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HEADER CELL ADHESION/CELL ADHESION 01-DEC-07 3BIW
TITLE CRYSTAL STRUCTURE OF THE NEUROLIGIN-1/NEUREXIN-1BETA
TITLE 2 SYNAPTIC ADHESION COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: EXTRACELLULAR ESTERASE DOMAIN OF NEUROLIGIN-1;
COMPND 5 SYNONYM: NEUROLIGIN I;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NEUREXIN-1-BETA;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 FRAGMENT: EXTRACELLULAR LNS DOMAIN OF NEUREXIN-1BETA;
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 GENE: NLGN1;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PACGP67A;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 10 ORGANISM_COMMON: RAT;
SOURCE 11 GENE: NRXN1;
SOURCE 12 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PACGP67A
KEYWDS PROTEIN-PROTEIN COMPLEX, ESTERASE DOMAIN, LNS DOMAIN, ALPHA-
KEYWDS 2 BETA HYDROLASE, ALTERNATIVE SPLICING, CELL ADHESION, CELL
KEYWDS 3 JUNCTION, GLYCOPROTEIN, MEMBRANE, POSTSYNAPTIC CELL
KEYWDS 4 MEMBRANE, SYNAPSE, TRANSMEMBRANE, ALTERNATIVE PROMOTER
KEYWDS 5 USAGE, CELL ADHESION/CELL ADHESION COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.ARAC,A.A.BOUCARD,E.OZKAN,P.STROP,E.NEWELL,T.C.SUDHOF,
AUTHOR 2 A.T.BRUNGER
REVDAT 1 18-DEC-07 3BIW 0
JRNL AUTH D.ARAC,A.A.BOUCARD,E.OZKAN,P.STROP,E.NEWELL,
JRNL AUTH 2 T.C.SUDHOF,A.T.BRUNGER
JRNL TITL STRUCTURES OF NEUROLIGIN-1 AND THE
JRNL TITL 2 NEUROLIGIN-1/NEUREXIN-1BETA COMPLEX REVEAL
JRNL TITL 3 SPECIFIC PROTEIN-PROTEIN AND PROTEIN-CA2+
JRNL TITL 4 INTERACTIONS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3736422.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 49818
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2539
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.72
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7480
REMARK 3 BIN R VALUE (WORKING SET) : 0.3400
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 392
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22180
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 258
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 133.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.24000
REMARK 3 B22 (A**2) : 12.52000
REMARK 3 B33 (A**2) : -4.27000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.49000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM SIGMAA (A) : 0.70
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.53
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.69
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.85
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 26.820; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 41.620; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 27.930; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 40.990; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 67.02
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3BIW COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB045575.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-2007
REMARK 200 TEMPERATURE (KELVIN) : 130.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53484
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.410
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.68800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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 (%): 57.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG6000, 0.1 M MGCL2, 0.1 M MES,
REMARK 280 PH 6.0, 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 114.91500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.39800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 114.91500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 74.39800
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 PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETEROTETRAMER OF TWO
REMARK 300 NEUREXIN-1BETA MOLECULES BOUND TO A NEUROLIGIN-1 DIMER.
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: TETRAMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, F, G
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 ALA A 43
REMARK 465 ASP A 44
REMARK 465 PRO 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 GLU A 163
REMARK 465 ASP A 164
REMARK 465 ASP A 185
REMARK 465 TYR A 445
REMARK 465 PRO A 446
REMARK 465 GLU A 447
REMARK 465 GLY A 448
REMARK 465 LYS A 449
REMARK 465 ASP A 450
REMARK 465 PRO A 577
REMARK 465 GLN A 578
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 ASN A 637
REMARK 465 ASP A 638
REMARK 465 HIS A 639
REMARK 465 HIS A 640
REMARK 465 HIS A 641
REMARK 465 HIS A 642
REMARK 465 HIS A 643
REMARK 465 HIS A 644
REMARK 465 ALA B 43
REMARK 465 ASP B 44
REMARK 465 PRO 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 ASP B 185
REMARK 465 TYR B 445
REMARK 465 PRO B 446
REMARK 465 GLU B 447
REMARK 465 GLY B 448
REMARK 465 LYS B 449
REMARK 465 ASP B 450
REMARK 465 PRO B 577
REMARK 465 GLN B 578
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 ASN B 637
REMARK 465 ASP B 638
REMARK 465 HIS B 639
REMARK 465 HIS B 640
REMARK 465 HIS B 641
REMARK 465 HIS B 642
REMARK 465 HIS B 643
REMARK 465 HIS B 644
REMARK 465 ALA C 43
REMARK 465 ASP C 44
REMARK 465 PRO C 45
REMARK 465 GLN C 46
REMARK 465 LYS C 47
REMARK 465 LEU C 48
REMARK 465 ASP C 49
REMARK 465 ASP C 50
REMARK 465 VAL C 51
REMARK 465 GLU C 163
REMARK 465 ASP C 164
REMARK 465 ASP C 185
REMARK 465 TYR C 445
REMARK 465 PRO C 446
REMARK 465 GLU C 447
REMARK 465 GLY C 448
REMARK 465 LYS C 449
REMARK 465 ASP C 450
REMARK 465 PRO C 577
REMARK 465 GLN C 578
REMARK 465 ASP C 579
REMARK 465 THR C 580
REMARK 465 LYS C 581
REMARK 465 PHE C 582
REMARK 465 ILE C 583
REMARK 465 HIS C 584
REMARK 465 THR C 585
REMARK 465 LYS C 586
REMARK 465 PRO C 587
REMARK 465 ASN C 588
REMARK 465 ARG C 589
REMARK 465 PHE C 590
REMARK 465 GLU C 591
REMARK 465 ASN C 637
REMARK 465 ASP C 638
REMARK 465 HIS C 639
REMARK 465 HIS C 640
REMARK 465 HIS C 641
REMARK 465 HIS C 642
REMARK 465 HIS C 643
REMARK 465 HIS C 644
REMARK 465 ALA D 43
REMARK 465 ASP D 44
REMARK 465 PRO D 45
REMARK 465 GLN D 46
REMARK 465 LYS D 47
REMARK 465 LEU D 48
REMARK 465 ASP D 49
REMARK 465 ASP D 50
REMARK 465 VAL D 51
REMARK 465 GLU D 163
REMARK 465 ASP D 164
REMARK 465 ASP D 185
REMARK 465 TYR D 445
REMARK 465 PRO D 446
REMARK 465 GLU D 447
REMARK 465 GLY D 448
REMARK 465 LYS D 449
REMARK 465 ASP D 450
REMARK 465 PRO D 577
REMARK 465 GLN D 578
REMARK 465 ASP D 579
REMARK 465 THR D 580
REMARK 465 LYS D 581
REMARK 465 PHE D 582
REMARK 465 ILE D 583
REMARK 465 HIS D 584
REMARK 465 THR D 585
REMARK 465 LYS D 586
REMARK 465 PRO D 587
REMARK 465 ASN D 588
REMARK 465 ARG D 589
REMARK 465 PHE D 590
REMARK 465 GLU D 591
REMARK 465 ASN D 637
REMARK 465 ASP D 638
REMARK 465 HIS D 639
REMARK 465 HIS D 640
REMARK 465 HIS D 641
REMARK 465 HIS D 642
REMARK 465 HIS D 643
REMARK 465 HIS D 644
REMARK 465 GLY E 33
REMARK 465 SER E 34
REMARK 465 PRO E 35
REMARK 465 GLY E 36
REMARK 465 ILE E 37
REMARK 465 SER E 38
REMARK 465 GLY E 39
REMARK 465 GLY E 40
REMARK 465 GLY E 41
REMARK 465 GLY E 42
REMARK 465 GLY E 43
REMARK 465 ILE E 44
REMARK 465 LEU E 45
REMARK 465 GLU E 46
REMARK 465 ALA E 47
REMARK 465 SER E 48
REMARK 465 SER E 49
REMARK 465 LEU E 50
REMARK 465 GLY E 51
REMARK 465 ALA E 52
REMARK 465 HIS E 53
REMARK 465 HIS E 54
REMARK 465 ILE E 55
REMARK 465 HIS E 56
REMARK 465 HIS E 57
REMARK 465 PHE E 58
REMARK 465 HIS E 59
REMARK 465 GLY E 60
REMARK 465 SER E 61
REMARK 465 SER E 62
REMARK 465 LYS E 63
REMARK 465 HIS E 64
REMARK 465 HIS E 65
REMARK 465 SER E 66
REMARK 465 VAL E 67
REMARK 465 PRO E 68
REMARK 465 ILE E 69
REMARK 465 ALA E 70
REMARK 465 ILE E 71
REMARK 465 TYR E 72
REMARK 465 ARG E 73
REMARK 465 SER E 74
REMARK 465 PRO E 75
REMARK 465 ALA E 76
REMARK 465 SER E 77
REMARK 465 LEU E 78
REMARK 465 ARG E 79
REMARK 465 GLY E 80
REMARK 465 GLY E 81
REMARK 465 GLY E 289
REMARK 465 GLU E 290
REMARK 465 VAL E 291
REMARK 465 PRO E 292
REMARK 465 SER E 293
REMARK 465 SER E 294
REMARK 465 MET E 295
REMARK 465 THR E 296
REMARK 465 THR E 297
REMARK 465 GLU E 298
REMARK 465 SER E 299
REMARK 465 HIS E 300
REMARK 465 HIS E 301
REMARK 465 HIS E 302
REMARK 465 HIS E 303
REMARK 465 HIS E 304
REMARK 465 HIS E 305
REMARK 465 GLY F 33
REMARK 465 SER F 34
REMARK 465 PRO F 35
REMARK 465 GLY F 36
REMARK 465 ILE F 37
REMARK 465 SER F 38
REMARK 465 GLY F 39
REMARK 465 GLY F 40
REMARK 465 GLY F 41
REMARK 465 GLY F 42
REMARK 465 GLY F 43
REMARK 465 ILE F 44
REMARK 465 LEU F 45
REMARK 465 GLU F 46
REMARK 465 ALA F 47
REMARK 465 SER F 48
REMARK 465 SER F 49
REMARK 465 LEU F 50
REMARK 465 GLY F 51
REMARK 465 ALA F 52
REMARK 465 HIS F 53
REMARK 465 HIS F 54
REMARK 465 ILE F 55
REMARK 465 HIS F 56
REMARK 465 HIS F 57
REMARK 465 PHE F 58
REMARK 465 HIS F 59
REMARK 465 GLY F 60
REMARK 465 SER F 61
REMARK 465 SER F 62
REMARK 465 LYS F 63
REMARK 465 HIS F 64
REMARK 465 HIS F 65
REMARK 465 SER F 66
REMARK 465 VAL F 67
REMARK 465 PRO F 68
REMARK 465 ILE F 69
REMARK 465 ALA F 70
REMARK 465 ILE F 71
REMARK 465 TYR F 72
REMARK 465 ARG F 73
REMARK 465 SER F 74
REMARK 465 PRO F 75
REMARK 465 ALA F 76
REMARK 465 SER F 77
REMARK 465 LEU F 78
REMARK 465 ARG F 79
REMARK 465 GLY F 80
REMARK 465 GLY F 81
REMARK 465 GLY F 289
REMARK 465 GLU F 290
REMARK 465 VAL F 291
REMARK 465 PRO F 292
REMARK 465 SER F 293
REMARK 465 SER F 294
REMARK 465 MET F 295
REMARK 465 THR F 296
REMARK 465 THR F 297
REMARK 465 GLU F 298
REMARK 465 SER F 299
REMARK 465 HIS F 300
REMARK 465 HIS F 301
REMARK 465 HIS F 302
REMARK 465 HIS F 303
REMARK 465 HIS F 304
REMARK 465 HIS F 305
REMARK 465 GLY G 33
REMARK 465 SER G 34
REMARK 465 PRO G 35
REMARK 465 GLY G 36
REMARK 465 ILE G 37
REMARK 465 SER G 38
REMARK 465 GLY G 39
REMARK 465 GLY G 40
REMARK 465 GLY G 41
REMARK 465 GLY G 42
REMARK 465 GLY G 43
REMARK 465 ILE G 44
REMARK 465 LEU G 45
REMARK 465 GLU G 46
REMARK 465 ALA G 47
REMARK 465 SER G 48
REMARK 465 SER G 49
REMARK 465 LEU G 50
REMARK 465 GLY G 51
REMARK 465 ALA G 52
REMARK 465 HIS G 53
REMARK 465 HIS G 54
REMARK 465 ILE G 55
REMARK 465 HIS G 56
REMARK 465 HIS G 57
REMARK 465 PHE G 58
REMARK 465 HIS G 59
REMARK 465 GLY G 60
REMARK 465 SER G 61
REMARK 465 SER G 62
REMARK 465 LYS G 63
REMARK 465 HIS G 64
REMARK 465 HIS G 65
REMARK 465 SER G 66
REMARK 465 VAL G 67
REMARK 465 PRO G 68
REMARK 465 ILE G 69
REMARK 465 ALA G 70
REMARK 465 ILE G 71
REMARK 465 TYR G 72
REMARK 465 ARG G 73
REMARK 465 SER G 74
REMARK 465 PRO G 75
REMARK 465 ALA G 76
REMARK 465 SER G 77
REMARK 465 LEU G 78
REMARK 465 ARG G 79
REMARK 465 GLY G 80
REMARK 465 GLY G 81
REMARK 465 GLY G 289
REMARK 465 GLU G 290
REMARK 465 VAL G 291
REMARK 465 PRO G 292
REMARK 465 SER G 293
REMARK 465 SER G 294
REMARK 465 MET G 295
REMARK 465 THR G 296
REMARK 465 THR G 297
REMARK 465 GLU G 298
REMARK 465 SER G 299
REMARK 465 HIS G 300
REMARK 465 HIS G 301
REMARK 465 HIS G 302
REMARK 465 HIS G 303
REMARK 465 HIS G 304
REMARK 465 HIS G 305
REMARK 465 GLY H 33
REMARK 465 SER H 34
REMARK 465 PRO H 35
REMARK 465 GLY H 36
REMARK 465 ILE H 37
REMARK 465 SER H 38
REMARK 465 GLY H 39
REMARK 465 GLY H 40
REMARK 465 GLY H 41
REMARK 465 GLY H 42
REMARK 465 GLY H 43
REMARK 465 ILE H 44
REMARK 465 LEU H 45
REMARK 465 GLU H 46
REMARK 465 ALA H 47
REMARK 465 SER H 48
REMARK 465 SER H 49
REMARK 465 LEU H 50
REMARK 465 GLY H 51
REMARK 465 ALA H 52
REMARK 465 HIS H 53
REMARK 465 HIS H 54
REMARK 465 ILE H 55
REMARK 465 HIS H 56
REMARK 465 HIS H 57
REMARK 465 PHE H 58
REMARK 465 HIS H 59
REMARK 465 GLY H 60
REMARK 465 SER H 61
REMARK 465 SER H 62
REMARK 465 LYS H 63
REMARK 465 HIS H 64
REMARK 465 HIS H 65
REMARK 465 SER H 66
REMARK 465 VAL H 67
REMARK 465 PRO H 68
REMARK 465 ILE H 69
REMARK 465 ALA H 70
REMARK 465 ILE H 71
REMARK 465 TYR H 72
REMARK 465 ARG H 73
REMARK 465 SER H 74
REMARK 465 PRO H 75
REMARK 465 ALA H 76
REMARK 465 SER H 77
REMARK 465 LEU H 78
REMARK 465 ARG H 79
REMARK 465 GLY H 80
REMARK 465 GLY H 81
REMARK 465 GLY H 289
REMARK 465 GLU H 290
REMARK 465 VAL H 291
REMARK 465 PRO H 292
REMARK 465 SER H 293
REMARK 465 SER H 294
REMARK 465 MET H 295
REMARK 465 THR H 296
REMARK 465 THR H 297
REMARK 465 GLU H 298
REMARK 465 SER H 299
REMARK 465 HIS H 300
REMARK 465 HIS H 301
REMARK 465 HIS H 302
REMARK 465 HIS H 303
REMARK 465 HIS H 304
REMARK 465 HIS H 305
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 O4 NAG E 306 C1 NAG E 307 1.40
REMARK 500 O4 NAG G 306 C1 NAG G 307 1.41
REMARK 500 O4 NAG F 306 C1 NAG F 307 1.41
REMARK 500 ND2 ASN G 184 C1 NAG G 306 1.45
REMARK 500 ND2 ASN D 547 C1 NAG D 703 1.45
REMARK 500 ND2 ASN F 184 C1 NAG F 306 1.45
REMARK 500 ND2 ASN D 109 C1 NAG D 701 1.46
REMARK 500 ND2 ASN D 343 C1 NAG D 702 1.46
REMARK 500 ND2 ASN E 184 C1 NAG E 306 1.46
REMARK 500 ND2 ASN C 547 C1 NAG C 703 1.46
REMARK 500 ND2 ASN B 547 C1 NAG B 703 1.46
REMARK 500 ND2 ASN A 547 C1 NAG A 703 1.46
REMARK 500 ND2 ASN B 343 C1 NAG B 702 1.47
REMARK 500 ND2 ASN A 343 C1 NAG A 702 1.47
REMARK 500 ND2 ASN C 109 C1 NAG C 701 1.47
REMARK 500 ND2 ASN A 109 C1 NAG A 701 1.47
REMARK 500 ND2 ASN C 343 C1 NAG C 702 1.47
REMARK 500 ND2 ASN B 109 C1 NAG B 701 1.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE1 TRP E 192 NE1 TRP E 192 2556 1.74
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 ASN A 70 27.26 -65.00
REMARK 500 ASP A 106 -146.28 -53.82
REMARK 500 ALA A 110 72.10 -113.34
REMARK 500 PRO A 115 150.27 -49.42
REMARK 500 ILE A 122 -77.22 -35.27
REMARK 500 ASP A 123 83.46 -59.76
REMARK 500 PRO A 127 83.76 -60.66
REMARK 500 GLU A 128 -50.89 -29.78
REMARK 500 ASN A 137 32.32 -68.63
REMARK 500 ASN A 138 32.63 -178.00
REMARK 500 ASP A 140 -78.99 -55.29
REMARK 500 SER A 144 29.58 -71.06
REMARK 500 TYR A 145 -51.28 -131.85
REMARK 500 SER A 150 145.12 179.02
REMARK 500 LEU A 154 80.54 -62.89
REMARK 500 SER A 203 10.38 -147.32
REMARK 500 TYR A 204 -7.71 87.93
REMARK 500 THR A 208 128.18 179.26
REMARK 500 SER A 219 -73.41 -66.85
REMARK 500 ASN A 222 47.60 76.52
REMARK 500 LEU A 232 -167.15 -111.21
REMARK 500 ASP A 242 -151.57 -119.50
REMARK 500 PRO A 272 0.79 -60.76
REMARK 500 ARG A 274 54.51 -144.39
REMARK 500 CYS A 342 -5.91 -164.82
REMARK 500 ASN A 343 62.88 -58.26
REMARK 500 LYS A 357 142.35 -36.52
REMARK 500 GLN A 365 -159.61 -64.28
REMARK 500 ASP A 366 73.67 -154.56
REMARK 500 ASP A 383 -72.04 -115.88
REMARK 500 ASP A 465 39.69 176.11
REMARK 500 ARG A 466 12.15 -58.00
REMARK 500 TRP A 485 -64.14 -126.03
REMARK 500 ASN A 498 -6.33 -52.03
REMARK 500 TYR A 509 67.86 -116.73
REMARK 500 HIS A 510 129.21 -176.28
REMARK 500 THR A 514 -166.12 -116.43
REMARK 500 PRO A 518 160.28 -48.43
REMARK 500 ALA A 523 108.88 -50.85
REMARK 500 PRO A 540 147.22 -39.87
REMARK 500 CYS A 546 138.46 -28.50
REMARK 500 ARG A 613 141.03 -171.50
REMARK 500 HIS A 617 70.59 47.74
REMARK 500 ARG A 619 36.46 35.23
REMARK 500 HIS A 634 11.13 -63.56
REMARK 500 ASN B 70 27.09 -65.33
REMARK 500 ASP B 106 -146.04 -53.89
REMARK 500 ALA B 110 72.22 -112.44
REMARK 500 PRO B 115 150.61 -49.43
REMARK 500 ILE B 122 -77.37 -35.05
REMARK 500 ASP B 123 84.11 -59.83
REMARK 500 PRO B 127 83.20 -59.87
REMARK 500 GLU B 128 -51.25 -28.77
REMARK 500 ASN B 137 32.77 -67.86
REMARK 500 ASN B 138 31.75 -178.33
REMARK 500 ASP B 140 -78.63 -55.56
REMARK 500 SER B 144 30.41 -71.41
REMARK 500 TYR B 145 -51.03 -132.03
REMARK 500 SER B 150 143.61 178.95
REMARK 500 LEU B 154 79.68 -61.84
REMARK 500 SER B 203 10.81 -146.82
REMARK 500 TYR B 204 -8.32 87.57
REMARK 500 THR B 208 127.70 178.70
REMARK 500 SER B 219 -72.60 -67.81
REMARK 500 ASN B 222 48.13 75.73
REMARK 500 LEU B 232 -167.29 -111.71
REMARK 500 ASP B 242 -151.14 -119.70
REMARK 500 PRO B 272 -0.24 -59.92
REMARK 500 ARG B 274 55.61 -143.39
REMARK 500 CYS B 342 -5.48 -165.13
REMARK 500 ASN B 343 62.87 -59.06
REMARK 500 LYS B 357 142.45 -35.69
REMARK 500 GLN B 365 -159.19 -65.09
REMARK 500 ASP B 366 73.59 -154.55
REMARK 500 ASP B 383 -71.82 -115.72
REMARK 500 ASP B 465 39.76 176.15
REMARK 500 ARG B 466 12.12 -58.64
REMARK 500 TRP B 485 -63.99 -126.45
REMARK 500 ASN B 498 -6.54 -52.61
REMARK 500 TYR B 509 67.62 -116.37
REMARK 500 HIS B 510 128.45 -175.79
REMARK 500 THR B 514 -165.90 -116.80
REMARK 500 PRO B 518 159.99 -48.54
REMARK 500 ALA B 523 108.78 -50.65
REMARK 500 CYS B 546 138.06 -27.90
REMARK 500 ARG B 613 141.51 -171.08
REMARK 500 HIS B 617 70.78 46.74
REMARK 500 ARG B 619 36.79 35.47
REMARK 500 HIS B 634 10.95 -63.16
REMARK 500 ASN C 70 26.78 -65.57
REMARK 500 ASP C 106 -146.14 -54.35
REMARK 500 ALA C 110 72.40 -113.45
REMARK 500 ILE C 122 -77.63 -35.52
REMARK 500 ASP C 123 83.37 -59.23
REMARK 500 PRO C 127 83.57 -60.31
REMARK 500 GLU C 128 -51.47 -29.00
REMARK 500 ASN C 137 32.37 -68.77
REMARK 500 ASN C 138 32.04 -178.30
REMARK 500 ASP C 140 -78.89 -55.06
REMARK 500 SER C 144 29.47 -70.98
REMARK 500 TYR C 145 -51.25 -131.74
REMARK 500 SER C 150 143.63 178.71
REMARK 500 LEU C 154 80.01 -62.83
REMARK 500 SER C 203 10.78 -147.23
REMARK 500 TYR C 204 -7.74 87.11
REMARK 500 THR C 208 128.44 178.77
REMARK 500 SER C 219 -72.63 -67.69
REMARK 500 ASN C 222 47.98 76.28
REMARK 500 LEU C 232 -167.33 -112.14
REMARK 500 ASP C 242 -151.46 -119.70
REMARK 500 PRO C 272 0.50 -60.13
REMARK 500 ARG C 274 54.30 -144.30
REMARK 500 CYS C 342 -6.16 -165.03
REMARK 500 ASN C 343 62.59 -58.06
REMARK 500 LYS C 357 141.89 -36.26
REMARK 500 GLN C 365 -160.07 -64.55
REMARK 500 ASP C 366 74.24 -153.80
REMARK 500 ASP C 383 -71.51 -117.24
REMARK 500 ASP C 421 168.34 -49.77
REMARK 500 ASP C 465 39.75 175.31
REMARK 500 ARG C 466 12.32 -58.51
REMARK 500 TRP C 485 -64.05 -125.29
REMARK 500 ASN C 498 -7.40 -52.01
REMARK 500 TYR C 509 68.22 -116.29
REMARK 500 HIS C 510 128.68 -176.29
REMARK 500 THR C 514 -166.25 -116.61
REMARK 500 PRO C 518 160.50 -48.41
REMARK 500 ALA C 523 108.62 -50.24
REMARK 500 CYS C 546 138.31 -27.83
REMARK 500 ARG C 613 141.08 -171.98
REMARK 500 HIS C 617 70.27 48.38
REMARK 500 ARG C 619 35.86 34.00
REMARK 500 ALA C 620 -39.87 -35.67
REMARK 500 HIS C 634 11.36 -63.30
REMARK 500 ASN D 70 25.60 -64.77
REMARK 500 ASP D 106 -146.44 -54.04
REMARK 500 ALA D 110 71.97 -113.08
REMARK 500 ILE D 122 -77.78 -35.59
REMARK 500 ASP D 123 83.81 -59.39
REMARK 500 PRO D 127 82.83 -59.77
REMARK 500 GLU D 128 -51.80 -28.35
REMARK 500 ASN D 137 32.34 -70.26
REMARK 500 ASN D 138 32.33 -178.02
REMARK 500 ASP D 140 -79.19 -54.84
REMARK 500 SER D 144 29.70 -71.27
REMARK 500 TYR D 145 -49.64 -131.66
REMARK 500 SER D 150 144.04 179.45
REMARK 500 LEU D 154 79.65 -62.48
REMARK 500 SER D 203 10.59 -147.95
REMARK 500 TYR D 204 -7.90 86.82
REMARK 500 THR D 208 128.55 178.98
REMARK 500 SER D 219 -72.70 -67.18
REMARK 500 ASN D 222 48.12 75.36
REMARK 500 LEU D 232 -167.15 -111.13
REMARK 500 ASP D 242 -151.45 -118.94
REMARK 500 PRO D 272 0.71 -60.24
REMARK 500 ARG D 274 54.80 -143.71
REMARK 500 CYS D 342 -6.00 -165.61
REMARK 500 ASN D 343 63.22 -59.12
REMARK 500 LYS D 357 142.34 -35.62
REMARK 500 GLN D 365 -160.18 -64.89
REMARK 500 ASP D 366 74.48 -153.65
REMARK 500 ASP D 383 -70.43 -116.83
REMARK 500 ASP D 421 168.24 -49.58
REMARK 500 ASP D 465 39.49 177.47
REMARK 500 ARG D 466 11.90 -58.28
REMARK 500 TRP D 485 -63.68 -126.00
REMARK 500 ASN D 498 -7.08 -52.89
REMARK 500 TYR D 509 67.69 -116.01
REMARK 500 HIS D 510 128.60 -175.95
REMARK 500 THR D 514 -166.08 -116.41
REMARK 500 PRO D 518 160.58 -48.80
REMARK 500 ALA D 523 108.24 -50.23
REMARK 500 PRO D 540 147.38 -39.21
REMARK 500 CYS D 546 138.13 -28.91
REMARK 500 ARG D 613 140.52 -171.54
REMARK 500 HIS D 617 71.83 48.09
REMARK 500 ARG D 619 36.06 33.53
REMARK 500 HIS D 634 8.30 -61.59
REMARK 500 GLN E 95 118.00 -169.56
REMARK 500 PRO E 102 -78.07 -10.75
REMARK 500 ASN E 103 25.90 -66.87
REMARK 500 SER E 118 114.90 -172.94
REMARK 500 ALA E 124 144.78 174.17
REMARK 500 SER E 132 129.24 -25.67
REMARK 500 SER E 133 130.69 -29.04
REMARK 500 ASP E 137 143.53 -24.27
REMARK 500 THR E 156 -109.65 -93.02
REMARK 500 ASN E 165 -73.69 -76.08
REMARK 500 ASN E 169 32.28 -91.21
REMARK 500 SER E 181 79.88 -151.63
REMARK 500 ASP E 190 -104.63 41.52
REMARK 500 PRO E 199 152.47 -25.93
REMARK 500 ALA E 200 -135.08 -46.89
REMARK 500 SER E 239 79.71 25.73
REMARK 500 GLN E 252 60.86 -162.04
REMARK 500 ASN E 264 51.59 39.29
REMARK 500 LYS E 267 66.30 -101.39
REMARK 500 GLU E 274 25.98 -79.36
REMARK 500 ASN E 275 75.44 42.13
REMARK 500 ASN E 284 42.90 -87.72
REMARK 500 GLN F 95 117.86 -169.43
REMARK 500 PRO F 102 -77.59 -11.60
REMARK 500 ASN F 103 26.03 -67.25
REMARK 500 SER F 118 115.05 -172.22
REMARK 500 ALA F 124 145.79 174.67
REMARK 500 SER F 132 130.00 -26.38
REMARK 500 SER F 133 131.06 -29.88
REMARK 500 ASP F 137 143.58 -24.14
REMARK 500 THR F 156 -109.76 -92.96
REMARK 500 ASN F 165 -72.58 -77.08
REMARK 500 ASN F 169 31.97 -90.85
REMARK 500 SER F 181 80.59 -150.57
REMARK 500 ASP F 190 -105.48 41.40
REMARK 500 PRO F 199 152.79 -25.93
REMARK 500 ALA F 200 -134.77 -46.62
REMARK 500 SER F 239 79.39 25.92
REMARK 500 GLN F 252 61.83 -162.00
REMARK 500 ASN F 264 51.52 38.73
REMARK 500 LYS F 267 65.98 -100.76
REMARK 500 GLU F 274 26.91 -79.58
REMARK 500 ASN F 275 75.55 41.55
REMARK 500 ASN F 284 42.00 -88.03
REMARK 500 GLN G 95 118.09 -170.42
REMARK 500 PRO G 102 -76.75 -11.70
REMARK 500 ASN G 103 25.93 -67.71
REMARK 500 SER G 118 115.85 -171.92
REMARK 500 ALA G 124 145.96 173.92
REMARK 500 SER G 132 129.64 -26.34
REMARK 500 SER G 133 130.20 -29.38
REMARK 500 ASP G 137 143.30 -23.99
REMARK 500 THR G 156 -108.99 -92.67
REMARK 500 ASN G 165 -73.62 -76.17
REMARK 500 ASN G 169 31.68 -91.15
REMARK 500 SER G 181 80.03 -150.73
REMARK 500 ASP G 190 -104.73 41.62
REMARK 500 PRO G 199 153.11 -26.56
REMARK 500 ALA G 200 -133.64 -47.57
REMARK 500 SER G 239 79.86 25.73
REMARK 500 GLN G 252 60.88 -161.56
REMARK 500 ASN G 264 51.26 37.81
REMARK 500 LYS G 267 66.79 -100.75
REMARK 500 GLU G 274 26.09 -78.98
REMARK 500 ASN G 275 75.74 41.92
REMARK 500 ASN G 284 42.74 -87.17
REMARK 500 GLN H 95 118.66 -170.61
REMARK 500 PRO H 102 -76.73 -11.98
REMARK 500 ASN H 103 25.63 -67.96
REMARK 500 SER H 118 114.66 -172.80
REMARK 500 ALA H 124 145.11 173.68
REMARK 500 SER H 132 129.98 -26.44
REMARK 500 SER H 133 131.09 -29.44
REMARK 500 ASP H 137 143.74 -24.24
REMARK 500 THR H 156 -110.22 -91.70
REMARK 500 ASN H 165 -72.55 -76.77
REMARK 500 ASN H 169 32.49 -91.49
REMARK 500 ASP H 190 -104.92 42.02
REMARK 500 PRO H 199 153.56 -26.60
REMARK 500 ALA H 200 -133.90 -48.67
REMARK 500 SER H 239 79.06 24.66
REMARK 500 GLN H 252 60.69 -161.52
REMARK 500 ASN H 264 51.62 39.02
REMARK 500 LYS H 267 66.34 -100.51
REMARK 500 GLU H 274 25.86 -79.45
REMARK 500 ASN H 275 75.78 41.94
REMARK 500 ASN H 284 42.94 -88.06
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 E 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 137 OD1
REMARK 620 2 ASP E 137 OD2 46.6
REMARK 620 3 VAL E 154 O 57.7 96.7
REMARK 620 4 ILE E 236 O 102.7 81.1 86.5
REMARK 620 5 ASN E 238 OD1 113.4 67.4 154.0 71.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 137 OD2
REMARK 620 2 VAL F 154 O 92.1
REMARK 620 3 ILE F 236 O 77.0 85.9
REMARK 620 4 ASN F 238 OD1 63.8 148.7 70.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 137 OD1
REMARK 620 2 ASP G 137 OD2 46.6
REMARK 620 3 VAL G 154 O 58.6 97.8
REMARK 620 4 ILE G 236 O 102.6 81.3 86.5
REMARK 620 5 ASN G 238 OD1 112.3 66.4 154.1 71.4
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BIX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NEUROLIGIN-1
DBREF 3BIW A 46 164 UNP Q62765 NLGN1_RAT 46 164
DBREF 3BIW A 185 297 UNP Q62765 NLGN1_RAT 185 297
DBREF 3BIW A 306 638 UNP Q62765 NLGN1_RAT 306 638
DBREF 3BIW B 46 164 UNP Q62765 NLGN1_RAT 46 164
DBREF 3BIW B 185 297 UNP Q62765 NLGN1_RAT 185 297
DBREF 3BIW B 306 638 UNP Q62765 NLGN1_RAT 306 638
DBREF 3BIW C 46 164 UNP Q62765 NLGN1_RAT 46 164
DBREF 3BIW C 185 297 UNP Q62765 NLGN1_RAT 185 297
DBREF 3BIW C 306 638 UNP Q62765 NLGN1_RAT 306 638
DBREF 3BIW D 46 164 UNP Q62765 NLGN1_RAT 46 164
DBREF 3BIW D 185 297 UNP Q62765 NLGN1_RAT 185 297
DBREF 3BIW D 306 638 UNP Q62765 NLGN1_RAT 306 638
DBREF 3BIW E 47 231 UNP Q63373 NRX1B_RAT 47 201
DBREF 3BIW E 232 299 UNP Q63373 NRX1B_RAT 232 299
DBREF 3BIW F 47 231 UNP Q63373 NRX1B_RAT 47 201
DBREF 3BIW F 232 299 UNP Q63373 NRX1B_RAT 232 299
DBREF 3BIW G 47 231 UNP Q63373 NRX1B_RAT 47 201
DBREF 3BIW G 232 299 UNP Q63373 NRX1B_RAT 232 299
DBREF 3BIW H 47 231 UNP Q63373 NRX1B_RAT 47 201
DBREF 3BIW H 232 299 UNP Q63373 NRX1B_RAT 232 299
SEQADV 3BIW ALA A 43 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW ASP A 44 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW PRO A 45 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS A 639 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS A 640 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS A 641 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS A 642 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS A 643 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS A 644 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW ALA B 43 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW ASP B 44 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW PRO B 45 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS B 639 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS B 640 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS B 641 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS B 642 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS B 643 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS B 644 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW ALA C 43 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW ASP C 44 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW PRO C 45 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS C 639 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS C 640 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS C 641 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS C 642 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS C 643 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS C 644 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW ALA D 43 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW ASP D 44 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW PRO D 45 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS D 639 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS D 640 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS D 641 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS D 642 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS D 643 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW HIS D 644 UNP Q62765 EXPRESSION TAG
SEQADV 3BIW GLY E 33 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW SER E 34 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW PRO E 35 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY E 36 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW ILE E 37 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW SER E 38 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY E 39 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY E 40 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY E 41 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY E 42 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY E 43 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW ILE E 44 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW LEU E 45 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLU E 46 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS E 300 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS E 301 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS E 302 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS E 303 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS E 304 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS E 305 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY F 33 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW SER F 34 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW PRO F 35 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY F 36 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW ILE F 37 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW SER F 38 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY F 39 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY F 40 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY F 41 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY F 42 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY F 43 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW ILE F 44 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW LEU F 45 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLU F 46 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS F 300 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS F 301 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS F 302 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS F 303 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS F 304 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS F 305 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY G 33 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW SER G 34 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW PRO G 35 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY G 36 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW ILE G 37 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW SER G 38 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY G 39 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY G 40 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY G 41 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY G 42 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY G 43 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW ILE G 44 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW LEU G 45 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLU G 46 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS G 300 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS G 301 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS G 302 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS G 303 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS G 304 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS G 305 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY H 33 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW SER H 34 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW PRO H 35 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY H 36 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW ILE H 37 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW SER H 38 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY H 39 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY H 40 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY H 41 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY H 42 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLY H 43 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW ILE H 44 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW LEU H 45 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW GLU H 46 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS H 300 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS H 301 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS H 302 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS H 303 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS H 304 UNP Q63373 EXPRESSION TAG
SEQADV 3BIW HIS H 305 UNP Q63373 EXPRESSION TAG
SEQRES 1 A 574 ALA ASP PRO GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL
SEQRES 2 A 574 THR THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU
SEQRES 3 A 574 LEU ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU
SEQRES 4 A 574 GLY VAL PRO TYR ALA ALA PRO PRO THR GLY GLU HIS ARG
SEQRES 5 A 574 PHE GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE
SEQRES 6 A 574 ARG ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN
SEQRES 7 A 574 ILE ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL
SEQRES 8 A 574 TRP PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL
SEQRES 9 A 574 GLN ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 10 A 574 VAL PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO
SEQRES 11 A 574 LYS PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET
SEQRES 12 A 574 GLU GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA
SEQRES 13 A 574 SER TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG
SEQRES 14 A 574 LEU GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA
SEQRES 15 A 574 ALA LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA
SEQRES 16 A 574 LEU ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY
SEQRES 17 A 574 ASP PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY
SEQRES 18 A 574 GLY SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER
SEQRES 19 A 574 GLU LYS GLY LEU PHE GLN ARG ALA ILE ALA GLN SER GLY
SEQRES 20 A 574 THR ALA LEU SER SER TRP ALA VAL SER PHE GLN PRO ALA
SEQRES 21 A 574 LYS TYR ALA ARG ILE LEU ALA THR LYS VAL GLY CYS ASN
SEQRES 22 A 574 VAL SER ASP THR VAL GLU LEU VAL GLU CYS LEU GLN LYS
SEQRES 23 A 574 LYS PRO TYR LYS GLU LEU VAL ASP GLN ASP VAL GLN PRO
SEQRES 24 A 574 ALA ARG TYR HIS ILE ALA PHE GLY PRO VAL ILE ASP GLY
SEQRES 25 A 574 ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU MET GLU GLN
SEQRES 26 A 574 GLY GLU PHE LEU ASN TYR ASP ILE MET LEU GLY VAL ASN
SEQRES 27 A 574 GLN GLY GLU GLY LEU LYS PHE VAL GLU ASN ILE VAL ASP
SEQRES 28 A 574 SER ASP ASP GLY VAL SER ALA SER ASP PHE ASP PHE ALA
SEQRES 29 A 574 VAL SER ASN PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU
SEQRES 30 A 574 GLY LYS ASP VAL LEU ARG GLU THR ILE LYS PHE MET TYR
SEQRES 31 A 574 THR ASP TRP ALA ASP ARG HIS ASN PRO GLU THR ARG ARG
SEQRES 32 A 574 LYS THR LEU LEU ALA LEU PHE THR ASP HIS GLN TRP VAL
SEQRES 33 A 574 ALA PRO ALA VAL ALA THR ALA ASP LEU HIS SER ASN PHE
SEQRES 34 A 574 GLY SER PRO THR TYR PHE TYR ALA PHE TYR HIS HIS CYS
SEQRES 35 A 574 GLN THR ASP GLN VAL PRO ALA TRP ALA ASP ALA ALA HIS
SEQRES 36 A 574 GLY ASP GLU VAL PRO TYR VAL LEU GLY ILE PRO MET ILE
SEQRES 37 A 574 GLY PRO THR GLU LEU PHE PRO CYS ASN PHE SER LYS ASN
SEQRES 38 A 574 ASP VAL MET LEU SER ALA VAL VAL MET THR TYR TRP THR
SEQRES 39 A 574 ASN PHE ALA LYS THR GLY ASP PRO ASN GLN PRO VAL PRO
SEQRES 40 A 574 GLN ASP THR LYS PHE ILE HIS THR LYS PRO ASN ARG PHE
SEQRES 41 A 574 GLU GLU VAL ALA TRP THR ARG TYR SER GLN LYS ASP GLN
SEQRES 42 A 574 LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG VAL LYS GLU
SEQRES 43 A 574 HIS TYR ARG ALA ASN LYS VAL ASN LEU TRP LEU GLU LEU
SEQRES 44 A 574 VAL PRO HIS LEU HIS ASN LEU ASN ASP HIS HIS HIS HIS
SEQRES 45 A 574 HIS HIS
SEQRES 1 B 574 ALA ASP PRO GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL
SEQRES 2 B 574 THR THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU
SEQRES 3 B 574 LEU ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU
SEQRES 4 B 574 GLY VAL PRO TYR ALA ALA PRO PRO THR GLY GLU HIS ARG
SEQRES 5 B 574 PHE GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE
SEQRES 6 B 574 ARG ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN
SEQRES 7 B 574 ILE ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL
SEQRES 8 B 574 TRP PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL
SEQRES 9 B 574 GLN ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 10 B 574 VAL PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO
SEQRES 11 B 574 LYS PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET
SEQRES 12 B 574 GLU GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA
SEQRES 13 B 574 SER TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG
SEQRES 14 B 574 LEU GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA
SEQRES 15 B 574 ALA LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA
SEQRES 16 B 574 LEU ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY
SEQRES 17 B 574 ASP PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY
SEQRES 18 B 574 GLY SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER
SEQRES 19 B 574 GLU LYS GLY LEU PHE GLN ARG ALA ILE ALA GLN SER GLY
SEQRES 20 B 574 THR ALA LEU SER SER TRP ALA VAL SER PHE GLN PRO ALA
SEQRES 21 B 574 LYS TYR ALA ARG ILE LEU ALA THR LYS VAL GLY CYS ASN
SEQRES 22 B 574 VAL SER ASP THR VAL GLU LEU VAL GLU CYS LEU GLN LYS
SEQRES 23 B 574 LYS PRO TYR LYS GLU LEU VAL ASP GLN ASP VAL GLN PRO
SEQRES 24 B 574 ALA ARG TYR HIS ILE ALA PHE GLY PRO VAL ILE ASP GLY
SEQRES 25 B 574 ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU MET GLU GLN
SEQRES 26 B 574 GLY GLU PHE LEU ASN TYR ASP ILE MET LEU GLY VAL ASN
SEQRES 27 B 574 GLN GLY GLU GLY LEU LYS PHE VAL GLU ASN ILE VAL ASP
SEQRES 28 B 574 SER ASP ASP GLY VAL SER ALA SER ASP PHE ASP PHE ALA
SEQRES 29 B 574 VAL SER ASN PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU
SEQRES 30 B 574 GLY LYS ASP VAL LEU ARG GLU THR ILE LYS PHE MET TYR
SEQRES 31 B 574 THR ASP TRP ALA ASP ARG HIS ASN PRO GLU THR ARG ARG
SEQRES 32 B 574 LYS THR LEU LEU ALA LEU PHE THR ASP HIS GLN TRP VAL
SEQRES 33 B 574 ALA PRO ALA VAL ALA THR ALA ASP LEU HIS SER ASN PHE
SEQRES 34 B 574 GLY SER PRO THR TYR PHE TYR ALA PHE TYR HIS HIS CYS
SEQRES 35 B 574 GLN THR ASP GLN VAL PRO ALA TRP ALA ASP ALA ALA HIS
SEQRES 36 B 574 GLY ASP GLU VAL PRO TYR VAL LEU GLY ILE PRO MET ILE
SEQRES 37 B 574 GLY PRO THR GLU LEU PHE PRO CYS ASN PHE SER LYS ASN
SEQRES 38 B 574 ASP VAL MET LEU SER ALA VAL VAL MET THR TYR TRP THR
SEQRES 39 B 574 ASN PHE ALA LYS THR GLY ASP PRO ASN GLN PRO VAL PRO
SEQRES 40 B 574 GLN ASP THR LYS PHE ILE HIS THR LYS PRO ASN ARG PHE
SEQRES 41 B 574 GLU GLU VAL ALA TRP THR ARG TYR SER GLN LYS ASP GLN
SEQRES 42 B 574 LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG VAL LYS GLU
SEQRES 43 B 574 HIS TYR ARG ALA ASN LYS VAL ASN LEU TRP LEU GLU LEU
SEQRES 44 B 574 VAL PRO HIS LEU HIS ASN LEU ASN ASP HIS HIS HIS HIS
SEQRES 45 B 574 HIS HIS
SEQRES 1 C 574 ALA ASP PRO GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL
SEQRES 2 C 574 THR THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU
SEQRES 3 C 574 LEU ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU
SEQRES 4 C 574 GLY VAL PRO TYR ALA ALA PRO PRO THR GLY GLU HIS ARG
SEQRES 5 C 574 PHE GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE
SEQRES 6 C 574 ARG ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN
SEQRES 7 C 574 ILE ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL
SEQRES 8 C 574 TRP PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL
SEQRES 9 C 574 GLN ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 10 C 574 VAL PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO
SEQRES 11 C 574 LYS PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET
SEQRES 12 C 574 GLU GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA
SEQRES 13 C 574 SER TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG
SEQRES 14 C 574 LEU GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA
SEQRES 15 C 574 ALA LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA
SEQRES 16 C 574 LEU ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY
SEQRES 17 C 574 ASP PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY
SEQRES 18 C 574 GLY SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER
SEQRES 19 C 574 GLU LYS GLY LEU PHE GLN ARG ALA ILE ALA GLN SER GLY
SEQRES 20 C 574 THR ALA LEU SER SER TRP ALA VAL SER PHE GLN PRO ALA
SEQRES 21 C 574 LYS TYR ALA ARG ILE LEU ALA THR LYS VAL GLY CYS ASN
SEQRES 22 C 574 VAL SER ASP THR VAL GLU LEU VAL GLU CYS LEU GLN LYS
SEQRES 23 C 574 LYS PRO TYR LYS GLU LEU VAL ASP GLN ASP VAL GLN PRO
SEQRES 24 C 574 ALA ARG TYR HIS ILE ALA PHE GLY PRO VAL ILE ASP GLY
SEQRES 25 C 574 ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU MET GLU GLN
SEQRES 26 C 574 GLY GLU PHE LEU ASN TYR ASP ILE MET LEU GLY VAL ASN
SEQRES 27 C 574 GLN GLY GLU GLY LEU LYS PHE VAL GLU ASN ILE VAL ASP
SEQRES 28 C 574 SER ASP ASP GLY VAL SER ALA SER ASP PHE ASP PHE ALA
SEQRES 29 C 574 VAL SER ASN PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU
SEQRES 30 C 574 GLY LYS ASP VAL LEU ARG GLU THR ILE LYS PHE MET TYR
SEQRES 31 C 574 THR ASP TRP ALA ASP ARG HIS ASN PRO GLU THR ARG ARG
SEQRES 32 C 574 LYS THR LEU LEU ALA LEU PHE THR ASP HIS GLN TRP VAL
SEQRES 33 C 574 ALA PRO ALA VAL ALA THR ALA ASP LEU HIS SER ASN PHE
SEQRES 34 C 574 GLY SER PRO THR TYR PHE TYR ALA PHE TYR HIS HIS CYS
SEQRES 35 C 574 GLN THR ASP GLN VAL PRO ALA TRP ALA ASP ALA ALA HIS
SEQRES 36 C 574 GLY ASP GLU VAL PRO TYR VAL LEU GLY ILE PRO MET ILE
SEQRES 37 C 574 GLY PRO THR GLU LEU PHE PRO CYS ASN PHE SER LYS ASN
SEQRES 38 C 574 ASP VAL MET LEU SER ALA VAL VAL MET THR TYR TRP THR
SEQRES 39 C 574 ASN PHE ALA LYS THR GLY ASP PRO ASN GLN PRO VAL PRO
SEQRES 40 C 574 GLN ASP THR LYS PHE ILE HIS THR LYS PRO ASN ARG PHE
SEQRES 41 C 574 GLU GLU VAL ALA TRP THR ARG TYR SER GLN LYS ASP GLN
SEQRES 42 C 574 LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG VAL LYS GLU
SEQRES 43 C 574 HIS TYR ARG ALA ASN LYS VAL ASN LEU TRP LEU GLU LEU
SEQRES 44 C 574 VAL PRO HIS LEU HIS ASN LEU ASN ASP HIS HIS HIS HIS
SEQRES 45 C 574 HIS HIS
SEQRES 1 D 574 ALA ASP PRO GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL
SEQRES 2 D 574 THR THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU
SEQRES 3 D 574 LEU ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU
SEQRES 4 D 574 GLY VAL PRO TYR ALA ALA PRO PRO THR GLY GLU HIS ARG
SEQRES 5 D 574 PHE GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE
SEQRES 6 D 574 ARG ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN
SEQRES 7 D 574 ILE ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL
SEQRES 8 D 574 TRP PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL
SEQRES 9 D 574 GLN ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 10 D 574 VAL PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO
SEQRES 11 D 574 LYS PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET
SEQRES 12 D 574 GLU GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA
SEQRES 13 D 574 SER TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG
SEQRES 14 D 574 LEU GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA
SEQRES 15 D 574 ALA LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA
SEQRES 16 D 574 LEU ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY
SEQRES 17 D 574 ASP PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY
SEQRES 18 D 574 GLY SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER
SEQRES 19 D 574 GLU LYS GLY LEU PHE GLN ARG ALA ILE ALA GLN SER GLY
SEQRES 20 D 574 THR ALA LEU SER SER TRP ALA VAL SER PHE GLN PRO ALA
SEQRES 21 D 574 LYS TYR ALA ARG ILE LEU ALA THR LYS VAL GLY CYS ASN
SEQRES 22 D 574 VAL SER ASP THR VAL GLU LEU VAL GLU CYS LEU GLN LYS
SEQRES 23 D 574 LYS PRO TYR LYS GLU LEU VAL ASP GLN ASP VAL GLN PRO
SEQRES 24 D 574 ALA ARG TYR HIS ILE ALA PHE GLY PRO VAL ILE ASP GLY
SEQRES 25 D 574 ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU MET GLU GLN
SEQRES 26 D 574 GLY GLU PHE LEU ASN TYR ASP ILE MET LEU GLY VAL ASN
SEQRES 27 D 574 GLN GLY GLU GLY LEU LYS PHE VAL GLU ASN ILE VAL ASP
SEQRES 28 D 574 SER ASP ASP GLY VAL SER ALA SER ASP PHE ASP PHE ALA
SEQRES 29 D 574 VAL SER ASN PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU
SEQRES 30 D 574 GLY LYS ASP VAL LEU ARG GLU THR ILE LYS PHE MET TYR
SEQRES 31 D 574 THR ASP TRP ALA ASP ARG HIS ASN PRO GLU THR ARG ARG
SEQRES 32 D 574 LYS THR LEU LEU ALA LEU PHE THR ASP HIS GLN TRP VAL
SEQRES 33 D 574 ALA PRO ALA VAL ALA THR ALA ASP LEU HIS SER ASN PHE
SEQRES 34 D 574 GLY SER PRO THR TYR PHE TYR ALA PHE TYR HIS HIS CYS
SEQRES 35 D 574 GLN THR ASP GLN VAL PRO ALA TRP ALA ASP ALA ALA HIS
SEQRES 36 D 574 GLY ASP GLU VAL PRO TYR VAL LEU GLY ILE PRO MET ILE
SEQRES 37 D 574 GLY PRO THR GLU LEU PHE PRO CYS ASN PHE SER LYS ASN
SEQRES 38 D 574 ASP VAL MET LEU SER ALA VAL VAL MET THR TYR TRP THR
SEQRES 39 D 574 ASN PHE ALA LYS THR GLY ASP PRO ASN GLN PRO VAL PRO
SEQRES 40 D 574 GLN ASP THR LYS PHE ILE HIS THR LYS PRO ASN ARG PHE
SEQRES 41 D 574 GLU GLU VAL ALA TRP THR ARG TYR SER GLN LYS ASP GLN
SEQRES 42 D 574 LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG VAL LYS GLU
SEQRES 43 D 574 HIS TYR ARG ALA ASN LYS VAL ASN LEU TRP LEU GLU LEU
SEQRES 44 D 574 VAL PRO HIS LEU HIS ASN LEU ASN ASP HIS HIS HIS HIS
SEQRES 45 D 574 HIS HIS
SEQRES 1 E 243 GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY ILE LEU
SEQRES 2 E 243 GLU ALA SER SER LEU GLY ALA HIS HIS ILE HIS HIS PHE
SEQRES 3 E 243 HIS GLY SER SER LYS HIS HIS SER VAL PRO ILE ALA ILE
SEQRES 4 E 243 TYR ARG SER PRO ALA SER LEU ARG GLY GLY HIS ALA GLY
SEQRES 5 E 243 THR THR TYR ILE PHE SER LYS GLY GLY GLY GLN ILE THR
SEQRES 6 E 243 TYR LYS TRP PRO PRO ASN ASP ARG PRO SER THR ARG ALA
SEQRES 7 E 243 ASP ARG LEU ALA ILE GLY PHE SER THR VAL GLN LYS GLU
SEQRES 8 E 243 ALA VAL LEU VAL ARG VAL ASP SER SER SER GLY LEU GLY
SEQRES 9 E 243 ASP TYR LEU GLU LEU HIS ILE HIS GLN GLY LYS ILE GLY
SEQRES 10 E 243 VAL LYS PHE ASN VAL GLY THR ASP ASP ILE ALA ILE GLU
SEQRES 11 E 243 GLU SER ASN ALA ILE ILE ASN ASP GLY LYS TYR HIS VAL
SEQRES 12 E 243 VAL ARG PHE THR ARG SER GLY GLY ASN ALA THR LEU GLN
SEQRES 13 E 243 VAL ASP SER TRP PRO VAL ILE GLU ARG TYR PRO ALA GLY
SEQRES 14 E 243 ARG GLN LEU THR ILE PHE ASN SER GLN ALA THR ILE ILE
SEQRES 15 E 243 ILE GLY GLY LYS GLU GLN GLY GLN PRO PHE GLN GLY GLN
SEQRES 16 E 243 LEU SER GLY LEU TYR TYR ASN GLY LEU LYS VAL LEU ASN
SEQRES 17 E 243 MET ALA ALA GLU ASN ASP ALA ASN ILE ALA ILE VAL GLY
SEQRES 18 E 243 ASN VAL ARG LEU VAL GLY GLU VAL PRO SER SER MET THR
SEQRES 19 E 243 THR GLU SER HIS HIS HIS HIS HIS HIS
SEQRES 1 F 243 GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY ILE LEU
SEQRES 2 F 243 GLU ALA SER SER LEU GLY ALA HIS HIS ILE HIS HIS PHE
SEQRES 3 F 243 HIS GLY SER SER LYS HIS HIS SER VAL PRO ILE ALA ILE
SEQRES 4 F 243 TYR ARG SER PRO ALA SER LEU ARG GLY GLY HIS ALA GLY
SEQRES 5 F 243 THR THR TYR ILE PHE SER LYS GLY GLY GLY GLN ILE THR
SEQRES 6 F 243 TYR LYS TRP PRO PRO ASN ASP ARG PRO SER THR ARG ALA
SEQRES 7 F 243 ASP ARG LEU ALA ILE GLY PHE SER THR VAL GLN LYS GLU
SEQRES 8 F 243 ALA VAL LEU VAL ARG VAL ASP SER SER SER GLY LEU GLY
SEQRES 9 F 243 ASP TYR LEU GLU LEU HIS ILE HIS GLN GLY LYS ILE GLY
SEQRES 10 F 243 VAL LYS PHE ASN VAL GLY THR ASP ASP ILE ALA ILE GLU
SEQRES 11 F 243 GLU SER ASN ALA ILE ILE ASN ASP GLY LYS TYR HIS VAL
SEQRES 12 F 243 VAL ARG PHE THR ARG SER GLY GLY ASN ALA THR LEU GLN
SEQRES 13 F 243 VAL ASP SER TRP PRO VAL ILE GLU ARG TYR PRO ALA GLY
SEQRES 14 F 243 ARG GLN LEU THR ILE PHE ASN SER GLN ALA THR ILE ILE
SEQRES 15 F 243 ILE GLY GLY LYS GLU GLN GLY GLN PRO PHE GLN GLY GLN
SEQRES 16 F 243 LEU SER GLY LEU TYR TYR ASN GLY LEU LYS VAL LEU ASN
SEQRES 17 F 243 MET ALA ALA GLU ASN ASP ALA ASN ILE ALA ILE VAL GLY
SEQRES 18 F 243 ASN VAL ARG LEU VAL GLY GLU VAL PRO SER SER MET THR
SEQRES 19 F 243 THR GLU SER HIS HIS HIS HIS HIS HIS
SEQRES 1 G 243 GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY ILE LEU
SEQRES 2 G 243 GLU ALA SER SER LEU GLY ALA HIS HIS ILE HIS HIS PHE
SEQRES 3 G 243 HIS GLY SER SER LYS HIS HIS SER VAL PRO ILE ALA ILE
SEQRES 4 G 243 TYR ARG SER PRO ALA SER LEU ARG GLY GLY HIS ALA GLY
SEQRES 5 G 243 THR THR TYR ILE PHE SER LYS GLY GLY GLY GLN ILE THR
SEQRES 6 G 243 TYR LYS TRP PRO PRO ASN ASP ARG PRO SER THR ARG ALA
SEQRES 7 G 243 ASP ARG LEU ALA ILE GLY PHE SER THR VAL GLN LYS GLU
SEQRES 8 G 243 ALA VAL LEU VAL ARG VAL ASP SER SER SER GLY LEU GLY
SEQRES 9 G 243 ASP TYR LEU GLU LEU HIS ILE HIS GLN GLY LYS ILE GLY
SEQRES 10 G 243 VAL LYS PHE ASN VAL GLY THR ASP ASP ILE ALA ILE GLU
SEQRES 11 G 243 GLU SER ASN ALA ILE ILE ASN ASP GLY LYS TYR HIS VAL
SEQRES 12 G 243 VAL ARG PHE THR ARG SER GLY GLY ASN ALA THR LEU GLN
SEQRES 13 G 243 VAL ASP SER TRP PRO VAL ILE GLU ARG TYR PRO ALA GLY
SEQRES 14 G 243 ARG GLN LEU THR ILE PHE ASN SER GLN ALA THR ILE ILE
SEQRES 15 G 243 ILE GLY GLY LYS GLU GLN GLY GLN PRO PHE GLN GLY GLN
SEQRES 16 G 243 LEU SER GLY LEU TYR TYR ASN GLY LEU LYS VAL LEU ASN
SEQRES 17 G 243 MET ALA ALA GLU ASN ASP ALA ASN ILE ALA ILE VAL GLY
SEQRES 18 G 243 ASN VAL ARG LEU VAL GLY GLU VAL PRO SER SER MET THR
SEQRES 19 G 243 THR GLU SER HIS HIS HIS HIS HIS HIS
SEQRES 1 H 243 GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY ILE LEU
SEQRES 2 H 243 GLU ALA SER SER LEU GLY ALA HIS HIS ILE HIS HIS PHE
SEQRES 3 H 243 HIS GLY SER SER LYS HIS HIS SER VAL PRO ILE ALA ILE
SEQRES 4 H 243 TYR ARG SER PRO ALA SER LEU ARG GLY GLY HIS ALA GLY
SEQRES 5 H 243 THR THR TYR ILE PHE SER LYS GLY GLY GLY GLN ILE THR
SEQRES 6 H 243 TYR LYS TRP PRO PRO ASN ASP ARG PRO SER THR ARG ALA
SEQRES 7 H 243 ASP ARG LEU ALA ILE GLY PHE SER THR VAL GLN LYS GLU
SEQRES 8 H 243 ALA VAL LEU VAL ARG VAL ASP SER SER SER GLY LEU GLY
SEQRES 9 H 243 ASP TYR LEU GLU LEU HIS ILE HIS GLN GLY LYS ILE GLY
SEQRES 10 H 243 VAL LYS PHE ASN VAL GLY THR ASP ASP ILE ALA ILE GLU
SEQRES 11 H 243 GLU SER ASN ALA ILE ILE ASN ASP GLY LYS TYR HIS VAL
SEQRES 12 H 243 VAL ARG PHE THR ARG SER GLY GLY ASN ALA THR LEU GLN
SEQRES 13 H 243 VAL ASP SER TRP PRO VAL ILE GLU ARG TYR PRO ALA GLY
SEQRES 14 H 243 ARG GLN LEU THR ILE PHE ASN SER GLN ALA THR ILE ILE
SEQRES 15 H 243 ILE GLY GLY LYS GLU GLN GLY GLN PRO PHE GLN GLY GLN
SEQRES 16 H 243 LEU SER GLY LEU TYR TYR ASN GLY LEU LYS VAL LEU ASN
SEQRES 17 H 243 MET ALA ALA GLU ASN ASP ALA ASN ILE ALA ILE VAL GLY
SEQRES 18 H 243 ASN VAL ARG LEU VAL GLY GLU VAL PRO SER SER MET THR
SEQRES 19 H 243 THR GLU SER HIS HIS HIS HIS HIS HIS
MODRES 3BIW ASN A 109 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN A 343 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN A 547 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN B 109 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN B 343 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN B 547 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN C 109 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN C 343 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN C 547 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN D 109 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN D 343 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN D 547 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN E 184 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN F 184 ASN GLYCOSYLATION SITE
MODRES 3BIW ASN G 184 ASN GLYCOSYLATION SITE
HET NAG A 701 14
HET NAG A 702 14
HET NAG A 703 14
HET NAG B 701 14
HET NAG B 702 14
HET NAG B 703 14
HET NAG C 701 14
HET NAG C 702 14
HET NAG C 703 14
HET NAG D 701 14
HET NAG D 702 14
HET NAG D 703 14
HET NAG E 306 14
HET NAG E 307 14
HET NAG F 306 14
HET NAG F 307 14
HET NAG G 306 14
HET NAG G 307 14
HET CA E 401 1
HET CA E 402 1
HET CA F 401 1
HET CA F 402 1
HET CA G 401 1
HET CA G 402 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CA CALCIUM ION
HETSYN NAG NAG
FORMUL 9 NAG 18(C8 H15 N O6)
FORMUL 24 CA 6(CA 2+)
HELIX 1 1 PRO A 132 ASN A 137 1 6
HELIX 2 2 ASN A 138 GLN A 147 1 10
HELIX 3 3 GLY A 214 ASN A 222 1 9
HELIX 4 4 LEU A 232 LEU A 238 1 7
HELIX 5 5 ASN A 248 ILE A 265 1 18
HELIX 6 6 GLY A 266 PHE A 268 5 3
HELIX 7 7 GLY A 281 THR A 291 1 11
HELIX 8 8 GLN A 328 VAL A 340 1 13
HELIX 9 9 ASP A 346 GLN A 355 1 10
HELIX 10 10 PRO A 358 VAL A 363 1 6
HELIX 11 11 ASP A 388 GLN A 395 1 8
HELIX 12 12 GLY A 412 ASN A 418 1 7
HELIX 13 13 SER A 427 TYR A 443 1 17
HELIX 14 14 VAL A 451 TYR A 460 1 10
HELIX 15 15 ASP A 462 ARG A 466 5 5
HELIX 16 16 ASN A 468 TRP A 485 1 18
HELIX 17 17 TRP A 485 PHE A 499 1 15
HELIX 18 18 GLU A 528 LEU A 533 1 6
HELIX 19 19 GLY A 534 GLY A 539 5 6
HELIX 20 20 SER A 549 GLY A 570 1 22
HELIX 21 21 ARG A 619 GLU A 628 1 10
HELIX 22 22 GLU A 628 HIS A 634 1 7
HELIX 23 23 PRO B 132 ASN B 137 1 6
HELIX 24 24 ASN B 138 GLN B 147 1 10
HELIX 25 25 GLY B 214 ASN B 222 1 9
HELIX 26 26 LEU B 232 LEU B 238 1 7
HELIX 27 27 ASN B 248 ILE B 265 1 18
HELIX 28 28 GLY B 266 PHE B 268 5 3
HELIX 29 29 GLY B 281 THR B 291 1 11
HELIX 30 30 GLN B 328 VAL B 340 1 13
HELIX 31 31 ASP B 346 GLN B 355 1 10
HELIX 32 32 PRO B 358 VAL B 363 1 6
HELIX 33 33 ASP B 388 GLN B 395 1 8
HELIX 34 34 GLY B 412 ASN B 418 1 7
HELIX 35 35 SER B 427 TYR B 443 1 17
HELIX 36 36 VAL B 451 TYR B 460 1 10
HELIX 37 37 ASP B 462 ARG B 466 5 5
HELIX 38 38 ASN B 468 TRP B 485 1 18
HELIX 39 39 TRP B 485 PHE B 499 1 15
HELIX 40 40 GLU B 528 LEU B 533 1 6
HELIX 41 41 GLY B 534 GLY B 539 5 6
HELIX 42 42 SER B 549 GLY B 570 1 22
HELIX 43 43 ARG B 619 GLU B 628 1 10
HELIX 44 44 GLU B 628 HIS B 634 1 7
HELIX 45 45 PRO C 132 ASN C 137 1 6
HELIX 46 46 ASN C 138 GLN C 147 1 10
HELIX 47 47 GLY C 214 ASN C 222 1 9
HELIX 48 48 LEU C 232 LEU C 238 1 7
HELIX 49 49 ASN C 248 ILE C 265 1 18
HELIX 50 50 GLY C 266 PHE C 268 5 3
HELIX 51 51 GLY C 281 THR C 291 1 11
HELIX 52 52 GLN C 328 VAL C 340 1 13
HELIX 53 53 ASP C 346 GLN C 355 1 10
HELIX 54 54 PRO C 358 VAL C 363 1 6
HELIX 55 55 ASP C 388 GLN C 395 1 8
HELIX 56 56 GLY C 412 ASN C 418 1 7
HELIX 57 57 SER C 427 TYR C 443 1 17
HELIX 58 58 VAL C 451 TYR C 460 1 10
HELIX 59 59 ASP C 462 ARG C 466 5 5
HELIX 60 60 ASN C 468 TRP C 485 1 18
HELIX 61 61 TRP C 485 PHE C 499 1 15
HELIX 62 62 GLU C 528 LEU C 533 1 6
HELIX 63 63 GLY C 534 GLY C 539 5 6
HELIX 64 64 SER C 549 GLY C 570 1 22
HELIX 65 65 ARG C 619 GLU C 628 1 10
HELIX 66 66 GLU C 628 HIS C 634 1 7
HELIX 67 67 PRO D 132 ASN D 137 1 6
HELIX 68 68 ASN D 138 GLN D 147 1 10
HELIX 69 69 GLY D 214 ASN D 222 1 9
HELIX 70 70 LEU D 232 LEU D 238 1 7
HELIX 71 71 ASN D 248 ILE D 265 1 18
HELIX 72 72 GLY D 266 PHE D 268 5 3
HELIX 73 73 GLY D 281 THR D 291 1 11
HELIX 74 74 GLN D 328 VAL D 340 1 13
HELIX 75 75 ASP D 346 GLN D 355 1 10
HELIX 76 76 PRO D 358 VAL D 363 1 6
HELIX 77 77 ASP D 388 GLN D 395 1 8
HELIX 78 78 GLY D 412 ASN D 418 1 7
HELIX 79 79 SER D 427 TYR D 443 1 17
HELIX 80 80 VAL D 451 TYR D 460 1 10
HELIX 81 81 ASP D 462 ARG D 466 5 5
HELIX 82 82 ASN D 468 TRP D 485 1 18
HELIX 83 83 TRP D 485 PHE D 499 1 15
HELIX 84 84 GLU D 528 LEU D 533 1 6
HELIX 85 85 GLY D 534 GLY D 539 5 6
HELIX 86 86 SER D 549 GLY D 570 1 22
HELIX 87 87 ARG D 619 GLU D 628 1 10
HELIX 88 88 GLU D 628 HIS D 634 1 7
HELIX 89 89 PRO E 101 ARG E 105 5 5
HELIX 90 90 LYS E 267 GLU E 274 1 8
HELIX 91 91 PRO F 101 ARG F 105 5 5
HELIX 92 92 LYS F 267 GLU F 274 1 8
HELIX 93 93 PRO G 101 ARG G 105 5 5
HELIX 94 94 LYS G 267 GLU G 274 1 8
HELIX 95 95 PRO H 101 ARG H 105 5 5
HELIX 96 96 LYS H 267 GLU H 274 1 8
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 LYS A 61
SHEET 1 B11 ILE A 65 LYS A 67 0
SHEET 2 B11 VAL A 77 PRO A 84 -1 O VAL A 77 N LYS A 67
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 THR A 227 N ASN A 157
SHEET 5 B11 LYS A 193 ILE A 199 1 N MET A 196 O ILE A 224
SHEET 6 B11 GLY A 270 SER A 280 1 O THR A 276 N VAL A 195
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 PHE A 508 N VAL A 407
SHEET 10 B11 LEU A 604 ILE A 608 1 O LEU A 606 N ALA A 507
SHEET 11 B11 ARG A 613 GLU A 616 -1 O LYS A 615 N TYR A 605
SHEET 1 C 3 LEU B 54 THR B 56 0
SHEET 2 C 3 LYS B 61 ARG B 63 -1 O ILE B 62 N VAL B 55
SHEET 3 C 3 ILE B 107 ASN B 109 1 O ARG B 108 N LYS B 61
SHEET 1 D11 ILE B 65 LYS B 67 0
SHEET 2 D11 VAL B 77 PRO B 84 -1 O VAL B 77 N LYS B 67
SHEET 3 D11 TYR B 155 PRO B 161 -1 O LEU B 156 N VAL B 83
SHEET 4 D11 ILE B 224 VAL B 228 -1 O THR B 227 N ASN B 157
SHEET 5 D11 LYS B 193 ILE B 199 1 N MET B 196 O ILE B 224
SHEET 6 D11 GLY B 270 SER B 280 1 O THR B 276 N VAL B 195
SHEET 7 D11 ARG B 311 GLN B 315 1 O GLN B 315 N GLY B 279
SHEET 8 D11 ASP B 402 ASN B 408 1 O ASP B 402 N ALA B 312
SHEET 9 D11 THR B 503 PHE B 508 1 O PHE B 508 N VAL B 407
SHEET 10 D11 LEU B 604 ILE B 608 1 O LEU B 606 N PHE B 505
SHEET 11 D11 ARG B 613 GLU B 616 -1 O LYS B 615 N TYR B 605
SHEET 1 E 3 LEU C 54 THR C 57 0
SHEET 2 E 3 GLY C 60 LYS C 67 -1 O ILE C 62 N VAL C 55
SHEET 3 E 3 ILE C 107 ALA C 110 1 O ARG C 108 N LYS C 61
SHEET 1 F12 LEU C 54 THR C 57 0
SHEET 2 F12 GLY C 60 LYS C 67 -1 O ILE C 62 N VAL C 55
SHEET 3 F12 VAL C 77 PRO C 84 -1 O VAL C 77 N LYS C 67
SHEET 4 F12 TYR C 155 PRO C 161 -1 O LEU C 156 N VAL C 83
SHEET 5 F12 ILE C 224 VAL C 228 -1 O THR C 227 N ASN C 157
SHEET 6 F12 LYS C 193 ILE C 199 1 N MET C 196 O ILE C 224
SHEET 7 F12 GLY C 270 SER C 280 1 O PHE C 278 N ILE C 199
SHEET 8 F12 ARG C 311 GLN C 315 1 O GLN C 315 N GLY C 279
SHEET 9 F12 ASP C 402 ASN C 408 1 O ASP C 402 N ALA C 312
SHEET 10 F12 THR C 503 PHE C 508 1 O PHE C 508 N VAL C 407
SHEET 11 F12 LEU C 604 ILE C 608 1 O LEU C 606 N ALA C 507
SHEET 12 F12 ARG C 613 GLU C 616 -1 O LYS C 615 N TYR C 605
SHEET 1 G 3 LEU D 54 THR D 56 0
SHEET 2 G 3 LYS D 61 LYS D 67 -1 O ILE D 62 N VAL D 55
SHEET 3 G 3 ILE D 107 ALA D 110 1 O ARG D 108 N LYS D 61
SHEET 1 H12 LEU D 54 THR D 56 0
SHEET 2 H12 LYS D 61 LYS D 67 -1 O ILE D 62 N VAL D 55
SHEET 3 H12 VAL D 77 PRO D 84 -1 O VAL D 77 N LYS D 67
SHEET 4 H12 TYR D 155 PRO D 161 -1 O LEU D 156 N VAL D 83
SHEET 5 H12 ILE D 224 VAL D 228 -1 O THR D 227 N ASN D 157
SHEET 6 H12 LYS D 193 ILE D 199 1 N MET D 196 O ILE D 224
SHEET 7 H12 GLY D 270 SER D 280 1 O THR D 276 N VAL D 195
SHEET 8 H12 ARG D 311 GLN D 315 1 O GLN D 315 N GLY D 279
SHEET 9 H12 ASP D 402 ASN D 408 1 O ASP D 402 N ALA D 312
SHEET 10 H12 THR D 503 PHE D 508 1 O PHE D 508 N VAL D 407
SHEET 11 H12 LEU D 604 ILE D 608 1 O LEU D 606 N ALA D 507
SHEET 12 H12 ARG D 613 GLU D 616 -1 O LYS D 615 N TYR D 605
SHEET 1 I11 ILE E 159 GLU E 162 0
SHEET 2 I11 LYS E 147 ASN E 153 -1 N VAL E 150 O ILE E 161
SHEET 3 I11 TYR E 138 HIS E 144 -1 N GLU E 140 O LYS E 151
SHEET 4 I11 GLU E 123 SER E 131 -1 N ALA E 124 O ILE E 143
SHEET 5 I11 GLN E 240 ILE E 245 -1 O ALA E 241 N ASP E 130
SHEET 6 I11 THR E 86 LYS E 99 -1 N ILE E 96 O ILE E 245
SHEET 7 I11 GLY E 256 TYR E 263 -1 O GLY E 256 N PHE E 89
SHEET 8 I11 ALA E 110 SER E 118 -1 N ALA E 114 O TYR E 262
SHEET 9 I11 HIS E 174 SER E 181 -1 O PHE E 178 N LEU E 113
SHEET 10 I11 ASN E 184 VAL E 189 -1 O THR E 186 N THR E 179
SHEET 11 I11 ILE E 195 ARG E 197 -1 O ILE E 195 N LEU E 187
SHEET 1 J 7 ILE E 159 GLU E 162 0
SHEET 2 J 7 LYS E 147 ASN E 153 -1 N VAL E 150 O ILE E 161
SHEET 3 J 7 TYR E 138 HIS E 144 -1 N GLU E 140 O LYS E 151
SHEET 4 J 7 GLU E 123 SER E 131 -1 N ALA E 124 O ILE E 143
SHEET 5 J 7 GLN E 240 ILE E 245 -1 O ALA E 241 N ASP E 130
SHEET 6 J 7 THR E 86 LYS E 99 -1 N ILE E 96 O ILE E 245
SHEET 7 J 7 ILE E 279 VAL E 288 -1 O ARG E 286 N ILE E 88
SHEET 1 K11 ILE F 159 GLU F 162 0
SHEET 2 K11 LYS F 147 ASN F 153 -1 N VAL F 150 O ILE F 161
SHEET 3 K11 TYR F 138 HIS F 144 -1 N GLU F 140 O LYS F 151
SHEET 4 K11 GLU F 123 SER F 131 -1 N ALA F 124 O ILE F 143
SHEET 5 K11 GLN F 240 ILE F 245 -1 O ALA F 241 N ASP F 130
SHEET 6 K11 THR F 86 LYS F 99 -1 N ILE F 96 O ILE F 245
SHEET 7 K11 GLY F 256 TYR F 263 -1 O GLY F 256 N PHE F 89
SHEET 8 K11 ALA F 110 SER F 118 -1 N ALA F 114 O TYR F 262
SHEET 9 K11 HIS F 174 SER F 181 -1 O PHE F 178 N LEU F 113
SHEET 10 K11 ASN F 184 VAL F 189 -1 O THR F 186 N THR F 179
SHEET 11 K11 ILE F 195 ARG F 197 -1 O ILE F 195 N LEU F 187
SHEET 1 L 7 ILE F 159 GLU F 162 0
SHEET 2 L 7 LYS F 147 ASN F 153 -1 N VAL F 150 O ILE F 161
SHEET 3 L 7 TYR F 138 HIS F 144 -1 N GLU F 140 O LYS F 151
SHEET 4 L 7 GLU F 123 SER F 131 -1 N ALA F 124 O ILE F 143
SHEET 5 L 7 GLN F 240 ILE F 245 -1 O ALA F 241 N ASP F 130
SHEET 6 L 7 THR F 86 LYS F 99 -1 N ILE F 96 O ILE F 245
SHEET 7 L 7 ILE F 279 VAL F 288 -1 O ARG F 286 N ILE F 88
SHEET 1 M11 ILE G 159 GLU G 162 0
SHEET 2 M11 LYS G 147 ASN G 153 -1 N VAL G 150 O ILE G 161
SHEET 3 M11 TYR G 138 HIS G 144 -1 N GLU G 140 O LYS G 151
SHEET 4 M11 GLU G 123 SER G 131 -1 N ALA G 124 O ILE G 143
SHEET 5 M11 GLN G 240 ILE G 245 -1 O ALA G 241 N ASP G 130
SHEET 6 M11 THR G 86 LYS G 99 -1 N ILE G 96 O ILE G 245
SHEET 7 M11 GLY G 256 TYR G 263 -1 O GLY G 256 N PHE G 89
SHEET 8 M11 ALA G 110 SER G 118 -1 N ALA G 114 O TYR G 262
SHEET 9 M11 HIS G 174 SER G 181 -1 O PHE G 178 N LEU G 113
SHEET 10 M11 ASN G 184 VAL G 189 -1 O THR G 186 N THR G 179
SHEET 11 M11 ILE G 195 ARG G 197 -1 O ILE G 195 N LEU G 187
SHEET 1 N 7 ILE G 159 GLU G 162 0
SHEET 2 N 7 LYS G 147 ASN G 153 -1 N VAL G 150 O ILE G 161
SHEET 3 N 7 TYR G 138 HIS G 144 -1 N GLU G 140 O LYS G 151
SHEET 4 N 7 GLU G 123 SER G 131 -1 N ALA G 124 O ILE G 143
SHEET 5 N 7 GLN G 240 ILE G 245 -1 O ALA G 241 N ASP G 130
SHEET 6 N 7 THR G 86 LYS G 99 -1 N ILE G 96 O ILE G 245
SHEET 7 N 7 ILE G 279 VAL G 288 -1 O ARG G 286 N ILE G 88
SHEET 1 O11 ILE H 159 GLU H 162 0
SHEET 2 O11 LYS H 147 ASN H 153 -1 N VAL H 150 O ILE H 161
SHEET 3 O11 TYR H 138 HIS H 144 -1 N GLU H 140 O LYS H 151
SHEET 4 O11 GLU H 123 SER H 131 -1 N VAL H 127 O LEU H 141
SHEET 5 O11 GLN H 240 ILE H 245 -1 O ALA H 241 N ASP H 130
SHEET 6 O11 THR H 86 LYS H 99 -1 N ILE H 96 O ILE H 245
SHEET 7 O11 GLY H 256 TYR H 263 -1 O GLY H 256 N PHE H 89
SHEET 8 O11 ALA H 110 SER H 118 -1 N ALA H 114 O TYR H 262
SHEET 9 O11 HIS H 174 SER H 181 -1 O PHE H 178 N LEU H 113
SHEET 10 O11 ASN H 184 VAL H 189 -1 O THR H 186 N THR H 179
SHEET 11 O11 ILE H 195 ARG H 197 -1 O ILE H 195 N LEU H 187
SHEET 1 P 7 ILE H 159 GLU H 162 0
SHEET 2 P 7 LYS H 147 ASN H 153 -1 N VAL H 150 O ILE H 161
SHEET 3 P 7 TYR H 138 HIS H 144 -1 N GLU H 140 O LYS H 151
SHEET 4 P 7 GLU H 123 SER H 131 -1 N VAL H 127 O LEU H 141
SHEET 5 P 7 GLN H 240 ILE H 245 -1 O ALA H 241 N ASP H 130
SHEET 6 P 7 THR H 86 LYS H 99 -1 N ILE H 96 O ILE H 245
SHEET 7 P 7 ILE H 279 VAL H 288 -1 O ARG H 286 N ILE H 88
SSBOND 1 CYS A 117 CYS A 153 1555 1555 2.04
SSBOND 2 CYS A 342 CYS A 353 1555 1555 2.04
SSBOND 3 CYS A 512 CYS A 546 1555 1555 2.03
SSBOND 4 CYS B 117 CYS B 153 1555 1555 2.04
SSBOND 5 CYS B 342 CYS B 353 1555 1555 2.04
SSBOND 6 CYS B 512 CYS B 546 1555 1555 2.03
SSBOND 7 CYS C 117 CYS C 153 1555 1555 2.04
SSBOND 8 CYS C 342 CYS C 353 1555 1555 2.04
SSBOND 9 CYS C 512 CYS C 546 1555 1555 2.04
SSBOND 10 CYS D 117 CYS D 153 1555 1555 2.03
SSBOND 11 CYS D 342 CYS D 353 1555 1555 2.03
SSBOND 12 CYS D 512 CYS D 546 1555 1555 2.03
LINK ND2 ASN A 109 C1 NAG A 701 1555 1555 1.47
LINK ND2 ASN A 343 C1 NAG A 702 1555 1555 1.47
LINK ND2 ASN A 547 C1 NAG A 703 1555 1555 1.46
LINK ND2 ASN B 109 C1 NAG B 701 1555 1555 1.47
LINK ND2 ASN B 343 C1 NAG B 702 1555 1555 1.47
LINK ND2 ASN B 547 C1 NAG B 703 1555 1555 1.46
LINK ND2 ASN C 109 C1 NAG C 701 1555 1555 1.47
LINK ND2 ASN C 343 C1 NAG C 702 1555 1555 1.47
LINK ND2 ASN C 547 C1 NAG C 703 1555 1555 1.46
LINK ND2 ASN D 109 C1 NAG D 701 1555 1555 1.46
LINK ND2 ASN D 343 C1 NAG D 702 1555 1555 1.46
LINK ND2 ASN D 547 C1 NAG D 703 1555 1555 1.45
LINK OD1 ASP E 137 CA CA E 401 1555 1555 2.97
LINK OD2 ASP E 137 CA CA E 401 1555 1555 2.34
LINK O VAL E 154 CA CA E 401 1555 1555 2.25
LINK ND2 ASN E 184 C1 NAG E 306 1555 1555 1.46
LINK O ILE E 236 CA CA E 401 1555 1555 2.43
LINK OD1 ASN E 238 CA CA E 401 1555 1555 2.14
LINK OD2 ASP F 137 CA CA F 401 1555 1555 2.50
LINK O VAL F 154 CA CA F 401 1555 1555 2.22
LINK ND2 ASN F 184 C1 NAG F 306 1555 1555 1.46
LINK O ILE F 236 CA CA F 401 1555 1555 2.46
LINK OD1 ASN F 238 CA CA F 401 1555 1555 2.21
LINK OD1 ASP G 137 CA CA G 401 1555 1555 2.98
LINK OD2 ASP G 137 CA CA G 401 1555 1555 2.37
LINK O VAL G 154 CA CA G 401 1555 1555 2.18
LINK ND2 ASN G 184 C1 NAG G 306 1555 1555 1.45
LINK O ILE G 236 CA CA G 401 1555 1555 2.45
LINK OD1 ASN G 238 CA CA G 401 1555 1555 2.21
LINK O4 NAG E 306 C1 NAG E 307 1555 1555 1.41
LINK O4 NAG F 306 C1 NAG F 307 1555 1555 1.41
LINK O4 NAG G 306 C1 NAG G 307 1555 1555 1.41
CISPEP 1 GLN A 574 PRO A 575 0 -0.15
CISPEP 2 GLN B 574 PRO B 575 0 -0.36
CISPEP 3 GLN C 574 PRO C 575 0 0.50
CISPEP 4 GLN D 574 PRO D 575 0 0.03
CRYST1 229.830 148.796 123.602 90.00 90.38 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 0.004351 0.000000 0.000028 0.00000
SCALE2 0.000000 0.006721 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008091 0.00000
TER 4187 LEU A 636
TER 8374 LEU B 636
TER 12561 LEU C 636
TER 16748 LEU D 636
TER 18108 VAL E 288
TER 19468 VAL F 288
TER 20828 VAL G 288
TER 22188 VAL H 288
MASTER 1030 0 24 96 130 0 0 622438 8 310 256
END |