HEADER SUGAR BINDING PROTEIN 23-SEP-01 1K12
TITLE FUCOSE BINDING LECTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LECTIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANGUILLA ANGUILLA;
SOURCE 3 ORGANISM_COMMON: EUROPEAN EEL;
SOURCE 4 ORGANISM_TAXID: 7936
KEYWDS BETA BARREL, PROTEIN CARBOHYDRATE COMPLEX, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.BIANCHET,E.W.ODOM,G.R.VASTA,L.M.AMZEL
REVDAT 3 29-JUL-20 1K12 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 24-FEB-09 1K12 1 VERSN
REVDAT 1 31-JUL-02 1K12 0
JRNL AUTH M.A.BIANCHET,E.W.ODOM,G.R.VASTA,L.M.AMZEL
JRNL TITL A NOVEL FUCOSE RECOGNITION FOLD INVOLVED IN INNATE IMMUNITY.
JRNL REF NAT.STRUCT.BIOL. V. 9 628 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 12091873
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2178865.510
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 16454
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) : 0.190
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1647
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2399
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 262
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1182
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.47000
REMARK 3 B22 (A**2) : 5.47000
REMARK 3 B33 (A**2) : -10.95000
REMARK 3 B12 (A**2) : 3.77000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.25
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.960
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.160 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.970 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.900 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.850 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 53.34
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16454
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.710
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.73
REMARK 200 R MERGE FOR SHELL (I) : 0.23700
REMARK 200 R SYM FOR SHELL (I) : 0.23700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: MLPHARE, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD 40-50%, 5MM FUCOSE 19 MM NA CL AND
REMARK 280 10 MM TRIS HCL PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 32.77000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 18.91977
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 81.71200
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 32.77000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 18.91977
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 81.71200
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 32.77000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 18.91977
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 81.71200
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 32.77000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 18.91977
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 81.71200
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 32.77000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 18.91977
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 81.71200
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 32.77000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 18.91977
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 81.71200
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 37.83954
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 163.42400
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 37.83954
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 163.42400
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 37.83954
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 163.42400
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 37.83954
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 163.42400
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 37.83954
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 163.42400
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 37.83954
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 163.42400
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
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 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 ILE A 2 73.62 76.75
REMARK 500 LEU A 66 -11.43 78.26
REMARK 500 CYS A 82 -177.58 -174.74
REMARK 500 SER A 100 60.95 63.51
REMARK 500 PRO A 138 47.36 -76.04
REMARK 500 GLU A 147 135.22 -173.90
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 CA A 160 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 35 O
REMARK 620 2 ASP A 38 OD1 75.5
REMARK 620 3 ASN A 40 O 164.2 91.4
REMARK 620 4 SER A 49 OG 101.6 70.6 81.8
REMARK 620 5 SER A 49 O 75.9 124.7 119.4 70.1
REMARK 620 6 CYS A 146 O 101.7 158.4 87.2 130.3 73.9
REMARK 620 7 GLU A 147 OE1 90.5 76.8 77.7 140.8 148.9 81.8
REMARK 620 N 1 2 3 4 5 6
DBREF 1K12 A 1 158 UNP Q7SIC1 Q7SIC1_ANGAN 1 158
SEQRES 1 A 158 VAL ILE PRO GLU GLY TYR THR GLN GLU ASN VAL ALA VAL
SEQRES 2 A 158 ARG GLY LYS ALA THR GLN SER ALA GLN LEU ARG GLY GLU
SEQRES 3 A 158 HIS ALA ALA ASN SER GLU ALA SER ASN ALA ILE ASP GLY
SEQRES 4 A 158 ASN ARG ASP SER ASN PHE TYR HIS GLY SER CYS THR HIS
SEQRES 5 A 158 SER SER GLY GLN ALA ASN PRO TRP TRP ARG VAL ASP LEU
SEQRES 6 A 158 LEU GLN VAL TYR THR ILE THR SER VAL THR ILE THR ASN
SEQRES 7 A 158 ARG GLY ASP CYS CYS GLY GLU ARG ILE SER GLY ALA GLU
SEQRES 8 A 158 ILE ASN ILE GLY GLN HIS LEU ALA SER ASN GLY VAL ASN
SEQRES 9 A 158 ASN PRO GLU CYS SER VAL ILE GLY SER MET ALA THR GLY
SEQRES 10 A 158 GLU THR LYS THR PHE HIS CYS PRO ALA PRO MET ILE GLY
SEQRES 11 A 158 ARG TYR VAL VAL THR TYR LEU PRO THR SER GLU SER LEU
SEQRES 12 A 158 HIS LEU CYS GLU VAL GLU VAL ASN VAL ASP LYS PRO ALA
SEQRES 13 A 158 ALA ALA
HET FUC A 159 11
HET CA A 160 1
HET CL A 301 1
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 FUC C6 H12 O5
FORMUL 3 CA CA 2+
FORMUL 4 CL CL 1-
FORMUL 5 HOH *130(H2 O)
HELIX 1 1 ALA A 12 GLY A 15 5 4
HELIX 2 2 HIS A 27 SER A 31 5 5
HELIX 3 3 GLU A 32 ASP A 38 5 7
HELIX 4 4 ASN A 44 GLY A 48 5 5
SHEET 1 A 5 GLU A 107 VAL A 110 0
SHEET 2 A 5 GLU A 91 GLY A 95 -1 N ILE A 92 O CYS A 108
SHEET 3 A 5 THR A 119 TYR A 136 -1 O VAL A 134 N ASN A 93
SHEET 4 A 5 TRP A 60 ASN A 78 -1 N ILE A 71 O MET A 128
SHEET 5 A 5 LYS A 16 GLN A 19 -1 N LYS A 16 O ASP A 64
SHEET 1 B 6 GLU A 107 VAL A 110 0
SHEET 2 B 6 GLU A 91 GLY A 95 -1 N ILE A 92 O CYS A 108
SHEET 3 B 6 THR A 119 TYR A 136 -1 O VAL A 134 N ASN A 93
SHEET 4 B 6 TRP A 60 ASN A 78 -1 N ILE A 71 O MET A 128
SHEET 5 B 6 LEU A 145 PRO A 155 -1 O CYS A 146 N THR A 77
SHEET 6 B 6 TYR A 6 ASN A 10 -1 N THR A 7 O LYS A 154
SSBOND 1 CYS A 50 CYS A 146 1555 1555 2.05
SSBOND 2 CYS A 82 CYS A 83 1555 1555 2.05
SSBOND 3 CYS A 108 CYS A 124 1555 1555 2.06
LINK O ASN A 35 CA CA A 160 1555 1555 2.42
LINK OD1 ASP A 38 CA CA A 160 1555 1555 2.56
LINK O ASN A 40 CA CA A 160 1555 1555 2.38
LINK OG SER A 49 CA CA A 160 1555 1555 2.59
LINK O SER A 49 CA CA A 160 1555 1555 2.49
LINK O CYS A 146 CA CA A 160 1555 1555 2.37
LINK OE1 GLU A 147 CA CA A 160 1555 1555 2.45
CRYST1 65.540 65.540 245.136 90.00 90.00 120.00 H 3 2 18
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 0.015258 0.008809 0.000000 0.00000
SCALE2 0.000000 0.017618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004079 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
