HEADER LIPID BINDING PROTEIN 11-MAY-04 1T80
TITLE ZN-ALPHA-2-GLYCOPROTEIN; CHO-ZAG PEG 200
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC-ALPHA-2-GLYCOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ZN-ALPHA-2-GLYCOPROTEIN, ZN-ALPHA-2-GP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AZGP1, ZAG, ZNGP1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBJ5-GS
KEYWDS MHC CLASS I HOMOLOG, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.L.DELKER,A.P.WEST JR.,L.MCDERMOTT,M.W.KENNEDY,P.J.BJORKMAN
REVDAT 7 23-AUG-23 1T80 1 REMARK
REVDAT 6 27-OCT-21 1T80 1 SEQADV HETSYN
REVDAT 5 29-JUL-20 1T80 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 11-OCT-17 1T80 1 REMARK
REVDAT 3 13-JUL-11 1T80 1 VERSN
REVDAT 2 24-FEB-09 1T80 1 VERSN
REVDAT 1 21-DEC-04 1T80 0
JRNL AUTH S.L.DELKER,A.P.WEST JR.,L.MCDERMOTT,M.W.KENNEDY,P.J.BJORKMAN
JRNL TITL CRYSTALLOGRAPHIC STUDIES OF LIGAND BINDING BY
JRNL TITL 2 ZN-ALPHA2-GLYCOPROTEIN.
JRNL REF J.STRUCT.BIOL. V. 148 205 2004
JRNL REFN ISSN 1047-8477
JRNL PMID 15477100
JRNL DOI 10.1016/J.JSB.2004.04.009
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.M.SANCHEZ,A.J.CHIRINO,P.J.BJORKMAN
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN ZAG, A FAT-DEPLETING FACTOR
REMARK 1 TITL 2 RELATED TO MHC MOLECULES
REMARK 1 REF SCIENCE V. 283 1914 1999
REMARK 1 REFN ISSN 0036-8075
REMARK 1 DOI 10.1126/SCIENCE.283.5409.1914
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 29531
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) : 0.236
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1344
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2761
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 152
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2232
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 185
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.61000
REMARK 3 B22 (A**2) : 1.61000
REMARK 3 B33 (A**2) : -3.22000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.24
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.530 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.500 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.270 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.440 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 54.68
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T80 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1271
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 1T7V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 200, HEPES, PH
REMARK 280 7.5, MICROBATCH, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 32.72250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 61.27250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 61.27250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.08375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 61.27250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 61.27250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 16.36125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 61.27250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.27250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 49.08375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 61.27250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.27250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 16.36125
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 32.72250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 458 LIES ON A SPECIAL POSITION.
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 GLN A 1
REMARK 465 GLU A 2
REMARK 465 ASN A 3
REMARK 465 GLN A 4
REMARK 465 SER A 278
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 34 -126.74 57.01
REMARK 500 ASP A 90 52.78 -142.85
REMARK 500 TRP A 115 105.54 -163.58
REMARK 500 PRO A 197 100.94 -55.28
REMARK 500 ALA A 256 156.33 -46.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZAG RELATED DB: PDB
REMARK 900 RELATED ID: 1T7V RELATED DB: PDB
REMARK 900 RELATED ID: 1T7W RELATED DB: PDB
REMARK 900 RELATED ID: 1T7X RELATED DB: PDB
REMARK 900 RELATED ID: 1T7Y RELATED DB: PDB
REMARK 900 RELATED ID: 1T7Z RELATED DB: PDB
DBREF 1T80 A 1 278 UNP P25311 ZA2G_HUMAN 18 295
SEQADV 1T80 LYS A 89 UNP P25311 ASN 106 ENGINEERED MUTATION
SEQADV 1T80 THR A 92 UNP P25311 ASN 109 ENGINEERED MUTATION
SEQRES 1 A 278 GLN GLU ASN GLN ASP GLY ARG TYR SER LEU THR TYR ILE
SEQRES 2 A 278 TYR THR GLY LEU SER LYS HIS VAL GLU ASP VAL PRO ALA
SEQRES 3 A 278 PHE GLN ALA LEU GLY SER LEU ASN ASP LEU GLN PHE PHE
SEQRES 4 A 278 ARG TYR ASN SER LYS ASP ARG LYS SER GLN PRO MET GLY
SEQRES 5 A 278 LEU TRP ARG GLN VAL GLU GLY MET GLU ASP TRP LYS GLN
SEQRES 6 A 278 ASP SER GLN LEU GLN LYS ALA ARG GLU ASP ILE PHE MET
SEQRES 7 A 278 GLU THR LEU LYS ASP ILE VAL GLU TYR TYR LYS ASP SER
SEQRES 8 A 278 THR GLY SER HIS VAL LEU GLN GLY ARG PHE GLY CYS GLU
SEQRES 9 A 278 ILE GLU ASN ASN ARG SER SER GLY ALA PHE TRP LYS TYR
SEQRES 10 A 278 TYR TYR ASP GLY LYS ASP TYR ILE GLU PHE ASN LYS GLU
SEQRES 11 A 278 ILE PRO ALA TRP VAL PRO PHE ASP PRO ALA ALA GLN ILE
SEQRES 12 A 278 THR LYS GLN LYS TRP GLU ALA GLU PRO VAL TYR VAL GLN
SEQRES 13 A 278 ARG ALA LYS ALA TYR LEU GLU GLU GLU CYS PRO ALA THR
SEQRES 14 A 278 LEU ARG LYS TYR LEU LYS TYR SER LYS ASN ILE LEU ASP
SEQRES 15 A 278 ARG GLN ASP PRO PRO SER VAL VAL VAL THR SER HIS GLN
SEQRES 16 A 278 ALA PRO GLY GLU LYS LYS LYS LEU LYS CYS LEU ALA TYR
SEQRES 17 A 278 ASP PHE TYR PRO GLY LYS ILE ASP VAL HIS TRP THR ARG
SEQRES 18 A 278 ALA GLY GLU VAL GLN GLU PRO GLU LEU ARG GLY ASP VAL
SEQRES 19 A 278 LEU HIS ASN GLY ASN GLY THR TYR GLN SER TRP VAL VAL
SEQRES 20 A 278 VAL ALA VAL PRO PRO GLN ASP THR ALA PRO TYR SER CYS
SEQRES 21 A 278 HIS VAL GLN HIS SER SER LEU ALA GLN PRO LEU VAL VAL
SEQRES 22 A 278 PRO TRP GLU ALA SER
MODRES 1T80 ASN A 108 ASN GLYCOSYLATION SITE
MODRES 1T80 ASN A 239 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG A 310 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
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
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 4 HOH *185(H2 O)
HELIX 1 1 GLY A 52 VAL A 57 5 6
HELIX 2 2 ASP A 62 TYR A 88 1 27
HELIX 3 3 ALA A 140 GLU A 149 1 10
HELIX 4 4 PRO A 152 GLU A 164 1 13
HELIX 5 5 GLU A 164 SER A 177 1 14
HELIX 6 6 SER A 177 ASP A 182 1 6
SHEET 1 A 8 GLN A 49 PRO A 50 0
SHEET 2 A 8 LEU A 36 ASN A 42 -1 N ARG A 40 O GLN A 49
SHEET 3 A 8 PHE A 27 LEU A 33 -1 N ALA A 29 O TYR A 41
SHEET 4 A 8 ARG A 7 LEU A 17 -1 N THR A 15 O GLN A 28
SHEET 5 A 8 VAL A 96 GLU A 106 -1 O PHE A 101 N TYR A 12
SHEET 6 A 8 ARG A 109 TYR A 119 -1 O TYR A 118 N GLN A 98
SHEET 7 A 8 LYS A 122 ASN A 128 -1 O ILE A 125 N TYR A 117
SHEET 8 A 8 ALA A 133 PRO A 136 -1 O ALA A 133 N ASN A 128
SHEET 1 B 4 SER A 188 GLN A 195 0
SHEET 2 B 4 LYS A 201 PHE A 210 -1 O LYS A 204 N THR A 192
SHEET 3 B 4 THR A 241 VAL A 250 -1 O VAL A 250 N LYS A 201
SHEET 4 B 4 LEU A 230 HIS A 236 -1 N HIS A 236 O THR A 241
SHEET 1 C 4 GLU A 224 VAL A 225 0
SHEET 2 C 4 ASP A 216 ARG A 221 -1 N ARG A 221 O GLU A 224
SHEET 3 C 4 TYR A 258 GLN A 263 -1 O HIS A 261 N HIS A 218
SHEET 4 C 4 LEU A 271 PRO A 274 -1 O LEU A 271 N VAL A 262
SSBOND 1 CYS A 205 CYS A 260 1555 1555 2.02
LINK ND2 ASN A 108 C1 NAG A 310 1555 1555 1.45
LINK ND2 ASN A 239 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.39
CISPEP 1 ILE A 131 PRO A 132 0 -0.64
CISPEP 2 TYR A 211 PRO A 212 0 -0.02
CRYST1 122.545 122.545 65.445 90.00 90.00 90.00 P 43 21 2 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 0.008160 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008160 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015280 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
