HEADER IMMUNE SYSTEM 20-JUN-14 4TTD
TITLE STRUCTURE OF A LYSOZYME ANTIBODY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 19-147;
COMPND 5 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C,ALLERGEN GAL D IV;
COMPND 6 EC: 3.2.1.17;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FAB HEAVY CHAIN;
COMPND 9 CHAIN: C, H;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: FAB LIGHT CHAIN;
COMPND 13 CHAIN: D, L;
COMPND 14 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: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 10 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 12 MOL_ID: 3;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS IMMUNE SYSTEM, AFFINITY MATURATION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.WENSLEY
REVDAT 2 15-JUL-15 4TTD 1 REMARK
REVDAT 1 08-JUL-15 4TTD 0
JRNL AUTH B.WENSLEY
JRNL TITL STRUCTURE OF A LYSOZYME ANTIBODY COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 57603
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) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 2808
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.37
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4300
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2785
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4087
REMARK 3 BIN R VALUE (WORKING SET) : 0.2769
REMARK 3 BIN FREE R VALUE : 0.3106
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.95
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 213
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 : 8296
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.22140
REMARK 3 B22 (A**2) : -0.19390
REMARK 3 B33 (A**2) : 3.41530
REMARK 3 B12 (A**2) : -5.97720
REMARK 3 B13 (A**2) : -1.85390
REMARK 3 B23 (A**2) : -1.15370
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.437
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.325
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.229
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.340
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.236
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 : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8497 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11564 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2778 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 170 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1251 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8497 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1113 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 8523 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.68
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.56
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 4TTD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000202253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57649
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 44.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 1.640
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.64
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PCTP PH 4.5, 25% W/V PEG3350,
REMARK 280 ETHANOL 5%, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, C
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 ARG A 128
REMARK 465 LEU A 129
REMARK 465 ARG B 128
REMARK 465 LEU B 129
REMARK 465 GLN C 1
REMARK 465 LYS C 129
REMARK 465 SER C 130
REMARK 465 THR C 131
REMARK 465 SER C 132
REMARK 465 LYS C 214
REMARK 465 SER C 215
REMARK 465 ASP C 216
REMARK 465 CYS C 217
REMARK 465 LYS C 218
REMARK 465 GLU D 212
REMARK 465 CYS D 213
REMARK 465 SER D 214
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 THR H 131
REMARK 465 SER H 132
REMARK 465 CYS H 217
REMARK 465 LYS H 218
REMARK 465 GLU L 212
REMARK 465 CYS L 213
REMARK 465 SER L 214
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 VAL C 211 O
REMARK 470 SER D 27 CB OG
REMARK 470 VAL H 211 O
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 GLN B 57 68.10 38.33
REMARK 500 ASP C 144 85.84 50.36
REMARK 500 ASN D 27B -92.91 -126.84
REMARK 500 ARG D 95A 65.43 63.00
REMARK 500 ASN D 129 34.04 72.39
REMARK 500 ASP D 152 -110.60 70.49
REMARK 500 PRO D 210 97.37 -64.11
REMARK 500 ASP H 144 85.58 50.57
REMARK 500 ASN L 27B -97.80 -122.45
REMARK 500 ASN L 129 34.06 72.45
REMARK 500 ASP L 152 -110.95 70.55
REMARK 500 PRO L 210 100.32 -57.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 229 DISTANCE = 7.55 ANGSTROMS
REMARK 525 HOH C 358 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH C 359 DISTANCE = 6.54 ANGSTROMS
DBREF 4TTD A 1 129 UNP P00698 LYSC_CHICK 19 147
DBREF 4TTD B 1 129 UNP P00698 LYSC_CHICK 19 147
DBREF 4TTD C 1 218 PDB 4TTD 4TTD 1 218
DBREF 4TTD D 1 214 PDB 4TTD 4TTD 1 214
DBREF 4TTD H 1 218 PDB 4TTD 4TTD 1 218
DBREF 4TTD L 1 214 PDB 4TTD 4TTD 1 214
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
SEQRES 1 B 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 B 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 B 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 B 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 B 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 B 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 B 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 B 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 B 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 B 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
SEQRES 1 C 222 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 C 222 PRO GLY GLY PRO LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 C 222 PHE THR ILE SER SER ASN TYR MET SER TRP VAL ARG GLN
SEQRES 4 C 222 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE TYR
SEQRES 5 C 222 SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY
SEQRES 6 C 222 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU
SEQRES 7 C 222 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA
SEQRES 8 C 222 VAL TYR TYR CYS ALA ARG GLU GLY PRO GLY ASP SER ILE
SEQRES 9 C 222 VAL TYR TRP GLY LYS GLY THR LEU VAL THR VAL SER SER
SEQRES 10 C 222 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 11 C 222 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY
SEQRES 12 C 222 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 C 222 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 14 C 222 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 15 C 222 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 16 C 222 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN
SEQRES 17 C 222 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER ASP CYS
SEQRES 18 C 222 LYS
SEQRES 1 D 217 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA
SEQRES 2 D 217 PRO GLY GLN ARG VAL SER ILE SER CYS THR GLY ARG SER
SEQRES 3 D 217 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN
SEQRES 4 D 217 GLN LEU PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY
SEQRES 5 D 217 ASN THR ASN ARG PRO SER GLY VAL PRO VAL ARG PHE SER
SEQRES 6 D 217 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR
SEQRES 7 D 217 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN
SEQRES 8 D 217 SER TYR ASP SER SER LEU ARG GLY SER VAL PHE GLY GLY
SEQRES 9 D 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA
SEQRES 10 D 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU
SEQRES 11 D 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP
SEQRES 12 D 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP
SEQRES 13 D 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO
SEQRES 14 D 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR
SEQRES 15 D 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER
SEQRES 16 D 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU
SEQRES 17 D 217 LYS THR VAL ALA PRO THR GLU CYS SER
SEQRES 1 H 222 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 222 PRO GLY GLY PRO LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 222 PHE THR ILE SER SER ASN TYR MET SER TRP VAL ARG GLN
SEQRES 4 H 222 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE TYR
SEQRES 5 H 222 SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY
SEQRES 6 H 222 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU
SEQRES 7 H 222 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA
SEQRES 8 H 222 VAL TYR TYR CYS ALA ARG GLU GLY PRO GLY ASP SER ILE
SEQRES 9 H 222 VAL TYR TRP GLY LYS GLY THR LEU VAL THR VAL SER SER
SEQRES 10 H 222 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 11 H 222 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY
SEQRES 12 H 222 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 H 222 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 14 H 222 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 15 H 222 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 16 H 222 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN
SEQRES 17 H 222 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER ASP CYS
SEQRES 18 H 222 LYS
SEQRES 1 L 217 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA
SEQRES 2 L 217 PRO GLY GLN ARG VAL SER ILE SER CYS THR GLY ARG SER
SEQRES 3 L 217 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN
SEQRES 4 L 217 GLN LEU PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY
SEQRES 5 L 217 ASN THR ASN ARG PRO SER GLY VAL PRO VAL ARG PHE SER
SEQRES 6 L 217 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR
SEQRES 7 L 217 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN
SEQRES 8 L 217 SER TYR ASP SER SER LEU ARG GLY SER VAL PHE GLY GLY
SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA
SEQRES 10 L 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU
SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP
SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP
SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO
SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR
SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER
SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU
SEQRES 17 L 217 LYS THR VAL ALA PRO THR GLU CYS SER
FORMUL 7 HOH *323(H2 O)
HELIX 1 AA1 GLY A 4 HIS A 15 1 12
HELIX 2 AA2 ASN A 19 TYR A 23 5 5
HELIX 3 AA3 SER A 24 ASN A 37 1 14
HELIX 4 AA4 PRO A 79 SER A 85 5 7
HELIX 5 AA5 ILE A 88 VAL A 99 1 12
HELIX 6 AA6 ASN A 103 ALA A 107 5 5
HELIX 7 AA7 TRP A 108 CYS A 115 1 8
HELIX 8 AA8 ASP A 119 ILE A 124 5 6
HELIX 9 AA9 GLY B 4 HIS B 15 1 12
HELIX 10 AB1 ASN B 19 TYR B 23 5 5
HELIX 11 AB2 SER B 24 ASN B 37 1 14
HELIX 12 AB3 PRO B 79 SER B 85 5 7
HELIX 13 AB4 ILE B 88 VAL B 99 1 12
HELIX 14 AB5 ASN B 103 ALA B 107 5 5
HELIX 15 AB6 TRP B 108 CYS B 115 1 8
HELIX 16 AB7 ASP B 119 ILE B 124 5 6
HELIX 17 AB8 THR C 28 ASN C 32 5 5
HELIX 18 AB9 ARG C 83 THR C 87 5 5
HELIX 19 AC1 SER C 156 ALA C 158 5 3
HELIX 20 AC2 SER C 187 LEU C 189 5 3
HELIX 21 AC3 ASN D 27B GLY D 30 5 5
HELIX 22 AC4 GLN D 79 GLU D 83 5 5
HELIX 23 AC5 SER D 122 GLN D 127 1 6
HELIX 24 AC6 THR D 183 SER D 189 1 7
HELIX 25 AC7 THR H 28 ASN H 32 5 5
HELIX 26 AC8 ARG H 83 THR H 87 5 5
HELIX 27 AC9 SER H 156 ALA H 158 5 3
HELIX 28 AD1 SER H 187 LEU H 189 5 3
HELIX 29 AD2 ASN L 27B GLY L 30 5 5
HELIX 30 AD3 GLN L 79 GLU L 83 5 5
HELIX 31 AD4 SER L 122 GLN L 127 1 6
HELIX 32 AD5 THR L 183 SER L 189 1 7
SHEET 1 AA1 3 THR A 43 ARG A 45 0
SHEET 2 AA1 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 AA1 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SHEET 1 AA2 3 THR B 43 ARG B 45 0
SHEET 2 AA2 3 THR B 51 TYR B 53 -1 O ASP B 52 N ASN B 44
SHEET 3 AA2 3 ILE B 58 ASN B 59 -1 O ILE B 58 N TYR B 53
SHEET 1 AA3 4 GLN C 3 SER C 7 0
SHEET 2 AA3 4 LEU C 18 SER C 25 -1 O SER C 21 N SER C 7
SHEET 3 AA3 4 THR C 77 MET C 82 -1 O LEU C 80 N LEU C 20
SHEET 4 AA3 4 PHE C 67 ASP C 72 -1 N THR C 68 O GLN C 81
SHEET 1 AA4 6 LEU C 11 VAL C 12 0
SHEET 2 AA4 6 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12
SHEET 3 AA4 6 ALA C 88 GLU C 95 -1 N TYR C 90 O THR C 107
SHEET 4 AA4 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 91
SHEET 5 AA4 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38
SHEET 6 AA4 6 THR C 57 TYR C 59 -1 O TYR C 58 N ALA C 50
SHEET 1 AA5 4 LEU C 11 VAL C 12 0
SHEET 2 AA5 4 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12
SHEET 3 AA5 4 ALA C 88 GLU C 95 -1 N TYR C 90 O THR C 107
SHEET 4 AA5 4 ILE C 100A TRP C 103 -1 O TYR C 102 N ARG C 94
SHEET 1 AA6 4 SER C 120 LEU C 124 0
SHEET 2 AA6 4 THR C 135 TYR C 145 -1 O GLY C 139 N LEU C 124
SHEET 3 AA6 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142
SHEET 4 AA6 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181
SHEET 1 AA7 4 SER C 120 LEU C 124 0
SHEET 2 AA7 4 THR C 135 TYR C 145 -1 O GLY C 139 N LEU C 124
SHEET 3 AA7 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142
SHEET 4 AA7 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177
SHEET 1 AA8 3 THR C 151 TRP C 154 0
SHEET 2 AA8 3 ILE C 195 HIS C 200 -1 O ASN C 197 N SER C 153
SHEET 3 AA8 3 THR C 205 ARG C 210 -1 O LYS C 209 N CYS C 196
SHEET 1 AA9 5 SER D 9 GLY D 13 0
SHEET 2 AA9 5 THR D 102 VAL D 106 1 O THR D 105 N VAL D 11
SHEET 3 AA9 5 ALA D 84 ASP D 92 -1 N ALA D 84 O LEU D 104
SHEET 4 AA9 5 HIS D 34 GLN D 38 -1 N GLN D 38 O ASP D 85
SHEET 5 AA9 5 LYS D 45 ILE D 48 -1 O LEU D 47 N TRP D 35
SHEET 1 AB1 4 SER D 9 GLY D 13 0
SHEET 2 AB1 4 THR D 102 VAL D 106 1 O THR D 105 N VAL D 11
SHEET 3 AB1 4 ALA D 84 ASP D 92 -1 N ALA D 84 O LEU D 104
SHEET 4 AB1 4 GLY D 95B PHE D 98 -1 O VAL D 97 N SER D 90
SHEET 1 AB2 3 VAL D 19 THR D 24 0
SHEET 2 AB2 3 SER D 70 ILE D 75 -1 O ILE D 75 N VAL D 19
SHEET 3 AB2 3 PHE D 62 SER D 67 -1 N SER D 63 O ALA D 74
SHEET 1 AB3 4 SER D 115 PHE D 119 0
SHEET 2 AB3 4 ALA D 131 PHE D 140 -1 O LEU D 136 N THR D 117
SHEET 3 AB3 4 TYR D 174 LEU D 182 -1 O SER D 178 N CYS D 135
SHEET 4 AB3 4 VAL D 160 THR D 162 -1 N GLU D 161 O TYR D 179
SHEET 1 AB4 4 SER D 115 PHE D 119 0
SHEET 2 AB4 4 ALA D 131 PHE D 140 -1 O LEU D 136 N THR D 117
SHEET 3 AB4 4 TYR D 174 LEU D 182 -1 O SER D 178 N CYS D 135
SHEET 4 AB4 4 SER D 166 LYS D 167 -1 N SER D 166 O ALA D 175
SHEET 1 AB5 4 SER D 154 VAL D 156 0
SHEET 2 AB5 4 THR D 146 ALA D 151 -1 N ALA D 151 O SER D 154
SHEET 3 AB5 4 TYR D 193 HIS D 199 -1 O GLN D 196 N ALA D 148
SHEET 4 AB5 4 SER D 202 VAL D 208 -1 O VAL D 204 N VAL D 197
SHEET 1 AB6 4 GLN H 3 SER H 7 0
SHEET 2 AB6 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7
SHEET 3 AB6 4 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20
SHEET 4 AB6 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81
SHEET 1 AB7 6 LEU H 11 VAL H 12 0
SHEET 2 AB7 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 AB7 6 ALA H 88 GLU H 95 -1 N TYR H 90 O THR H 107
SHEET 4 AB7 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 AB7 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 AB7 6 THR H 57 TYR H 59 -1 O TYR H 58 N ALA H 50
SHEET 1 AB8 4 LEU H 11 VAL H 12 0
SHEET 2 AB8 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 AB8 4 ALA H 88 GLU H 95 -1 N TYR H 90 O THR H 107
SHEET 4 AB8 4 ILE H 100A TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 AB9 4 SER H 120 LEU H 124 0
SHEET 2 AB9 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AB9 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 AB9 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 AC1 4 SER H 120 LEU H 124 0
SHEET 2 AC1 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AC1 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 AC1 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 AC2 3 THR H 151 TRP H 154 0
SHEET 2 AC2 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 AC2 3 THR H 205 ARG H 210 -1 O LYS H 209 N CYS H 196
SHEET 1 AC3 5 SER L 9 GLY L 13 0
SHEET 2 AC3 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 AC3 5 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104
SHEET 4 AC3 5 HIS L 34 GLN L 38 -1 N GLN L 38 O ASP L 85
SHEET 5 AC3 5 LYS L 45 ILE L 48 -1 O LEU L 47 N TRP L 35
SHEET 1 AC4 4 SER L 9 GLY L 13 0
SHEET 2 AC4 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 AC4 4 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104
SHEET 4 AC4 4 GLY L 95B PHE L 98 -1 O VAL L 97 N SER L 90
SHEET 1 AC5 3 VAL L 19 THR L 24 0
SHEET 2 AC5 3 SER L 70 ILE L 75 -1 O ILE L 75 N VAL L 19
SHEET 3 AC5 3 PHE L 62 SER L 67 -1 N SER L 63 O ALA L 74
SHEET 1 AC6 4 SER L 115 PHE L 119 0
SHEET 2 AC6 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 AC6 4 TYR L 174 LEU L 182 -1 O SER L 178 N CYS L 135
SHEET 4 AC6 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 179
SHEET 1 AC7 4 SER L 115 PHE L 119 0
SHEET 2 AC7 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 AC7 4 TYR L 174 LEU L 182 -1 O SER L 178 N CYS L 135
SHEET 4 AC7 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 175
SHEET 1 AC8 4 SER L 154 VAL L 156 0
SHEET 2 AC8 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154
SHEET 3 AC8 4 TYR L 193 HIS L 199 -1 O GLN L 196 N ALA L 148
SHEET 4 AC8 4 SER L 202 VAL L 208 -1 O VAL L 208 N TYR L 193
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.04
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.04
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.04
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.04
SSBOND 5 CYS B 6 CYS B 127 1555 1555 2.04
SSBOND 6 CYS B 30 CYS B 115 1555 1555 2.04
SSBOND 7 CYS B 64 CYS B 80 1555 1555 2.04
SSBOND 8 CYS B 76 CYS B 94 1555 1555 2.05
SSBOND 9 CYS C 22 CYS C 92 1555 1555 2.04
SSBOND 10 CYS C 140 CYS C 196 1555 1555 2.04
SSBOND 11 CYS D 23 CYS D 88 1555 1555 2.05
SSBOND 12 CYS D 135 CYS D 195 1555 1555 2.04
SSBOND 13 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 14 CYS H 140 CYS H 196 1555 1555 2.04
SSBOND 15 CYS L 23 CYS L 88 1555 1555 2.05
SSBOND 16 CYS L 135 CYS L 195 1555 1555 2.05
CISPEP 1 PHE C 146 PRO C 147 0 0.74
CISPEP 2 GLU C 148 PRO C 149 0 7.48
CISPEP 3 TYR D 141 PRO D 142 0 1.09
CISPEP 4 PHE H 146 PRO H 147 0 0.48
CISPEP 5 GLU H 148 PRO H 149 0 7.19
CISPEP 6 TYR L 141 PRO L 142 0 0.95
CRYST1 63.900 64.300 76.600 102.40 101.80 102.40 P 1 2
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 0.015649 0.003441 0.004363 0.00000
SCALE2 0.000000 0.015924 0.004475 0.00000
SCALE3 0.000000 0.000000 0.013853 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
