 1 H 3 VAL D 43 ASN D 45 0
SHEET 2 H 3 ARG D 50 ARG D 52 -1 O VAL D 51 N VAL D 44
SHEET 3 H 3 VAL D 96 ASN D 98 1 O ARG D 97 N ARG D 52
SHEET 1 I11 VAL D 54 ARG D 56 0
SHEET 2 I11 VAL D 66 PRO D 73 -1 O GLN D 68 N VAL D 54
SHEET 3 I11 TYR D 143 PRO D 149 -1 O LEU D 146 N PHE D 69
SHEET 4 I11 ILE D 208 THR D 211 -1 O THR D 211 N ASN D 145
SHEET 5 I11 LYS D 177 LEU D 183 1 N MET D 180 O VAL D 210
SHEET 6 I11 GLY D 254 GLY D 263 1 O THR D 260 N VAL D 179
SHEET 7 I11 LYS D 286 GLN D 290 1 O ILE D 288 N ILE D 261
SHEET 8 I11 ASP D 377 ASN D 383 1 O LEU D 379 N ALA D 289
SHEET 9 I11 VAL D 478 TYR D 484 1 O TYR D 481 N ILE D 380
SHEET 10 I11 TYR D 580 GLY D 584 1 O LEU D 581 N PHE D 480
SHEET 11 I11 VAL D 589 ARG D 590 -1 O ARG D 590 N TYR D 580
SSBOND 1 CYS A 106 CYS A 141 1555 1555 2.03
SSBOND 2 CYS A 317 CYS A 328 1555 1555 2.06
SSBOND 3 CYS A 487 CYS A 521 1555 1555 2.06
SSBOND 4 CYS B 106 CYS B 141 1555 1555 2.03
SSBOND 5 CYS B 317 CYS B 328 1555 1555 2.04
SSBOND 6 CYS B 487 CYS B 521 1555 1555 2.04
SSBOND 7 CYS C 106 CYS C 141 1555 1555 2.04
SSBOND 8 CYS C 317 CYS C 328 1555 1555 2.05
SSBOND 9 CYS C 487 CYS C 521 1555 1555 2.04
SSBOND 10 CYS D 106 CYS D 141 1555 1555 2.03
SSBOND 11 CYS D 317 CYS D 328 1555 1555 2.03
SSBOND 12 CYS D 487 CYS D 521 1555 1555 2.04
LINK ND2 ASN A 98 C1 NAG A 701 1555 1555 1.44
LINK ND2 ASN B 98 C1 NAG B 801 1555 1555 1.39
LINK ND2 ASN B 136 C1 NAG B 810 1555 1555 1.45
LINK O4 NAG A 701 C1 NAG A 702 1555 1555 1.44
LINK O4 NAG A 702 C1 MAN A 703 1555 1555 1.47
LINK O4 NAG B 801 C1 NAG B 802 1555 1555 1.44
LINK O4 NAG B 802 C1 BMA B 803 1555 1555 1.46
LINK O3 BMA B 803 C1 MAN B 806 1555 1555 1.44
LINK O6 BMA B 803 C1 MAN B 804 1555 1555 1.43
LINK O3 MAN B 806 C1 MAN B 807 1555 1555 1.45
LINK O6 MAN B 806 C1 MAN B 805 1555 1555 1.46
CISPEP 1 GLN B 549 PRO B 550 0 24.68
SITE 1 AC1 5 LYS A 41 ARG A 52 ASN A 98 ASN A 574
SITE 2 AC1 5 LYS A 576
SITE 1 AC2 2 ARG A 52 LYS A 576
SITE 1 AC3 3 THR A 132 TYR A 133 ASN A 136
SITE 1 AC4 5 LYS A 230 ASP A 356 GLY A 357 ASP A 358
SITE 2 AC4 5 ASN B 98
SITE 1 AC5 3 GLY A 225 LYS A 230 ASP A 356
SITE 1 AC7 5 THR A 224 GLY A 225 GLN A 303 PRO A 304
SITE 2 AC7 5 LEU A 305
SITE 1 AC8 1 ASP A 362
SITE 1 AC9 2 TYR A 302 ASP A 363
SITE 1 BC1 2 ASN B 136 HOH B 812
CRYST1 214.723 92.567 188.408 90.00 98.36 90.00 C 1 2 1 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 0.004657 0.000000 0.000684 0.00000
SCALE2 0.000000 0.010803 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005365 0.00000
TER 4359 HIS A 609
TER 8643 LEU B 608
TER 12926 ASN C 610
TER 17176 ASN D 610
MASTER 733 0 12 88 54 0 12 617374 4 177 180
END |