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HEADER CELL ADHESION 16-NOV-07 3BE8
TITLE CRYSTAL STRUCTURE OF THE SYNAPTIC PROTEIN NEUROLIGIN 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-4, X-LINKED;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EXTRACELLULAR CHOLINESTERASE-LIKE DOMAIN;
COMPND 5 SYNONYM: NEUROLIGIN X, HNLX;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: NLGN4X;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;
SOURCE 8 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY CELLS (HEK)
KEYWDS NEUROLIGIN, CELL ADHESION PROTEIN, SYNAPTIC PROTEIN, A/B-
KEYWDS 2 HYDROLASE FOLD, FOUR-HELIX BUNDLE, ALTERNATIVE SPLICING,
KEYWDS 3 GLYCOPROTEIN, MEMBRANE, POLYMORPHISM, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.P.FABRICHNY,P.LEONE,G.SULZENBACHER,D.COMOLETTI,M.T.MILLER,
AUTHOR 2 P.TAYLOR,Y.BOURNE,P.MARCHOT
REVDAT 1 29-JAN-08 3BE8 0
JRNL AUTH I.P.FABRICHNY,P.LEONE,G.SULZENBACHER,D.COMOLETTI,
JRNL AUTH 2 M.T.MILLER,P.TAYLOR,Y.BOURNE,P.MARCHOT
JRNL TITL STRUCTURAL ANALYSIS OF THE SYNAPTIC PROTEIN
JRNL TITL 2 NEUROLIGIN AND ITS BETA-NEUREXIN COMPLEX:
JRNL TITL 3 DETERMINANTS FOR FOLDING AND CELL ADHESION
JRNL REF NEURON V. 56 979 2007
JRNL REFN ASTM NERNET US ISSN 0896-6273
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 85129
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4474
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6218
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 350
REMARK 3 BIN FREE R VALUE : 0.2390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 9309
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : 0.17000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.116
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8966 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7829 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12250 ; 1.389 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18291 ; 0.865 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1104 ; 6.169 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 423 ;34.652 ;24.610
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1392 ;14.795 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;20.784 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1331 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10011 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1787 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1675 ; 0.208 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7683 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4296 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4552 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 541 ; 0.152 ; 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): 21 ; 0.233 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.294 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.197 ; 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): 5555 ; 0.758 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2192 ; 0.149 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8812 ; 1.268 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3931 ; 1.906 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3421 ; 2.837 ; 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 : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -2 A 110
REMARK 3 RESIDUE RANGE : A 142 A 291
REMARK 3 RESIDUE RANGE : A 340 A 373
REMARK 3 RESIDUE RANGE : A 449 A 472
REMARK 3 RESIDUE RANGE : A 561 A 582
REMARK 3 ORIGIN FOR THE GROUP (A): 116.5901 34.6875 55.3565
REMARK 3 T TENSOR
REMARK 3 T11: -.1122 T22: -.0739
REMARK 3 T33: -.1488 T12: -.0219
REMARK 3 T13: .0092 T23: .0234
REMARK 3 L TENSOR
REMARK 3 L11: 2.1190 L22: 1.1930
REMARK 3 L33: 1.1698 L12: .6349
REMARK 3 L13: -.0694 L23: -.0320
REMARK 3 S TENSOR
REMARK 3 S11: -.0310 S12: -.1157 S13: -.1473
REMARK 3 S21: -.0338 S22: -.0146 S23: -.1763
REMARK 3 S31: -.0298 S32: .2963 S33: .0456
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 : A 111 A 141
REMARK 3 ORIGIN FOR THE GROUP (A): 114.2138 33.9719 75.6563
REMARK 3 T TENSOR
REMARK 3 T11: .2455 T22: .2827
REMARK 3 T33: .1055 T12: .0513
REMARK 3 T13: -.0836 T23: .0332
REMARK 3 L TENSOR
REMARK 3 L11: 8.7869 L22: 9.8741
REMARK 3 L33: 11.1136 L12: 5.0372
REMARK 3 L13: -2.3888 L23: -1.9974
REMARK 3 S TENSOR
REMARK 3 S11: .3396 S12: -.6729 S13: -.6204
REMARK 3 S21: .8152 S22: -.1878 S23: .9479
REMARK 3 S31: .7276 S32: -.2378 S33: -.1518
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 : A 292 A 339
REMARK 3 ORIGIN FOR THE GROUP (A): 113.1148 55.3180 72.6100
REMARK 3 T TENSOR
REMARK 3 T11: .1230 T22: .1556
REMARK 3 T33: -.0031 T12: -.0506
REMARK 3 T13: -.0277 T23: -.1984
REMARK 3 L TENSOR
REMARK 3 L11: 3.1345 L22: 1.9380
REMARK 3 L33: 2.6985 L12: 1.2458
REMARK 3 L13: -.3781 L23: .3105
REMARK 3 S TENSOR
REMARK 3 S11: -.0400 S12: -.6205 S13: .5809
REMARK 3 S21: .1755 S22: .1017 S23: -.0217
REMARK 3 S31: -.4839 S32: .2532 S33: -.0617
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 : A 374 A 448
REMARK 3 RESIDUE RANGE : A 583 A 597
REMARK 3 ORIGIN FOR THE GROUP (A): 86.8907 33.0914 69.6751
REMARK 3 T TENSOR
REMARK 3 T11: -.0767 T22: .0354
REMARK 3 T33: -.0859 T12: -.0094
REMARK 3 T13: .0292 T23: -.0428
REMARK 3 L TENSOR
REMARK 3 L11: 4.6164 L22: 2.5205
REMARK 3 L33: 2.6283 L12: 1.0598
REMARK 3 L13: -.0167 L23: -.6463
REMARK 3 S TENSOR
REMARK 3 S11: .0839 S12: -.6275 S13: .2565
REMARK 3 S21: .2933 S22: -.0631 S23: .3001
REMARK 3 S31: -.1531 S32: -.2305 S33: -.0208
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 473 A 560
REMARK 3 ORIGIN FOR THE GROUP (A): 110.0662 18.1991 61.1115
REMARK 3 T TENSOR
REMARK 3 T11: -.0396 T22: -.1215
REMARK 3 T33: .0121 T12: -.0016
REMARK 3 T13: -.0057 T23: .0500
REMARK 3 L TENSOR
REMARK 3 L11: 3.2295 L22: 2.3815
REMARK 3 L33: 1.6238 L12: .0838
REMARK 3 L13: -.0466 L23: -.5589
REMARK 3 S TENSOR
REMARK 3 S11: .0510 S12: -.4279 S13: -.4090
REMARK 3 S21: .3076 S22: .0161 S23: -.2214
REMARK 3 S31: .0942 S32: .1789 S33: -.0671
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -2 B 110
REMARK 3 RESIDUE RANGE : B 142 B 291
REMARK 3 RESIDUE RANGE : B 340 B 373
REMARK 3 RESIDUE RANGE : B 449 B 472
REMARK 3 RESIDUE RANGE : B 561 B 582
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5738 18.6618 64.4688
REMARK 3 T TENSOR
REMARK 3 T11: -.1037 T22: -.1594
REMARK 3 T33: -.1673 T12: .0382
REMARK 3 T13: .0115 T23: -.0309
REMARK 3 L TENSOR
REMARK 3 L11: 1.3923 L22: 1.5118
REMARK 3 L33: .7605 L12: -.0565
REMARK 3 L13: .0768 L23: -.1365
REMARK 3 S TENSOR
REMARK 3 S11: .0350 S12: -.0291 S13: -.1126
REMARK 3 S21: .1089 S22: -.0643 S23: .0391
REMARK 3 S31: .0092 S32: -.0247 S33: .0293
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 111 B 141
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6971 23.7111 45.4671
REMARK 3 T TENSOR
REMARK 3 T11: .2152 T22: .2898
REMARK 3 T33: .0688 T12: .0604
REMARK 3 T13: -.0410 T23: -.0525
REMARK 3 L TENSOR
REMARK 3 L11: 5.5430 L22: 2.2792
REMARK 3 L33: 2.7607 L12: -1.4862
REMARK 3 L13: -3.2601 L23: -.3853
REMARK 3 S TENSOR
REMARK 3 S11: .0089 S12: 1.0708 S13: .0359
REMARK 3 S21: -.4896 S22: .0165 S23: -.2951
REMARK 3 S31: .0568 S32: .1808 S33: -.0253
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 292 B 339
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8102 42.6897 52.1192
REMARK 3 T TENSOR
REMARK 3 T11: -.0129 T22: -.0968
REMARK 3 T33: -.1458 T12: .0548
REMARK 3 T13: .0194 T23: .0406
REMARK 3 L TENSOR
REMARK 3 L11: 4.7532 L22: 2.5007
REMARK 3 L33: 1.9410 L12: -1.5976
REMARK 3 L13: 1.0487 L23: -.4453
REMARK 3 S TENSOR
REMARK 3 S11: -.0377 S12: .2402 S13: .2948
REMARK 3 S21: .0269 S22: -.0890 S23: -.0476
REMARK 3 S31: -.2794 S32: .0134 S33: .1267
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 374 B 448
REMARK 3 RESIDUE RANGE : B 583 B 597
REMARK 3 ORIGIN FOR THE GROUP (A): 70.2672 32.1416 52.2720
REMARK 3 T TENSOR
REMARK 3 T11: -.0475 T22: -.0273
REMARK 3 T33: .0019 T12: .0114
REMARK 3 T13: -.0495 T23: .0501
REMARK 3 L TENSOR
REMARK 3 L11: 5.5907 L22: 2.2557
REMARK 3 L33: 2.1834 L12: .1939
REMARK 3 L13: -.8985 L23: .0112
REMARK 3 S TENSOR
REMARK 3 S11: .0047 S12: .4802 S13: .4089
REMARK 3 S21: -.3437 S22: -.0084 S23: .0180
REMARK 3 S31: -.3027 S32: .0384 S33: .0037
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 473 B 560
REMARK 3 ORIGIN FOR THE GROUP (A): 54.8196 7.6608 55.3570
REMARK 3 T TENSOR
REMARK 3 T11: -.0236 T22: -.0704
REMARK 3 T33: .0147 T12: .0651
REMARK 3 T13: .0357 T23: -.0841
REMARK 3 L TENSOR
REMARK 3 L11: 3.3536 L22: 2.4527
REMARK 3 L33: 2.8264 L12: .5018
REMARK 3 L13: -.1270 L23: -.0398
REMARK 3 S TENSOR
REMARK 3 S11: -.0254 S12: .5832 S13: -.3000
REMARK 3 S21: -.4275 S22: .0476 S23: -.2196
REMARK 3 S31: .1057 S32: .1990 S33: -.0222
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 3BE8 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB045409.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89603
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 FOR THE DATA SET : 21.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47000
REMARK 200 FOR SHELL : 4.500
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: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG-3000, 0.1M SODIUM PHOSPHATE
REMARK 280 -CITRATE, 0.3M SODIUM CHLORIDE, 0.01M CALCIUM CHLORIDE, PH
REMARK 280 4.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 69.86500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.02500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 69.86500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.02500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 5290 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASP A -12
REMARK 465 TYR A -11
REMARK 465 LYS A -10
REMARK 465 ASP A -9
REMARK 465 HIS A 160
REMARK 465 ASP A 161
REMARK 465 GLN A 162
REMARK 465 ASN A 163
REMARK 465 GLN A 542
REMARK 465 ASP A 543
REMARK 465 THR A 544
REMARK 465 LYS A 545
REMARK 465 PHE A 546
REMARK 465 ILE A 547
REMARK 465 HIS A 548
REMARK 465 THR A 549
REMARK 465 LYS A 550
REMARK 465 PRO A 551
REMARK 465 ASN A 552
REMARK 465 ARG A 553
REMARK 465 PHE A 554
REMARK 465 GLU A 555
REMARK 465 GLU A 556
REMARK 465 HIS A 598
REMARK 465 ASN A 599
REMARK 465 LEU A 600
REMARK 465 ASN A 601
REMARK 465 GLU A 602
REMARK 465 ILE A 603
REMARK 465 PHE A 604
REMARK 465 GLN A 605
REMARK 465 TYR A 606
REMARK 465 VAL A 607
REMARK 465 SER A 608
REMARK 465 THR A 609
REMARK 465 THR A 610
REMARK 465 THR A 611
REMARK 465 LYS A 612
REMARK 465 VAL A 613
REMARK 465 PRO A 614
REMARK 465 PRO A 615
REMARK 465 PRO A 616
REMARK 465 ASP A 617
REMARK 465 MET A 618
REMARK 465 THR A 619
REMARK 465 ASP B -12
REMARK 465 TYR B -11
REMARK 465 LYS B -10
REMARK 465 ASP B -9
REMARK 465 ASP B -8
REMARK 465 ASP B -7
REMARK 465 ASP B -6
REMARK 465 LYS B -5
REMARK 465 LEU B -4
REMARK 465 ALA B -3
REMARK 465 ASP B 157
REMARK 465 ASP B 158
REMARK 465 ILE B 159
REMARK 465 HIS B 160
REMARK 465 ASP B 161
REMARK 465 GLN B 162
REMARK 465 ASN B 163
REMARK 465 PRO B 541
REMARK 465 GLN B 542
REMARK 465 ASP B 543
REMARK 465 THR B 544
REMARK 465 LYS B 545
REMARK 465 PHE B 546
REMARK 465 ILE B 547
REMARK 465 HIS B 548
REMARK 465 THR B 549
REMARK 465 LYS B 550
REMARK 465 PRO B 551
REMARK 465 ASN B 552
REMARK 465 ARG B 553
REMARK 465 PHE B 554
REMARK 465 GLU B 555
REMARK 465 HIS B 598
REMARK 465 ASN B 599
REMARK 465 LEU B 600
REMARK 465 ASN B 601
REMARK 465 GLU B 602
REMARK 465 ILE B 603
REMARK 465 PHE B 604
REMARK 465 GLN B 605
REMARK 465 TYR B 606
REMARK 465 VAL B 607
REMARK 465 SER B 608
REMARK 465 THR B 609
REMARK 465 THR B 610
REMARK 465 THR B 611
REMARK 465 LYS B 612
REMARK 465 VAL B 613
REMARK 465 PRO B 614
REMARK 465 PRO B 615
REMARK 465 PRO B 616
REMARK 465 ASP B 617
REMARK 465 MET B 618
REMARK 465 THR B 619
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 115 124.30 -38.86
REMARK 500 GLN A 140 32.64 -147.07
REMARK 500 ASP A 141 58.11 -140.32
REMARK 500 CYS A 146 10.38 -142.29
REMARK 500 TYR A 177 -4.95 71.59
REMARK 500 CYS A 306 60.63 -113.44
REMARK 500 ASP A 347 -71.51 -138.84
REMARK 500 ASP A 429 60.29 -166.90
REMARK 500 TRP A 449 -51.38 -123.62
REMARK 500 PRO A 595 10.14 -57.64
REMARK 500 PHE B 128 -75.00 -57.14
REMARK 500 LEU B 132 -71.74 -90.59
REMARK 500 CYS B 146 10.03 -140.31
REMARK 500 TYR B 177 -2.10 75.73
REMARK 500 CYS B 306 68.58 -108.19
REMARK 500 ASP B 347 -75.02 -139.26
REMARK 500 GLU B 411 108.07 -47.68
REMARK 500 ASP B 429 61.68 -155.65
REMARK 500 TRP B 449 -50.40 -121.64
REMARK 500 SER B 509 3.15 84.75
REMARK 500 PRO B 595 -4.43 -57.49
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 PHE B 508 SER B 509 32.13
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 NA A 626 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 62 O
REMARK 620 2 ASN A 64 O 84.0
REMARK 620 3 LEU A 67 O 119.1 87.4
REMARK 620 4 HOH A 854 O 70.2 82.8 165.8
REMARK 620 5 HOH A 790 O 88.1 154.5 75.4 117.1
REMARK 620 6 HOH A 843 O 153.6 99.2 87.4 84.1 98.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 621
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 621
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: FLC BINDING SITE FOR RESIDUE A 622
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: PO4 BINDING SITE FOR RESIDUE A 623
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE A 624
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE A 625
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR RESIDUE A 626
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE A 627
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE B 622
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: FLC BINDING SITE FOR RESIDUE B 623
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: PO4 BINDING SITE FOR RESIDUE B 624
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE B 625
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE B 626
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE A 628
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE B 627
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS IS SPONTANEOUS MUTAGENESIS OF CDNA CLONES.
DBREF 3BE8 A 44 619 UNP Q8N0W4 NLGNX_HUMAN 44 619
DBREF 3BE8 B 44 619 UNP Q8N0W4 NLGNX_HUMAN 44 619
SEQADV 3BE8 ASP A -12 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 TYR A -11 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 LYS A -10 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ASP A -9 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ASP A -8 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ASP A -7 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ASP A -6 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 LYS A -5 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 LEU A -4 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ALA A -3 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ALA A -2 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ALA A -1 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ARG A 561 UNP Q8N0W4 LYS 561 SEE REMARK 999
SEQADV 3BE8 ASP B -12 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 TYR B -11 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 LYS B -10 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ASP B -9 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ASP B -8 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ASP B -7 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ASP B -6 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 LYS B -5 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 LEU B -4 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ALA B -3 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ALA B -2 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ALA B -1 UNP Q8N0W4 EXPRESSION TAG
SEQADV 3BE8 ARG B 561 UNP Q8N0W4 LYS 561 SEE REMARK 999
SEQRES 1 A 588 ASP TYR LYS ASP ASP ASP ASP LYS LEU ALA ALA ALA GLN
SEQRES 2 A 588 TYR PRO VAL VAL ASN THR ASN TYR GLY LYS ILE ARG GLY
SEQRES 3 A 588 LEU ARG THR PRO LEU PRO ASN GLU ILE LEU GLY PRO VAL
SEQRES 4 A 588 GLU GLN TYR LEU GLY VAL PRO TYR ALA SER PRO PRO THR
SEQRES 5 A 588 GLY GLU ARG ARG PHE GLN PRO PRO GLU PRO PRO SER SER
SEQRES 6 A 588 TRP THR GLY ILE ARG ASN THR THR GLN PHE ALA ALA VAL
SEQRES 7 A 588 CYS PRO GLN HIS LEU ASP GLU ARG SER LEU LEU HIS ASP
SEQRES 8 A 588 MET LEU PRO ILE TRP PHE THR ALA ASN LEU ASP THR LEU
SEQRES 9 A 588 MET THR TYR VAL GLN ASP GLN ASN GLU ASP CYS LEU TYR
SEQRES 10 A 588 LEU ASN ILE TYR VAL PRO THR GLU ASP ASP ILE HIS ASP
SEQRES 11 A 588 GLN ASN SER LYS LYS PRO VAL MET VAL TYR ILE HIS GLY
SEQRES 12 A 588 GLY SER TYR MET GLU GLY THR GLY ASN MET ILE ASP GLY
SEQRES 13 A 588 SER ILE LEU ALA SER TYR GLY ASN VAL ILE VAL ILE THR
SEQRES 14 A 588 ILE ASN TYR ARG LEU GLY ILE LEU GLY PHE LEU SER THR
SEQRES 15 A 588 GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU ASP
SEQRES 16 A 588 GLN ILE GLN ALA LEU ARG TRP ILE GLU GLU ASN VAL GLY
SEQRES 17 A 588 ALA PHE GLY GLY ASP PRO LYS ARG VAL THR ILE PHE GLY
SEQRES 18 A 588 SER GLY ALA GLY ALA SER CYS VAL SER LEU LEU THR LEU
SEQRES 19 A 588 SER HIS TYR SER GLU GLY LEU PHE GLN LYS ALA ILE ILE
SEQRES 20 A 588 GLN SER GLY THR ALA LEU SER SER TRP ALA VAL ASN TYR
SEQRES 21 A 588 GLN PRO ALA LYS TYR THR ARG ILE LEU ALA ASP LYS VAL
SEQRES 22 A 588 GLY CYS ASN MET LEU ASP THR THR ASP MET VAL GLU CYS
SEQRES 23 A 588 LEU ARG ASN LYS ASN TYR LYS GLU LEU ILE GLN GLN THR
SEQRES 24 A 588 ILE THR PRO ALA THR TYR HIS ILE ALA PHE GLY PRO VAL
SEQRES 25 A 588 ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU
SEQRES 26 A 588 MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET LEU
SEQRES 27 A 588 GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL ASP GLY
SEQRES 28 A 588 ILE VAL ASP ASN GLU ASP GLY VAL THR PRO ASN ASP PHE
SEQRES 29 A 588 ASP PHE SER VAL SER ASN PHE VAL ASP ASN LEU TYR GLY
SEQRES 30 A 588 TYR PRO GLU GLY LYS ASP THR LEU ARG GLU THR ILE LYS
SEQRES 31 A 588 PHE MET TYR THR ASP TRP ALA ASP LYS GLU ASN PRO GLU
SEQRES 32 A 588 THR ARG ARG LYS THR LEU VAL ALA LEU PHE THR ASP HIS
SEQRES 33 A 588 GLN TRP VAL ALA PRO ALA VAL ALA THR ALA ASP LEU HIS
SEQRES 34 A 588 ALA GLN TYR GLY SER PRO THR TYR PHE TYR ALA PHE TYR
SEQRES 35 A 588 HIS HIS CYS GLN SER GLU MET LYS PRO SER TRP ALA ASP
SEQRES 36 A 588 SER ALA HIS GLY ASP GLU VAL PRO TYR VAL PHE GLY ILE
SEQRES 37 A 588 PRO MET ILE GLY PRO THR GLU LEU PHE SER CYS ASN PHE
SEQRES 38 A 588 SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET THR
SEQRES 39 A 588 TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN GLN
SEQRES 40 A 588 PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS PRO
SEQRES 41 A 588 ASN ARG PHE GLU GLU VAL ALA TRP SER ARG TYR ASN PRO
SEQRES 42 A 588 LYS ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG
SEQRES 43 A 588 VAL ARG ASP HIS TYR ARG ALA THR LYS VAL ALA PHE TRP
SEQRES 44 A 588 LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU ASN GLU ILE
SEQRES 45 A 588 PHE GLN TYR VAL SER THR THR THR LYS VAL PRO PRO PRO
SEQRES 46 A 588 ASP MET THR
SEQRES 1 B 588 ASP TYR LYS ASP ASP ASP ASP LYS LEU ALA ALA ALA GLN
SEQRES 2 B 588 TYR PRO VAL VAL ASN THR ASN TYR GLY LYS ILE ARG GLY
SEQRES 3 B 588 LEU ARG THR PRO LEU PRO ASN GLU ILE LEU GLY PRO VAL
SEQRES 4 B 588 GLU GLN TYR LEU GLY VAL PRO TYR ALA SER PRO PRO THR
SEQRES 5 B 588 GLY GLU ARG ARG PHE GLN PRO PRO GLU PRO PRO SER SER
SEQRES 6 B 588 TRP THR GLY ILE ARG ASN THR THR GLN PHE ALA ALA VAL
SEQRES 7 B 588 CYS PRO GLN HIS LEU ASP GLU ARG SER LEU LEU HIS ASP
SEQRES 8 B 588 MET LEU PRO ILE TRP PHE THR ALA ASN LEU ASP THR LEU
SEQRES 9 B 588 MET THR TYR VAL GLN ASP GLN ASN GLU ASP CYS LEU TYR
SEQRES 10 B 588 LEU ASN ILE TYR VAL PRO THR GLU ASP ASP ILE HIS ASP
SEQRES 11 B 588 GLN ASN SER LYS LYS PRO VAL MET VAL TYR ILE HIS GLY
SEQRES 12 B 588 GLY SER TYR MET GLU GLY THR GLY ASN MET ILE ASP GLY
SEQRES 13 B 588 SER ILE LEU ALA SER TYR GLY ASN VAL ILE VAL ILE THR
SEQRES 14 B 588 ILE ASN TYR ARG LEU GLY ILE LEU GLY PHE LEU SER THR
SEQRES 15 B 588 GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU ASP
SEQRES 16 B 588 GLN ILE GLN ALA LEU ARG TRP ILE GLU GLU ASN VAL GLY
SEQRES 17 B 588 ALA PHE GLY GLY ASP PRO LYS ARG VAL THR ILE PHE GLY
SEQRES 18 B 588 SER GLY ALA GLY ALA SER CYS VAL SER LEU LEU THR LEU
SEQRES 19 B 588 SER HIS TYR SER GLU GLY LEU PHE GLN LYS ALA ILE ILE
SEQRES 20 B 588 GLN SER GLY THR ALA LEU SER SER TRP ALA VAL ASN TYR
SEQRES 21 B 588 GLN PRO ALA LYS TYR THR ARG ILE LEU ALA ASP LYS VAL
SEQRES 22 B 588 GLY CYS ASN MET LEU ASP THR THR ASP MET VAL GLU CYS
SEQRES 23 B 588 LEU ARG ASN LYS ASN TYR LYS GLU LEU ILE GLN GLN THR
SEQRES 24 B 588 ILE THR PRO ALA THR TYR HIS ILE ALA PHE GLY PRO VAL
SEQRES 25 B 588 ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU
SEQRES 26 B 588 MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET LEU
SEQRES 27 B 588 GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL ASP GLY
SEQRES 28 B 588 ILE VAL ASP ASN GLU ASP GLY VAL THR PRO ASN ASP PHE
SEQRES 29 B 588 ASP PHE SER VAL SER ASN PHE VAL ASP ASN LEU TYR GLY
SEQRES 30 B 588 TYR PRO GLU GLY LYS ASP THR LEU ARG GLU THR ILE LYS
SEQRES 31 B 588 PHE MET TYR THR ASP TRP ALA ASP LYS GLU ASN PRO GLU
SEQRES 32 B 588 THR ARG ARG LYS THR LEU VAL ALA LEU PHE THR ASP HIS
SEQRES 33 B 588 GLN TRP VAL ALA PRO ALA VAL ALA THR ALA ASP LEU HIS
SEQRES 34 B 588 ALA GLN TYR GLY SER PRO THR TYR PHE TYR ALA PHE TYR
SEQRES 35 B 588 HIS HIS CYS GLN SER GLU MET LYS PRO SER TRP ALA ASP
SEQRES 36 B 588 SER ALA HIS GLY ASP GLU VAL PRO TYR VAL PHE GLY ILE
SEQRES 37 B 588 PRO MET ILE GLY PRO THR GLU LEU PHE SER CYS ASN PHE
SEQRES 38 B 588 SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET THR
SEQRES 39 B 588 TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN GLN
SEQRES 40 B 588 PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS PRO
SEQRES 41 B 588 ASN ARG PHE GLU GLU VAL ALA TRP SER ARG TYR ASN PRO
SEQRES 42 B 588 LYS ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG
SEQRES 43 B 588 VAL ARG ASP HIS TYR ARG ALA THR LYS VAL ALA PHE TRP
SEQRES 44 B 588 LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU ASN GLU ILE
SEQRES 45 B 588 PHE GLN TYR VAL SER THR THR THR LYS VAL PRO PRO PRO
SEQRES 46 B 588 ASP MET THR
MODRES 3BE8 ASN A 102 ASN GLYCOSYLATION SITE
MODRES 3BE8 ASN A 511 ASN GLYCOSYLATION SITE
MODRES 3BE8 ASN B 102 ASN GLYCOSYLATION SITE
MODRES 3BE8 ASN B 511 ASN GLYCOSYLATION SITE
HET NAG A 620 14
HET NAG A 621 14
HET NAG B 620 14
HET NAG B 621 14
HET FLC A 622 13
HET PO4 A 623 5
HET CL A 624 1
HET CL A 625 1
HET NA A 626 1
HET CL A 627 1
HET CL B 622 1
HET FLC B 623 13
HET PO4 B 624 5
HET CL B 625 1
HET CL B 626 1
HET GOL A 628 6
HET GOL B 627 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FLC CITRATE ANION
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN NAG NAG
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 7 FLC 2(C6 H5 O7 3-)
FORMUL 8 PO4 2(O4 P 3-)
FORMUL 9 CL 6(CL 1-)
FORMUL 11 NA NA 1+
FORMUL 18 GOL 2(C3 H8 O3)
FORMUL 20 HOH *592(H2 O)
HELIX 1 2 THR A 83 ARG A 87 5 5
HELIX 2 3 SER A 118 MET A 123 1 6
HELIX 3 4 TRP A 127 LEU A 135 1 9
HELIX 4 5 LEU A 135 ASP A 141 1 7
HELIX 5 6 THR A 181 ILE A 185 5 5
HELIX 6 7 GLY A 187 ASN A 195 1 9
HELIX 7 8 LEU A 205 LEU A 211 1 7
HELIX 8 9 ASN A 221 VAL A 238 1 18
HELIX 9 10 GLY A 239 PHE A 241 5 3
HELIX 10 11 GLY A 254 THR A 264 1 11
HELIX 11 12 LEU A 265 GLU A 270 5 6
HELIX 12 13 GLN A 292 VAL A 304 1 13
HELIX 13 14 ASP A 310 ASN A 320 1 11
HELIX 14 15 ASN A 322 GLN A 328 1 7
HELIX 15 16 ASP A 352 GLN A 359 1 8
HELIX 16 17 GLY A 360 TYR A 365 5 6
HELIX 17 18 GLY A 376 ASP A 381 5 6
HELIX 18 19 THR A 391 TYR A 407 1 17
HELIX 19 20 GLY A 412 TYR A 424 1 13
HELIX 20 21 ASN A 432 TRP A 449 1 18
HELIX 21 22 TRP A 449 GLN A 462 1 14
HELIX 22 23 GLU A 492 PHE A 497 1 6
HELIX 23 24 GLY A 498 ILE A 502 5 5
HELIX 24 25 SER A 513 GLY A 534 1 22
HELIX 25 26 ARG A 583 GLU A 592 1 10
HELIX 26 27 LEU A 593 LEU A 597 5 5
HELIX 27 28 THR B 83 ARG B 87 5 5
HELIX 28 29 SER B 118 MET B 123 1 6
HELIX 29 30 LEU B 135 GLN B 140 1 6
HELIX 30 31 THR B 181 ILE B 185 5 5
HELIX 31 32 GLY B 187 ASN B 195 1 9
HELIX 32 33 LEU B 205 LEU B 211 1 7
HELIX 33 34 ASN B 221 VAL B 238 1 18
HELIX 34 35 GLY B 239 PHE B 241 5 3
HELIX 35 36 GLY B 254 LEU B 265 1 12
HELIX 36 37 SER B 266 GLU B 270 5 5
HELIX 37 38 GLN B 292 VAL B 304 1 13
HELIX 38 39 ASP B 310 ASN B 320 1 11
HELIX 39 40 ASN B 322 GLN B 328 1 7
HELIX 40 41 ASP B 352 GLY B 360 1 9
HELIX 41 42 GLY B 376 ASP B 381 5 6
HELIX 42 43 THR B 391 TYR B 407 1 17
HELIX 43 44 GLY B 412 TYR B 424 1 13
HELIX 44 45 ASN B 432 TRP B 449 1 18
HELIX 45 46 TRP B 449 GLN B 462 1 14
HELIX 46 47 GLU B 492 PHE B 497 1 6
HELIX 47 48 GLY B 498 ILE B 502 5 5
HELIX 48 49 SER B 513 GLY B 534 1 22
HELIX 49 50 ARG B 583 GLU B 592 1 10
HELIX 50 51 LEU B 593 LEU B 597 5 5
SHEET 1 A 3 VAL A 47 THR A 50 0
SHEET 2 A 3 GLY A 53 ARG A 56 -1 O ILE A 55 N VAL A 48
SHEET 3 A 3 ILE A 100 ASN A 102 1 O ARG A 101 N LYS A 54
SHEET 1 B11 LEU A 58 THR A 60 0
SHEET 2 B11 VAL A 70 PRO A 77 -1 O VAL A 70 N THR A 60
SHEET 3 B11 TYR A 148 PRO A 154 -1 O VAL A 153 N GLU A 71
SHEET 4 B11 ILE A 197 ILE A 201 -1 O THR A 200 N ASN A 150
SHEET 5 B11 LYS A 166 ILE A 172 1 N MET A 169 O ILE A 197
SHEET 6 B11 GLY A 243 SER A 253 1 O THR A 249 N VAL A 170
SHEET 7 B11 LYS A 275 GLN A 279 1 O ILE A 277 N ILE A 250
SHEET 8 B11 ASP A 366 ASN A 372 1 O MET A 368 N ILE A 278
SHEET 9 B11 THR A 467 PHE A 472 1 O PHE A 472 N VAL A 371
SHEET 10 B11 LEU A 568 ILE A 572 1 O ILE A 572 N ALA A 471
SHEET 11 B11 ARG A 577 ASP A 580 -1 O ARG A 577 N HIS A 571
SHEET 1 C 2 GLU A 506 LEU A 507 0
SHEET 2 C 2 CYS A 510 ASN A 511 -1 O CYS A 510 N LEU A 507
SHEET 1 D 3 VAL B 47 THR B 50 0
SHEET 2 D 3 GLY B 53 ARG B 56 -1 O ILE B 55 N VAL B 48
SHEET 3 D 3 ILE B 100 ASN B 102 1 O ARG B 101 N LYS B 54
SHEET 1 E11 LEU B 58 THR B 60 0
SHEET 2 E11 VAL B 70 PRO B 77 -1 O VAL B 70 N THR B 60
SHEET 3 E11 TYR B 148 PRO B 154 -1 O VAL B 153 N GLU B 71
SHEET 4 E11 ILE B 197 ILE B 201 -1 O THR B 200 N ASN B 150
SHEET 5 E11 LYS B 166 ILE B 172 1 N TYR B 171 O ILE B 199
SHEET 6 E11 GLY B 243 SER B 253 1 O PHE B 251 N ILE B 172
SHEET 7 E11 LYS B 275 GLN B 279 1 O LYS B 275 N ILE B 250
SHEET 8 E11 ASP B 366 ASN B 372 1 O MET B 368 N ILE B 278
SHEET 9 E11 THR B 467 PHE B 472 1 O PHE B 472 N VAL B 371
SHEET 10 E11 LEU B 568 ILE B 572 1 O ILE B 572 N ALA B 471
SHEET 11 E11 ARG B 577 ASP B 580 -1 O ARG B 577 N HIS B 571
SSBOND 1 CYS A 110 CYS A 146 1555 1555 2.08
SSBOND 2 CYS A 306 CYS A 317 1555 1555 2.56
SSBOND 3 CYS A 476 CYS A 510 1555 1555 2.04
SSBOND 4 CYS B 110 CYS B 146 1555 1555 2.05
SSBOND 5 CYS B 306 CYS B 317 1555 1555 2.76
SSBOND 6 CYS B 476 CYS B 510 1555 1555 2.05
LINK O LEU A 62 NA NA A 626 1555 1555 2.30
LINK O ASN A 64 NA NA A 626 1555 1555 2.48
LINK O LEU A 67 NA NA A 626 1555 1555 2.42
LINK ND2 ASN A 102 C1 NAG A 620 1555 1555 1.38
LINK ND2 ASN A 511 C1 NAG A 621 1555 1555 1.36
LINK ND2 ASN B 102 C1 NAG B 620 1555 1555 1.36
LINK ND2 ASN B 511 C1 NAG B 621 1555 1555 1.36
LINK NA NA A 626 O HOH A 854 1555 1555 2.74
LINK NA NA A 626 O HOH A 790 1555 1555 2.51
LINK NA NA A 626 O HOH A 843 1555 1555 2.43
CISPEP 1 GLN A 538 PRO A 539 0 1.85
SITE 1 AC1 4 GLN A 477 SER A 478 GLU A 479 ASN A 511
SITE 1 AC2 5 GLN B 477 SER B 478 GLU B 479 SER B 509
SITE 2 AC2 5 ASN B 511
SITE 1 AC3 7 TYR A 473 HIS A 474 HIS A 571 GLY A 573
SITE 2 AC3 7 LEU A 574 LYS A 575 ARG A 577
SITE 1 AC4 9 MET A 123 LEU A 124 PRO A 125 GLY A 174
SITE 2 AC4 9 GLY A 175 SER A 176 GLY A 254 ALA A 255
SITE 3 AC4 9 HIS A 489
SITE 1 AC5 3 SER A 95 HOH A 725 HOH A 757
SITE 1 AC6 5 ARG A 583 THR A 585 LYS A 586 HOH A 848
SITE 2 AC6 5 HOH A 865
SITE 1 AC7 6 LEU A 62 ASN A 64 LEU A 67 HOH A 790
SITE 2 AC7 6 HOH A 843 HOH A 854
SITE 1 AC8 2 TYR A 171 GLY A 174
SITE 1 AC9 3 TYR B 171 GLY B 174 MET B 184
SITE 1 BC1 9 TYR B 473 HIS B 474 HIS B 571 GLY B 573
SITE 2 BC1 9 LEU B 574 LYS B 575 ARG B 577 HOH B 768
SITE 3 BC1 9 HOH B 861
SITE 1 BC2 9 MET B 123 LEU B 124 PRO B 125 GLY B 174
SITE 2 BC2 9 GLY B 175 SER B 176 GLY B 254 ALA B 255
SITE 3 BC2 9 HIS B 489
SITE 1 BC3 2 SER B 95 HOH B 712
SITE 1 BC4 4 ARG B 583 THR B 585 LYS B 586 HOH B 857
SITE 1 BC5 8 SER A 212 GLY A 214 ASP A 215 GLN A 216
SITE 2 BC5 8 ALA A 218 LYS A 219 ASP A 345 HOH A 786
SITE 1 BC6 8 SER B 212 GLY B 214 ASP B 215 GLN B 216
SITE 2 BC6 8 ALA B 218 LYS B 219 ASP B 345 HOH B 767
CRYST1 139.730 154.050 81.300 90.00 90.00 90.00 P 21 21 2 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 0.007157 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012300 0.00000
TER 4346 LEU A 597
TER 8608 LEU B 597
MASTER 626 0 17 50 30 0 27 6 9309 2 128 92
END |