HEADER IMMUNE SYSTEM 12-MAR-14 4P4K
TITLE STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: BRIDGING THE GAP
TITLE 2 BETWEEN ALLERGIC HYPERSENSITIVITY AND AUTO IMMUNITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN;
COMPND 3 CHAIN: A, E;
COMPND 4 FRAGMENT: UNP RESIDUES 32-214;
COMPND 5 SYNONYM: DP(W3),DP(W4),HLA-SB ALPHA CHAIN,MHC CLASS II DP3-ALPHA,MHC
COMPND 6 CLASS II DPA1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: MIM2 PEPTIDE,HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP
COMPND 10 BETA 1 CHAIN;
COMPND 11 CHAIN: B, F;
COMPND 12 FRAGMENT: UNP RESIDUES 32-218;
COMPND 13 SYNONYM: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,DP(W4) BETA CHAIN,
COMPND 14 MHC CLASS II ANTIGEN DPB1;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: HTCRAV22 ALPHA CHAIN;
COMPND 18 CHAIN: C, G;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: HTCRAV22 BETA CHAIN;
COMPND 22 CHAIN: D, H;
COMPND 23 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-DPA1, HLA-DP1A, HLASB;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BTI TN 5B1 4;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: HLA-DPB1, HLA-DP1B;
SOURCE 14 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BE BOUND COMPLEX, CHRONIC BERYLLIUM DISEASE, TCR-MHC PEPTIDE-BE2+,
KEYWDS 2 IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.CLAYTON,F.CRAWFORD,J.W.KAPPLER
REVDAT 3 29-JUL-20 4P4K 1 COMPND SOURCE REMARK SEQADV
REVDAT 3 2 1 HETNAM LINK SITE
REVDAT 2 07-JAN-15 4P4K 1 DBREF
REVDAT 1 16-JUL-14 4P4K 0
JRNL AUTH G.M.CLAYTON,Y.WANG,F.CRAWFORD,A.NOVIKOV,B.T.WIMBERLY,
JRNL AUTH 2 J.S.KIEFT,M.T.FALTA,N.A.BOWERMAN,P.MARRACK,A.P.FONTENOT,
JRNL AUTH 3 S.DAI,J.W.KAPPLER
JRNL TITL STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: LINKING
JRNL TITL 2 ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY.
JRNL REF CELL V. 158 132 2014
JRNL REFN ISSN 1097-4172
JRNL PMID 24995984
JRNL DOI 10.1016/J.CELL.2014.04.048
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 58168
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2949
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4227
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2496
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4006
REMARK 3 BIN R VALUE (WORKING SET) : 0.2461
REMARK 3 BIN FREE R VALUE : 0.3123
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.23
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 221
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12872
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.90830
REMARK 3 B22 (A**2) : 0.81900
REMARK 3 B33 (A**2) : 5.08930
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) : 0.364
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.959
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.332
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.336
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 13314 ; 1.500 ; HARMONIC
REMARK 3 BOND ANGLES : 18175 ; 1.500 ; HARMONIC
REMARK 3 TORSION ANGLES : 4349 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 354 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1954 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 13314 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1725 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : 10 ; 1.000 ; HARMONIC
REMARK 3 UTILITY ANGLES : 12 ; 1.000 ; HARMONIC
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 14914 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.39
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.74
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4P4K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200667.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5-6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58169
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 14.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6700
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 <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: NULL
REMARK 200 STARTING MODEL: 3LQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8K, NA CACODYLATE, GLYCEROL, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 39.70000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.56500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.62000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 106.56500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.70000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.62000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ILE A 1
REMARK 465 ALA A 180
REMARK 465 GLN A 181
REMARK 465 GLU A 182
REMARK 465 PRO A 183
REMARK 465 GLY B -13
REMARK 465 GLY B -12
REMARK 465 SER B -11
REMARK 465 LEU B -10
REMARK 465 VAL B -9
REMARK 465 PRO B -8
REMARK 465 ARG B -7
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 GLY B -4
REMARK 465 GLY B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 MET C 1
REMARK 465 PRO C 206
REMARK 465 GLU C 207
REMARK 465 SER C 208
REMARK 465 SER C 209
REMARK 465 MET D 2
REMARK 465 GLU E 182
REMARK 465 PRO E 183
REMARK 465 GLY F -13
REMARK 465 GLY F -12
REMARK 465 SER F -11
REMARK 465 LEU F -10
REMARK 465 VAL F -9
REMARK 465 PRO F -8
REMARK 465 ARG F -7
REMARK 465 GLY F -6
REMARK 465 SER F -5
REMARK 465 GLY F -4
REMARK 465 GLY F -3
REMARK 465 GLY F -2
REMARK 465 GLY F -1
REMARK 465 MET G 1
REMARK 465 ASN G 2
REMARK 465 PRO G 206
REMARK 465 GLU G 207
REMARK 465 SER G 208
REMARK 465 SER G 209
REMARK 465 MET H 2
REMARK 465 ALA H 242
REMARK 465 ASP H 243
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 2 CG CD CE NZ
REMARK 470 LEU A 99 CG CD1 CD2
REMARK 470 GLN A 172 CG CD OE1 NE2
REMARK 470 GLN B -25 CG CD OE1 NE2
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 LEU B 89 CG CD1 CD2
REMARK 470 GLN B 90 CG CD OE1 NE2
REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 LEU B 107 CG CD1 CD2
REMARK 470 HIS B 109 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 165 CG CD OE1 NE2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 GLN B 189 CG CD OE1 NE2
REMARK 470 LYS C 68 CG CD CE NZ
REMARK 470 LYS C 107 CG CD CE NZ
REMARK 470 ARG C 128 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 146 CG CD OE1 NE2
REMARK 470 ASN C 148 CG OD1 ND2
REMARK 470 GLN C 151 CG CD OE1 NE2
REMARK 470 LYS C 153 CG CD CE NZ
REMARK 470 ASP C 156 CG OD1 OD2
REMARK 470 LYS C 162 CG CD CE NZ
REMARK 470 ARG C 168 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 193 CG OD1 ND2
REMARK 470 ASN C 194 CG OD1 ND2
REMARK 470 GLU C 199 CG CD OE1 OE2
REMARK 470 ASP C 200 CG OD1 OD2
REMARK 470 SER C 205 OG
REMARK 470 ARG D 9 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 117 CG CD CE NZ
REMARK 470 GLU D 131 CG CD OE1 OE2
REMARK 470 ILE D 134 CG1 CG2 CD1
REMARK 470 SER D 135 OG
REMARK 470 LYS D 163 CG CD CE NZ
REMARK 470 GLN D 174 CG CD OE1 NE2
REMARK 470 LEU D 182 CG CD1 CD2
REMARK 470 GLN D 201 CG CD OE1 NE2
REMARK 470 ASN D 219 CG OD1 ND2
REMARK 470 GLU D 221 CG CD OE1 OE2
REMARK 470 ASP D 243 CG OD1 OD2
REMARK 470 LYS E 2 CG CD CE NZ
REMARK 470 GLU E 158 CG CD OE1 OE2
REMARK 470 GLN E 181 CG CD OE1 NE2
REMARK 470 GLN F -25 CG CD OE1 NE2
REMARK 470 LYS F 63 CG CD CE NZ
REMARK 470 LYS F 103 CG CD CE NZ
REMARK 470 LYS F 104 CG CD CE NZ
REMARK 470 LEU F 107 CG CD1 CD2
REMARK 470 GLN F 189 CG CD OE1 NE2
REMARK 470 TYR G 30 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS G 60 CG CD CE NZ
REMARK 470 LYS G 68 CG CD CE NZ
REMARK 470 LYS G 107 CG CD CE NZ
REMARK 470 GLN G 118 CG CD OE1 NE2
REMARK 470 LYS G 131 CG CD CE NZ
REMARK 470 ASP G 134 CG OD1 OD2
REMARK 470 LYS G 135 CG CD CE NZ
REMARK 470 GLN G 146 CG CD OE1 NE2
REMARK 470 GLN G 151 CG CD OE1 NE2
REMARK 470 LYS G 153 CG CD CE NZ
REMARK 470 ASP G 156 CG OD1 OD2
REMARK 470 LYS G 162 CG CD CE NZ
REMARK 470 ARG G 168 CG CD NE CZ NH1 NH2
REMARK 470 ASN G 182 CG OD1 ND2
REMARK 470 LYS G 183 CG CD CE NZ
REMARK 470 SER G 184 OG
REMARK 470 ASN G 194 CG OD1 ND2
REMARK 470 GLU G 199 CG CD OE1 OE2
REMARK 470 ARG H 9 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 67 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 117 CG CD CE NZ
REMARK 470 GLU H 131 CG CD OE1 OE2
REMARK 470 LYS H 163 CG CD CE NZ
REMARK 470 GLN H 174 CG CD OE1 NE2
REMARK 470 LYS H 177 CG CD CE NZ
REMARK 470 ARG H 204 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 218 CG CD OE1 OE2
REMARK 470 GLN H 224 CG CD OE1 NE2
REMARK 470 ASP H 225 CG OD1 OD2
REMARK 470 ARG H 241 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN B 6 O HOH B 339 2.14
REMARK 500 OE1 GLU F -17 OE2 GLU F 69 2.15
REMARK 500 O ALA B 47 O HOH B 327 2.17
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 GLU A 28 -4.16 67.97
REMARK 500 GLU A 158 43.22 -98.12
REMARK 500 ASN B 31 -104.14 59.72
REMARK 500 ARG B 75 -94.80 -97.32
REMARK 500 THR B 88 -52.28 -123.42
REMARK 500 GLN B 108 -39.59 -157.45
REMARK 500 HIS B 109 -173.54 -68.97
REMARK 500 ASN B 144 161.88 70.56
REMARK 500 ALA B 188 -33.80 -37.36
REMARK 500 ASP C 54 -9.76 86.58
REMARK 500 ASN C 59 143.89 -170.90
REMARK 500 PHE C 73 58.52 -140.18
REMARK 500 ALA C 86 -174.81 -174.60
REMARK 500 ASN C 119 76.44 -119.58
REMARK 500 LYS C 131 -73.43 -87.79
REMARK 500 SER C 155 -70.13 -59.95
REMARK 500 MET C 167 37.12 -86.86
REMARK 500 ARG C 168 -54.69 2.92
REMARK 500 ASN C 182 42.00 -76.30
REMARK 500 LYS C 183 -167.27 55.22
REMARK 500 ALA C 191 -59.61 -29.06
REMARK 500 PHE C 192 56.71 -108.55
REMARK 500 LEU D 46 -63.88 -97.97
REMARK 500 GLU D 52 -22.26 69.88
REMARK 500 ASN D 59 77.69 -107.45
REMARK 500 SER D 72 -6.63 78.68
REMARK 500 ALA D 87 -177.65 -171.79
REMARK 500 ASP D 152 48.36 -82.13
REMARK 500 LEU D 182 122.68 -179.45
REMARK 500 GLU E 28 -5.73 69.48
REMARK 500 GLU E 158 40.92 -94.55
REMARK 500 ASN F 31 -104.97 61.90
REMARK 500 ARG F 75 -94.46 -97.68
REMARK 500 THR F 88 -53.21 -122.43
REMARK 500 LYS F 104 45.72 -97.24
REMARK 500 PRO F 106 -137.23 -87.46
REMARK 500 GLN F 108 -14.63 65.74
REMARK 500 ASN F 144 161.88 69.84
REMARK 500 MET G 7 115.50 -36.34
REMARK 500 PRO G 40 -82.26 -10.14
REMARK 500 ASP G 54 -9.41 85.95
REMARK 500 ASN G 59 145.13 -172.19
REMARK 500 ALA G 86 -174.69 -174.27
REMARK 500 ASN G 119 56.83 72.40
REMARK 500 LYS G 131 -71.80 -88.61
REMARK 500 ASP G 142 16.08 55.27
REMARK 500 SER G 155 -70.36 -59.98
REMARK 500 MET G 167 36.41 -86.93
REMARK 500 ARG G 168 -54.32 2.67
REMARK 500 ALA G 191 -73.09 -35.96
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B -20 OD1
REMARK 620 2 ASP B -20 OD2 44.0
REMARK 620 3 GLU B -17 OE1 104.3 148.2
REMARK 620 4 GLU B 68 OE2 137.3 97.2 111.1
REMARK 620 5 GLU B 69 OE1 54.6 76.8 85.7 148.5
REMARK 620 6 GLU B 69 OE2 96.2 120.6 54.3 123.6 45.4
REMARK 620 7 HOH B 344 O 102.0 93.1 91.5 55.2 154.4 144.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 0BE B 203 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B -20 OD1
REMARK 620 2 GLU B 26 OE1 114.1
REMARK 620 3 GLU B 69 OE1 111.8 113.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA F 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F -20 OD2
REMARK 620 2 GLU F -17 OE1 135.1
REMARK 620 3 GLU F 68 OE2 111.5 103.9
REMARK 620 4 GLU F 69 OE1 72.8 78.4 167.7
REMARK 620 5 GLU F 69 OE2 115.4 50.3 130.0 42.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 0BE F 202 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F -20 OD1
REMARK 620 2 GLU F 26 OE1 101.7
REMARK 620 3 GLU F 69 OE1 103.5 108.7
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P4R RELATED DB: PDB
REMARK 900 RELATED ID: 4P57 RELATED DB: PDB
REMARK 900 RELATED ID: 4P5M RELATED DB: PDB
REMARK 900 RELATED ID: 4P5K RELATED DB: PDB
DBREF 4P4K A 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P4K B -25 -15 PDB 4P4K 4P4K -25 -15
DBREF 4P4K B 3 189 UNP P04440 DPB1_HUMAN 32 218
DBREF 4P4K C 1 209 PDB 4P4K 4P4K 1 209
DBREF 4P4K D 2 243 PDB 4P4K 4P4K 2 243
DBREF 4P4K E 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P4K F -25 -15 PDB 4P4K 4P4K -25 -15
DBREF 4P4K F 3 189 UNP P04440 DPB1_HUMAN 32 218
DBREF 4P4K G 1 209 PDB 4P4K 4P4K 1 209
DBREF 4P4K H 2 243 PDB 4P4K 4P4K 2 243
SEQADV 4P4K GLY B -14 UNP P04440 LINKER
SEQADV 4P4K GLY B -13 UNP P04440 LINKER
SEQADV 4P4K GLY B -12 UNP P04440 LINKER
SEQADV 4P4K SER B -11 UNP P04440 LINKER
SEQADV 4P4K LEU B -10 UNP P04440 LINKER
SEQADV 4P4K VAL B -9 UNP P04440 LINKER
SEQADV 4P4K PRO B -8 UNP P04440 LINKER
SEQADV 4P4K ARG B -7 UNP P04440 LINKER
SEQADV 4P4K GLY B -6 UNP P04440 LINKER
SEQADV 4P4K SER B -5 UNP P04440 LINKER
SEQADV 4P4K GLY B -4 UNP P04440 LINKER
SEQADV 4P4K GLY B -3 UNP P04440 LINKER
SEQADV 4P4K GLY B -2 UNP P04440 LINKER
SEQADV 4P4K GLY B -1 UNP P04440 LINKER
SEQADV 4P4K SER B 3 UNP P04440 THR 32 VARIANT
SEQADV 4P4K VAL B 36 UNP P04440 ALA 65 VARIANT
SEQADV 4P4K ASP B 55 UNP P04440 ALA 84 VARIANT
SEQADV 4P4K GLU B 56 UNP P04440 ALA 85 VARIANT
SEQADV 4P4K GLU B 69 UNP P04440 LYS 98 VARIANT
SEQADV 4P4K GLY F -14 UNP P04440 LINKER
SEQADV 4P4K GLY F -13 UNP P04440 LINKER
SEQADV 4P4K GLY F -12 UNP P04440 LINKER
SEQADV 4P4K SER F -11 UNP P04440 LINKER
SEQADV 4P4K LEU F -10 UNP P04440 LINKER
SEQADV 4P4K VAL F -9 UNP P04440 LINKER
SEQADV 4P4K PRO F -8 UNP P04440 LINKER
SEQADV 4P4K ARG F -7 UNP P04440 LINKER
SEQADV 4P4K GLY F -6 UNP P04440 LINKER
SEQADV 4P4K SER F -5 UNP P04440 LINKER
SEQADV 4P4K GLY F -4 UNP P04440 LINKER
SEQADV 4P4K GLY F -3 UNP P04440 LINKER
SEQADV 4P4K GLY F -2 UNP P04440 LINKER
SEQADV 4P4K GLY F -1 UNP P04440 LINKER
SEQADV 4P4K SER F 3 UNP P04440 THR 32 VARIANT
SEQADV 4P4K VAL F 36 UNP P04440 ALA 65 VARIANT
SEQADV 4P4K ASP F 55 UNP P04440 ALA 84 VARIANT
SEQADV 4P4K GLU F 56 UNP P04440 ALA 85 VARIANT
SEQADV 4P4K GLU F 69 UNP P04440 LYS 98 VARIANT
SEQRES 1 A 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 A 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 A 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 A 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 A 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 A 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 A 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 A 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 A 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 A 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 A 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 A 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 A 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 A 183 PRO
SEQRES 1 B 212 GLN ALA PHE TRP ILE ASP LEU PHE GLU THR ILE GLY GLY
SEQRES 2 B 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 B 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 B 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 B 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 B 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 B 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 B 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 B 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 B 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 B 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 B 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 B 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 B 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 B 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 B 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 B 212 TRP LYS ALA GLN
SEQRES 1 C 209 MET ASN SER VAL THR GLN MET GLU GLY PRO VAL THR LEU
SEQRES 2 C 209 SER GLU GLU ALA PHE LEU THR ILE ASN CYS THR TYR THR
SEQRES 3 C 209 ALA THR GLY TYR PRO SER LEU PHE TRP TYR VAL GLN TYR
SEQRES 4 C 209 PRO GLY GLU GLY LEU GLN LEU LEU LEU LYS ALA THR LYS
SEQRES 5 C 209 ALA ASP ASP LYS GLY SER ASN LYS GLY PHE GLU ALA THR
SEQRES 6 C 209 TYR ARG LYS GLU THR THR SER PHE HIS LEU GLU LYS GLY
SEQRES 7 C 209 SER VAL GLN VAL SER ASP SER ALA VAL TYR PHE CYS ALA
SEQRES 8 C 209 LEU SER LEU TYR SER GLY ALA GLY SER TYR GLN LEU THR
SEQRES 9 C 209 PHE GLY LYS GLY THR LYS LEU SER VAL ILE PRO ASN ILE
SEQRES 10 C 209 GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER
SEQRES 11 C 209 LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE
SEQRES 12 C 209 ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP
SEQRES 13 C 209 VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER
SEQRES 14 C 209 MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN
SEQRES 15 C 209 LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER
SEQRES 16 C 209 ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER
SEQRES 17 C 209 SER
SEQRES 1 D 242 MET GLY VAL THR GLN THR PRO ARG TYR LEU ILE LYS THR
SEQRES 2 D 242 ARG GLY GLN GLN VAL THR LEU SER CYS SER PRO ILE SER
SEQRES 3 D 242 GLY HIS ARG SER VAL SER TRP TYR GLN GLN THR PRO GLY
SEQRES 4 D 242 GLN GLY LEU GLN PHE LEU PHE GLU TYR PHE SER GLU THR
SEQRES 5 D 242 GLN ARG ASN LYS GLY ASN PHE PRO GLY ARG PHE SER GLY
SEQRES 6 D 242 ARG GLN PHE SER ASN SER ARG SER GLU MET ASN VAL SER
SEQRES 7 D 242 THR LEU GLU LEU GLY ASP SER ALA LEU TYR LEU CYS ALA
SEQRES 8 D 242 SER SER LEU ALA GLN GLY GLY GLU THR GLN TYR PHE GLY
SEQRES 9 D 242 PRO GLY THR ARG LEU LEU VAL LEU GLU ASP LEU LYS ASN
SEQRES 10 D 242 VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU
SEQRES 11 D 242 ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS
SEQRES 12 D 242 LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER
SEQRES 13 D 242 TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS
SEQRES 14 D 242 THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN
SEQRES 15 D 242 ASP SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER
SEQRES 16 D 242 ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS
SEQRES 17 D 242 GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP
SEQRES 18 D 242 THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER
SEQRES 19 D 242 ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 E 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 E 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 E 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 E 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 E 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 E 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 E 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 E 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 E 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 E 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 E 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 E 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 E 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 E 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 E 183 PRO
SEQRES 1 F 212 GLN ALA PHE TRP ILE ASP LEU PHE GLU THR ILE GLY GLY
SEQRES 2 F 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 F 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 F 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 F 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 F 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 F 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 F 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 F 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 F 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 F 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 F 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 F 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 F 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 F 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 F 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 F 212 TRP LYS ALA GLN
SEQRES 1 G 209 MET ASN SER VAL THR GLN MET GLU GLY PRO VAL THR LEU
SEQRES 2 G 209 SER GLU GLU ALA PHE LEU THR ILE ASN CYS THR TYR THR
SEQRES 3 G 209 ALA THR GLY TYR PRO SER LEU PHE TRP TYR VAL GLN TYR
SEQRES 4 G 209 PRO GLY GLU GLY LEU GLN LEU LEU LEU LYS ALA THR LYS
SEQRES 5 G 209 ALA ASP ASP LYS GLY SER ASN LYS GLY PHE GLU ALA THR
SEQRES 6 G 209 TYR ARG LYS GLU THR THR SER PHE HIS LEU GLU LYS GLY
SEQRES 7 G 209 SER VAL GLN VAL SER ASP SER ALA VAL TYR PHE CYS ALA
SEQRES 8 G 209 LEU SER LEU TYR SER GLY ALA GLY SER TYR GLN LEU THR
SEQRES 9 G 209 PHE GLY LYS GLY THR LYS LEU SER VAL ILE PRO ASN ILE
SEQRES 10 G 209 GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER
SEQRES 11 G 209 LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE
SEQRES 12 G 209 ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP
SEQRES 13 G 209 VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER
SEQRES 14 G 209 MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN
SEQRES 15 G 209 LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER
SEQRES 16 G 209 ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER
SEQRES 17 G 209 SER
SEQRES 1 H 242 MET GLY VAL THR GLN THR PRO ARG TYR LEU ILE LYS THR
SEQRES 2 H 242 ARG GLY GLN GLN VAL THR LEU SER CYS SER PRO ILE SER
SEQRES 3 H 242 GLY HIS ARG SER VAL SER TRP TYR GLN GLN THR PRO GLY
SEQRES 4 H 242 GLN GLY LEU GLN PHE LEU PHE GLU TYR PHE SER GLU THR
SEQRES 5 H 242 GLN ARG ASN LYS GLY ASN PHE PRO GLY ARG PHE SER GLY
SEQRES 6 H 242 ARG GLN PHE SER ASN SER ARG SER GLU MET ASN VAL SER
SEQRES 7 H 242 THR LEU GLU LEU GLY ASP SER ALA LEU TYR LEU CYS ALA
SEQRES 8 H 242 SER SER LEU ALA GLN GLY GLY GLU THR GLN TYR PHE GLY
SEQRES 9 H 242 PRO GLY THR ARG LEU LEU VAL LEU GLU ASP LEU LYS ASN
SEQRES 10 H 242 VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU
SEQRES 11 H 242 ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS
SEQRES 12 H 242 LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER
SEQRES 13 H 242 TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS
SEQRES 14 H 242 THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN
SEQRES 15 H 242 ASP SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER
SEQRES 16 H 242 ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS
SEQRES 17 H 242 GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP
SEQRES 18 H 242 THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER
SEQRES 19 H 242 ALA GLU ALA TRP GLY ARG ALA ASP
HET NAG A 201 14
HET NAG A 202 14
HET NAG B 201 14
HET NA B 202 1
HET 0BE B 203 1
HET NAG E 201 14
HET NAG E 202 14
HET NA F 201 1
HET 0BE F 202 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM NA SODIUM ION
HETNAM 0BE BERYLLIUM
FORMUL 9 NAG 5(C8 H15 N O6)
FORMUL 12 NA 2(NA 1+)
FORMUL 13 0BE 2(BE 2+)
FORMUL 18 HOH *330(H2 O)
HELIX 1 AA1 LEU A 45 PHE A 52 1 8
HELIX 2 AA2 ALA A 56 SER A 77 1 22
HELIX 3 AA3 THR B 49 LEU B 51 5 3
HELIX 4 AA4 GLY B 52 SER B 61 1 10
HELIX 5 AA5 GLN B 62 ALA B 71 1 10
HELIX 6 AA6 ARG B 75 GLY B 84 1 10
HELIX 7 AA7 GLN C 81 SER C 85 5 5
HELIX 8 AA8 ARG C 168 ASP C 171 5 4
HELIX 9 AA9 ALA C 187 PHE C 192 1 6
HELIX 10 AB1 GLU D 82 SER D 86 5 5
HELIX 11 AB2 SER D 130 GLN D 138 1 9
HELIX 12 AB3 ALA D 197 GLN D 201 1 5
HELIX 13 AB4 LEU E 45 PHE E 52 1 8
HELIX 14 AB5 ALA E 56 SER E 77 1 22
HELIX 15 AB6 THR F 49 LEU F 51 5 3
HELIX 16 AB7 GLY F 52 SER F 61 1 10
HELIX 17 AB8 GLN F 62 ALA F 71 1 10
HELIX 18 AB9 ARG F 75 GLY F 84 1 10
HELIX 19 AC1 GLN G 81 SER G 85 5 5
HELIX 20 AC2 ARG G 168 ASP G 171 5 4
HELIX 21 AC3 ALA G 187 PHE G 192 1 6
HELIX 22 AC4 GLU H 82 SER H 86 5 5
HELIX 23 AC5 SER H 130 GLN H 138 1 9
HELIX 24 AC6 ALA H 197 ASN H 202 1 6
SHEET 1 AA1 8 GLU A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N TYR A 33 O VAL A 42
SHEET 3 AA1 8 GLY A 20 PHE A 26 -1 N PHE A 24 O PHE A 32
SHEET 4 AA1 8 HIS A 5 GLN A 14 -1 N THR A 8 O GLU A 25
SHEET 5 AA1 8 LEU B 8 PHE B 18 -1 O GLY B 11 N ALA A 11
SHEET 6 AA1 8 THR B 21 TYR B 30 -1 O ILE B 29 N GLN B 10
SHEET 7 AA1 8 GLU B 33 ASP B 39 -1 O GLU B 33 N TYR B 30
SHEET 8 AA1 8 PHE B 45 ARG B 46 -1 O ARG B 46 N ARG B 37
SHEET 1 AA2 4 GLU A 88 PRO A 93 0
SHEET 2 AA2 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 AA2 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 AA2 4 VAL A 132 GLU A 134 -1 N ALA A 133 O TYR A 150
SHEET 1 AA3 4 GLU A 88 PRO A 93 0
SHEET 2 AA3 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 AA3 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 AA3 4 LEU A 138 PRO A 139 -1 N LEU A 138 O HIS A 146
SHEET 1 AA4 4 GLU A 126 VAL A 128 0
SHEET 2 AA4 4 ASN A 118 CYS A 123 -1 N CYS A 123 O GLU A 126
SHEET 3 AA4 4 TYR A 161 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 AA4 4 LEU A 174 TRP A 178 -1 O TRP A 178 N TYR A 161
SHEET 1 AA5 4 ARG B 96 PRO B 101 0
SHEET 2 AA5 4 ASN B 111 PHE B 120 -1 O THR B 118 N ARG B 96
SHEET 3 AA5 4 PHE B 153 MET B 161 -1 O LEU B 159 N LEU B 113
SHEET 4 AA5 4 VAL B 140 SER B 142 -1 N VAL B 141 O MET B 158
SHEET 1 AA6 4 ARG B 96 PRO B 101 0
SHEET 2 AA6 4 ASN B 111 PHE B 120 -1 O THR B 118 N ARG B 96
SHEET 3 AA6 4 PHE B 153 MET B 161 -1 O LEU B 159 N LEU B 113
SHEET 4 AA6 4 ILE B 146 ARG B 147 -1 N ILE B 146 O GLN B 154
SHEET 1 AA7 4 GLN B 134 GLU B 136 0
SHEET 2 AA7 4 GLN B 126 LEU B 131 -1 N LEU B 131 O GLN B 134
SHEET 3 AA7 4 VAL B 168 GLU B 174 -1 O GLN B 172 N ARG B 128
SHEET 4 AA7 4 VAL B 182 LYS B 187 -1 O TRP B 186 N TYR B 169
SHEET 1 AA8 2 SER C 3 GLN C 6 0
SHEET 2 AA8 2 CYS C 23 THR C 26 -1 O THR C 24 N THR C 5
SHEET 1 AA9 5 VAL C 11 SER C 14 0
SHEET 2 AA9 5 THR C 109 ILE C 114 1 O ILE C 114 N LEU C 13
SHEET 3 AA9 5 ALA C 86 TYR C 95 -1 N TYR C 88 O THR C 109
SHEET 4 AA9 5 SER C 32 GLN C 38 -1 N TYR C 36 O PHE C 89
SHEET 5 AA9 5 LEU C 44 ALA C 50 -1 O GLN C 45 N VAL C 37
SHEET 1 AB1 4 VAL C 11 SER C 14 0
SHEET 2 AB1 4 THR C 109 ILE C 114 1 O ILE C 114 N LEU C 13
SHEET 3 AB1 4 ALA C 86 TYR C 95 -1 N TYR C 88 O THR C 109
SHEET 4 AB1 4 TYR C 101 PHE C 105 -1 O GLN C 102 N LEU C 94
SHEET 1 AB2 4 LEU C 19 ILE C 21 0
SHEET 2 AB2 4 LEU C 75 LYS C 77 -1 O LYS C 77 N LEU C 19
SHEET 3 AB2 4 PHE C 62 THR C 65 -1 N GLU C 63 O GLU C 76
SHEET 4 AB2 4 LYS C 56 ASN C 59 -1 N GLY C 57 O ALA C 64
SHEET 1 AB3 4 ALA C 123 ARG C 128 0
SHEET 2 AB3 4 SER C 136 THR C 141 -1 O LEU C 139 N TYR C 125
SHEET 3 AB3 4 LYS C 173 SER C 181 -1 O ALA C 179 N CYS C 138
SHEET 4 AB3 4 VAL C 157 ILE C 159 -1 N TYR C 158 O TRP C 180
SHEET 1 AB4 4 ALA C 123 ARG C 128 0
SHEET 2 AB4 4 SER C 136 THR C 141 -1 O LEU C 139 N TYR C 125
SHEET 3 AB4 4 LYS C 173 SER C 181 -1 O ALA C 179 N CYS C 138
SHEET 4 AB4 4 CYS C 163 ASP C 166 -1 N LEU C 165 O SER C 174
SHEET 1 AB5 4 THR D 5 THR D 7 0
SHEET 2 AB5 4 VAL D 19 SER D 24 -1 O SER D 24 N THR D 5
SHEET 3 AB5 4 SER D 74 VAL D 78 -1 O MET D 76 N LEU D 21
SHEET 4 AB5 4 PHE D 64 GLN D 68 -1 N SER D 65 O ASN D 77
SHEET 1 AB6 6 TYR D 10 THR D 14 0
SHEET 2 AB6 6 THR D 108 LEU D 113 1 O LEU D 113 N LYS D 13
SHEET 3 AB6 6 ALA D 87 SER D 94 -1 N ALA D 87 O LEU D 110
SHEET 4 AB6 6 SER D 31 THR D 38 -1 N SER D 33 O ALA D 92
SHEET 5 AB6 6 GLY D 42 PHE D 50 -1 O LEU D 46 N TRP D 34
SHEET 6 AB6 6 THR D 53 LYS D 57 -1 O ASN D 56 N GLU D 48
SHEET 1 AB7 4 TYR D 10 THR D 14 0
SHEET 2 AB7 4 THR D 108 LEU D 113 1 O LEU D 113 N LYS D 13
SHEET 3 AB7 4 ALA D 87 SER D 94 -1 N ALA D 87 O LEU D 110
SHEET 4 AB7 4 TYR D 103 PHE D 104 -1 O TYR D 103 N SER D 93
SHEET 1 AB8 4 GLU D 123 PHE D 127 0
SHEET 2 AB8 4 LYS D 139 PHE D 149 -1 O VAL D 143 N PHE D 127
SHEET 3 AB8 4 TYR D 187 SER D 196 -1 O VAL D 195 N ALA D 140
SHEET 4 AB8 4 VAL D 169 THR D 171 -1 N CYS D 170 O ARG D 192
SHEET 1 AB9 4 GLU D 123 PHE D 127 0
SHEET 2 AB9 4 LYS D 139 PHE D 149 -1 O VAL D 143 N PHE D 127
SHEET 3 AB9 4 TYR D 187 SER D 196 -1 O VAL D 195 N ALA D 140
SHEET 4 AB9 4 LEU D 176 LYS D 177 -1 N LEU D 176 O SER D 188
SHEET 1 AC1 4 LYS D 163 VAL D 165 0
SHEET 2 AC1 4 VAL D 154 VAL D 160 -1 N VAL D 160 O LYS D 163
SHEET 3 AC1 4 HIS D 206 PHE D 213 -1 O ARG D 208 N TRP D 159
SHEET 4 AC1 4 GLN D 232 TRP D 239 -1 O GLN D 232 N PHE D 213
SHEET 1 AC2 8 GLU E 40 TRP E 43 0
SHEET 2 AC2 8 ASP E 29 ASP E 35 -1 N TYR E 33 O VAL E 42
SHEET 3 AC2 8 GLY E 20 PHE E 26 -1 N PHE E 24 O PHE E 32
SHEET 4 AC2 8 HIS E 5 VAL E 13 -1 N THR E 8 O GLU E 25
SHEET 5 AC2 8 PHE F 9 PHE F 18 -1 O PHE F 9 N VAL E 13
SHEET 6 AC2 8 THR F 21 TYR F 30 -1 O ILE F 29 N GLN F 10
SHEET 7 AC2 8 GLU F 33 ASP F 39 -1 O GLU F 33 N TYR F 30
SHEET 8 AC2 8 PHE F 45 ALA F 47 -1 O ARG F 46 N ARG F 37
SHEET 1 AC3 4 GLU E 88 PRO E 93 0
SHEET 2 AC3 4 ASN E 103 PHE E 112 -1 O HIS E 108 N THR E 90
SHEET 3 AC3 4 PHE E 145 PHE E 153 -1 O LEU E 151 N LEU E 105
SHEET 4 AC3 4 VAL E 132 GLU E 134 -1 N ALA E 133 O TYR E 150
SHEET 1 AC4 4 GLU E 88 PRO E 93 0
SHEET 2 AC4 4 ASN E 103 PHE E 112 -1 O HIS E 108 N THR E 90
SHEET 3 AC4 4 PHE E 145 PHE E 153 -1 O LEU E 151 N LEU E 105
SHEET 4 AC4 4 LEU E 138 PRO E 139 -1 N LEU E 138 O HIS E 146
SHEET 1 AC5 4 GLU E 126 VAL E 128 0
SHEET 2 AC5 4 ASN E 118 CYS E 123 -1 N CYS E 123 O GLU E 126
SHEET 3 AC5 4 TYR E 161 GLU E 166 -1 O ARG E 164 N THR E 120
SHEET 4 AC5 4 LEU E 174 TRP E 178 -1 O TRP E 178 N TYR E 161
SHEET 1 AC6 4 ARG F 96 PRO F 101 0
SHEET 2 AC6 4 ASN F 111 PHE F 120 -1 O THR F 118 N ARG F 96
SHEET 3 AC6 4 PHE F 153 MET F 161 -1 O MET F 161 N ASN F 111
SHEET 4 AC6 4 VAL F 140 SER F 142 -1 N VAL F 141 O MET F 158
SHEET 1 AC7 4 ARG F 96 PRO F 101 0
SHEET 2 AC7 4 ASN F 111 PHE F 120 -1 O THR F 118 N ARG F 96
SHEET 3 AC7 4 PHE F 153 MET F 161 -1 O MET F 161 N ASN F 111
SHEET 4 AC7 4 ILE F 146 ARG F 147 -1 N ILE F 146 O GLN F 154
SHEET 1 AC8 4 GLN F 134 GLU F 136 0
SHEET 2 AC8 4 GLN F 126 LEU F 131 -1 N LEU F 131 O GLN F 134
SHEET 3 AC8 4 VAL F 168 GLU F 174 -1 O GLN F 172 N ARG F 128
SHEET 4 AC8 4 VAL F 182 LYS F 187 -1 O TRP F 186 N TYR F 169
SHEET 1 AC9 2 VAL G 4 GLN G 6 0
SHEET 2 AC9 2 CYS G 23 TYR G 25 -1 O THR G 24 N THR G 5
SHEET 1 AD1 5 VAL G 11 SER G 14 0
SHEET 2 AD1 5 THR G 109 ILE G 114 1 O SER G 112 N LEU G 13
SHEET 3 AD1 5 ALA G 86 TYR G 95 -1 N ALA G 86 O LEU G 111
SHEET 4 AD1 5 SER G 32 GLN G 38 -1 N TYR G 36 O PHE G 89
SHEET 5 AD1 5 GLN G 45 ALA G 50 -1 O GLN G 45 N VAL G 37
SHEET 1 AD2 4 VAL G 11 SER G 14 0
SHEET 2 AD2 4 THR G 109 ILE G 114 1 O SER G 112 N LEU G 13
SHEET 3 AD2 4 ALA G 86 TYR G 95 -1 N ALA G 86 O LEU G 111
SHEET 4 AD2 4 TYR G 101 PHE G 105 -1 O GLN G 102 N LEU G 94
SHEET 1 AD3 4 LEU G 19 ILE G 21 0
SHEET 2 AD3 4 LEU G 75 LYS G 77 -1 O LEU G 75 N ILE G 21
SHEET 3 AD3 4 PHE G 62 THR G 65 -1 N GLU G 63 O GLU G 76
SHEET 4 AD3 4 LYS G 56 ASN G 59 -1 N GLY G 57 O ALA G 64
SHEET 1 AD4 4 ALA G 123 ARG G 128 0
SHEET 2 AD4 4 SER G 136 THR G 141 -1 O LEU G 139 N TYR G 125
SHEET 3 AD4 4 LYS G 173 SER G 181 -1 O ALA G 179 N CYS G 138
SHEET 4 AD4 4 VAL G 157 ILE G 159 -1 N TYR G 158 O TRP G 180
SHEET 1 AD5 4 ALA G 123 ARG G 128 0
SHEET 2 AD5 4 SER G 136 THR G 141 -1 O LEU G 139 N TYR G 125
SHEET 3 AD5 4 LYS G 173 SER G 181 -1 O ALA G 179 N CYS G 138
SHEET 4 AD5 4 CYS G 163 ASP G 166 -1 N LEU G 165 O SER G 174
SHEET 1 AD6 4 THR H 5 THR H 7 0
SHEET 2 AD6 4 VAL H 19 SER H 24 -1 O SER H 22 N THR H 7
SHEET 3 AD6 4 SER H 74 VAL H 78 -1 O MET H 76 N LEU H 21
SHEET 4 AD6 4 PHE H 64 GLN H 68 -1 N SER H 65 O ASN H 77
SHEET 1 AD7 6 TYR H 10 THR H 14 0
SHEET 2 AD7 6 THR H 108 LEU H 113 1 O LEU H 113 N LYS H 13
SHEET 3 AD7 6 ALA H 87 SER H 94 -1 N ALA H 87 O LEU H 110
SHEET 4 AD7 6 SER H 31 THR H 38 -1 N GLN H 37 O LEU H 88
SHEET 5 AD7 6 GLY H 42 PHE H 50 -1 O TYR H 49 N VAL H 32
SHEET 6 AD7 6 THR H 53 LYS H 57 -1 O THR H 53 N PHE H 50
SHEET 1 AD8 4 TYR H 10 THR H 14 0
SHEET 2 AD8 4 THR H 108 LEU H 113 1 O LEU H 113 N LYS H 13
SHEET 3 AD8 4 ALA H 87 SER H 94 -1 N ALA H 87 O LEU H 110
SHEET 4 AD8 4 TYR H 103 PHE H 104 -1 O TYR H 103 N SER H 93
SHEET 1 AD9 4 GLU H 123 PHE H 127 0
SHEET 2 AD9 4 LYS H 139 PHE H 149 -1 O VAL H 143 N PHE H 127
SHEET 3 AD9 4 TYR H 187 SER H 196 -1 O VAL H 195 N ALA H 140
SHEET 4 AD9 4 VAL H 169 THR H 171 -1 N CYS H 170 O ARG H 192
SHEET 1 AE1 4 GLU H 123 PHE H 127 0
SHEET 2 AE1 4 LYS H 139 PHE H 149 -1 O VAL H 143 N PHE H 127
SHEET 3 AE1 4 TYR H 187 SER H 196 -1 O VAL H 195 N ALA H 140
SHEET 4 AE1 4 LEU H 176 LYS H 177 -1 N LEU H 176 O SER H 188
SHEET 1 AE2 4 LYS H 163 VAL H 165 0
SHEET 2 AE2 4 VAL H 154 VAL H 160 -1 N VAL H 160 O LYS H 163
SHEET 3 AE2 4 HIS H 206 PHE H 213 -1 O ARG H 208 N TRP H 159
SHEET 4 AE2 4 GLN H 232 TRP H 239 -1 O GLN H 232 N PHE H 213
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.01
SSBOND 2 CYS B 15 CYS B 77 1555 1555 2.04
SSBOND 3 CYS B 115 CYS B 171 1555 1555 2.03
SSBOND 4 CYS C 23 CYS C 90 1555 1555 2.02
SSBOND 5 CYS C 138 CYS C 188 1555 1555 2.04
SSBOND 6 CYS C 163 CYS D 170 1555 1555 2.03
SSBOND 7 CYS D 23 CYS D 91 1555 1555 2.02
SSBOND 8 CYS D 144 CYS D 209 1555 1555 2.01
SSBOND 9 CYS E 107 CYS E 163 1555 1555 2.03
SSBOND 10 CYS F 15 CYS F 77 1555 1555 2.04
SSBOND 11 CYS F 115 CYS F 171 1555 1555 2.03
SSBOND 12 CYS G 23 CYS G 90 1555 1555 2.03
SSBOND 13 CYS G 138 CYS G 188 1555 1555 2.06
SSBOND 14 CYS G 163 CYS H 170 1555 1555 2.04
SSBOND 15 CYS H 23 CYS H 91 1555 1555 2.01
SSBOND 16 CYS H 144 CYS H 209 1555 1555 2.01
LINK ND2 ASN A 78 C1 NAG A 201 1555 1555 1.44
LINK ND2 ASN A 118 C1 NAG A 202 1555 1555 1.43
LINK ND2 ASN B 19 C1 NAG B 201 1555 1555 1.44
LINK ND2 ASN E 78 C1 NAG E 202 1555 1555 1.44
LINK ND2 ASN E 118 C1 NAG E 201 1555 1555 1.43
LINK OD1 ASP B -20 NA NA B 202 1555 1555 2.98
LINK OD2 ASP B -20 NA NA B 202 1555 1555 2.82
LINK OD1 ASP B -20 BE 0BE B 203 1555 1555 1.65
LINK OE1 GLU B -17 NA NA B 202 1555 1555 2.06
LINK OE1 GLU B 26 BE 0BE B 203 1555 1555 1.67
LINK OE2 GLU B 68 NA NA B 202 1555 1555 2.98
LINK OE1 GLU B 69 NA NA B 202 1555 1555 2.97
LINK OE2 GLU B 69 NA NA B 202 1555 1555 2.67
LINK OE1 GLU B 69 BE 0BE B 203 1555 1555 1.65
LINK NA NA B 202 O HOH B 344 1555 1555 2.70
LINK OD2 ASP F -20 NA NA F 201 1555 1555 3.13
LINK OD1 ASP F -20 BE 0BE F 202 1555 1555 1.82
LINK OE1 GLU F -17 NA NA F 201 1555 1555 2.23
LINK OE1 GLU F 26 BE 0BE F 202 1555 1555 1.96
LINK OE2 GLU F 68 NA NA F 201 1555 1555 2.83
LINK OE1 GLU F 69 NA NA F 201 1555 1555 3.17
LINK OE2 GLU F 69 NA NA F 201 1555 1555 2.72
LINK OE1 GLU F 69 BE 0BE F 202 1555 1555 1.74
CISPEP 1 ARG A 17 PRO A 18 0 -0.12
CISPEP 2 PHE A 113 PRO A 114 0 1.58
CISPEP 3 TYR B 121 PRO B 122 0 -0.37
CISPEP 4 LYS C 183 SER C 184 0 -3.44
CISPEP 5 THR D 7 PRO D 8 0 -5.30
CISPEP 6 SER D 27 GLY D 28 0 -0.94
CISPEP 7 TYR D 150 PRO D 151 0 0.46
CISPEP 8 ARG E 17 PRO E 18 0 0.03
CISPEP 9 PHE E 113 PRO E 114 0 1.22
CISPEP 10 TYR F 121 PRO F 122 0 -0.06
CISPEP 11 ASN G 193 ASN G 194 0 2.24
CISPEP 12 ASN G 194 SER G 195 0 7.65
CISPEP 13 THR H 7 PRO H 8 0 -5.41
CISPEP 14 SER H 27 GLY H 28 0 0.72
CISPEP 15 TYR H 150 PRO H 151 0 0.13
CRYST1 79.400 137.240 213.130 90.00 90.00 90.00 P 21 21 21 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 0.012594 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007287 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004692 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
