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HEADER MEMBRANE PROTEIN 14-SEP-04 1XFD
TITLE STRUCTURE OF A HUMAN A-TYPE POTASSIUM CHANNEL ACCELERATING
TITLE 2 FACTOR DPPX, A MEMBER OF THE DIPEPTIDYL AMINOPEPTIDASE
TITLE 3 FAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 SYNONYM: DIPEPTIDYLPEPTIDASE VI; DIPEPTIDYLPEPTIDASE 6;
COMPND 6 DIPEPTIDYL PEPTIDASE IV LIKE PROTEIN; DIPEPTIDYL
COMPND 7 AMINOPEPTIDASE-RELATED PROTEIN; DPPX; DIPEPTIDYLPEPTIDASE
COMPND 8 VI; DIPEPTIDYL AMINOPEPTIDASE IV-RELATED PROTEIN;
COMPND 9 DIPEPTIDYLPEPTIDASE VI ISOFORM 2;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DPPX;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 OTHER_DETAILS: INSECT EXPRESSION SYSTEM
KEYWDS DPPX; DPP6; KV4; KV; KAF
EXPDTA X-RAY DIFFRACTION
AUTHOR P.STROP,A.J.BANKOVICH,K.C.HANSEN,C.K.GARCIA,A.T.BRUNGER
REVDAT 1 26-OCT-04 1XFD 0
JRNL AUTH P.STROP,A.J.BANKOVICH,K.C.HANSEN,C.K.GARCIA,
JRNL AUTH 2 A.T.BRUNGER
JRNL TITL STRUCTURE OF A HUMAN A-TYPE POTASSIUM CHANNEL
JRNL TITL 2 INTERACTING PROTEIN DPPX, A MEMBER OF THE
JRNL TITL 3 DIPEPTIDYL AMINOPEPTIDASE FAMILY
JRNL REF J.MOL.BIOL. 2004
JRNL REFN ASTM JMOBAK UK ESSN 1089-8638
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2096050.210
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 65968
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) : 0.248
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3338
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7319
REMARK 3 BIN R VALUE (WORKING SET) : 0.3600
REMARK 3 BIN FREE R VALUE : 0.4040
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 413
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23348
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 825
REMARK 3 SOLVENT ATOMS : 51
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.51000
REMARK 3 B22 (A**2) : -27.24000
REMARK 3 B33 (A**2) : 14.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM SIGMAA (A) : 0.63
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) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.66
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.87
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) : 2.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.510 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.550 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.140 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 40.10
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 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XFD COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PRAGUE ON 30-SEP-2004.
REMARK 100 THE RCSB ID CODE IS RCSB030298.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JAN-2004
REMARK 200 TEMPERATURE (KELVIN) : 113.0
REMARK 200 PH : 6.25
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) : 1.0781
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76240
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 18.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: HOMOLOGY MODEL BASED ON PDB ENTRY 1N1M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, NACL, PEG MME 2000, MAGNESIUM
REMARK 280 CHLORIDE, PH 6.25, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 85.11500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 OG SER C 473 OD1 ASN D 362 2546 2.13
REMARK 500 OG SER A 473 OD1 ASN B 362 2655 2.17
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN A 161 CD GLN A 161 OE1 0.096
REMARK 500 GLN A 161 CD GLN A 161 NE2 -0.098
REMARK 500 ASN A 206 CG ASN A 206 OD1 0.103
REMARK 500 ASN A 206 CG ASN A 206 ND2 -0.096
REMARK 500 GLN A 212 CD GLN A 212 OE1 0.102
REMARK 500 GLN A 212 CD GLN A 212 NE2 -0.097
REMARK 500 ASN A 260 CG ASN A 260 OD1 0.094
REMARK 500 ASN A 260 CG ASN A 260 ND2 -0.099
REMARK 500 ASN A 351 CG ASN A 351 OD1 0.095
REMARK 500 ASN A 351 CG ASN A 351 ND2 -0.101
REMARK 500 ASN A 362 CG ASN A 362 OD1 0.097
REMARK 500 ASN A 362 CG ASN A 362 ND2 -0.097
REMARK 500 ASN A 400 CG ASN A 400 OD1 0.101
REMARK 500 ASN A 400 CG ASN A 400 ND2 -0.096
REMARK 500 ASN A 476 CG ASN A 476 OD1 0.097
REMARK 500 ASN A 476 CG ASN A 476 ND2 -0.098
REMARK 500 GLN A 513 CD GLN A 513 OE1 0.100
REMARK 500 GLN A 513 CD GLN A 513 NE2 -0.100
REMARK 500 ASN A 518 CG ASN A 518 OD1 0.096
REMARK 500 ASN A 518 CG ASN A 518 ND2 -0.096
REMARK 500 GLN A 526 CD GLN A 526 OE1 0.100
REMARK 500 GLN A 526 CD GLN A 526 NE2 -0.096
REMARK 500 ASN A 579 CG ASN A 579 OD1 0.098
REMARK 500 ASN A 579 CG ASN A 579 ND2 -0.098
REMARK 500 ASN A 587 CG ASN A 587 OD1 0.099
REMARK 500 ASN A 587 CG ASN A 587 ND2 -0.096
REMARK 500 GLN A 668 CD GLN A 668 OE1 0.097
REMARK 500 GLN A 668 CD GLN A 668 NE2 -0.095
REMARK 500 GLN A 688 CD GLN A 688 OE1 0.100
REMARK 500 GLN A 688 CD GLN A 688 NE2 -0.098
REMARK 500 GLN A 731 CD GLN A 731 OE1 0.099
REMARK 500 GLN A 731 CD GLN A 731 NE2 -0.095
REMARK 500 GLN A 783 CD GLN A 783 OE1 0.098
REMARK 500 GLN A 783 CD GLN A 783 NE2 -0.096
REMARK 500 GLN A 798 CD GLN A 798 OE1 0.097
REMARK 500 GLN A 798 CD GLN A 798 NE2 -0.100
REMARK 500 GLN A 817 CD GLN A 817 OE1 0.100
REMARK 500 GLN A 817 CD GLN A 817 NE2 -0.097
REMARK 500 ILE A 840 CB ILE A 840 CG2 -0.075
REMARK 500 GLN B 161 CD GLN B 161 OE1 0.097
REMARK 500 GLN B 161 CD GLN B 161 NE2 -0.099
REMARK 500 ASN B 260 CG ASN B 260 OD1 0.099
REMARK 500 ASN B 260 CG ASN B 260 ND2 -0.094
REMARK 500 ASN B 351 CG ASN B 351 OD1 0.095
REMARK 500 ASN B 351 CG ASN B 351 ND2 -0.100
REMARK 500 ASN B 362 CG ASN B 362 OD1 0.089
REMARK 500 ASN B 362 CG ASN B 362 ND2 -0.095
REMARK 500 ASN B 400 CG ASN B 400 OD1 0.096
REMARK 500 ASN B 400 CG ASN B 400 ND2 -0.103
REMARK 500 ASN B 476 CG ASN B 476 OD1 0.097
REMARK 500 ASN B 476 CG ASN B 476 ND2 -0.097
REMARK 500 GLN B 513 CD GLN B 513 OE1 0.094
REMARK 500 GLN B 513 CD GLN B 513 NE2 -0.100
REMARK 500 ASN B 518 CG ASN B 518 OD1 0.096
REMARK 500 ASN B 518 CG ASN B 518 ND2 -0.095
REMARK 500 GLN B 526 CD GLN B 526 OE1 0.098
REMARK 500 GLN B 526 CD GLN B 526 NE2 -0.099
REMARK 500 ASN B 579 CG ASN B 579 OD1 0.099
REMARK 500 ASN B 579 CG ASN B 579 ND2 -0.096
REMARK 500 ASN B 587 CG ASN B 587 OD1 0.100
REMARK 500 ASN B 587 CG ASN B 587 ND2 -0.096
REMARK 500 GLN B 668 CD GLN B 668 OE1 0.095
REMARK 500 GLN B 668 CD GLN B 668 NE2 -0.099
REMARK 500 GLN B 688 CD GLN B 688 OE1 0.094
REMARK 500 GLN B 688 CD GLN B 688 NE2 -0.099
REMARK 500 GLN B 699 CD GLN B 699 OE1 0.099
REMARK 500 GLN B 699 CD GLN B 699 NE2 -0.097
REMARK 500 GLN B 731 CD GLN B 731 OE1 0.098
REMARK 500 GLN B 731 CD GLN B 731 NE2 -0.096
REMARK 500 GLN B 783 CD GLN B 783 OE1 0.101
REMARK 500 GLN B 783 CD GLN B 783 NE2 -0.095
REMARK 500 GLN B 798 CD GLN B 798 OE1 0.098
REMARK 500 GLN B 798 CD GLN B 798 NE2 -0.100
REMARK 500 GLN B 817 CD GLN B 817 OE1 0.094
REMARK 500 GLN B 817 CD GLN B 817 NE2 -0.098
REMARK 500 ILE B 840 CB ILE B 840 CG2 -0.073
REMARK 500 GLN C 161 CD GLN C 161 OE1 0.097
REMARK 500 GLN C 161 CD GLN C 161 NE2 -0.096
REMARK 500 ARG C 191 CG ARG C 191 CD -0.136
REMARK 500 ARG C 191 CD ARG C 191 NE -0.136
REMARK 500 ARG C 191 NE ARG C 191 CZ -0.107
REMARK 500 ARG C 191 CZ ARG C 191 NH2 -0.113
REMARK 500 GLN C 212 CD GLN C 212 OE1 0.100
REMARK 500 GLN C 212 CD GLN C 212 NE2 -0.096
REMARK 500 ASN C 260 CG ASN C 260 OD1 0.097
REMARK 500 ASN C 260 CG ASN C 260 ND2 -0.096
REMARK 500 ASN C 362 CG ASN C 362 OD1 0.097
REMARK 500 ASN C 362 CG ASN C 362 ND2 -0.095
REMARK 500 ASN C 400 CG ASN C 400 OD1 0.097
REMARK 500 ASN C 400 CG ASN C 400 ND2 -0.098
REMARK 500 ASN C 476 CG ASN C 476 OD1 0.096
REMARK 500 ASN C 476 CG ASN C 476 ND2 -0.097
REMARK 500 GLN C 513 CD GLN C 513 OE1 0.099
REMARK 500 GLN C 513 CD GLN C 513 NE2 -0.096
REMARK 500 ASN C 518 CG ASN C 518 OD1 0.098
REMARK 500 ASN C 518 CG ASN C 518 ND2 -0.096
REMARK 500 GLN C 526 CD GLN C 526 OE1 0.100
REMARK 500 GLN C 526 CD GLN C 526 NE2 -0.098
REMARK 500 ASN C 579 CG ASN C 579 OD1 0.095
REMARK 500 ASN C 579 CG ASN C 579 ND2 -0.099
REMARK 500 ASN C 587 CG ASN C 587 OD1 0.098
REMARK 500 ASN C 587 CG ASN C 587 ND2 -0.096
REMARK 500 GLN C 668 CD GLN C 668 OE1 0.098
REMARK 500 GLN C 668 CD GLN C 668 NE2 -0.095
REMARK 500 GLN C 688 CD GLN C 688 OE1 0.098
REMARK 500 GLN C 688 CD GLN C 688 NE2 -0.101
REMARK 500 GLN C 731 CD GLN C 731 OE1 0.098
REMARK 500 GLN C 731 CD GLN C 731 NE2 -0.094
REMARK 500 GLN C 783 CD GLN C 783 OE1 0.101
REMARK 500 GLN C 783 CD GLN C 783 NE2 -0.094
REMARK 500 GLN C 798 CD GLN C 798 OE1 0.097
REMARK 500 GLN C 798 CD GLN C 798 NE2 -0.100
REMARK 500 GLN C 817 CD GLN C 817 OE1 0.101
REMARK 500 GLN C 817 CD GLN C 817 NE2 -0.099
REMARK 500 ILE C 840 CB ILE C 840 CG1 -0.110
REMARK 500 ILE C 840 CB ILE C 840 CG2 -0.267
REMARK 500 GLN D 161 CD GLN D 161 OE1 0.096
REMARK 500 GLN D 161 CD GLN D 161 NE2 -0.097
REMARK 500 GLN D 212 CD GLN D 212 OE1 0.097
REMARK 500 GLN D 212 CD GLN D 212 NE2 -0.095
REMARK 500 ASN D 260 CG ASN D 260 OD1 0.100
REMARK 500 ASN D 260 CG ASN D 260 ND2 -0.098
REMARK 500 ASN D 362 CG ASN D 362 OD1 0.090
REMARK 500 ASN D 362 CG ASN D 362 ND2 -0.096
REMARK 500 ASN D 400 CG ASN D 400 OD1 0.096
REMARK 500 ASN D 400 CG ASN D 400 ND2 -0.100
REMARK 500 ASN D 476 CG ASN D 476 OD1 0.097
REMARK 500 ASN D 476 CG ASN D 476 ND2 -0.098
REMARK 500 GLN D 513 CD GLN D 513 OE1 0.096
REMARK 500 GLN D 513 CD GLN D 513 NE2 -0.100
REMARK 500 ASN D 518 CG ASN D 518 OD1 0.098
REMARK 500 ASN D 518 CG ASN D 518 ND2 -0.095
REMARK 500 GLN D 526 CD GLN D 526 OE1 0.100
REMARK 500 GLN D 526 CD GLN D 526 NE2 -0.099
REMARK 500 ASN D 579 CG ASN D 579 OD1 0.095
REMARK 500 ASN D 579 CG ASN D 579 ND2 -0.098
REMARK 500 ASN D 587 CG ASN D 587 OD1 0.098
REMARK 500 ASN D 587 CG ASN D 587 ND2 -0.095
REMARK 500 GLN D 668 CD GLN D 668 OE1 0.099
REMARK 500 GLN D 668 CD GLN D 668 NE2 -0.097
REMARK 500 GLN D 688 CD GLN D 688 OE1 0.095
REMARK 500 GLN D 688 CD GLN D 688 NE2 -0.101
REMARK 500 GLN D 731 CD GLN D 731 OE1 0.097
REMARK 500 GLN D 731 CD GLN D 731 NE2 -0.096
REMARK 500 GLN D 783 CD GLN D 783 OE1 0.099
REMARK 500 GLN D 783 CD GLN D 783 NE2 -0.096
REMARK 500 GLN D 798 CD GLN D 798 OE1 0.099
REMARK 500 GLN D 798 CD GLN D 798 NE2 -0.098
REMARK 500 GLN D 817 CD GLN D 817 OE1 0.097
REMARK 500 GLN D 817 CD GLN D 817 NE2 -0.099
REMARK 500 ILE D 840 CB ILE D 840 CG2 -0.066
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ILE A 224 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO A 225 C - N - CA ANGL. DEV. =-11.7 DEGREES
REMARK 500 ASP A 228 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASP A 290 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 GLU A 296 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ILE A 383 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 SER A 472 N - CA - C ANGL. DEV. = 11.7 DEGREES
REMARK 500 VAL A 487 N - CA - C ANGL. DEV. =-12.6 DEGREES
REMARK 500 GLY A 521 N - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500 LEU A 532 N - CA - C ANGL. DEV. =-13.3 DEGREES
REMARK 500 TYR A 538 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 SER A 540 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 PRO A 613 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 ILE A 742 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 ALA A 766 N - CA - C ANGL. DEV. =-12.2 DEGREES
REMARK 500 THR A 790 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 GLN A 817 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 TYR A 825 N - CA - C ANGL. DEV. = 15.9 DEGREES
REMARK 500 VAL B 207 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 GLU B 208 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ILE B 210 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 GLN B 212 N - CA - C ANGL. DEV. =-18.3 DEGREES
REMARK 500 HIS B 213 CB - CG - CD2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 HIS B 213 CB - CG - ND1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 ILE B 224 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO B 225 C - N - CA ANGL. DEV. =-11.5 DEGREES
REMARK 500 ASP B 290 N - CA - C ANGL. DEV. =-12.0 DEGREES
REMARK 500 GLU B 296 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 ILE B 383 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 SER B 472 N - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 ASN B 476 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 VAL B 487 N - CA - C ANGL. DEV. =-12.4 DEGREES
REMARK 500 GLY B 521 N - CA - C ANGL. DEV. = 12.6 DEGREES
REMARK 500 LEU B 532 N - CA - C ANGL. DEV. =-13.4 DEGREES
REMARK 500 TYR B 538 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 SER B 540 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 PRO B 613 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 ILE B 742 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 ALA B 766 N - CA - C ANGL. DEV. =-12.2 DEGREES
REMARK 500 THR B 790 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 TYR B 825 N - CA - C ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG C 191 CG - CD - NE ANGL. DEV. =-11.3 DEGREES
REMARK 500 ARG C 191 CD - NE - CZ ANGL. DEV. =-11.2 DEGREES
REMARK 500 SER C 214 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 ILE C 224 N - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO C 225 C - N - CA ANGL. DEV. =-11.5 DEGREES
REMARK 500 ASP C 228 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 GLY C 246 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASP C 290 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 GLU C 296 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 ILE C 383 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 SER C 472 N - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 ASN C 476 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 VAL C 487 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 GLY C 521 N - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500 LEU C 532 N - CA - C ANGL. DEV. =-13.2 DEGREES
REMARK 500 TYR C 538 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 SER C 540 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 LEU C 552 CA - CB - CG ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO C 613 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 ILE C 742 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 ALA C 766 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 THR C 790 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 TYR C 825 N - CA - C ANGL. DEV. = 15.9 DEGREES
REMARK 500 ILE C 840 CG1 - CB - CG2 ANGL. DEV. =-19.3 DEGREES
REMARK 500 SER D 214 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 ILE D 224 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO D 225 C - N - CA ANGL. DEV. =-11.6 DEGREES
REMARK 500 ASP D 228 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 ASP D 290 N - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 GLU D 296 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ILE D 383 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 SER D 472 N - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 ASN D 476 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 VAL D 487 N - CA - C ANGL. DEV. =-12.7 DEGREES
REMARK 500 GLY D 521 N - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 LEU D 532 N - CA - C ANGL. DEV. =-13.5 DEGREES
REMARK 500 TYR D 538 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 SER D 540 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 PRO D 613 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 ILE D 742 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 ALA D 766 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 THR D 790 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 TYR D 825 N - CA - C ANGL. DEV. = 16.0 DEGREES
DBREF 1XFD A 127 849 GB 18765698 NP_570629 127 849
DBREF 1XFD B 127 849 GB 18765698 NP_570629 127 849
DBREF 1XFD C 127 849 GB 18765698 NP_570629 127 849
DBREF 1XFD D 127 849 GB 18765698 NP_570629 127 849
SEQRES 1 A 723 GLN LYS LYS LYS VAL THR VAL GLU ASP LEU PHE SER GLU
SEQRES 2 A 723 ASP PHE LYS ILE HIS ASP PRO GLU ALA LYS TRP ILE SER
SEQRES 3 A 723 ASP THR GLU PHE ILE TYR ARG GLU GLN LYS GLY THR VAL
SEQRES 4 A 723 ARG LEU TRP ASN VAL GLU THR ASN THR SER THR VAL LEU
SEQRES 5 A 723 ILE GLU GLY LYS LYS ILE GLU SER LEU ARG ALA ILE ARG
SEQRES 6 A 723 TYR GLU ILE SER PRO ASP ARG GLU TYR ALA LEU PHE SER
SEQRES 7 A 723 TYR ASN VAL GLU PRO ILE TYR GLN HIS SER TYR THR GLY
SEQRES 8 A 723 TYR TYR VAL LEU SER LYS ILE PRO HIS GLY ASP PRO GLN
SEQRES 9 A 723 SER LEU ASP PRO PRO GLU VAL SER ASN ALA LYS LEU GLN
SEQRES 10 A 723 TYR ALA GLY TRP GLY PRO LYS GLY GLN GLN LEU ILE PHE
SEQRES 11 A 723 ILE PHE GLU ASN ASN ILE TYR TYR CYS ALA HIS VAL GLY
SEQRES 12 A 723 LYS GLN ALA ILE ARG VAL VAL SER THR GLY LYS GLU GLY
SEQRES 13 A 723 VAL ILE TYR ASN GLY LEU SER ASP TRP LEU TYR GLU GLU
SEQRES 14 A 723 GLU ILE LEU LYS THR HIS ILE ALA HIS TRP TRP SER PRO
SEQRES 15 A 723 ASP GLY THR ARG LEU ALA TYR ALA ALA ILE ASN ASP SER
SEQRES 16 A 723 ARG VAL PRO ILE MET GLU LEU PRO THR TYR THR GLY SER
SEQRES 17 A 723 ILE TYR PRO THR VAL LYS PRO TYR HIS TYR PRO LYS ALA
SEQRES 18 A 723 GLY SER GLU ASN PRO SER ILE SER LEU HIS VAL ILE GLY
SEQRES 19 A 723 LEU ASN GLY PRO THR HIS ASP LEU GLU MET MET PRO PRO
SEQRES 20 A 723 ASP ASP PRO ARG MET ARG GLU TYR TYR ILE THR MET VAL
SEQRES 21 A 723 LYS TRP ALA THR SER THR LYS VAL ALA VAL THR TRP LEU
SEQRES 22 A 723 ASN ARG ALA GLN ASN VAL SER ILE LEU THR LEU CYS ASP
SEQRES 23 A 723 ALA THR THR GLY VAL CYS THR LYS LYS HIS GLU ASP GLU
SEQRES 24 A 723 SER GLU ALA TRP LEU HIS ARG GLN ASN GLU GLU PRO VAL
SEQRES 25 A 723 PHE SER LYS ASP GLY ARG LYS PHE PHE PHE ILE ARG ALA
SEQRES 26 A 723 ILE PRO GLN GLY GLY ARG GLY LYS PHE TYR HIS ILE THR
SEQRES 27 A 723 VAL SER SER SER GLN PRO ASN SER SER ASN ASP ASN ILE
SEQRES 28 A 723 GLN SER ILE THR SER GLY ASP TRP ASP VAL THR LYS ILE
SEQRES 29 A 723 LEU ALA TYR ASP GLU LYS GLY ASN LYS ILE TYR PHE LEU
SEQRES 30 A 723 SER THR GLU ASP LEU PRO ARG ARG ARG GLN LEU TYR SER
SEQRES 31 A 723 ALA ASN THR VAL GLY ASN PHE ASN ARG GLN CYS LEU SER
SEQRES 32 A 723 CYS ASP LEU VAL GLU ASN CYS THR TYR PHE SER ALA SER
SEQRES 33 A 723 PHE SER HIS SER MET ASP PHE PHE LEU LEU LYS CYS GLU
SEQRES 34 A 723 GLY PRO GLY VAL PRO MET VAL THR VAL HIS ASN THR THR
SEQRES 35 A 723 ASP LYS LYS LYS MET PHE ASP LEU GLU THR ASN GLU HIS
SEQRES 36 A 723 VAL LYS LYS ALA ILE ASN ASP ARG GLN MET PRO LYS VAL
SEQRES 37 A 723 GLU TYR ARG ASP ILE GLU ILE ASP ASP TYR ASN LEU PRO
SEQRES 38 A 723 MET GLN ILE LEU LYS PRO ALA THR PHE THR ASP THR THR
SEQRES 39 A 723 HIS TYR PRO LEU LEU LEU VAL VAL ASP GLY THR PRO GLY
SEQRES 40 A 723 SER GLN SER VAL ALA GLU LYS PHE GLU VAL SER TRP GLU
SEQRES 41 A 723 THR VAL MET VAL SER SER HIS GLY ALA VAL VAL VAL LYS
SEQRES 42 A 723 CYS ASP GLY ARG GLY SER GLY PHE GLN GLY THR LYS LEU
SEQRES 43 A 723 LEU HIS GLU VAL ARG ARG ARG LEU GLY LEU LEU GLU GLU
SEQRES 44 A 723 LYS ASP GLN MET GLU ALA VAL ARG THR MET LEU LYS GLU
SEQRES 45 A 723 GLN TYR ILE ASP ARG THR ARG VAL ALA VAL PHE GLY LYS
SEQRES 46 A 723 ASP TYR GLY GLY TYR LEU SER THR TYR ILE LEU PRO ALA
SEQRES 47 A 723 LYS GLY GLU ASN GLN GLY GLN THR PHE THR CYS GLY SER
SEQRES 48 A 723 ALA LEU SER PRO ILE THR ASP PHE LYS LEU TYR ALA SER
SEQRES 49 A 723 ALA PHE SER GLU ARG TYR LEU GLY LEU HIS GLY LEU ASP
SEQRES 50 A 723 ASN ARG ALA TYR GLU MET THR LYS VAL ALA HIS ARG VAL
SEQRES 51 A 723 SER ALA LEU GLU GLU GLN GLN PHE LEU ILE ILE HIS PRO
SEQRES 52 A 723 THR ALA ASP GLU LYS ILE HIS PHE GLN HIS THR ALA GLU
SEQRES 53 A 723 LEU ILE THR GLN LEU ILE ARG GLY LYS ALA ASN TYR SER
SEQRES 54 A 723 LEU GLN ILE TYR PRO ASP GLU SER HIS TYR PHE THR SER
SEQRES 55 A 723 SER SER LEU LYS GLN HIS LEU TYR ARG SER ILE ILE ASN
SEQRES 56 A 723 PHE PHE VAL GLU CYS PHE ARG ILE
SEQRES 1 B 723 GLN LYS LYS LYS VAL THR VAL GLU ASP LEU PHE SER GLU
SEQRES 2 B 723 ASP PHE LYS ILE HIS ASP PRO GLU ALA LYS TRP ILE SER
SEQRES 3 B 723 ASP THR GLU PHE ILE TYR ARG GLU GLN LYS GLY THR VAL
SEQRES 4 B 723 ARG LEU TRP ASN VAL GLU THR ASN THR SER THR VAL LEU
SEQRES 5 B 723 ILE GLU GLY LYS LYS ILE GLU SER LEU ARG ALA ILE ARG
SEQRES 6 B 723 TYR GLU ILE SER PRO ASP ARG GLU TYR ALA LEU PHE SER
SEQRES 7 B 723 TYR ASN VAL GLU PRO ILE TYR GLN HIS SER TYR THR GLY
SEQRES 8 B 723 TYR TYR VAL LEU SER LYS ILE PRO HIS GLY ASP PRO GLN
SEQRES 9 B 723 SER LEU ASP PRO PRO GLU VAL SER ASN ALA LYS LEU GLN
SEQRES 10 B 723 TYR ALA GLY TRP GLY PRO LYS GLY GLN GLN LEU ILE PHE
SEQRES 11 B 723 ILE PHE GLU ASN ASN ILE TYR TYR CYS ALA HIS VAL GLY
SEQRES 12 B 723 LYS GLN ALA ILE ARG VAL VAL SER THR GLY LYS GLU GLY
SEQRES 13 B 723 VAL ILE TYR ASN GLY LEU SER ASP TRP LEU TYR GLU GLU
SEQRES 14 B 723 GLU ILE LEU LYS THR HIS ILE ALA HIS TRP TRP SER PRO
SEQRES 15 B 723 ASP GLY THR ARG LEU ALA TYR ALA ALA ILE ASN ASP SER
SEQRES 16 B 723 ARG VAL PRO ILE MET GLU LEU PRO THR TYR THR GLY SER
SEQRES 17 B 723 ILE TYR PRO THR VAL LYS PRO TYR HIS TYR PRO LYS ALA
SEQRES 18 B 723 GLY SER GLU ASN PRO SER ILE SER LEU HIS VAL ILE GLY
SEQRES 19 B 723 LEU ASN GLY PRO THR HIS ASP LEU GLU MET MET PRO PRO
SEQRES 20 B 723 ASP ASP PRO ARG MET ARG GLU TYR TYR ILE THR MET VAL
SEQRES 21 B 723 LYS TRP ALA THR SER THR LYS VAL ALA VAL THR TRP LEU
SEQRES 22 B 723 ASN ARG ALA GLN ASN VAL SER ILE LEU THR LEU CYS ASP
SEQRES 23 B 723 ALA THR THR GLY VAL CYS THR LYS LYS HIS GLU ASP GLU
SEQRES 24 B 723 SER GLU ALA TRP LEU HIS ARG GLN ASN GLU GLU PRO VAL
SEQRES 25 B 723 PHE SER LYS ASP GLY ARG LYS PHE PHE PHE ILE ARG ALA
SEQRES 26 B 723 ILE PRO GLN GLY GLY ARG GLY LYS PHE TYR HIS ILE THR
SEQRES 27 B 723 VAL SER SER SER GLN PRO ASN SER SER ASN ASP ASN ILE
SEQRES 28 B 723 GLN SER ILE THR SER GLY ASP TRP ASP VAL THR LYS ILE
SEQRES 29 B 723 LEU ALA TYR ASP GLU LYS GLY ASN LYS ILE TYR PHE LEU
SEQRES 30 B 723 SER THR GLU ASP LEU PRO ARG ARG ARG GLN LEU TYR SER
SEQRES 31 B 723 ALA ASN THR VAL GLY ASN PHE ASN ARG GLN CYS LEU SER
SEQRES 32 B 723 CYS ASP LEU VAL GLU ASN CYS THR TYR PHE SER ALA SER
SEQRES 33 B 723 PHE SER HIS SER MET ASP PHE PHE LEU LEU LYS CYS GLU
SEQRES 34 B 723 GLY PRO GLY VAL PRO MET VAL THR VAL HIS ASN THR THR
SEQRES 35 B 723 ASP LYS LYS LYS MET PHE ASP LEU GLU THR ASN GLU HIS
SEQRES 36 B 723 VAL LYS LYS ALA ILE ASN ASP ARG GLN MET PRO LYS VAL
SEQRES 37 B 723 GLU TYR ARG ASP ILE GLU ILE ASP ASP TYR ASN LEU PRO
SEQRES 38 B 723 MET GLN ILE LEU LYS PRO ALA THR PHE THR ASP THR THR
SEQRES 39 B 723 HIS TYR PRO LEU LEU LEU VAL VAL ASP GLY THR PRO GLY
SEQRES 40 B 723 SER GLN SER VAL ALA GLU LYS PHE GLU VAL SER TRP GLU
SEQRES 41 B 723 THR VAL MET VAL SER SER HIS GLY ALA VAL VAL VAL LYS
SEQRES 42 B 723 CYS ASP GLY ARG GLY SER GLY PHE GLN GLY THR LYS LEU
SEQRES 43 B 723 LEU HIS GLU VAL ARG ARG ARG LEU GLY LEU LEU GLU GLU
SEQRES 44 B 723 LYS ASP GLN MET GLU ALA VAL ARG THR MET LEU LYS GLU
SEQRES 45 B 723 GLN TYR ILE ASP ARG THR ARG VAL ALA VAL PHE GLY LYS
SEQRES 46 B 723 ASP TYR GLY GLY TYR LEU SER THR TYR ILE LEU PRO ALA
SEQRES 47 B 723 LYS GLY GLU ASN GLN GLY GLN THR PHE THR CYS GLY SER
SEQRES 48 B 723 ALA LEU SER PRO ILE THR ASP PHE LYS LEU TYR ALA SER
SEQRES 49 B 723 ALA PHE SER GLU ARG TYR LEU GLY LEU HIS GLY LEU ASP
SEQRES 50 B 723 ASN ARG ALA TYR GLU MET THR LYS VAL ALA HIS ARG VAL
SEQRES 51 B 723 SER ALA LEU GLU GLU GLN GLN PHE LEU ILE ILE HIS PRO
SEQRES 52 B 723 THR ALA ASP GLU LYS ILE HIS PHE GLN HIS THR ALA GLU
SEQRES 53 B 723 LEU ILE THR GLN LEU ILE ARG GLY LYS ALA ASN TYR SER
SEQRES 54 B 723 LEU GLN ILE TYR PRO ASP GLU SER HIS TYR PHE THR SER
SEQRES 55 B 723 SER SER LEU LYS GLN HIS LEU TYR ARG SER ILE ILE ASN
SEQRES 56 B 723 PHE PHE VAL GLU CYS PHE ARG ILE
SEQRES 1 C 723 GLN LYS LYS LYS VAL THR VAL GLU ASP LEU PHE SER GLU
SEQRES 2 C 723 ASP PHE LYS ILE HIS ASP PRO GLU ALA LYS TRP ILE SER
SEQRES 3 C 723 ASP THR GLU PHE ILE TYR ARG GLU GLN LYS GLY THR VAL
SEQRES 4 C 723 ARG LEU TRP ASN VAL GLU THR ASN THR SER THR VAL LEU
SEQRES 5 C 723 ILE GLU GLY LYS LYS ILE GLU SER LEU ARG ALA ILE ARG
SEQRES 6 C 723 TYR GLU ILE SER PRO ASP ARG GLU TYR ALA LEU PHE SER
SEQRES 7 C 723 TYR ASN VAL GLU PRO ILE TYR GLN HIS SER TYR THR GLY
SEQRES 8 C 723 TYR TYR VAL LEU SER LYS ILE PRO HIS GLY ASP PRO GLN
SEQRES 9 C 723 SER LEU ASP PRO PRO GLU VAL SER ASN ALA LYS LEU GLN
SEQRES 10 C 723 TYR ALA GLY TRP GLY PRO LYS GLY GLN GLN LEU ILE PHE
SEQRES 11 C 723 ILE PHE GLU ASN ASN ILE TYR TYR CYS ALA HIS VAL GLY
SEQRES 12 C 723 LYS GLN ALA ILE ARG VAL VAL SER THR GLY LYS GLU GLY
SEQRES 13 C 723 VAL ILE TYR ASN GLY LEU SER ASP TRP LEU TYR GLU GLU
SEQRES 14 C 723 GLU ILE LEU LYS THR HIS ILE ALA HIS TRP TRP SER PRO
SEQRES 15 C 723 ASP GLY THR ARG LEU ALA TYR ALA ALA ILE ASN ASP SER
SEQRES 16 C 723 ARG VAL PRO ILE MET GLU LEU PRO THR TYR THR GLY SER
SEQRES 17 C 723 ILE TYR PRO THR VAL LYS PRO TYR HIS TYR PRO LYS ALA
SEQRES 18 C 723 GLY SER GLU ASN PRO SER ILE SER LEU HIS VAL ILE GLY
SEQRES 19 C 723 LEU ASN GLY PRO THR HIS ASP LEU GLU MET MET PRO PRO
SEQRES 20 C 723 ASP ASP PRO ARG MET ARG GLU TYR TYR ILE THR MET VAL
SEQRES 21 C 723 LYS TRP ALA THR SER THR LYS VAL ALA VAL THR TRP LEU
SEQRES 22 C 723 ASN ARG ALA GLN ASN VAL SER ILE LEU THR LEU CYS ASP
SEQRES 23 C 723 ALA THR THR GLY VAL CYS THR LYS LYS HIS GLU ASP GLU
SEQRES 24 C 723 SER GLU ALA TRP LEU HIS ARG GLN ASN GLU GLU PRO VAL
SEQRES 25 C 723 PHE SER LYS ASP GLY ARG LYS PHE PHE PHE ILE ARG ALA
SEQRES 26 C 723 ILE PRO GLN GLY GLY ARG GLY LYS PHE TYR HIS ILE THR
SEQRES 27 C 723 VAL SER SER SER GLN PRO ASN SER SER ASN ASP ASN ILE
SEQRES 28 C 723 GLN SER ILE THR SER GLY ASP TRP ASP VAL THR LYS ILE
SEQRES 29 C 723 LEU ALA TYR ASP GLU LYS GLY ASN LYS ILE TYR PHE LEU
SEQRES 30 C 723 SER THR GLU ASP LEU PRO ARG ARG ARG GLN LEU TYR SER
SEQRES 31 C 723 ALA ASN THR VAL GLY ASN PHE ASN ARG GLN CYS LEU SER
SEQRES 32 C 723 CYS ASP LEU VAL GLU ASN CYS THR TYR PHE SER ALA SER
SEQRES 33 C 723 PHE SER HIS SER MET ASP PHE PHE LEU LEU LYS CYS GLU
SEQRES 34 C 723 GLY PRO GLY VAL PRO MET VAL THR VAL HIS ASN THR THR
SEQRES 35 C 723 ASP LYS LYS LYS MET PHE ASP LEU GLU THR ASN GLU HIS
SEQRES 36 C 723 VAL LYS LYS ALA ILE ASN ASP ARG GLN MET PRO LYS VAL
SEQRES 37 C 723 GLU TYR ARG ASP ILE GLU ILE ASP ASP TYR ASN LEU PRO
SEQRES 38 C 723 MET GLN ILE LEU LYS PRO ALA THR PHE THR ASP THR THR
SEQRES 39 C 723 HIS TYR PRO LEU LEU LEU VAL VAL ASP GLY THR PRO GLY
SEQRES 40 C 723 SER GLN SER VAL ALA GLU LYS PHE GLU VAL SER TRP GLU
SEQRES 41 C 723 THR VAL MET VAL SER SER HIS GLY ALA VAL VAL VAL LYS
SEQRES 42 C 723 CYS ASP GLY ARG GLY SER GLY PHE GLN GLY THR LYS LEU
SEQRES 43 C 723 LEU HIS GLU VAL ARG ARG ARG LEU GLY LEU LEU GLU GLU
SEQRES 44 C 723 LYS ASP GLN MET GLU ALA VAL ARG THR MET LEU LYS GLU
SEQRES 45 C 723 GLN TYR ILE ASP ARG THR ARG VAL ALA VAL PHE GLY LYS
SEQRES 46 C 723 ASP TYR GLY GLY TYR LEU SER THR TYR ILE LEU PRO ALA
SEQRES 47 C 723 LYS GLY GLU ASN GLN GLY GLN THR PHE THR CYS GLY SER
SEQRES 48 C 723 ALA LEU SER PRO ILE THR ASP PHE LYS LEU TYR ALA SER
SEQRES 49 C 723 ALA PHE SER GLU ARG TYR LEU GLY LEU HIS GLY LEU ASP
SEQRES 50 C 723 ASN ARG ALA TYR GLU MET THR LYS VAL ALA HIS ARG VAL
SEQRES 51 C 723 SER ALA LEU GLU GLU GLN GLN PHE LEU ILE ILE HIS PRO
SEQRES 52 C 723 THR ALA ASP GLU LYS ILE HIS PHE GLN HIS THR ALA GLU
SEQRES 53 C 723 LEU ILE THR GLN LEU ILE ARG GLY LYS ALA ASN TYR SER
SEQRES 54 C 723 LEU GLN ILE TYR PRO ASP GLU SER HIS TYR PHE THR SER
SEQRES 55 C 723 SER SER LEU LYS GLN HIS LEU TYR ARG SER ILE ILE ASN
SEQRES 56 C 723 PHE PHE VAL GLU CYS PHE ARG ILE
SEQRES 1 D 723 GLN LYS LYS LYS VAL THR VAL GLU ASP LEU PHE SER GLU
SEQRES 2 D 723 ASP PHE LYS ILE HIS ASP PRO GLU ALA LYS TRP ILE SER
SEQRES 3 D 723 ASP THR GLU PHE ILE TYR ARG GLU GLN LYS GLY THR VAL
SEQRES 4 D 723 ARG LEU TRP ASN VAL GLU THR ASN THR SER THR VAL LEU
SEQRES 5 D 723 ILE GLU GLY LYS LYS ILE GLU SER LEU ARG ALA ILE ARG
SEQRES 6 D 723 TYR GLU ILE SER PRO ASP ARG GLU TYR ALA LEU PHE SER
SEQRES 7 D 723 TYR ASN VAL GLU PRO ILE TYR GLN HIS SER TYR THR GLY
SEQRES 8 D 723 TYR TYR VAL LEU SER LYS ILE PRO HIS GLY ASP PRO GLN
SEQRES 9 D 723 SER LEU ASP PRO PRO GLU VAL SER ASN ALA LYS LEU GLN
SEQRES 10 D 723 TYR ALA GLY TRP GLY PRO LYS GLY GLN GLN LEU ILE PHE
SEQRES 11 D 723 ILE PHE GLU ASN ASN ILE TYR TYR CYS ALA HIS VAL GLY
SEQRES 12 D 723 LYS GLN ALA ILE ARG VAL VAL SER THR GLY LYS GLU GLY
SEQRES 13 D 723 VAL ILE TYR ASN GLY LEU SER ASP TRP LEU TYR GLU GLU
SEQRES 14 D 723 GLU ILE LEU LYS THR HIS ILE ALA HIS TRP TRP SER PRO
SEQRES 15 D 723 ASP GLY THR ARG LEU ALA TYR ALA ALA ILE ASN ASP SER
SEQRES 16 D 723 ARG VAL PRO ILE MET GLU LEU PRO THR TYR THR GLY SER
SEQRES 17 D 723 ILE TYR PRO THR VAL LYS PRO TYR HIS TYR PRO LYS ALA
SEQRES 18 D 723 GLY SER GLU ASN PRO SER ILE SER LEU HIS VAL ILE GLY
SEQRES 19 D 723 LEU ASN GLY PRO THR HIS ASP LEU GLU MET MET PRO PRO
SEQRES 20 D 723 ASP ASP PRO ARG MET ARG GLU TYR TYR ILE THR MET VAL
SEQRES 21 D 723 LYS TRP ALA THR SER THR LYS VAL ALA VAL THR TRP LEU
SEQRES 22 D 723 ASN ARG ALA GLN ASN VAL SER ILE LEU THR LEU CYS ASP
SEQRES 23 D 723 ALA THR THR GLY VAL CYS THR LYS LYS HIS GLU ASP GLU
SEQRES 24 D 723 SER GLU ALA TRP LEU HIS ARG GLN ASN GLU GLU PRO VAL
SEQRES 25 D 723 PHE SER LYS ASP GLY ARG LYS PHE PHE PHE ILE ARG ALA
SEQRES 26 D 723 ILE PRO GLN GLY GLY ARG GLY LYS PHE TYR HIS ILE THR
SEQRES 27 D 723 VAL SER SER SER GLN PRO ASN SER SER ASN ASP ASN ILE
SEQRES 28 D 723 GLN SER ILE THR SER GLY ASP TRP ASP VAL THR LYS ILE
SEQRES 29 D 723 LEU ALA TYR ASP GLU LYS GLY ASN LYS ILE TYR PHE LEU
SEQRES 30 D 723 SER THR GLU ASP LEU PRO ARG ARG ARG GLN LEU TYR SER
SEQRES 31 D 723 ALA ASN THR VAL GLY ASN PHE ASN ARG GLN CYS LEU SER
SEQRES 32 D 723 CYS ASP LEU VAL GLU ASN CYS THR TYR PHE SER ALA SER
SEQRES 33 D 723 PHE SER HIS SER MET ASP PHE PHE LEU LEU LYS CYS GLU
SEQRES 34 D 723 GLY PRO GLY VAL PRO MET VAL THR VAL HIS ASN THR THR
SEQRES 35 D 723 ASP LYS LYS LYS MET PHE ASP LEU GLU THR ASN GLU HIS
SEQRES 36 D 723 VAL LYS LYS ALA ILE ASN ASP ARG GLN MET PRO LYS VAL
SEQRES 37 D 723 GLU TYR ARG ASP ILE GLU ILE ASP ASP TYR ASN LEU PRO
SEQRES 38 D 723 MET GLN ILE LEU LYS PRO ALA THR PHE THR ASP THR THR
SEQRES 39 D 723 HIS TYR PRO LEU LEU LEU VAL VAL ASP GLY THR PRO GLY
SEQRES 40 D 723 SER GLN SER VAL ALA GLU LYS PHE GLU VAL SER TRP GLU
SEQRES 41 D 723 THR VAL MET VAL SER SER HIS GLY ALA VAL VAL VAL LYS
SEQRES 42 D 723 CYS ASP GLY ARG GLY SER GLY PHE GLN GLY THR LYS LEU
SEQRES 43 D 723 LEU HIS GLU VAL ARG ARG ARG LEU GLY LEU LEU GLU GLU
SEQRES 44 D 723 LYS ASP GLN MET GLU ALA VAL ARG THR MET LEU LYS GLU
SEQRES 45 D 723 GLN TYR ILE ASP ARG THR ARG VAL ALA VAL PHE GLY LYS
SEQRES 46 D 723 ASP TYR GLY GLY TYR LEU SER THR TYR ILE LEU PRO ALA
SEQRES 47 D 723 LYS GLY GLU ASN GLN GLY GLN THR PHE THR CYS GLY SER
SEQRES 48 D 723 ALA LEU SER PRO ILE THR ASP PHE LYS LEU TYR ALA SER
SEQRES 49 D 723 ALA PHE SER GLU ARG TYR LEU GLY LEU HIS GLY LEU ASP
SEQRES 50 D 723 ASN ARG ALA TYR GLU MET THR LYS VAL ALA HIS ARG VAL
SEQRES 51 D 723 SER ALA LEU GLU GLU GLN GLN PHE LEU ILE ILE HIS PRO
SEQRES 52 D 723 THR ALA ASP GLU LYS ILE HIS PHE GLN HIS THR ALA GLU
SEQRES 53 D 723 LEU ILE THR GLN LEU ILE ARG GLY LYS ALA ASN TYR SER
SEQRES 54 D 723 LEU GLN ILE TYR PRO ASP GLU SER HIS TYR PHE THR SER
SEQRES 55 D 723 SER SER LEU LYS GLN HIS LEU TYR ARG SER ILE ILE ASN
SEQRES 56 D 723 PHE PHE VAL GLU CYS PHE ARG ILE
MODRES 1XFD ASN A 173 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN A 319 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN A 404 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN A 535 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN A 566 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN A 813 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN B 173 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN B 319 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN B 404 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN B 535 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN B 566 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN B 813 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN C 173 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN C 319 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN C 404 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN C 535 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN C 813 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN D 173 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN D 319 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN D 404 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN D 535 ASN GLYCOSYLATION SITE
MODRES 1XFD ASN D 813 ASN GLYCOSYLATION SITE
HET NAG A1319 14
HET NAG A2319 14
HET MAN A3319 11
HET NAG A1173 14
HET NAG A2173 14
HET MAN A3173 11
HET MAN A4173 11
HET NAG A1404 14
HET NAG A2404 14
HET MAN A3404 11
HET NAG A1813 14
HET NAG A2813 14
HET MAN A3813 11
HET MAN A4813 11
HET NAG A1535 14
HET NAG A2535 14
HET MAN A3535 11
HET NAG A1566 14
HET NAG A2566 14
HET NAG B1319 14
HET NAG B2319 14
HET MAN B3319 11
HET NAG B1173 14
HET NAG B2173 14
HET MAN B3173 11
HET NAG B1404 14
HET NAG B2404 14
HET NAG B1813 14
HET NAG B2813 14
HET MAN B3813 11
HET NAG B1535 14
HET NAG B2535 14
HET NAG B1566 14
HET NAG B2566 14
HET NAG C1319 14
HET NAG C2319 14
HET MAN C3319 11
HET NAG C1173 14
HET NAG C2173 14
HET MAN C3173 11
HET NAG C1404 14
HET NAG C2404 14
HET NAG C1813 14
HET NAG C2813 14
HET MAN C3813 11
HET NAG C1535 14
HET NAG C2535 14
HET NAG D1319 14
HET NAG D2319 14
HET MAN D3319 11
HET NAG D1173 14
HET NAG D2173 14
HET MAN D3173 11
HET NAG D1404 14
HET NAG D2404 14
HET MAN D3404 11
HET MAN D4404 11
HET NAG D1813 14
HET NAG D2813 14
HET MAN D3813 11
HET NAG D1535 14
HET NAG D2535 14
HET MAN D3535 11
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETSYN NAG NAG
FORMUL 5 NAG 44(C8 H15 N1 O6)
FORMUL 5 MAN 19(C6 H12 O6)
FORMUL 27 HOH *51(H2 O1)
HELIX 1 1 THR A 132 PHE A 137 1 6
HELIX 2 2 ASN A 169 ASN A 173 5 5
HELIX 3 3 ASP A 290 GLU A 296 1 7
HELIX 4 4 ASP A 375 ARG A 379 5 5
HELIX 5 5 ASN A 579 ASP A 588 1 10
HELIX 6 6 SER A 644 SER A 652 1 9
HELIX 7 7 GLN A 668 GLU A 675 1 8
HELIX 8 8 LEU A 682 LYS A 697 1 16
HELIX 9 9 ASP A 712 ILE A 721 1 10
HELIX 10 10 ALA A 749 GLY A 758 1 10
HELIX 11 11 VAL A 772 SER A 777 1 6
HELIX 12 12 HIS A 796 GLY A 810 1 15
HELIX 13 13 SER A 828 VAL A 844 1 17
HELIX 14 14 THR B 132 PHE B 137 1 6
HELIX 15 15 ASN B 169 ASN B 173 5 5
HELIX 16 16 ASP B 290 GLU B 296 1 7
HELIX 17 17 ASP B 375 ARG B 379 5 5
HELIX 18 18 ASN B 579 ASP B 588 1 10
HELIX 19 19 SER B 644 SER B 652 1 9
HELIX 20 20 GLN B 668 GLU B 675 1 8
HELIX 21 21 LEU B 682 LYS B 697 1 16
HELIX 22 22 ASP B 712 ILE B 721 1 10
HELIX 23 23 ALA B 749 GLY B 758 1 10
HELIX 24 24 VAL B 772 SER B 777 1 6
HELIX 25 25 HIS B 796 GLY B 810 1 15
HELIX 26 26 SER B 828 VAL B 844 1 17
HELIX 27 27 THR C 132 PHE C 137 1 6
HELIX 28 28 ASN C 169 ASN C 173 5 5
HELIX 29 29 ASP C 290 GLU C 296 1 7
HELIX 30 30 ASP C 375 ARG C 379 5 5
HELIX 31 31 ASN C 579 ASP C 588 1 10
HELIX 32 32 SER C 644 SER C 652 1 9
HELIX 33 33 GLN C 668 GLU C 675 1 8
HELIX 34 34 LEU C 682 LYS C 697 1 16
HELIX 35 35 ASP C 712 ILE C 721 1 10
HELIX 36 36 ALA C 749 GLY C 758 1 10
HELIX 37 37 VAL C 772 SER C 777 1 6
HELIX 38 38 HIS C 796 GLY C 810 1 15
HELIX 39 39 SER C 828 VAL C 844 1 17
HELIX 40 40 THR D 132 PHE D 137 1 6
HELIX 41 41 ASN D 169 ASN D 173 5 5
HELIX 42 42 ASP D 290 GLU D 296 1 7
HELIX 43 43 ASP D 375 ARG D 379 5 5
HELIX 44 44 ASN D 579 ASP D 588 1 10
HELIX 45 45 SER D 644 SER D 652 1 9
HELIX 46 46 GLN D 668 GLU D 675 1 8
HELIX 47 47 LEU D 682 LYS D 697 1 16
HELIX 48 48 ASP D 712 ILE D 721 1 10
HELIX 49 49 ALA D 749 GLY D 758 1 10
HELIX 50 50 VAL D 772 SER D 777 1 6
HELIX 51 51 HIS D 796 GLY D 810 1 15
HELIX 52 52 SER D 828 VAL D 844 1 17
SHEET 1 A 2 VAL A 165 LEU A 167 0
SHEET 2 A 2 THR A 176 ILE A 179 -1 O ILE A 179 N VAL A 165
SHEET 1 B 4 ARG A 191 ILE A 194 0
SHEET 2 B 4 TYR A 200 TYR A 205 -1 O LEU A 202 N GLU A 193
SHEET 3 B 4 TYR A 218 LYS A 223 -1 O VAL A 220 N PHE A 203
SHEET 4 B 4 GLN A 230 SER A 231 -1 O GLN A 230 N LEU A 221
SHEET 1 C 3 LEU A 254 PHE A 258 0
SHEET 2 C 3 ASN A 261 CYS A 265 -1 O CYS A 265 N LEU A 254
SHEET 3 C 3 ILE A 273 VAL A 276 -1 O ILE A 273 N TYR A 264
SHEET 1 D 6 LEU A 368 GLU A 369 0
SHEET 2 D 6 SER A 353 GLY A 360 -1 N VAL A 358 O LEU A 368
SHEET 3 D 6 ARG A 312 ASN A 319 -1 N ASN A 319 O SER A 353
SHEET 4 D 6 ILE A 302 TRP A 306 -1 N TRP A 305 O ALA A 314
SHEET 5 D 6 ILE A 284 LEU A 288 -1 N GLY A 287 O ALA A 303
SHEET 6 D 6 ARG A 312 ASN A 319 -1 O ILE A 318 N TYR A 285
SHEET 1 E 2 ILE A 325 LEU A 328 0
SHEET 2 E 2 LYS A 340 HIS A 343 -1 O LYS A 340 N LEU A 328
SHEET 1 F 4 TYR A 381 TRP A 388 0
SHEET 2 F 4 LYS A 393 ASN A 400 -1 O LEU A 399 N TYR A 382
SHEET 3 F 4 VAL A 405 ASP A 412 -1 O THR A 409 N VAL A 396
SHEET 4 F 4 CYS A 418 GLU A 425 -1 O ASP A 424 N SER A 406
SHEET 1 G 3 VAL A 438 PHE A 439 0
SHEET 2 G 3 PHE A 446 ILE A 452 -1 O PHE A 447 N VAL A 438
SHEET 3 G 3 PHE A 460 SER A 466 -1 O SER A 466 N PHE A 446
SHEET 1 H 3 VAL A 487 ASP A 494 0
SHEET 2 H 3 LYS A 499 SER A 504 -1 O TYR A 501 N LEU A 491
SHEET 3 H 3 GLN A 513 ALA A 517 -1 O TYR A 515 N PHE A 502
SHEET 1 I 4 SER A 540 PHE A 543 0
SHEET 2 I 4 PHE A 549 LYS A 553 -1 O LYS A 553 N SER A 540
SHEET 3 I 4 VAL A 562 ASN A 566 -1 O THR A 563 N LEU A 552
SHEET 4 I 4 LYS A 572 GLU A 577 -1 O GLU A 577 N VAL A 562
SHEET 1 J 2 ILE A 599 ILE A 601 0
SHEET 2 J 2 TYR A 604 LEU A 606 -1 O LEU A 606 N ILE A 599
SHEET 1 K 7 ILE A 610 LEU A 611 0
SHEET 2 K 7 VAL A 656 VAL A 658 -1 O VAL A 657 N LEU A 611
SHEET 3 K 7 TYR A 622 VAL A 627 1 N LEU A 625 O VAL A 656
SHEET 4 K 7 ILE A 701 LYS A 711 1 O ALA A 707 N LEU A 626
SHEET 5 K 7 CYS A 735 LEU A 739 1 O LEU A 739 N GLY A 710
SHEET 6 K 7 GLN A 783 PRO A 789 1 O ILE A 787 N ALA A 738
SHEET 7 K 7 SER A 815 TYR A 819 1 O SER A 815 N ILE A 786
SHEET 1 L 2 VAL B 165 LEU B 167 0
SHEET 2 L 2 THR B 176 ILE B 179 -1 O ILE B 179 N VAL B 165
SHEET 1 M 4 ARG B 191 ILE B 194 0
SHEET 2 M 4 TYR B 200 TYR B 205 -1 O LEU B 202 N GLU B 193
SHEET 3 M 4 TYR B 218 LYS B 223 -1 O VAL B 220 N PHE B 203
SHEET 4 M 4 GLN B 230 SER B 231 -1 O GLN B 230 N LEU B 221
SHEET 1 N 3 LEU B 254 PHE B 258 0
SHEET 2 N 3 ASN B 261 CYS B 265 -1 O CYS B 265 N LEU B 254
SHEET 3 N 3 ILE B 273 VAL B 276 -1 O ILE B 273 N TYR B 264
SHEET 1 O 6 LEU B 368 GLU B 369 0
SHEET 2 O 6 SER B 353 GLY B 360 -1 N VAL B 358 O LEU B 368
SHEET 3 O 6 ARG B 312 ASN B 319 -1 N ASN B 319 O SER B 353
SHEET 4 O 6 ILE B 302 TRP B 306 -1 N TRP B 305 O ALA B 314
SHEET 5 O 6 ILE B 284 LEU B 288 -1 N GLY B 287 O ALA B 303
SHEET 6 O 6 ARG B 312 ASN B 319 -1 O ILE B 318 N TYR B 285
SHEET 1 P 2 ILE B 325 LEU B 328 0
SHEET 2 P 2 LYS B 340 HIS B 343 -1 O LYS B 340 N LEU B 328
SHEET 1 Q 4 TYR B 381 TRP B 388 0
SHEET 2 Q 4 LYS B 393 ASN B 400 -1 O LEU B 399 N TYR B 382
SHEET 3 Q 4 VAL B 405 ASP B 412 -1 O THR B 409 N VAL B 396
SHEET 4 Q 4 CYS B 418 GLU B 425 -1 O ASP B 424 N SER B 406
SHEET 1 R 3 VAL B 438 PHE B 439 0
SHEET 2 R 3 PHE B 446 ILE B 452 -1 O PHE B 447 N VAL B 438
SHEET 3 R 3 PHE B 460 SER B 466 -1 O SER B 466 N PHE B 446
SHEET 1 S 3 VAL B 487 ASP B 494 0
SHEET 2 S 3 LYS B 499 SER B 504 -1 O TYR B 501 N LEU B 491
SHEET 3 S 3 GLN B 513 ALA B 517 -1 O TYR B 515 N PHE B 502
SHEET 1 T 4 SER B 540 PHE B 543 0
SHEET 2 T 4 PHE B 549 LYS B 553 -1 O LYS B 553 N SER B 540
SHEET 3 T 4 VAL B 562 ASN B 566 -1 O THR B 563 N LEU B 552
SHEET 4 T 4 LYS B 572 GLU B 577 -1 O GLU B 577 N VAL B 562
SHEET 1 U 2 ILE B 599 ILE B 601 0
SHEET 2 U 2 TYR B 604 LEU B 606 -1 O LEU B 606 N ILE B 599
SHEET 1 V 7 ILE B 610 LEU B 611 0
SHEET 2 V 7 VAL B 656 VAL B 658 -1 O VAL B 657 N LEU B 611
SHEET 3 V 7 TYR B 622 VAL B 627 1 N LEU B 625 O VAL B 656
SHEET 4 V 7 ILE B 701 LYS B 711 1 O ALA B 707 N LEU B 624
SHEET 5 V 7 CYS B 735 LEU B 739 1 O LEU B 739 N GLY B 710
SHEET 6 V 7 GLN B 783 PRO B 789 1 O ILE B 787 N ALA B 738
SHEET 7 V 7 SER B 815 TYR B 819 1 O SER B 815 N ILE B 786
SHEET 1 W 2 VAL C 165 LEU C 167 0
SHEET 2 W 2 THR C 176 ILE C 179 -1 O ILE C 179 N VAL C 165
SHEET 1 X 4 ARG C 191 ILE C 194 0
SHEET 2 X 4 TYR C 200 TYR C 205 -1 O LEU C 202 N GLU C 193
SHEET 3 X 4 TYR C 218 LYS C 223 -1 O TYR C 218 N TYR C 205
SHEET 4 X 4 GLN C 230 SER C 231 -1 O GLN C 230 N LEU C 221
SHEET 1 Y 3 LEU C 254 PHE C 258 0
SHEET 2 Y 3 ASN C 261 CYS C 265 -1 O CYS C 265 N LEU C 254
SHEET 3 Y 3 ILE C 273 VAL C 276 -1 O ILE C 273 N TYR C 264
SHEET 1 Z 6 LEU C 368 GLU C 369 0
SHEET 2 Z 6 SER C 353 GLY C 360 -1 N VAL C 358 O LEU C 368
SHEET 3 Z 6 ARG C 312 ASN C 319 -1 N ASN C 319 O SER C 353
SHEET 4 Z 6 ILE C 302 TRP C 306 -1 N TRP C 305 O ALA C 314
SHEET 5 Z 6 ILE C 284 LEU C 288 -1 N GLY C 287 O ALA C 303
SHEET 6 Z 6 ARG C 312 ASN C 319 -1 O ILE C 318 N TYR C 285
SHEET 1 AA 2 ILE C 325 LEU C 328 0
SHEET 2 AA 2 LYS C 340 HIS C 343 -1 O LYS C 340 N LEU C 328
SHEET 1 AB 4 TYR C 381 TRP C 388 0
SHEET 2 AB 4 LYS C 393 ASN C 400 -1 O LEU C 399 N TYR C 382
SHEET 3 AB 4 VAL C 405 ASP C 412 -1 O THR C 409 N VAL C 396
SHEET 4 AB 4 CYS C 418 GLU C 425 -1 O ASP C 424 N SER C 406
SHEET 1 AC 3 VAL C 438 PHE C 439 0
SHEET 2 AC 3 PHE C 446 ILE C 452 -1 O PHE C 447 N VAL C 438
SHEET 3 AC 3 PHE C 460 SER C 466 -1 O SER C 466 N PHE C 446
SHEET 1 AD 3 VAL C 487 ASP C 494 0
SHEET 2 AD 3 LYS C 499 SER C 504 -1 O TYR C 501 N LEU C 491
SHEET 3 AD 3 GLN C 513 ALA C 517 -1 O TYR C 515 N PHE C 502
SHEET 1 AE 4 SER C 540 PHE C 543 0
SHEET 2 AE 4 PHE C 549 LYS C 553 -1 O LYS C 553 N SER C 540
SHEET 3 AE 4 VAL C 562 ASN C 566 -1 O THR C 563 N LEU C 552
SHEET 4 AE 4 LYS C 572 GLU C 577 -1 O GLU C 577 N VAL C 562
SHEET 1 AF 2 ILE C 599 ILE C 601 0
SHEET 2 AF 2 TYR C 604 LEU C 606 -1 O LEU C 606 N ILE C 599
SHEET 1 AG 7 ILE C 610 LEU C 611 0
SHEET 2 AG 7 VAL C 656 VAL C 658 -1 O VAL C 657 N LEU C 611
SHEET 3 AG 7 TYR C 622 VAL C 627 1 N LEU C 625 O VAL C 656
SHEET 4 AG 7 ILE C 701 LYS C 711 1 O ALA C 707 N LEU C 626
SHEET 5 AG 7 CYS C 735 LEU C 739 1 O LEU C 739 N GLY C 710
SHEET 6 AG 7 GLN C 783 PRO C 789 1 O GLN C 783 N GLY C 736
SHEET 7 AG 7 SER C 815 TYR C 819 1 O SER C 815 N ILE C 786
SHEET 1 AH 2 VAL D 165 LEU D 167 0
SHEET 2 AH 2 THR D 176 ILE D 179 -1 O ILE D 179 N VAL D 165
SHEET 1 AI 4 ARG D 191 ILE D 194 0
SHEET 2 AI 4 TYR D 200 TYR D 205 -1 O LEU D 202 N GLU D 193
SHEET 3 AI 4 TYR D 218 LYS D 223 -1 O VAL D 220 N PHE D 203
SHEET 4 AI 4 GLN D 230 SER D 231 -1 O GLN D 230 N LEU D 221
SHEET 1 AJ 3 LEU D 254 PHE D 258 0
SHEET 2 AJ 3 ASN D 261 CYS D 265 -1 O CYS D 265 N LEU D 254
SHEET 3 AJ 3 ILE D 273 VAL D 276 -1 O ILE D 273 N TYR D 264
SHEET 1 AK 6 LEU D 368 GLU D 369 0
SHEET 2 AK 6 SER D 353 GLY D 360 -1 N VAL D 358 O LEU D 368
SHEET 3 AK 6 ARG D 312 ASN D 319 -1 N ASN D 319 O SER D 353
SHEET 4 AK 6 ILE D 302 TRP D 306 -1 N TRP D 305 O ALA D 314
SHEET 5 AK 6 ILE D 284 LEU D 288 -1 N GLY D 287 O ALA D 303
SHEET 6 AK 6 ARG D 312 ASN D 319 -1 O ILE D 318 N TYR D 285
SHEET 1 AL 2 ILE D 325 LEU D 328 0
SHEET 2 AL 2 LYS D 340 HIS D 343 -1 O LYS D 340 N LEU D 328
SHEET 1 AM 4 TYR D 381 TRP D 388 0
SHEET 2 AM 4 LYS D 393 ASN D 400 -1 O LEU D 399 N TYR D 382
SHEET 3 AM 4 VAL D 405 ASP D 412 -1 O THR D 409 N VAL D 396
SHEET 4 AM 4 CYS D 418 GLU D 425 -1 O ASP D 424 N SER D 406
SHEET 1 AN 3 VAL D 438 PHE D 439 0
SHEET 2 AN 3 PHE D 446 ILE D 452 -1 O PHE D 447 N VAL D 438
SHEET 3 AN 3 PHE D 460 SER D 466 -1 O SER D 466 N PHE D 446
SHEET 1 AO 3 VAL D 487 ASP D 494 0
SHEET 2 AO 3 LYS D 499 SER D 504 -1 O TYR D 501 N LEU D 491
SHEET 3 AO 3 GLN D 513 ALA D 517 -1 O TYR D 515 N PHE D 502
SHEET 1 AP 4 SER D 540 PHE D 543 0
SHEET 2 AP 4 PHE D 549 LYS D 553 -1 O LYS D 553 N SER D 540
SHEET 3 AP 4 VAL D 562 ASN D 566 -1 O THR D 563 N LEU D 552
SHEET 4 AP 4 LYS D 572 GLU D 577 -1 O GLU D 577 N VAL D 562
SHEET 1 AQ 2 ILE D 599 ILE D 601 0
SHEET 2 AQ 2 TYR D 604 LEU D 606 -1 O LEU D 606 N ILE D 599
SHEET 1 AR 7 ILE D 610 LEU D 611 0
SHEET 2 AR 7 VAL D 656 VAL D 658 -1 O VAL D 657 N LEU D 611
SHEET 3 AR 7 TYR D 622 VAL D 627 1 N LEU D 625 O VAL D 656
SHEET 4 AR 7 ILE D 701 LYS D 711 1 O ALA D 707 N LEU D 626
SHEET 5 AR 7 CYS D 735 LEU D 739 1 O LEU D 739 N GLY D 710
SHEET 6 AR 7 GLN D 783 PRO D 789 1 O ILE D 787 N ALA D 738
SHEET 7 AR 7 SER D 815 TYR D 819 1 O SER D 815 N ILE D 786
SSBOND 1 CYS A 411 CYS A 418
SSBOND 2 CYS A 527 CYS A 530
SSBOND 3 CYS A 536 CYS A 554
SSBOND 4 CYS A 735 CYS A 846
SSBOND 5 CYS B 411 CYS B 418
SSBOND 6 CYS B 527 CYS B 530
SSBOND 7 CYS B 536 CYS B 554
SSBOND 8 CYS B 735 CYS B 846
SSBOND 9 CYS C 411 CYS C 418
SSBOND 10 CYS C 527 CYS C 530
SSBOND 11 CYS C 536 CYS C 554
SSBOND 12 CYS C 735 CYS C 846
SSBOND 13 CYS D 411 CYS D 418
SSBOND 14 CYS D 527 CYS D 530
SSBOND 15 CYS D 536 CYS D 554
SSBOND 16 CYS D 735 CYS D 846
LINK ND2 ASN A 173 C1 NAG A1173
LINK ND2 ASN A 319 C1 NAG A1319
LINK ND2 ASN A 404 C1 NAG A1404
LINK ND2 ASN A 535 C1 NAG A1535
LINK ND2 ASN A 566 C1 NAG A1566
LINK ND2 ASN A 813 C1 NAG A1813
LINK ND2 ASN B 173 C1 NAG B1173
LINK ND2 ASN B 319 C1 NAG B1319
LINK ND2 ASN B 404 C1 NAG B1404
LINK ND2 ASN B 535 C1 NAG B1535
LINK ND2 ASN B 566 C1 NAG B1566
LINK ND2 ASN B 813 C1 NAG B1813
LINK ND2 ASN C 173 C1 NAG C1173
LINK ND2 ASN C 319 C1 NAG C1319
LINK ND2 ASN C 404 C1 NAG C1404
LINK ND2 ASN C 535 C1 NAG C1535
LINK ND2 ASN C 813 C1 NAG C1813
LINK ND2 ASN D 173 C1 NAG D1173
LINK ND2 ASN D 319 C1 NAG D1319
LINK ND2 ASN D 404 C1 NAG D1404
LINK ND2 ASN D 535 C1 NAG D1535
LINK ND2 ASN D 813 C1 NAG D1813
LINK O4 NAG A1319 C1 NAG A2319
LINK O4 NAG A2319 C1 MAN A3319
LINK O4 NAG A1173 C1 NAG A2173
LINK O4 NAG A2173 C1 MAN A3173
LINK O4 MAN A3173 C1 MAN A4173
LINK O4 NAG A1404 C1 NAG A2404
LINK O4 NAG A2404 C1 MAN A3404
LINK O4 NAG A1813 C1 NAG A2813
LINK O4 NAG A2813 C1 MAN A3813
LINK O4 MAN A3813 C1 MAN A4813
LINK O4 NAG A1535 C1 NAG A2535
LINK O4 NAG A2535 C1 MAN A3535
LINK O4 NAG A1566 C1 NAG A2566
LINK O4 NAG B1319 C1 NAG B2319
LINK O4 NAG B2319 C1 MAN B3319
LINK O4 NAG B1173 C1 NAG B2173
LINK O4 NAG B2173 C1 MAN B3173
LINK O4 NAG B1404 C1 NAG B2404
LINK O4 NAG B1813 C1 NAG B2813
LINK O4 NAG B2813 C1 MAN B3813
LINK O4 NAG B1535 C1 NAG B2535
LINK O4 NAG B1566 C1 NAG B2566
LINK O4 NAG C1319 C1 NAG C2319
LINK O4 NAG C2319 C1 MAN C3319
LINK O4 NAG C1173 C1 NAG C2173
LINK O4 NAG C2173 C1 MAN C3173
LINK O4 NAG C1404 C1 NAG C2404
LINK O4 NAG C1813 C1 NAG C2813
LINK O4 NAG C2813 C1 MAN C3813
LINK O4 NAG C1535 C1 NAG C2535
LINK O4 NAG D1319 C1 NAG D2319
LINK O4 NAG D2319 C1 MAN D3319
LINK O4 NAG D1173 C1 NAG D2173
LINK O4 NAG D2173 C1 MAN D3173
LINK O4 NAG D1404 C1 NAG D2404
LINK O4 NAG D2404 C1 MAN D3404
LINK O4 MAN D3404 C1 MAN D4404
LINK O4 NAG D1813 C1 NAG D2813
LINK O4 NAG D2813 C1 MAN D3813
LINK O4 NAG D1535 C1 NAG D2535
LINK O4 NAG D2535 C1 MAN D3535
CISPEP 1 GLY A 556 PRO A 557 0 -0.26
CISPEP 2 GLY B 556 PRO B 557 0 -0.15
CISPEP 3 GLY C 556 PRO C 557 0 -0.21
CISPEP 4 GLY D 556 PRO D 557 0 -0.06
CRYST1 68.980 170.230 159.316 90.00 92.11 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014497 0.000000 0.000534 0.00000
SCALE2 0.000000 0.005874 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006281 0.00000
TER 5838 ILE A 849
TER 11676 ILE B 849
TER 17514 ILE C 849
TER 23352 ILE D 849
MASTER 494 0 63 52 160 0 0 624224 4 879 224
END |