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HEADER CELL ADHESION 01-DEC-07 3BIX
TITLE CRYSTAL STRUCTURE OF THE EXTRACELLULAR ESTERASE DOMAIN OF
TITLE 2 NEUROLIGIN-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: EXTRACELLULAR ESTERASE DOMAIN;
COMPND 5 SYNONYM: NEUROLIGIN I;
COMPND 6 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
KEYWDS ESTERASE DOMAIN, ALPHA-BETA HYDROLASE, ALTERNATIVE SPLICING,
KEYWDS 2 CELL ADHESION, CELL JUNCTION, GLYCOPROTEIN, MEMBRANE,
KEYWDS 3 POSTSYNAPTIC CELL MEMBRANE, SYNAPSE, TRANSMEMBRANE
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 3BIX 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1687471.750
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 334460
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) : 0.185
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 16809
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 52025
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2813
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17702
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 170
REMARK 3 SOLVENT ATOMS : 1965
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.13000
REMARK 3 B22 (A**2) : 2.13000
REMARK 3 B33 (A**2) : -4.26000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.81
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) : 1.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.020 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.150 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 54.31
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 : EDO.PAR
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 3BIX 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 RCSB045576.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-2007
REMARK 200 TEMPERATURE (KELVIN) : 130.0
REMARK 200 PH : 8.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
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 : 360486
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
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 (%) : 98.3
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.60100
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 (%): 66.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M TRI-SODIUM CITRATE, 0.1 M
REMARK 280 TRIS, PH 8.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.03000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.01500
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 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: 4440 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -36.01500
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 4880 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 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 ILE A 186
REMARK 465 ARG A 187
REMARK 465 ASP A 188
REMARK 465 SER A 189
REMARK 465 GLY A 190
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 ILE B 186
REMARK 465 ARG B 187
REMARK 465 ASP B 188
REMARK 465 SER B 189
REMARK 465 GLY B 190
REMARK 465 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 ILE C 186
REMARK 465 ARG C 187
REMARK 465 ASP C 188
REMARK 465 SER C 189
REMARK 465 GLY C 190
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 ILE D 186
REMARK 465 ARG D 187
REMARK 465 ASP D 188
REMARK 465 SER D 189
REMARK 465 GLY D 190
REMARK 465 HIS D 643
REMARK 465 HIS D 644
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 PRO A 53 96.58 -68.92
REMARK 500 ASP A 106 -158.38 -99.48
REMARK 500 ASN A 138 44.91 -141.59
REMARK 500 TYR A 204 -6.96 81.37
REMARK 500 ASP A 242 -158.05 -140.54
REMARK 500 ALA A 375 -63.56 -93.75
REMARK 500 ASP A 383 -76.75 -122.68
REMARK 500 VAL A 451 -32.70 -140.03
REMARK 500 ASP A 465 49.21 -164.98
REMARK 500 TRP A 485 -51.83 -124.25
REMARK 500 THR A 585 -16.09 71.45
REMARK 500 ARG A 613 161.34 177.70
REMARK 500 ARG A 619 44.43 39.72
REMARK 500 ASP B 106 -158.20 -100.17
REMARK 500 TYR B 204 -7.52 80.64
REMARK 500 ASP B 242 -156.84 -145.21
REMARK 500 ALA B 375 -63.43 -93.76
REMARK 500 ASP B 383 -74.02 -127.34
REMARK 500 VAL B 451 -32.79 -138.75
REMARK 500 ASP B 465 50.41 -165.32
REMARK 500 TRP B 485 -51.51 -124.53
REMARK 500 THR B 585 -17.43 69.37
REMARK 500 ARG B 613 160.73 178.99
REMARK 500 ARG B 619 45.16 38.84
REMARK 500 PRO C 53 98.22 -67.85
REMARK 500 ASP C 106 -157.68 -96.97
REMARK 500 TYR C 204 -8.44 82.34
REMARK 500 ASP C 242 -159.87 -143.65
REMARK 500 ALA C 375 -62.25 -93.19
REMARK 500 ASP C 383 -73.32 -128.81
REMARK 500 VAL C 451 -34.50 -137.41
REMARK 500 ASP C 465 50.74 -168.18
REMARK 500 TRP C 485 -51.00 -123.75
REMARK 500 THR C 585 -17.45 71.59
REMARK 500 ARG C 613 160.28 179.74
REMARK 500 ARG C 619 46.08 39.26
REMARK 500 PRO D 53 92.12 -63.89
REMARK 500 ASP D 106 -157.69 -99.28
REMARK 500 PRO D 127 95.46 -69.28
REMARK 500 ASN D 138 42.50 -140.00
REMARK 500 TYR D 204 -8.64 82.05
REMARK 500 ASP D 242 -156.73 -138.08
REMARK 500 ALA D 375 -61.92 -94.00
REMARK 500 ASP D 383 -72.99 -126.83
REMARK 500 VAL D 451 -33.29 -138.10
REMARK 500 ASP D 465 49.39 -165.82
REMARK 500 TRP D 485 -51.85 -123.41
REMARK 500 THR D 585 -15.81 70.56
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 NI A 2 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 640 NE2
REMARK 620 2 HIS A 642 NE2 113.6
REMARK 620 3 HIS D 640 NE2 114.8 112.1
REMARK 620 4 HIS D 642 NE2 111.0 93.9 109.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 1 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 640 NE2
REMARK 620 2 HIS B 642 NE2 112.1
REMARK 620 3 HIS C 640 NE2 114.1 113.7
REMARK 620 4 HIS C 642 NE2 108.6 95.5 111.3
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BIW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NEUROLIGIN-1/NEUREXIN-1BETA COMPLEX
DBREF 3BIX A 46 164 UNP Q62765 NLGN1_RAT 46 164
DBREF 3BIX A 185 297 UNP Q62765 NLGN1_RAT 185 297
DBREF 3BIX A 306 638 UNP Q62765 NLGN1_RAT 306 638
DBREF 3BIX B 46 164 UNP Q62765 NLGN1_RAT 46 164
DBREF 3BIX B 185 297 UNP Q62765 NLGN1_RAT 185 297
DBREF 3BIX B 306 638 UNP Q62765 NLGN1_RAT 306 638
DBREF 3BIX C 46 164 UNP Q62765 NLGN1_RAT 46 164
DBREF 3BIX C 185 297 UNP Q62765 NLGN1_RAT 185 297
DBREF 3BIX C 306 638 UNP Q62765 NLGN1_RAT 306 638
DBREF 3BIX D 46 164 UNP Q62765 NLGN1_RAT 46 164
DBREF 3BIX D 185 297 UNP Q62765 NLGN1_RAT 185 297
DBREF 3BIX D 306 638 UNP Q62765 NLGN1_RAT 306 638
SEQADV 3BIX ALA A 43 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX ASP A 44 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX PRO A 45 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS A 639 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS A 640 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS A 641 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS A 642 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS A 643 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS A 644 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX ALA B 43 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX ASP B 44 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX PRO B 45 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS B 639 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS B 640 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS B 641 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS B 642 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS B 643 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS B 644 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX ALA C 43 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX ASP C 44 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX PRO C 45 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS C 639 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS C 640 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS C 641 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS C 642 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS C 643 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS C 644 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX ALA D 43 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX ASP D 44 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX PRO D 45 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS D 639 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS D 640 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS D 641 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS D 642 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS D 643 UNP Q62765 EXPRESSION TAG
SEQADV 3BIX HIS D 644 UNP Q62765 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
MODRES 3BIX ASN A 109 ASN GLYCOSYLATION SITE
MODRES 3BIX ASN A 343 ASN GLYCOSYLATION SITE
MODRES 3BIX ASN B 109 ASN GLYCOSYLATION SITE
MODRES 3BIX ASN B 343 ASN GLYCOSYLATION SITE
MODRES 3BIX ASN C 109 ASN GLYCOSYLATION SITE
MODRES 3BIX ASN C 343 ASN GLYCOSYLATION SITE
MODRES 3BIX ASN D 109 ASN GLYCOSYLATION SITE
MODRES 3BIX ASN D 343 ASN GLYCOSYLATION SITE
HET NAG A 1 14
HET NAG B 2 14
HET NAG C 3 14
HET NAG D 4 14
HET NAG D 5 14
HET NAG C 6 14
HET NAG B 7 14
HET NAG A 8 14
HET NI B 1 1
HET NI A 2 1
HET EDO A 645 4
HET EDO C 2 4
HET EDO A 4 4
HET EDO D 645 4
HET EDO B 6 4
HET EDO B 645 4
HET EDO A 646 4
HET EDO D 9 4
HET EDO C 10 4
HET EDO B 11 4
HET EDO D 12 4
HET EDO C 13 4
HET EDO D 14 4
HET EDO C 15 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NI NICKEL (II) ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG NAG
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 NAG 8(C8 H15 N O6)
FORMUL 13 NI 2(NI 2+)
FORMUL 15 EDO 14(C2 H6 O2)
FORMUL 29 HOH *1965(H2 O)
HELIX 1 1 THR A 90 ARG A 94 5 5
HELIX 2 2 PRO A 132 ASN A 137 1 6
HELIX 3 3 ASN A 138 VAL A 146 1 9
HELIX 4 4 THR A 208 TYR A 212 5 5
HELIX 5 5 GLY A 214 ASN A 222 1 9
HELIX 6 6 LEU A 232 LEU A 238 1 7
HELIX 7 7 ASN A 248 ILE A 265 1 18
HELIX 8 8 GLY A 266 PHE A 268 5 3
HELIX 9 9 GLY A 281 LEU A 292 1 12
HELIX 10 10 GLN A 328 GLY A 341 1 14
HELIX 11 11 ASP A 346 GLN A 355 1 10
HELIX 12 12 PRO A 358 ASP A 364 1 7
HELIX 13 13 ASP A 388 GLN A 395 1 8
HELIX 14 14 GLY A 412 GLU A 417 1 6
HELIX 15 15 SER A 427 GLY A 444 1 18
HELIX 16 16 VAL A 451 TYR A 460 1 10
HELIX 17 17 ASP A 462 ARG A 466 5 5
HELIX 18 18 ASN A 468 TRP A 485 1 18
HELIX 19 19 TRP A 485 PHE A 499 1 15
HELIX 20 20 GLU A 528 LEU A 533 1 6
HELIX 21 21 GLY A 534 GLY A 539 5 6
HELIX 22 22 SER A 549 GLY A 570 1 22
HELIX 23 23 LYS A 581 THR A 585 5 5
HELIX 24 24 ARG A 619 GLU A 628 1 10
HELIX 25 25 GLU A 628 ASN A 635 1 8
HELIX 26 26 THR B 90 ARG B 94 5 5
HELIX 27 27 PRO B 132 ASN B 137 1 6
HELIX 28 28 ASN B 138 VAL B 146 1 9
HELIX 29 29 THR B 208 TYR B 212 5 5
HELIX 30 30 GLY B 214 ASN B 222 1 9
HELIX 31 31 LEU B 232 LEU B 238 1 7
HELIX 32 32 ASN B 248 ILE B 265 1 18
HELIX 33 33 GLY B 266 PHE B 268 5 3
HELIX 34 34 GLY B 281 LEU B 292 1 12
HELIX 35 35 GLN B 328 GLY B 341 1 14
HELIX 36 36 ASP B 346 GLN B 355 1 10
HELIX 37 37 PRO B 358 ASP B 364 1 7
HELIX 38 38 ASP B 388 GLN B 395 1 8
HELIX 39 39 GLY B 412 GLU B 417 1 6
HELIX 40 40 SER B 427 GLY B 444 1 18
HELIX 41 41 VAL B 451 TYR B 460 1 10
HELIX 42 42 ASN B 468 TRP B 485 1 18
HELIX 43 43 TRP B 485 PHE B 499 1 15
HELIX 44 44 GLU B 528 LEU B 533 1 6
HELIX 45 45 GLY B 534 GLY B 539 5 6
HELIX 46 46 SER B 549 GLY B 570 1 22
HELIX 47 47 LYS B 581 THR B 585 5 5
HELIX 48 48 ARG B 619 GLU B 628 1 10
HELIX 49 49 GLU B 628 ASN B 635 1 8
HELIX 50 50 THR C 90 ARG C 94 5 5
HELIX 51 51 PRO C 132 ASN C 137 1 6
HELIX 52 52 ASN C 138 VAL C 146 1 9
HELIX 53 53 THR C 208 TYR C 212 5 5
HELIX 54 54 GLY C 214 ASN C 222 1 9
HELIX 55 55 LEU C 232 LEU C 238 1 7
HELIX 56 56 ASN C 248 ILE C 265 1 18
HELIX 57 57 GLY C 266 PHE C 268 5 3
HELIX 58 58 GLY C 281 LEU C 292 1 12
HELIX 59 59 GLN C 328 VAL C 340 1 13
HELIX 60 60 ASP C 346 GLN C 355 1 10
HELIX 61 61 PRO C 358 ASP C 364 1 7
HELIX 62 62 ASP C 388 GLN C 395 1 8
HELIX 63 63 GLY C 412 GLU C 417 1 6
HELIX 64 64 SER C 427 GLY C 444 1 18
HELIX 65 65 VAL C 451 TYR C 460 1 10
HELIX 66 66 ASP C 462 ARG C 466 5 5
HELIX 67 67 ASN C 468 TRP C 485 1 18
HELIX 68 68 TRP C 485 PHE C 499 1 15
HELIX 69 69 GLU C 528 LEU C 533 1 6
HELIX 70 70 GLY C 534 GLY C 539 5 6
HELIX 71 71 SER C 549 GLY C 570 1 22
HELIX 72 72 LYS C 581 THR C 585 5 5
HELIX 73 73 ARG C 619 GLU C 628 1 10
HELIX 74 74 GLU C 628 ASN C 635 1 8
HELIX 75 75 THR D 90 ARG D 94 5 5
HELIX 76 76 PRO D 132 ASN D 137 1 6
HELIX 77 77 ASN D 138 VAL D 146 1 9
HELIX 78 78 THR D 208 TYR D 212 5 5
HELIX 79 79 GLY D 214 ASN D 222 1 9
HELIX 80 80 LEU D 232 LEU D 238 1 7
HELIX 81 81 ASN D 248 ILE D 265 1 18
HELIX 82 82 GLY D 266 PHE D 268 5 3
HELIX 83 83 GLY D 281 LEU D 292 1 12
HELIX 84 84 GLN D 328 GLY D 341 1 14
HELIX 85 85 ASP D 346 GLN D 355 1 10
HELIX 86 86 PRO D 358 ASP D 364 1 7
HELIX 87 87 ASP D 388 GLN D 395 1 8
HELIX 88 88 GLY D 412 GLU D 417 1 6
HELIX 89 89 SER D 427 GLY D 444 1 18
HELIX 90 90 VAL D 451 TYR D 460 1 10
HELIX 91 91 ASP D 462 ARG D 466 5 5
HELIX 92 92 ASN D 468 TRP D 485 1 18
HELIX 93 93 TRP D 485 PHE D 499 1 15
HELIX 94 94 GLU D 528 LEU D 533 1 6
HELIX 95 95 GLY D 534 GLY D 539 5 6
HELIX 96 96 SER D 549 GLY D 570 1 22
HELIX 97 97 LYS D 581 THR D 585 5 5
HELIX 98 98 ARG D 619 GLU D 628 1 10
HELIX 99 99 GLU D 628 ASN D 635 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 LEU A 156 N VAL A 83
SHEET 4 B11 ILE A 224 VAL A 228 -1 O VAL A 225 N TYR A 159
SHEET 5 B11 LYS A 193 TYR A 198 1 N TYR A 198 O ILE A 226
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 MET A 404 N ALA A 314
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 ILE A 608 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 2 TYR A 445 PRO A 446 0
SHEET 2 C 2 HIS A 639 HIS A 640 -1 O HIS A 640 N TYR A 445
SHEET 1 D 3 LEU B 54 THR B 57 0
SHEET 2 D 3 GLY B 60 ARG B 63 -1 O ILE B 62 N VAL B 55
SHEET 3 D 3 ILE B 107 ASN B 109 1 O ARG B 108 N LYS B 61
SHEET 1 E11 ILE B 65 LYS B 67 0
SHEET 2 E11 VAL B 77 PRO B 84 -1 O GLN B 79 N ILE B 65
SHEET 3 E11 TYR B 155 PRO B 161 -1 O VAL B 160 N ILE B 78
SHEET 4 E11 ILE B 224 VAL B 228 -1 O VAL B 225 N TYR B 159
SHEET 5 E11 LYS B 193 TYR B 198 1 N TYR B 198 O ILE B 226
SHEET 6 E11 GLY B 270 SER B 280 1 O THR B 276 N VAL B 195
SHEET 7 E11 ARG B 311 GLN B 315 1 O GLN B 315 N GLY B 279
SHEET 8 E11 ASP B 402 ASN B 408 1 O MET B 404 N ALA B 314
SHEET 9 E11 THR B 503 PHE B 508 1 O PHE B 508 N VAL B 407
SHEET 10 E11 LEU B 604 ILE B 608 1 O LEU B 606 N PHE B 505
SHEET 11 E11 ARG B 613 GLU B 616 -1 O LYS B 615 N TYR B 605
SHEET 1 F 2 TYR B 445 PRO B 446 0
SHEET 2 F 2 HIS B 639 HIS B 640 -1 O HIS B 640 N TYR B 445
SHEET 1 G 3 LEU C 54 THR C 57 0
SHEET 2 G 3 GLY C 60 ARG C 63 -1 O ILE C 62 N VAL C 55
SHEET 3 G 3 ILE C 107 ASN C 109 1 O ARG C 108 N LYS C 61
SHEET 1 H11 ILE C 65 LYS C 67 0
SHEET 2 H11 VAL C 77 PRO C 84 -1 O VAL C 77 N LYS C 67
SHEET 3 H11 TYR C 155 PRO C 161 -1 O VAL C 160 N ILE C 78
SHEET 4 H11 ILE C 224 VAL C 228 -1 O VAL C 225 N TYR C 159
SHEET 5 H11 LYS C 193 TYR C 198 1 N TYR C 198 O ILE C 226
SHEET 6 H11 GLY C 270 SER C 280 1 O ASP C 271 N LYS C 193
SHEET 7 H11 ARG C 311 GLN C 315 1 O GLN C 315 N GLY C 279
SHEET 8 H11 ASP C 402 ASN C 408 1 O MET C 404 N ALA C 314
SHEET 9 H11 THR C 503 PHE C 508 1 O PHE C 508 N VAL C 407
SHEET 10 H11 LEU C 604 ILE C 608 1 O ILE C 608 N ALA C 507
SHEET 11 H11 ARG C 613 GLU C 616 -1 O LYS C 615 N TYR C 605
SHEET 1 I 2 TYR C 445 PRO C 446 0
SHEET 2 I 2 HIS C 639 HIS C 640 -1 O HIS C 640 N TYR C 445
SHEET 1 J 3 LEU D 54 THR D 57 0
SHEET 2 J 3 GLY D 60 ARG D 63 -1 O ILE D 62 N VAL D 55
SHEET 3 J 3 ILE D 107 ASN D 109 1 O ARG D 108 N LYS D 61
SHEET 1 K11 ILE D 65 LYS D 67 0
SHEET 2 K11 VAL D 77 PRO D 84 -1 O VAL D 77 N LYS D 67
SHEET 3 K11 TYR D 155 PRO D 161 -1 O LEU D 156 N VAL D 83
SHEET 4 K11 ILE D 224 VAL D 228 -1 O VAL D 225 N TYR D 159
SHEET 5 K11 LYS D 193 TYR D 198 1 N TYR D 198 O ILE D 226
SHEET 6 K11 GLY D 270 SER D 280 1 O THR D 276 N VAL D 195
SHEET 7 K11 ARG D 311 GLN D 315 1 O GLN D 315 N GLY D 279
SHEET 8 K11 ASP D 402 ASN D 408 1 O MET D 404 N ALA D 314
SHEET 9 K11 THR D 503 PHE D 508 1 O PHE D 508 N VAL D 407
SHEET 10 K11 LEU D 604 ILE D 608 1 O ILE D 608 N ALA D 507
SHEET 11 K11 ARG D 613 GLU D 616 -1 O LYS D 615 N TYR D 605
SHEET 1 L 2 TYR D 445 PRO D 446 0
SHEET 2 L 2 HIS D 639 HIS D 640 -1 O HIS D 640 N TYR D 445
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 2.03
SSBOND 10 CYS D 117 CYS D 153 1555 1555 2.04
SSBOND 11 CYS D 342 CYS D 353 1555 1555 2.04
SSBOND 12 CYS D 512 CYS D 546 1555 1555 2.03
LINK ND2 ASN A 109 C1 NAG A 1 1555 1555 1.45
LINK ND2 ASN A 343 C1 NAG A 8 1555 1555 1.45
LINK NE2 HIS A 640 NI NI A 2 1555 1555 2.19
LINK NE2 HIS A 642 NI NI A 2 1555 1555 2.05
LINK ND2 ASN B 109 C1 NAG B 2 1555 1555 1.45
LINK ND2 ASN B 343 C1 NAG B 7 1555 1555 1.45
LINK NE2 HIS B 640 NI NI B 1 1555 1555 2.20
LINK NE2 HIS B 642 NI NI B 1 1555 1555 2.07
LINK ND2 ASN C 109 C1 NAG C 3 1555 1555 1.45
LINK ND2 ASN C 343 C1 NAG C 6 1555 1555 1.45
LINK NE2 HIS C 640 NI NI B 1 1555 1555 2.16
LINK NE2 HIS C 642 NI NI B 1 1555 1555 2.05
LINK ND2 ASN D 109 C1 NAG D 4 1555 1555 1.45
LINK ND2 ASN D 343 C1 NAG D 5 1555 1555 1.45
LINK NE2 HIS D 640 NI NI A 2 1555 1555 2.16
LINK NE2 HIS D 642 NI NI A 2 1555 1555 2.07
CISPEP 1 GLN A 574 PRO A 575 0 0.13
CISPEP 2 GLN B 574 PRO B 575 0 0.20
CISPEP 3 GLN C 574 PRO C 575 0 0.09
CISPEP 4 GLN D 574 PRO D 575 0 0.08
CRYST1 173.744 173.744 108.045 90.00 90.00 120.00 P 32 12
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 0.005756 0.003323 0.000000 0.00000
SCALE2 0.000000 0.006646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009255 0.00000
TER 4437 HIS A 642
TER 8860 HIS B 642
TER 13265 HIS C 642
TER 17702 HIS D 642
MASTER 406 0 24 99 64 0 0 619833 4 210 180
END |