HEADER IMMUNE SYSTEM 20-MAY-01 1J88
TITLE HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), TETRAGONAL
TITLE 2 CRYSTAL FORM 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A, B, C, D, E;
COMPND 5 FRAGMENT: EXTRACELLULAR FRAGMENT;
COMPND 6 SYNONYM: FC(EPSILON)RI(ALPHA); IGE FC RECEPTOR, ALPHA-SUBUNIT; FC-
COMPND 7 EPSILON RI-ALPHA;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: GLYCOSYLATED PROTEIN, CHAIN A BY SUGARS F, B BY SUGARS
COMPND 10 G, C BY SUGARS H, D BY SUGARS I, E BY SUGARS J
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: LDLD.LEC1;
SOURCE 9 EXPRESSION_SYSTEM_ORGAN: OVARY
KEYWDS IMMUNE SYSTEM, FC RECEPTOR, IGE RECEPTOR, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.GARMAN,S.SECHI,J.P.KINET,T.S.JARDETZKY
REVDAT 6 16-AUG-23 1J88 1 HETSYN
REVDAT 5 29-JUL-20 1J88 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 13-JUL-11 1J88 1 VERSN
REVDAT 3 24-FEB-09 1J88 1 VERSN
REVDAT 2 01-APR-03 1J88 1 JRNL
REVDAT 1 29-AUG-01 1J88 0
JRNL AUTH S.C.GARMAN,S.SECHI,J.P.KINET,T.S.JARDETZKY
JRNL TITL THE ANALYSIS OF THE HUMAN HIGH AFFINITY IGE RECEPTOR FC
JRNL TITL 2 EPSILON RI ALPHA FROM MULTIPLE CRYSTAL FORMS.
JRNL REF J.MOL.BIOL. V. 311 1049 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11531339
JRNL DOI 10.1006/JMBI.2001.4929
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1760998.430
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 21343
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : SHELLS
REMARK 3 R VALUE (WORKING SET) : 0.262
REMARK 3 FREE R VALUE : 0.310
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1065
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3107
REMARK 3 BIN R VALUE (WORKING SET) : 0.3560
REMARK 3 BIN FREE R VALUE : 0.3930
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 125
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.035
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6905
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 701
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 79.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 126.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.64000
REMARK 3 B22 (A**2) : 2.64000
REMARK 3 B33 (A**2) : -5.28000
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) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : 0.76
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) : 0.85
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
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) : 14.110; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 19.910; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 18.790; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 28.590; 4.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.20
REMARK 3 BSOL : 108.5
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 0.04 ; 300.0
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; 2.0
REMARK 3 GROUP 2 POSITIONAL (A) : 0.04 ; 300.0
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; 2.0
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 300 KCAL/MOL/A^2 NCS RESTRAINTS APPLIED TO ALL PROTEIN ATOMS
REMARK 3 EXCEPT THOSE IN FLEXIBLE LOOPS, IN CRYSTAL CONTACTS, OR WITH
REMARK 3 ATTACHED CARBOHYDRATE. NCS GROUP 1 REPRESENTS DOMAIN 1; GROUP2
REMARK 3 REPRESENTS DOMAIN2.
REMARK 4
REMARK 4 1J88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-96
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.914
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21357
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.36300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: 1F2Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000, AMMONIUM CITRATE, SODIUM
REMARK 280 CHLORIDE, PH 5.6, VAPOR DIFFUSION, HANGING DROP AT 293K, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.37000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.05500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 15.68500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A PROTEIN MONOMER WITH ATTACHED
REMARK 300 CARBOHYDRATE
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, G, H, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, L, M, N
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, O, P, Q
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, R
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL A 1
REMARK 465 PRO A 2
REMARK 465 GLN A 3
REMARK 465 ALA A 172
REMARK 465 VAL B 1
REMARK 465 PRO B 2
REMARK 465 GLN B 3
REMARK 465 ALA B 172
REMARK 465 VAL C 1
REMARK 465 PRO C 2
REMARK 465 GLN C 3
REMARK 465 ALA C 172
REMARK 465 VAL D 1
REMARK 465 PRO D 2
REMARK 465 GLN D 3
REMARK 465 ALA D 172
REMARK 465 VAL E 1
REMARK 465 PRO E 2
REMARK 465 GLN E 3
REMARK 465 ALA E 172
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 NE ARG A 111 O GLY C 28 1554 2.12
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PHE B 31 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 27 159.28 175.97
REMARK 500 SER A 36 61.37 62.01
REMARK 500 ASN A 57 75.06 -9.28
REMARK 500 GLU A 75 150.48 -49.93
REMARK 500 GLU A 99 124.54 -38.58
REMARK 500 ARG A 111 17.39 44.88
REMARK 500 TRP A 113 -171.25 -62.53
REMARK 500 LEU A 127 -51.25 -133.32
REMARK 500 TYR A 131 -80.87 -75.03
REMARK 500 THR A 139 -70.14 -80.17
REMARK 500 TRP A 156 -94.63 63.52
REMARK 500 GLN A 157 12.45 -143.55
REMARK 500 CYS B 26 43.71 -95.66
REMARK 500 ASN B 27 145.29 -170.29
REMARK 500 THR B 49 -30.61 -135.85
REMARK 500 ASN B 57 88.76 -8.60
REMARK 500 PRO B 78 157.45 -36.99
REMARK 500 ARG B 111 18.70 45.90
REMARK 500 TRP B 113 -170.57 -59.99
REMARK 500 LEU B 127 -52.89 -130.79
REMARK 500 TYR B 131 -76.68 -87.74
REMARK 500 ASN B 133 165.85 -42.31
REMARK 500 ILE B 136 109.65 -46.64
REMARK 500 THR B 139 -83.23 -75.77
REMARK 500 TRP B 156 -94.81 64.11
REMARK 500 GLN B 157 12.25 -143.41
REMARK 500 ASN C 29 42.60 17.68
REMARK 500 ASN C 50 151.69 -49.60
REMARK 500 ASN C 57 86.62 -6.75
REMARK 500 PRO C 78 154.51 -44.63
REMARK 500 ARG C 111 18.96 44.87
REMARK 500 TRP C 113 -171.18 -62.06
REMARK 500 LEU C 127 -54.69 -130.26
REMARK 500 TYR C 131 -81.46 -80.33
REMARK 500 ILE C 136 118.98 -37.99
REMARK 500 THR C 139 -73.35 -82.18
REMARK 500 TRP C 156 -93.93 64.69
REMARK 500 GLN C 157 12.67 -144.46
REMARK 500 ASN D 27 -29.70 -140.11
REMARK 500 SER D 35 -63.36 -109.79
REMARK 500 VAL D 56 -168.53 -101.54
REMARK 500 ASN D 57 89.02 -10.54
REMARK 500 GLU D 75 150.13 -44.01
REMARK 500 ARG D 111 18.82 45.91
REMARK 500 TRP D 113 -172.26 -62.16
REMARK 500 LEU D 127 -51.67 -131.37
REMARK 500 HIS D 134 -144.63 -119.53
REMARK 500 THR D 139 -73.10 -72.76
REMARK 500 TRP D 156 -94.12 64.10
REMARK 500 GLN D 157 12.48 -143.98
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR C 129 0.07 SIDE CHAIN
REMARK 500 TYR D 131 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F2Q RELATED DB: PDB
REMARK 900 MONOCLINIC CRYSTAL FORM 1
REMARK 900 RELATED ID: 1F6A RELATED DB: PDB
REMARK 900 COMPLEX WITH IGE-FC C(EPSILON)3-4
REMARK 900 RELATED ID: 1J86 RELATED DB: PDB
REMARK 900 MONOCLINIC CRYSTAL FORM 2
REMARK 900 RELATED ID: 1J87 RELATED DB: PDB
REMARK 900 HEXAGONAL CRYSTAL FORM 1
REMARK 900 RELATED ID: 1J89 RELATED DB: PDB
REMARK 900 TETRAGONAL CRYSTAL FORM 2
DBREF 1J88 A 1 172 UNP P12319 FCEA_HUMAN 26 197
DBREF 1J88 B 1 172 UNP P12319 FCEA_HUMAN 26 197
DBREF 1J88 C 1 172 UNP P12319 FCEA_HUMAN 26 197
DBREF 1J88 D 1 172 UNP P12319 FCEA_HUMAN 26 197
DBREF 1J88 E 1 172 UNP P12319 FCEA_HUMAN 26 197
SEQRES 1 A 172 VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP
SEQRES 2 A 172 ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS
SEQRES 3 A 172 ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP
SEQRES 4 A 172 PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER
SEQRES 5 A 172 LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU
SEQRES 6 A 172 TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO
SEQRES 7 A 172 VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN
SEQRES 8 A 172 ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE
SEQRES 9 A 172 LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS
SEQRES 10 A 172 VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP
SEQRES 11 A 172 TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL
SEQRES 12 A 172 GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP
SEQRES 13 A 172 GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL
SEQRES 14 A 172 ILE LYS ALA
SEQRES 1 B 172 VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP
SEQRES 2 B 172 ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS
SEQRES 3 B 172 ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP
SEQRES 4 B 172 PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER
SEQRES 5 B 172 LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU
SEQRES 6 B 172 TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO
SEQRES 7 B 172 VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN
SEQRES 8 B 172 ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE
SEQRES 9 B 172 LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS
SEQRES 10 B 172 VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP
SEQRES 11 B 172 TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL
SEQRES 12 B 172 GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP
SEQRES 13 B 172 GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL
SEQRES 14 B 172 ILE LYS ALA
SEQRES 1 C 172 VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP
SEQRES 2 C 172 ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS
SEQRES 3 C 172 ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP
SEQRES 4 C 172 PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER
SEQRES 5 C 172 LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU
SEQRES 6 C 172 TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO
SEQRES 7 C 172 VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN
SEQRES 8 C 172 ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE
SEQRES 9 C 172 LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS
SEQRES 10 C 172 VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP
SEQRES 11 C 172 TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL
SEQRES 12 C 172 GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP
SEQRES 13 C 172 GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL
SEQRES 14 C 172 ILE LYS ALA
SEQRES 1 D 172 VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP
SEQRES 2 D 172 ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS
SEQRES 3 D 172 ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP
SEQRES 4 D 172 PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER
SEQRES 5 D 172 LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU
SEQRES 6 D 172 TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO
SEQRES 7 D 172 VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN
SEQRES 8 D 172 ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE
SEQRES 9 D 172 LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS
SEQRES 10 D 172 VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP
SEQRES 11 D 172 TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL
SEQRES 12 D 172 GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP
SEQRES 13 D 172 GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL
SEQRES 14 D 172 ILE LYS ALA
SEQRES 1 E 172 VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP
SEQRES 2 E 172 ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS
SEQRES 3 E 172 ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP
SEQRES 4 E 172 PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER
SEQRES 5 E 172 LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU
SEQRES 6 E 172 TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO
SEQRES 7 E 172 VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN
SEQRES 8 E 172 ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE
SEQRES 9 E 172 LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS
SEQRES 10 E 172 VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP
SEQRES 11 E 172 TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL
SEQRES 12 E 172 GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP
SEQRES 13 E 172 GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL
SEQRES 14 E 172 ILE LYS ALA
MODRES 1J88 ASN E 140 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN A 42 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN C 74 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN B 166 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN A 166 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN D 166 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN E 166 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN C 42 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN C 166 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN C 21 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN E 21 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN A 21 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN D 140 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN B 140 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN E 74 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN D 74 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN B 74 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN A 135 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN D 21 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN C 140 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN E 42 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN A 74 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN B 21 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN C 50 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN D 42 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN A 140 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN A 50 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN D 135 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN B 42 ASN GLYCOSYLATION SITE
MODRES 1J88 ASN B 135 ASN GLYCOSYLATION SITE
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET NAG G 1 14
HET NAG G 2 14
HET MAN G 3 11
HET MAN G 4 11
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET BMA M 3 11
HET NAG N 1 14
HET NAG N 2 14
HET NAG O 1 14
HET NAG O 2 14
HET BMA O 3 11
HET NAG P 1 14
HET NAG P 2 14
HET BMA P 3 11
HET NAG Q 1 14
HET NAG Q 2 14
HET NAG R 1 14
HET NAG R 2 14
HET BMA R 3 11
HET MAN R 4 11
HET NAG A 274 14
HET NAG A 335 14
HET NAG A 340 14
HET NAG B 221 14
HET NAG B 274 14
HET NAG B 335 14
HET NAG B 340 14
HET NAG C 250 14
HET NAG C 274 14
HET NAG C 340 14
HET NAG D 274 14
HET NAG D 335 14
HET NAG D 340 14
HET NAG E 221 14
HET NAG E 274 14
HET NAG E 340 14
HET NAG E 366 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 6 NAG 43(C8 H15 N O6)
FORMUL 6 BMA 6(C6 H12 O6)
FORMUL 7 MAN 3(C6 H12 O6)
HELIX 1 1 LYS A 59 SER A 63 5 5
HELIX 2 2 ARG A 111 TRP A 113 5 3
HELIX 3 3 LYS B 59 SER B 63 5 5
HELIX 4 4 ARG B 111 TRP B 113 5 3
HELIX 5 5 LYS C 59 SER C 63 5 5
HELIX 6 6 ARG C 111 TRP C 113 5 3
HELIX 7 7 LYS D 59 SER D 63 5 5
HELIX 8 8 ARG D 111 TRP D 113 5 3
HELIX 9 9 LYS E 59 SER E 63 5 5
HELIX 10 10 ARG E 111 TRP E 113 5 3
SHEET 1 A 3 SER A 8 ASN A 10 0
SHEET 2 A 3 VAL A 22 THR A 25 -1 N THR A 23 O ASN A 10
SHEET 3 A 3 SER A 52 ILE A 55 -1 O LEU A 53 N LEU A 24
SHEET 1 B 3 ARG A 15 PHE A 17 0
SHEET 2 B 3 VAL A 79 PHE A 84 1 O GLU A 82 N ILE A 16
SHEET 3 B 3 GLY A 64 TYR A 66 -1 O GLY A 64 N LEU A 81
SHEET 1 C 3 SER A 44 LEU A 45 0
SHEET 2 C 3 LYS A 38 HIS A 41 -1 N HIS A 41 O SER A 44
SHEET 3 C 3 CYS A 68 GLN A 69 -1 O GLN A 69 N LYS A 38
SHEET 1 D 3 LEU A 88 ALA A 92 0
SHEET 2 D 3 LEU A 103 GLY A 109 -1 O ARG A 106 N GLN A 91
SHEET 3 D 3 SER A 137 ILE A 138 -1 O ILE A 138 N LEU A 103
SHEET 1 E 4 GLU A 125 GLU A 132 0
SHEET 2 E 4 VAL A 115 LYS A 122 -1 N LYS A 117 O TYR A 131
SHEET 3 E 4 GLY A 147 VAL A 155 -1 O TYR A 150 N TYR A 121
SHEET 4 E 4 LEU A 158 GLU A 161 -1 N LEU A 158 O VAL A 155
SHEET 1 F 5 GLU A 125 GLU A 132 0
SHEET 2 F 5 VAL A 115 LYS A 122 -1 N LYS A 117 O TYR A 131
SHEET 3 F 5 GLY A 147 VAL A 155 -1 O TYR A 150 N TYR A 121
SHEET 4 F 5 LEU A 165 ILE A 170 -1 N LEU A 165 O TYR A 149
SHEET 5 F 5 VAL A 96 MET A 98 1 N VAL A 97 O THR A 168
SHEET 1 G 3 SER B 8 ASN B 10 0
SHEET 2 G 3 VAL B 22 THR B 25 -1 N THR B 23 O ASN B 10
SHEET 3 G 3 SER B 52 ILE B 55 -1 O LEU B 53 N LEU B 24
SHEET 1 H 3 ARG B 15 PHE B 17 0
SHEET 2 H 3 VAL B 79 PHE B 84 1 O GLU B 82 N ILE B 16
SHEET 3 H 3 GLY B 64 TYR B 66 -1 N GLY B 64 O LEU B 81
SHEET 1 I 3 SER B 44 LEU B 45 0
SHEET 2 I 3 LYS B 38 HIS B 41 -1 N HIS B 41 O SER B 44
SHEET 3 I 3 CYS B 68 GLN B 69 -1 O GLN B 69 N LYS B 38
SHEET 1 J 3 LEU B 88 ALA B 92 0
SHEET 2 J 3 LEU B 103 GLY B 109 -1 O ARG B 106 N GLN B 91
SHEET 3 J 3 SER B 137 ILE B 138 -1 O ILE B 138 N LEU B 103
SHEET 1 K 4 GLU B 125 GLU B 132 0
SHEET 2 K 4 VAL B 115 LYS B 122 -1 N LYS B 117 O TYR B 131
SHEET 3 K 4 GLY B 147 VAL B 155 -1 O TYR B 150 N TYR B 121
SHEET 4 K 4 LEU B 158 GLU B 161 -1 O LEU B 158 N VAL B 155
SHEET 1 L 5 GLU B 125 GLU B 132 0
SHEET 2 L 5 VAL B 115 LYS B 122 -1 N LYS B 117 O TYR B 131
SHEET 3 L 5 GLY B 147 VAL B 155 -1 O TYR B 150 N TYR B 121
SHEET 4 L 5 LEU B 165 ILE B 170 -1 N LEU B 165 O TYR B 149
SHEET 5 L 5 VAL B 96 MET B 98 1 N VAL B 97 O THR B 168
SHEET 1 M 3 SER C 8 ASN C 10 0
SHEET 2 M 3 VAL C 22 THR C 25 -1 N THR C 23 O ASN C 10
SHEET 3 M 3 SER C 52 ILE C 55 -1 N LEU C 53 O LEU C 24
SHEET 1 N 3 ARG C 15 PHE C 17 0
SHEET 2 N 3 VAL C 79 PHE C 84 1 O GLU C 82 N ILE C 16
SHEET 3 N 3 GLY C 64 TYR C 66 -1 O GLY C 64 N LEU C 81
SHEET 1 O 3 SER C 44 LEU C 45 0
SHEET 2 O 3 LYS C 38 HIS C 41 -1 N HIS C 41 O SER C 44
SHEET 3 O 3 CYS C 68 GLN C 69 -1 O GLN C 69 N LYS C 38
SHEET 1 P 3 LEU C 88 ALA C 92 0
SHEET 2 P 3 LEU C 103 GLY C 109 -1 O ARG C 106 N GLN C 91
SHEET 3 P 3 SER C 137 ILE C 138 -1 O ILE C 138 N LEU C 103
SHEET 1 Q 4 GLU C 125 GLU C 132 0
SHEET 2 Q 4 VAL C 115 LYS C 122 -1 N LYS C 117 O TYR C 131
SHEET 3 Q 4 GLY C 147 VAL C 155 -1 O TYR C 150 N TYR C 121
SHEET 4 Q 4 LEU C 158 GLU C 161 -1 N LEU C 158 O VAL C 155
SHEET 1 R 5 GLU C 125 GLU C 132 0
SHEET 2 R 5 VAL C 115 LYS C 122 -1 N LYS C 117 O TYR C 131
SHEET 3 R 5 GLY C 147 VAL C 155 -1 O TYR C 150 N TYR C 121
SHEET 4 R 5 LEU C 165 ILE C 170 -1 N LEU C 165 O TYR C 149
SHEET 5 R 5 VAL C 96 MET C 98 1 N VAL C 97 O THR C 168
SHEET 1 S 3 SER D 8 ASN D 10 0
SHEET 2 S 3 VAL D 22 THR D 25 -1 N THR D 23 O ASN D 10
SHEET 3 S 3 SER D 52 ILE D 55 -1 O LEU D 53 N LEU D 24
SHEET 1 T 3 ARG D 15 PHE D 17 0
SHEET 2 T 3 VAL D 79 PHE D 84 1 O GLU D 82 N ILE D 16
SHEET 3 T 3 GLY D 64 TYR D 66 -1 O GLY D 64 N LEU D 81
SHEET 1 U 3 SER D 44 LEU D 45 0
SHEET 2 U 3 LYS D 38 HIS D 41 -1 N HIS D 41 O SER D 44
SHEET 3 U 3 CYS D 68 GLN D 69 -1 O GLN D 69 N LYS D 38
SHEET 1 V 3 LEU D 88 ALA D 92 0
SHEET 2 V 3 LEU D 103 GLY D 109 -1 O ARG D 106 N GLN D 91
SHEET 3 V 3 SER D 137 ILE D 138 -1 O ILE D 138 N LEU D 103
SHEET 1 W 4 GLU D 125 GLU D 132 0
SHEET 2 W 4 VAL D 115 LYS D 122 -1 N LYS D 117 O TYR D 131
SHEET 3 W 4 GLY D 147 VAL D 155 -1 O TYR D 150 N TYR D 121
SHEET 4 W 4 LEU D 158 GLU D 161 -1 N LEU D 158 O VAL D 155
SHEET 1 X 5 GLU D 125 GLU D 132 0
SHEET 2 X 5 VAL D 115 LYS D 122 -1 N LYS D 117 O TYR D 131
SHEET 3 X 5 GLY D 147 VAL D 155 -1 O TYR D 150 N TYR D 121
SHEET 4 X 5 LEU D 165 ILE D 170 -1 N LEU D 165 O TYR D 149
SHEET 5 X 5 VAL D 96 MET D 98 1 N VAL D 97 O THR D 168
SHEET 1 Y 3 SER E 8 ASN E 10 0
SHEET 2 Y 3 VAL E 22 THR E 25 -1 N THR E 23 O ASN E 10
SHEET 3 Y 3 SER E 52 ILE E 55 -1 O LEU E 53 N LEU E 24
SHEET 1 Z 3 ARG E 15 PHE E 17 0
SHEET 2 Z 3 VAL E 79 PHE E 84 1 O GLU E 82 N ILE E 16
SHEET 3 Z 3 GLY E 64 TYR E 66 -1 N GLY E 64 O LEU E 81
SHEET 1 AA 3 SER E 44 LEU E 45 0
SHEET 2 AA 3 LYS E 38 HIS E 41 -1 N HIS E 41 O SER E 44
SHEET 3 AA 3 CYS E 68 GLN E 69 -1 O GLN E 69 N LYS E 38
SHEET 1 AB 3 LEU E 88 ALA E 92 0
SHEET 2 AB 3 LEU E 103 GLY E 109 -1 O ARG E 106 N GLN E 91
SHEET 3 AB 3 SER E 137 ILE E 138 -1 O ILE E 138 N LEU E 103
SHEET 1 AC 4 GLU E 125 GLU E 132 0
SHEET 2 AC 4 VAL E 115 LYS E 122 -1 N LYS E 117 O TYR E 131
SHEET 3 AC 4 GLY E 147 VAL E 155 -1 O TYR E 150 N TYR E 121
SHEET 4 AC 4 LEU E 158 GLU E 161 -1 O LEU E 158 N VAL E 155
SHEET 1 AD 5 GLU E 125 GLU E 132 0
SHEET 2 AD 5 VAL E 115 LYS E 122 -1 N LYS E 117 O TYR E 131
SHEET 3 AD 5 GLY E 147 VAL E 155 -1 O TYR E 150 N TYR E 121
SHEET 4 AD 5 LEU E 165 ILE E 170 -1 N LEU E 165 O TYR E 149
SHEET 5 AD 5 VAL E 96 MET E 98 1 N VAL E 97 O THR E 168
SSBOND 1 CYS A 26 CYS A 68 1555 1555 2.04
SSBOND 2 CYS A 107 CYS A 151 1555 1555 2.05
SSBOND 3 CYS B 26 CYS B 68 1555 1555 2.04
SSBOND 4 CYS B 107 CYS B 151 1555 1555 2.06
SSBOND 5 CYS C 26 CYS C 68 1555 1555 2.03
SSBOND 6 CYS C 107 CYS C 151 1555 1555 2.04
SSBOND 7 CYS D 26 CYS D 68 1555 1555 2.04
SSBOND 8 CYS D 107 CYS D 151 1555 1555 2.05
SSBOND 9 CYS E 26 CYS E 68 1555 1555 2.04
SSBOND 10 CYS E 107 CYS E 151 1555 1555 2.05
LINK ND2 ASN A 21 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN A 42 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN A 50 C1 NAG H 1 1555 1555 1.46
LINK ND2 ASN A 74 C1 NAG A 274 1555 1555 1.46
LINK ND2 ASN A 135 C1 NAG A 335 1555 1555 1.45
LINK ND2 ASN A 140 C1 NAG A 340 1555 1555 1.46
LINK ND2 ASN A 166 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN B 21 C1 NAG B 221 1555 1555 1.46
LINK ND2 ASN B 42 C1 NAG J 1 1555 1555 1.46
LINK ND2 ASN B 74 C1 NAG B 274 1555 1555 1.45
LINK ND2 ASN B 135 C1 NAG B 335 1555 1555 1.46
LINK ND2 ASN B 140 C1 NAG B 340 1555 1555 1.45
LINK ND2 ASN B 166 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN C 21 C1 NAG L 1 1555 1555 1.45
LINK ND2 ASN C 42 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN C 50 C1 NAG C 250 1555 1555 1.46
LINK ND2 ASN C 74 C1 NAG C 274 1555 1555 1.44
LINK ND2 ASN C 140 C1 NAG C 340 1555 1555 1.45
LINK ND2 ASN C 166 C1 NAG N 1 1555 1555 1.44
LINK ND2 ASN D 21 C1 NAG O 1 1555 1555 1.45
LINK ND2 ASN D 42 C1 NAG P 1 1555 1555 1.46
LINK ND2 ASN D 74 C1 NAG D 274 1555 1555 1.45
LINK ND2 ASN D 135 C1 NAG D 335 1555 1555 1.46
LINK ND2 ASN D 140 C1 NAG D 340 1555 1555 1.45
LINK ND2 ASN D 166 C1 NAG Q 1 1555 1555 1.44
LINK ND2 ASN E 21 C1 NAG E 221 1555 1555 1.45
LINK ND2 ASN E 42 C1 NAG R 1 1555 1555 1.46
LINK ND2 ASN E 74 C1 NAG E 274 1555 1555 1.45
LINK ND2 ASN E 140 C1 NAG E 340 1555 1555 1.43
LINK ND2 ASN E 166 C1 NAG E 366 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.38
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.40
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.38
LINK O4 NAG G 2 C1 MAN G 3 1555 1555 1.38
LINK O3 MAN G 3 C1 MAN G 4 1555 1555 1.41
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.39
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.39
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.39
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.37
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.37
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.37
LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.37
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.38
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.40
LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.41
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.40
LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.39
LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.38
LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.40
LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.38
LINK O6 BMA R 3 C1 MAN R 4 1555 1555 1.41
CISPEP 1 ASN A 10 PRO A 11 0 -0.66
CISPEP 2 ASN B 10 PRO B 11 0 0.11
CISPEP 3 ASN C 10 PRO C 11 0 0.43
CISPEP 4 ASN D 10 PRO D 11 0 -0.11
CISPEP 5 ASN E 10 PRO E 11 0 -0.04
CRYST1 145.080 145.080 62.740 90.00 90.00 90.00 P 43 20
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 0.006893 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006893 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015939 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
