HEADER HYDROLASE/IMMUNE SYSTEM 01-JUN-05 1ZV5
TITLE CRYSTAL STRUCTURE OF THE VARIABLE DOMAIN OF THE CAMELID HEAVY-CHAIN
TITLE 2 ANTIBODY D2-L29 IN COMPLEX WITH HEN EGG WHITE LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: L;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D 4, GAL D IV;
COMPND 5 EC: 3.2.1.17;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: IMMUNOGLOBULIN HEAVY CHAIN ANTIBODY VARIABLE DOMAIN;
COMPND 8 CHAIN: A;
COMPND 9 FRAGMENT: VHH D2-L29;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS;
SOURCE 7 ORGANISM_COMMON: ARABIAN CAMEL;
SOURCE 8 ORGANISM_TAXID: 9838;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: WK6SU-;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PHEN06
KEYWDS BETA-SANDWICH, IMMUNOGLOBULIN FOLD, PROTEIN-PROTEIN HETEROCOMPLEX,
KEYWDS 2 ALPHA-BETA ORTHOGONAL BUNDLE, HYDROLASE-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DE GENST,K.SILENCE,K.DECANNIERE,K.CONRATH,R.LORIS,J.KINNE,
AUTHOR 2 S.MUYLDERMANS,L.WYNS
REVDAT 4 23-AUG-23 1ZV5 1 REMARK
REVDAT 3 11-OCT-17 1ZV5 1 REMARK
REVDAT 2 24-FEB-09 1ZV5 1 VERSN
REVDAT 1 04-APR-06 1ZV5 0
JRNL AUTH E.DE GENST,K.SILENCE,K.DECANNIERE,K.CONRATH,R.LORIS,J.KINNE,
JRNL AUTH 2 S.MUYLDERMANS,L.WYNS
JRNL TITL MOLECULAR BASIS FOR THE PREFERENTIAL CLEFT RECOGNITION BY
JRNL TITL 2 DROMEDARY HEAVY-CHAIN ANTIBODIES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 4586 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16537393
JRNL DOI 10.1073/PNAS.0505379103
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2209106.750
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 16470
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) : 0.217
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 830
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2540
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 140
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 : 1824
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.09000
REMARK 3 B22 (A**2) : -3.09000
REMARK 3 B33 (A**2) : 6.18000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.110
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) : 1.370 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.090 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.030 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.920 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 65.62
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
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.TOP
REMARK 3 PARAMETER FILE 2 : WATER.TOP
REMARK 3 PARAMETER FILE 3 : PO4_XPLOR_TOP.TXT
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 3 : PO4_XPLOR_PAR.TXT
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1ZV5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033156.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8123
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16498
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
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: PHASER
REMARK 200 STARTING MODEL: ENTITY 1: CHAIN L OF 1JTT, ENTITY 2: 1YCV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PEG 400, PH 7.4,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 17.83650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 57.03650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 57.03650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.75475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 57.03650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 57.03650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 8.91825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 57.03650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.03650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.75475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 57.03650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.03650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 8.91825
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 17.83650
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, 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 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 ASP A 1
REMARK 465 SER A 121
REMARK 465 ARG A 122
REMARK 465 GLY A 123
REMARK 465 ARG A 124
REMARK 465 HIS A 125
REMARK 465 HIS A 126
REMARK 465 HIS A 127
REMARK 465 HIS A 128
REMARK 465 HIS A 129
REMARK 465 HIS A 130
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 L 1 CE NZ
REMARK 470 ARG L 21 CD NE CZ NH1 NH2
REMARK 470 GLN L 41 CD OE1 NE2
REMARK 470 ARG L 61 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG L 68 CG CD NE CZ NH1 NH2
REMARK 470 ARG L 73 CG CD NE CZ NH1 NH2
REMARK 470 ASN L 77 OD1 ND2
REMARK 470 LYS L 97 CG CD CE NZ
REMARK 470 ASN L 103 CG OD1 ND2
REMARK 470 LYS L 116 CD CE NZ
REMARK 470 ASP L 119 CB CG OD1 OD2
REMARK 470 GLN L 121 CG CD OE1 NE2
REMARK 470 ARG L 125 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG L 128 CB CG CD NE CZ NH1 NH2
REMARK 470 GLN A 13 CG CD OE1 NE2
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 LYS A 65 CG CD CE NZ
REMARK 470 LYS A 76 CD CE NZ
REMARK 470 LYS A 87 CD CE NZ
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 ALA A 14 151.12 -48.41
REMARK 500 VAL A 48 -67.46 -109.33
REMARK 500 ASN A 77 50.66 36.80
REMARK 500 ALA A 92 172.19 174.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 132
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF A CAMELID HEAVY-CHAIN ANTIBODY
REMARK 999 HAS NOT BEEN DEPOSITED INTO ANY SEQUENCE DATABASE.
DBREF 1ZV5 L 1 129 UNP P00698 LYSC_CHICK 19 147
DBREF 1ZV5 A 1 130 PDB 1ZV5 1ZV5 1 130
SEQRES 1 L 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 L 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 L 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 L 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 L 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 L 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 L 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 L 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 L 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 L 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
SEQRES 1 A 130 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN
SEQRES 2 A 130 ALA GLY GLU SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 A 130 VAL THR TYR LYS ASN TYR CYS ILE GLY TRP PHE ARG GLN
SEQRES 4 A 130 ALA PRO GLY LYS ASP ARG GLU GLY VAL VAL PHE ILE ASN
SEQRES 5 A 130 SER ASP GLY GLY ILE THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 A 130 GLY ARG PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR
SEQRES 7 A 130 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR
SEQRES 8 A 130 ALA SER TYR TYR CYS ALA ALA GLY TYR ARG ASN TYR GLY
SEQRES 9 A 130 GLN CYS ALA THR ARG TYR TRP GLY GLN GLY THR GLN VAL
SEQRES 10 A 130 THR VAL SER SER ARG GLY ARG HIS HIS HIS HIS HIS HIS
HET PO4 A 131 5
HET PO4 A 132 5
HETNAM PO4 PHOSPHATE ION
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 5 HOH *46(H2 O)
HELIX 1 1 GLY L 4 ARG L 14 1 11
HELIX 2 2 ASN L 19 TYR L 23 5 5
HELIX 3 3 SER L 24 ASN L 37 1 14
HELIX 4 4 PRO L 79 SER L 85 5 7
HELIX 5 5 ILE L 88 VAL L 99 1 12
HELIX 6 6 ASN L 103 ALA L 107 5 5
HELIX 7 7 TRP L 108 CYS L 115 1 8
HELIX 8 8 ASP L 119 ARG L 125 5 7
HELIX 9 9 ALA A 61 LYS A 65 5 5
HELIX 10 10 ASN A 74 LYS A 76 5 3
HELIX 11 11 LYS A 87 THR A 91 5 5
SHEET 1 A 3 THR L 43 ARG L 45 0
SHEET 2 A 3 THR L 51 TYR L 53 -1 O ASP L 52 N ASN L 44
SHEET 3 A 3 ILE L 58 ASN L 59 -1 O ILE L 58 N TYR L 53
SHEET 1 B 4 GLN A 3 SER A 7 0
SHEET 2 B 4 LEU A 18 SER A 25 -1 O ALA A 23 N VAL A 5
SHEET 3 B 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18
SHEET 4 B 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80
SHEET 1 C 6 GLY A 10 GLN A 13 0
SHEET 2 C 6 THR A 115 SER A 120 1 O THR A 118 N GLY A 10
SHEET 3 C 6 ALA A 92 ASN A 102 -1 N TYR A 94 O THR A 115
SHEET 4 C 6 TYR A 32 GLN A 39 -1 N GLY A 35 O ALA A 97
SHEET 5 C 6 GLU A 46 ASN A 52 -1 O GLU A 46 N ARG A 38
SHEET 6 C 6 ILE A 57 TYR A 59 -1 O THR A 58 N PHE A 50
SHEET 1 D 4 GLY A 10 GLN A 13 0
SHEET 2 D 4 THR A 115 SER A 120 1 O THR A 118 N GLY A 10
SHEET 3 D 4 ALA A 92 ASN A 102 -1 N TYR A 94 O THR A 115
SHEET 4 D 4 GLN A 105 TRP A 111 -1 O GLN A 105 N ASN A 102
SSBOND 1 CYS L 6 CYS L 127 1555 1555 2.03
SSBOND 2 CYS L 30 CYS L 115 1555 1555 2.03
SSBOND 3 CYS L 64 CYS L 80 1555 1555 2.03
SSBOND 4 CYS L 76 CYS L 94 1555 1555 2.03
SSBOND 5 CYS A 22 CYS A 96 1555 1555 2.02
SSBOND 6 CYS A 33 CYS A 106 1555 1555 2.03
SITE 1 AC1 9 ASN A 52 ARG A 101 TYR A 103 GLY A 104
SITE 2 AC1 9 HOH A 155 HOH A 164 HIS L 15 ASN L 93
SITE 3 AC1 9 LYS L 96
SITE 1 AC2 4 GLN A 39 ASP A 44 ARG A 45 ARG L 45
CRYST1 114.073 114.073 35.673 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 0.008770 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008770 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028030 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
