| content |
HEADER CELL ADHESION 15-NOV-11 3VKF
TITLE CRYSTAL STRUCTURE OF NEUREXIN 1BETA/NEUROLIGIN 1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ACETYLCHOLINESTERASE-LIKE DOMAIN (UNP RESIDUES 45-638);
COMPND 5 SYNONYM: NEUROLIGIN I;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NEUREXIN-1-BETA;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: LNS DOMAIN (UNP RESIDUES 83-290);
COMPND 11 SYNONYM: NEUREXIN I-BETA;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: NLGN1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: LEC 3.2.8.1;
SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: CHO;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PSGHV0;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 15 ORGANISM_COMMON: BOVINE;
SOURCE 16 ORGANISM_TAXID: 9913;
SOURCE 17 GENE: NRXN1;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLUSMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PGEX-3T
KEYWDS ALPHA/BETA HYDROLASE, BETA-SANDWICH, SYNAPSE MATULATION, CALCIUM
KEYWDS 2 BINDING, N-GLYCOSYLATION, MEMBRANE, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.TANAKA,N.MIYAZAKI,T.NOGI,K.IWASAKI,J.TAKAGI
REVDAT 1 01-AUG-12 3VKF 0
JRNL AUTH H.TANAKA,N.MIYAZAKI,T.NOGI,K.IWASAKI,J.TAKAGI
JRNL TITL HIGHER-ORDER ARCHITECTURE OF CELL ADHESION MEDIATED BY
JRNL TITL 2 POLYMORPHIC SYNAPTIC ADHESION MOLECULES NEUREXIN AND
JRNL TITL 3 NEUROLIGIN
JRNL REF CELL REP V. 2 101 2012
JRNL REFN ESSN 2211-1247
JRNL DOI 10.1016/J.CELREP.2012.06.009
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) : 48.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 22921
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2586
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) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1591
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11251
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.22000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : 0.36000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.32000
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): 0.697
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.534
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 72.166
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.842
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11623 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15843 ; 1.046 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1435 ; 5.323 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 539 ;38.123 ;24.490
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1801 ;17.007 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;15.609 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1740 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8978 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5474 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7816 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 370 ; 0.122 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.165 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 93 ; 0.157 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.055 ; 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): 7314 ; 0.225 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11574 ; 0.410 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4903 ; 0.388 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4269 ; 0.656 ; 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 : NULL
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 82 C 288
REMARK 3 RESIDUE RANGE : C 2001 C 2001
REMARK 3 ORIGIN FOR THE GROUP (A): -49.457 -7.102 49.912
REMARK 3 T TENSOR
REMARK 3 T11: -0.2104 T22: -0.4154
REMARK 3 T33: -0.1857 T12: -0.0204
REMARK 3 T13: -0.0118 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 7.8904 L22: 4.7144
REMARK 3 L33: 2.2680 L12: -1.9851
REMARK 3 L13: -2.3528 L23: 1.0554
REMARK 3 S TENSOR
REMARK 3 S11: 0.0879 S12: 0.0029 S13: -0.1383
REMARK 3 S21: 0.0762 S22: -0.0961 S23: 0.3074
REMARK 3 S31: 0.0011 S32: -0.0206 S33: 0.0082
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 82 D 288
REMARK 3 RESIDUE RANGE : D 2001 D 2001
REMARK 3 ORIGIN FOR THE GROUP (A): 24.865 -2.006 -15.517
REMARK 3 T TENSOR
REMARK 3 T11: -0.1153 T22: -0.1062
REMARK 3 T33: -0.1704 T12: 0.0454
REMARK 3 T13: -0.0477 T23: 0.0822
REMARK 3 L TENSOR
REMARK 3 L11: 10.8740 L22: 3.6856
REMARK 3 L33: 3.4474 L12: 0.9156
REMARK 3 L13: -2.3434 L23: 1.8463
REMARK 3 S TENSOR
REMARK 3 S11: 0.1303 S12: -0.2886 S13: 0.5725
REMARK 3 S21: 0.0364 S22: 0.0506 S23: -0.1518
REMARK 3 S31: 0.0014 S32: 0.0844 S33: -0.1809
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 52 A 634
REMARK 3 RESIDUE RANGE : A 2001 A 2004
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3500 -1.1511 48.7848
REMARK 3 T TENSOR
REMARK 3 T11: -0.2943 T22: -0.3711
REMARK 3 T33: -0.1999 T12: -0.0230
REMARK 3 T13: 0.0230 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 2.0882 L22: 1.3837
REMARK 3 L33: 2.3528 L12: -0.1052
REMARK 3 L13: 0.0420 L23: 0.1139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0107 S12: -0.0125 S13: 0.0242
REMARK 3 S21: -0.1276 S22: -0.0211 S23: -0.1185
REMARK 3 S31: -0.1122 S32: 0.0891 S33: 0.0104
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 52 B 634
REMARK 3 RESIDUE RANGE : B 2001 B 2001
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6257 1.8414 -12.2669
REMARK 3 T TENSOR
REMARK 3 T11: -0.1337 T22: -0.1156
REMARK 3 T33: -0.1722 T12: -0.0430
REMARK 3 T13: -0.0201 T23: -0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 1.8259 L22: 0.9964
REMARK 3 L33: 4.2944 L12: -0.1321
REMARK 3 L13: 0.2580 L23: -0.6897
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: 0.0825 S13: -0.0786
REMARK 3 S21: -0.0202 S22: -0.0637 S23: 0.0870
REMARK 3 S31: -0.1460 S32: -0.1315 S33: 0.0320
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3VKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-DEC-11.
REMARK 100 THE RCSB ID CODE IS RCSB095155.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25519
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 48.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.31100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CHLORIDE, 0.005M CALCIUM
REMARK 280 CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING 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 47.59300
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, 3, 4, 5
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, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 45
REMARK 465 GLN A 46
REMARK 465 LYS A 47
REMARK 465 LEU A 48
REMARK 465 ASP A 49
REMARK 465 ASP A 50
REMARK 465 VAL A 51
REMARK 465 ASP A 579
REMARK 465 THR A 580
REMARK 465 LYS A 581
REMARK 465 PHE A 582
REMARK 465 ILE A 583
REMARK 465 HIS A 584
REMARK 465 THR A 585
REMARK 465 LYS A 586
REMARK 465 PRO A 587
REMARK 465 ASN A 588
REMARK 465 ARG A 589
REMARK 465 PHE A 590
REMARK 465 GLU A 591
REMARK 465 GLU A 592
REMARK 465 ASN A 635
REMARK 465 LEU A 636
REMARK 465 ASN A 637
REMARK 465 ASP A 638
REMARK 465 SER B 45
REMARK 465 GLN B 46
REMARK 465 LYS B 47
REMARK 465 LEU B 48
REMARK 465 ASP B 49
REMARK 465 ASP B 50
REMARK 465 VAL B 51
REMARK 465 GLU B 163
REMARK 465 ASP B 164
REMARK 465 VAL B 165
REMARK 465 LYS B 166
REMARK 465 ARG B 167
REMARK 465 ILE B 168
REMARK 465 SER B 169
REMARK 465 LYS B 170
REMARK 465 GLU B 171
REMARK 465 CYS B 172
REMARK 465 ALA B 173
REMARK 465 ARG B 174
REMARK 465 LYS B 175
REMARK 465 PRO B 176
REMARK 465 GLY B 177
REMARK 465 LYS B 178
REMARK 465 LYS B 179
REMARK 465 ILE B 180
REMARK 465 CYS B 181
REMARK 465 ARG B 182
REMARK 465 LYS B 183
REMARK 465 GLY B 184
REMARK 465 ASP B 185
REMARK 465 ILE B 186
REMARK 465 ARG B 187
REMARK 465 ASP B 188
REMARK 465 SER B 189
REMARK 465 GLY B 190
REMARK 465 GLY B 444
REMARK 465 TYR B 445
REMARK 465 PRO B 446
REMARK 465 GLU B 447
REMARK 465 GLY B 448
REMARK 465 ASP B 579
REMARK 465 THR B 580
REMARK 465 LYS B 581
REMARK 465 PHE B 582
REMARK 465 ILE B 583
REMARK 465 HIS B 584
REMARK 465 THR B 585
REMARK 465 LYS B 586
REMARK 465 PRO B 587
REMARK 465 ASN B 588
REMARK 465 ARG B 589
REMARK 465 PHE B 590
REMARK 465 GLU B 591
REMARK 465 GLU B 592
REMARK 465 ASN B 635
REMARK 465 LEU B 636
REMARK 465 ASN B 637
REMARK 465 ASP B 638
REMARK 465 GLY C 81
REMARK 465 GLU C 289
REMARK 465 VAL C 290
REMARK 465 SER C 291
REMARK 465 GLY D 81
REMARK 465 GLU D 289
REMARK 465 VAL D 290
REMARK 465 SER D 291
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 GLU A 72 -57.45 -23.77
REMARK 500 ILE A 73 -81.31 -69.02
REMARK 500 ASP A 106 -154.91 -94.92
REMARK 500 ARG A 125 4.25 -65.50
REMARK 500 LYS A 183 72.04 -155.56
REMARK 500 SER A 203 28.17 -143.73
REMARK 500 THR A 208 127.87 -172.20
REMARK 500 LEU A 232 -162.56 -116.95
REMARK 500 ASP A 242 -145.45 -176.32
REMARK 500 PRO A 272 3.09 -66.88
REMARK 500 VAL A 367 76.03 -114.25
REMARK 500 ASP A 383 -81.44 -152.80
REMARK 500 GLU A 397 59.22 -110.19
REMARK 500 GLU A 417 48.53 -65.66
REMARK 500 ASN A 418 -35.32 -143.91
REMARK 500 ASP A 424 63.46 39.42
REMARK 500 TYR A 445 -109.68 -103.45
REMARK 500 PRO A 446 -177.65 -61.49
REMARK 500 GLU A 447 -56.70 108.11
REMARK 500 ASP A 465 65.45 -151.38
REMARK 500 PHE A 499 36.71 -87.90
REMARK 500 THR A 514 -150.54 -86.77
REMARK 500 ASP A 522 -153.46 -86.10
REMARK 500 ASP A 527 -16.73 -45.57
REMARK 500 TRP A 595 96.93 -63.55
REMARK 500 HIS A 617 80.57 45.65
REMARK 500 GLU A 628 -60.02 -103.22
REMARK 500 ASN B 70 40.58 -79.05
REMARK 500 PRO B 88 109.19 -49.36
REMARK 500 ASP B 106 -143.86 -95.52
REMARK 500 ASN B 109 71.52 -66.85
REMARK 500 SER B 203 14.25 -140.06
REMARK 500 ALA B 218 -70.00 -64.80
REMARK 500 ASN B 343 86.86 -68.92
REMARK 500 SER B 345 -71.47 -45.42
REMARK 500 TYR B 372 -6.69 80.52
REMARK 500 ASP B 383 -70.82 -136.32
REMARK 500 ASN B 418 3.55 -62.40
REMARK 500 PRO B 502 88.57 -60.20
REMARK 500 ASN B 547 98.02 -60.33
REMARK 500 ASP B 571 108.94 -167.60
REMARK 500 GLN B 603 63.83 38.93
REMARK 500 HIS B 617 75.83 40.67
REMARK 500 HIS B 632 72.27 -105.01
REMARK 500 SER C 89 -158.44 -121.51
REMARK 500 LYS C 90 123.20 -34.34
REMARK 500 PRO C 100 137.70 -37.60
REMARK 500 THR C 155 -87.85 -91.50
REMARK 500 GLU C 162 90.22 -69.13
REMARK 500 ASN C 164 61.72 -110.73
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL D 153 O
REMARK 620 2 ILE D 235 O 97.6
REMARK 620 3 ASN D 237 OD1 150.5 102.6
REMARK 620 4 ASP D 136 OD2 78.2 97.8 77.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 237 OD1
REMARK 620 2 VAL C 153 O 135.1
REMARK 620 3 ASP C 136 OD2 68.8 75.7
REMARK 620 4 ILE C 235 O 72.2 70.9 71.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2001
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE OF THE CHAIN A/B WAS BASED ON ISOFORM 3 OF DATABASE Q62765
REMARK 999 (NLGN1_RAT). SEQUENCE OF THE CHAIN C/D WAS BASED ON ISOFORM 3B OF
REMARK 999 DATABASE Q28142 (NRX1B_BOVIN).
DBREF 3VKF A 45 638 UNP Q62765 NLGN1_RAT 45 638
DBREF 3VKF B 45 638 UNP Q62765 NLGN1_RAT 45 638
DBREF 3VKF C 83 290 UNP Q28142 NRX1B_BOVIN 83 290
DBREF 3VKF D 83 290 UNP Q28142 NRX1B_BOVIN 83 290
SEQADV 3VKF GLY C 81 UNP Q28142 EXPRESSION TAG
SEQADV 3VKF SER C 82 UNP Q28142 EXPRESSION TAG
SEQADV 3VKF SER C 291 UNP Q28142 EXPRESSION TAG
SEQADV 3VKF GLY D 81 UNP Q28142 EXPRESSION TAG
SEQADV 3VKF SER D 82 UNP Q28142 EXPRESSION TAG
SEQADV 3VKF SER D 291 UNP Q28142 EXPRESSION TAG
SEQRES 1 A 585 SER GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL THR THR
SEQRES 2 A 585 ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU LEU ASN
SEQRES 3 A 585 ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU GLY VAL
SEQRES 4 A 585 PRO TYR ALA ALA PRO PRO THR GLY GLU HIS ARG PHE GLN
SEQRES 5 A 585 PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE ARG ASN
SEQRES 6 A 585 ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN ILE ILE
SEQRES 7 A 585 ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL TRP PHE
SEQRES 8 A 585 THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL GLN ASP
SEQRES 9 A 585 GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR VAL PRO
SEQRES 10 A 585 THR GLU ASP VAL LYS ARG ILE SER LYS GLU CYS ALA ARG
SEQRES 11 A 585 LYS PRO GLY LYS LYS ILE CYS ARG LYS GLY ASP ILE ARG
SEQRES 12 A 585 ASP SER GLY GLY PRO LYS PRO VAL MET VAL TYR ILE HIS
SEQRES 13 A 585 GLY GLY SER TYR MET GLU GLY THR GLY ASN LEU TYR ASP
SEQRES 14 A 585 GLY SER VAL LEU ALA SER TYR GLY ASN VAL ILE VAL ILE
SEQRES 15 A 585 THR VAL ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU SER
SEQRES 16 A 585 THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU
SEQRES 17 A 585 ASP LEU ILE GLN ALA LEU ARG TRP THR SER GLU ASN ILE
SEQRES 18 A 585 GLY PHE PHE GLY GLY ASP PRO LEU ARG ILE THR VAL PHE
SEQRES 19 A 585 GLY SER GLY ALA GLY GLY SER CYS VAL ASN LEU LEU THR
SEQRES 20 A 585 LEU SER HIS TYR SER GLU GLY LEU PHE GLN ARG ALA ILE
SEQRES 21 A 585 ALA GLN SER GLY THR ALA LEU SER SER TRP ALA VAL SER
SEQRES 22 A 585 PHE GLN PRO ALA LYS TYR ALA ARG ILE LEU ALA THR LYS
SEQRES 23 A 585 VAL GLY CYS ASN VAL SER ASP THR VAL GLU LEU VAL GLU
SEQRES 24 A 585 CYS LEU GLN LYS LYS PRO TYR LYS GLU LEU VAL ASP GLN
SEQRES 25 A 585 ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY PRO
SEQRES 26 A 585 VAL ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLN ILE
SEQRES 27 A 585 LEU MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET
SEQRES 28 A 585 LEU GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL GLU
SEQRES 29 A 585 ASN ILE VAL ASP SER ASP ASP GLY VAL SER ALA SER ASP
SEQRES 30 A 585 PHE ASP PHE ALA VAL SER ASN PHE VAL ASP ASN LEU TYR
SEQRES 31 A 585 GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR ILE
SEQRES 32 A 585 LYS PHE MET TYR THR ASP TRP ALA ASP ARG HIS ASN PRO
SEQRES 33 A 585 GLU THR ARG ARG LYS THR LEU LEU ALA LEU PHE THR ASP
SEQRES 34 A 585 HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA ASP LEU
SEQRES 35 A 585 HIS SER ASN PHE GLY SER PRO THR TYR PHE TYR ALA PHE
SEQRES 36 A 585 TYR HIS HIS CYS GLN THR ASP GLN VAL PRO ALA TRP ALA
SEQRES 37 A 585 ASP ALA ALA HIS GLY ASP GLU VAL PRO TYR VAL LEU GLY
SEQRES 38 A 585 ILE PRO MET ILE GLY PRO THR GLU LEU PHE PRO CYS ASN
SEQRES 39 A 585 PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET
SEQRES 40 A 585 THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN
SEQRES 41 A 585 GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS
SEQRES 42 A 585 PRO ASN ARG PHE GLU GLU VAL ALA TRP THR ARG TYR SER
SEQRES 43 A 585 GLN LYS ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO
SEQRES 44 A 585 ARG VAL LYS GLU HIS TYR ARG ALA ASN LYS VAL ASN LEU
SEQRES 45 A 585 TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU ASN ASP
SEQRES 1 B 585 SER GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL THR THR
SEQRES 2 B 585 ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU LEU ASN
SEQRES 3 B 585 ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU GLY VAL
SEQRES 4 B 585 PRO TYR ALA ALA PRO PRO THR GLY GLU HIS ARG PHE GLN
SEQRES 5 B 585 PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE ARG ASN
SEQRES 6 B 585 ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN ILE ILE
SEQRES 7 B 585 ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL TRP PHE
SEQRES 8 B 585 THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL GLN ASP
SEQRES 9 B 585 GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR VAL PRO
SEQRES 10 B 585 THR GLU ASP VAL LYS ARG ILE SER LYS GLU CYS ALA ARG
SEQRES 11 B 585 LYS PRO GLY LYS LYS ILE CYS ARG LYS GLY ASP ILE ARG
SEQRES 12 B 585 ASP SER GLY GLY PRO LYS PRO VAL MET VAL TYR ILE HIS
SEQRES 13 B 585 GLY GLY SER TYR MET GLU GLY THR GLY ASN LEU TYR ASP
SEQRES 14 B 585 GLY SER VAL LEU ALA SER TYR GLY ASN VAL ILE VAL ILE
SEQRES 15 B 585 THR VAL ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU SER
SEQRES 16 B 585 THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU
SEQRES 17 B 585 ASP LEU ILE GLN ALA LEU ARG TRP THR SER GLU ASN ILE
SEQRES 18 B 585 GLY PHE PHE GLY GLY ASP PRO LEU ARG ILE THR VAL PHE
SEQRES 19 B 585 GLY SER GLY ALA GLY GLY SER CYS VAL ASN LEU LEU THR
SEQRES 20 B 585 LEU SER HIS TYR SER GLU GLY LEU PHE GLN ARG ALA ILE
SEQRES 21 B 585 ALA GLN SER GLY THR ALA LEU SER SER TRP ALA VAL SER
SEQRES 22 B 585 PHE GLN PRO ALA LYS TYR ALA ARG ILE LEU ALA THR LYS
SEQRES 23 B 585 VAL GLY CYS ASN VAL SER ASP THR VAL GLU LEU VAL GLU
SEQRES 24 B 585 CYS LEU GLN LYS LYS PRO TYR LYS GLU LEU VAL ASP GLN
SEQRES 25 B 585 ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY PRO
SEQRES 26 B 585 VAL ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLN ILE
SEQRES 27 B 585 LEU MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET
SEQRES 28 B 585 LEU GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL GLU
SEQRES 29 B 585 ASN ILE VAL ASP SER ASP ASP GLY VAL SER ALA SER ASP
SEQRES 30 B 585 PHE ASP PHE ALA VAL SER ASN PHE VAL ASP ASN LEU TYR
SEQRES 31 B 585 GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR ILE
SEQRES 32 B 585 LYS PHE MET TYR THR ASP TRP ALA ASP ARG HIS ASN PRO
SEQRES 33 B 585 GLU THR ARG ARG LYS THR LEU LEU ALA LEU PHE THR ASP
SEQRES 34 B 585 HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA ASP LEU
SEQRES 35 B 585 HIS SER ASN PHE GLY SER PRO THR TYR PHE TYR ALA PHE
SEQRES 36 B 585 TYR HIS HIS CYS GLN THR ASP GLN VAL PRO ALA TRP ALA
SEQRES 37 B 585 ASP ALA ALA HIS GLY ASP GLU VAL PRO TYR VAL LEU GLY
SEQRES 38 B 585 ILE PRO MET ILE GLY PRO THR GLU LEU PHE PRO CYS ASN
SEQRES 39 B 585 PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET
SEQRES 40 B 585 THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN
SEQRES 41 B 585 GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS
SEQRES 42 B 585 PRO ASN ARG PHE GLU GLU VAL ALA TRP THR ARG TYR SER
SEQRES 43 B 585 GLN LYS ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO
SEQRES 44 B 585 ARG VAL LYS GLU HIS TYR ARG ALA ASN LYS VAL ASN LEU
SEQRES 45 B 585 TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU ASN ASP
SEQRES 1 C 181 GLY SER GLY THR THR TYR ILE PHE SER LYS GLY GLY GLY
SEQRES 2 C 181 GLN ILE THR TYR LYS TRP PRO PRO ASN ASP ARG PRO SER
SEQRES 3 C 181 THR ARG ALA ASP ARG LEU ALA ILE GLY PHE SER THR VAL
SEQRES 4 C 181 GLN LYS GLU ALA VAL LEU VAL ARG VAL ASP SER SER SER
SEQRES 5 C 181 GLY LEU GLY ASP TYR LEU GLU LEU HIS ILE HIS GLN GLY
SEQRES 6 C 181 LYS ILE GLY VAL LYS PHE ASN VAL GLY THR ASP ASP ILE
SEQRES 7 C 181 ALA ILE GLU GLU SER ASN ALA ILE ILE ASN ASP GLY LYS
SEQRES 8 C 181 TYR HIS VAL VAL ARG PHE THR ARG SER GLY GLY ASN ALA
SEQRES 9 C 181 THR LEU GLN VAL ASP SER TRP PRO VAL ILE GLU ARG TYR
SEQRES 10 C 181 PRO ALA GLY ARG GLN LEU THR ILE PHE ASN SER GLN ALA
SEQRES 11 C 181 THR ILE ILE ILE GLY GLY LYS GLU GLN GLY GLN PRO PHE
SEQRES 12 C 181 GLN GLY GLN LEU SER GLY LEU TYR TYR ASN GLY LEU LYS
SEQRES 13 C 181 VAL LEU ASN MET ALA ALA GLU ASN ASP ALA ASN ILE ALA
SEQRES 14 C 181 ILE VAL GLY ASN VAL ARG LEU VAL GLY GLU VAL SER
SEQRES 1 D 181 GLY SER GLY THR THR TYR ILE PHE SER LYS GLY GLY GLY
SEQRES 2 D 181 GLN ILE THR TYR LYS TRP PRO PRO ASN ASP ARG PRO SER
SEQRES 3 D 181 THR ARG ALA ASP ARG LEU ALA ILE GLY PHE SER THR VAL
SEQRES 4 D 181 GLN LYS GLU ALA VAL LEU VAL ARG VAL ASP SER SER SER
SEQRES 5 D 181 GLY LEU GLY ASP TYR LEU GLU LEU HIS ILE HIS GLN GLY
SEQRES 6 D 181 LYS ILE GLY VAL LYS PHE ASN VAL GLY THR ASP ASP ILE
SEQRES 7 D 181 ALA ILE GLU GLU SER ASN ALA ILE ILE ASN ASP GLY LYS
SEQRES 8 D 181 TYR HIS VAL VAL ARG PHE THR ARG SER GLY GLY ASN ALA
SEQRES 9 D 181 THR LEU GLN VAL ASP SER TRP PRO VAL ILE GLU ARG TYR
SEQRES 10 D 181 PRO ALA GLY ARG GLN LEU THR ILE PHE ASN SER GLN ALA
SEQRES 11 D 181 THR ILE ILE ILE GLY GLY LYS GLU GLN GLY GLN PRO PHE
SEQRES 12 D 181 GLN GLY GLN LEU SER GLY LEU TYR TYR ASN GLY LEU LYS
SEQRES 13 D 181 VAL LEU ASN MET ALA ALA GLU ASN ASP ALA ASN ILE ALA
SEQRES 14 D 181 ILE VAL GLY ASN VAL ARG LEU VAL GLY GLU VAL SER
MODRES 3VKF ASN A 343 ASN GLYCOSYLATION SITE
MODRES 3VKF ASN B 343 ASN GLYCOSYLATION SITE
MODRES 3VKF ASN A 547 ASN GLYCOSYLATION SITE
HET CA C2001 1
HET CA D2001 1
HET NAG A2001 14
HET NAG A2002 14
HET NAG A2003 14
HET BMA A2004 11
HET NAG B2001 14
HETNAM CA CALCIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
FORMUL 5 CA 2(CA 2+)
FORMUL 7 NAG 4(C8 H15 N O6)
FORMUL 8 BMA C6 H12 O6
HELIX 1 1 THR A 90 ARG A 94 5 5
HELIX 2 2 PRO A 132 ASN A 138 1 7
HELIX 3 3 ASN A 138 GLN A 147 1 10
HELIX 4 4 ILE A 168 LYS A 175 1 8
HELIX 5 5 LYS A 178 LYS A 183 1 6
HELIX 6 6 THR A 208 TYR A 212 5 5
HELIX 7 7 GLY A 214 GLY A 221 1 8
HELIX 8 8 ASN A 248 GLY A 269 1 22
HELIX 9 9 GLY A 281 SER A 293 1 13
HELIX 10 10 HIS A 294 GLU A 297 5 4
HELIX 11 11 GLN A 328 VAL A 340 1 13
HELIX 12 12 ASP A 346 LYS A 357 1 12
HELIX 13 13 PRO A 358 ASP A 364 1 7
HELIX 14 14 ASP A 388 GLN A 395 1 8
HELIX 15 15 GLY A 412 VAL A 416 5 5
HELIX 16 16 SER A 427 TYR A 443 1 17
HELIX 17 17 GLY A 448 TYR A 460 1 13
HELIX 18 18 ASP A 462 ARG A 466 5 5
HELIX 19 19 ASN A 468 TRP A 485 1 18
HELIX 20 20 TRP A 485 PHE A 499 1 15
HELIX 21 21 GLU A 528 GLY A 534 1 7
HELIX 22 22 ILE A 535 ILE A 538 5 4
HELIX 23 23 SER A 549 GLY A 570 1 22
HELIX 24 24 ARG A 619 GLU A 628 1 10
HELIX 25 25 LEU A 629 LEU A 633 5 5
HELIX 26 26 THR B 90 ARG B 94 5 5
HELIX 27 27 PRO B 132 ASN B 138 1 7
HELIX 28 28 ASN B 138 SER B 143 1 6
HELIX 29 29 THR B 208 TYR B 212 5 5
HELIX 30 30 GLY B 214 ASN B 222 1 9
HELIX 31 31 LEU B 232 LEU B 238 1 7
HELIX 32 32 ASN B 248 ILE B 265 1 18
HELIX 33 33 GLY B 281 LEU B 292 1 12
HELIX 34 34 SER B 293 GLU B 297 5 5
HELIX 35 35 GLN B 328 VAL B 340 1 13
HELIX 36 36 ASP B 346 LYS B 357 1 12
HELIX 37 37 PRO B 358 ASP B 364 1 7
HELIX 38 38 GLN B 390 GLN B 395 1 6
HELIX 39 39 GLY B 412 GLU B 417 1 6
HELIX 40 40 ASN B 418 VAL B 420 5 3
HELIX 41 41 SER B 427 TYR B 443 1 17
HELIX 42 42 ASP B 450 TYR B 460 1 11
HELIX 43 43 GLU B 470 TRP B 485 1 16
HELIX 44 44 TRP B 485 ASN B 498 1 14
HELIX 45 45 GLU B 528 LEU B 533 1 6
HELIX 46 46 GLY B 534 ILE B 538 5 5
HELIX 47 47 SER B 549 GLY B 570 1 22
HELIX 48 48 ARG B 619 LEU B 629 1 11
HELIX 49 49 PRO C 100 ARG C 104 5 5
HELIX 50 50 VAL C 267 GLU C 273 1 7
HELIX 51 51 PRO D 100 ARG D 104 5 5
HELIX 52 52 GLY D 246 GLY D 250 5 5
HELIX 53 53 VAL D 267 ALA D 271 1 5
HELIX 54 54 ALA D 272 ASN D 274 5 3
SHEET 1 A 3 LEU A 54 THR A 57 0
SHEET 2 A 3 GLY A 60 ARG A 63 -1 O ILE A 62 N VAL A 55
SHEET 3 A 3 ILE A 107 ASN A 109 1 O ARG A 108 N ARG A 63
SHEET 1 B11 ILE A 65 LYS A 67 0
SHEET 2 B11 VAL A 77 PRO A 84 -1 O GLN A 79 N ILE A 65
SHEET 3 B11 TYR A 155 PRO A 161 -1 O VAL A 160 N ILE A 78
SHEET 4 B11 ILE A 224 VAL A 228 -1 O VAL A 225 N TYR A 159
SHEET 5 B11 LYS A 193 ILE A 199 1 N MET A 196 O ILE A 226
SHEET 6 B11 GLY A 270 SER A 280 1 O PHE A 278 N VAL A 197
SHEET 7 B11 ARG A 311 GLN A 315 1 O GLN A 315 N GLY A 279
SHEET 8 B11 ASP A 402 ASN A 408 1 O ASP A 402 N ALA A 312
SHEET 9 B11 THR A 503 PHE A 508 1 O TYR A 504 N LEU A 405
SHEET 10 B11 LEU A 604 ILE A 608 1 O LEU A 606 N PHE A 505
SHEET 11 B11 ARG A 613 GLU A 616 -1 O ARG A 613 N HIS A 607
SHEET 1 C 3 LEU B 54 THR B 57 0
SHEET 2 C 3 GLY B 60 ARG B 63 -1 O GLY B 60 N THR B 57
SHEET 3 C 3 ILE B 107 ASN B 109 1 O ARG B 108 N LYS B 61
SHEET 1 D 8 ILE B 65 LYS B 67 0
SHEET 2 D 8 VAL B 77 PRO B 84 -1 O GLN B 79 N ILE B 65
SHEET 3 D 8 TYR B 155 PRO B 161 -1 O VAL B 160 N ILE B 78
SHEET 4 D 8 ILE B 224 VAL B 228 -1 O THR B 227 N ASN B 157
SHEET 5 D 8 LYS B 193 ILE B 199 1 N TYR B 198 O ILE B 226
SHEET 6 D 8 GLY B 270 SER B 280 1 O PHE B 278 N VAL B 197
SHEET 7 D 8 ARG B 311 GLN B 315 1 O GLN B 315 N GLY B 279
SHEET 8 D 8 ASP B 402 MET B 404 1 O ASP B 402 N ALA B 312
SHEET 1 E 4 VAL B 407 ASN B 408 0
SHEET 2 E 4 PHE B 505 PHE B 508 1 O TYR B 506 N VAL B 407
SHEET 3 E 4 LEU B 604 ILE B 608 1 O ILE B 608 N ALA B 507
SHEET 4 E 4 ARG B 613 GLU B 616 -1 O ARG B 613 N HIS B 607
SHEET 1 F 8 ILE C 158 GLU C 161 0
SHEET 2 F 8 LYS C 146 ASN C 152 -1 N PHE C 151 O ILE C 158
SHEET 3 F 8 TYR C 137 HIS C 143 -1 N GLU C 139 O LYS C 150
SHEET 4 F 8 ALA C 123 SER C 130 -1 N VAL C 126 O LEU C 140
SHEET 5 F 8 GLN C 239 ILE C 244 -1 O ILE C 243 N ARG C 127
SHEET 6 F 8 TYR C 86 LYS C 98 -1 N TYR C 97 O ILE C 242
SHEET 7 F 8 GLY C 255 TYR C 262 -1 O LEU C 257 N TYR C 86
SHEET 8 F 8 LEU C 265 LYS C 266 -1 O LEU C 265 N TYR C 262
SHEET 1 G 7 ILE C 194 ARG C 196 0
SHEET 2 G 7 ASN C 183 VAL C 188 -1 N LEU C 186 O ILE C 194
SHEET 3 G 7 HIS C 173 SER C 180 -1 N ARG C 176 O GLN C 187
SHEET 4 G 7 ALA C 109 THR C 118 -1 N LEU C 112 O PHE C 177
SHEET 5 G 7 GLY C 255 TYR C 262 -1 O SER C 258 N GLY C 115
SHEET 6 G 7 TYR C 86 LYS C 98 -1 N TYR C 86 O LEU C 257
SHEET 7 G 7 ILE C 278 LEU C 286 -1 O ARG C 285 N ILE C 87
SHEET 1 H 8 ILE D 158 GLU D 161 0
SHEET 2 H 8 LYS D 146 ASN D 152 -1 N VAL D 149 O ILE D 160
SHEET 3 H 8 TYR D 137 HIS D 143 -1 N HIS D 143 O LYS D 146
SHEET 4 H 8 ALA D 123 SER D 130 -1 N VAL D 126 O LEU D 140
SHEET 5 H 8 GLN D 239 ILE D 244 -1 O ALA D 240 N ASP D 129
SHEET 6 H 8 THR D 85 LYS D 98 -1 N TYR D 97 O ILE D 242
SHEET 7 H 8 GLY D 255 TYR D 262 -1 O GLY D 255 N PHE D 88
SHEET 8 H 8 LEU D 265 LYS D 266 -1 O LEU D 265 N TYR D 262
SHEET 1 I 7 ILE D 194 ARG D 196 0
SHEET 2 I 7 ASN D 183 VAL D 188 -1 N ALA D 184 O ARG D 196
SHEET 3 I 7 HIS D 173 SER D 180 -1 N THR D 178 O THR D 185
SHEET 4 I 7 ALA D 109 THR D 118 -1 N LEU D 112 O PHE D 177
SHEET 5 I 7 GLY D 255 TYR D 262 -1 O TYR D 261 N ALA D 113
SHEET 6 I 7 THR D 85 LYS D 98 -1 N PHE D 88 O GLY D 255
SHEET 7 I 7 ALA D 279 LEU D 286 -1 O ARG D 285 N ILE D 87
SSBOND 1 CYS A 117 CYS A 153 1555 1555 2.05
SSBOND 2 CYS A 172 CYS A 181 1555 1555 2.03
SSBOND 3 CYS A 342 CYS A 353 1555 1555 2.03
SSBOND 4 CYS A 512 CYS A 546 1555 1555 2.04
SSBOND 5 CYS B 117 CYS B 153 1555 1555 2.04
SSBOND 6 CYS B 342 CYS B 353 1555 1555 2.04
SSBOND 7 CYS B 512 CYS B 546 1555 1555 2.04
LINK ND2 ASN A 343 C1 NAG A2001 1555 1555 1.44
LINK ND2 ASN B 343 C1 NAG B2001 1555 1555 1.45
LINK O4 NAG A2002 C1 NAG A2003 1555 1555 1.45
LINK O4 NAG A2003 C1 BMA A2004 1555 1555 1.45
LINK ND2 ASN A 547 C1 NAG A2002 1555 1555 1.45
LINK O VAL D 153 CA CA D2001 1555 1555 2.09
LINK O ILE D 235 CA CA D2001 1555 1555 2.30
LINK OD1 ASN C 237 CA CA C2001 1555 1555 2.31
LINK O VAL C 153 CA CA C2001 1555 1555 2.38
LINK OD1 ASN D 237 CA CA D2001 1555 1555 2.39
LINK OD2 ASP D 136 CA CA D2001 1555 1555 2.45
LINK OD2 ASP C 136 CA CA C2001 1555 1555 2.49
LINK O ILE C 235 CA CA C2001 1555 1555 2.75
CISPEP 1 GLN A 574 PRO A 575 0 0.09
CISPEP 2 GLN B 574 PRO B 575 0 -5.57
SITE 1 AC1 4 ASP C 136 VAL C 153 ILE C 235 ASN C 237
SITE 1 AC2 4 ASP D 136 VAL D 153 ILE D 235 ASN D 237
SITE 1 AC3 3 ARG A 334 THR A 338 ASN A 343
SITE 1 AC4 2 ASN A 547 NAG A2003
SITE 1 AC5 2 NAG A2002 BMA A2004
SITE 1 AC6 1 NAG A2003
SITE 1 AC7 3 ARG B 334 THR B 338 ASN B 343
CRYST1 81.261 95.186 120.396 90.00 108.62 90.00 P 1 21 1 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 0.012306 0.000000 0.004146 0.00000
SCALE2 0.000000 0.010506 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008765 0.00000
TER 4400 HIS A 634
TER 8545 HIS B 634
TER 9900 GLY C 288
TER 11255 GLY D 288
MASTER 551 0 7 54 59 0 7 611320 4 94 118
END |