HEADER HYDROLASE 20-OCT-05 2D4K
TITLE MONOCLINIC HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A, N;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D 4, GAL D IV;
COMPND 5 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS PHASE TRANSITION, RIGID-BODY MOTION, TLS ANALYSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HARATA,T.AKIBA
REVDAT 4 25-OCT-23 2D4K 1 REMARK LINK
REVDAT 3 11-OCT-17 2D4K 1 REMARK
REVDAT 2 24-FEB-09 2D4K 1 VERSN
REVDAT 1 11-JUL-06 2D4K 0
JRNL AUTH K.HARATA,T.AKIBA
JRNL TITL STRUCTURAL PHASE TRANSITION OF MONOCLINIC CRYSTALS OF HEN
JRNL TITL 2 EGG-WHITE LYSOZYME
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 62 375 2006
JRNL REFN ISSN 0907-4449
JRNL PMID 16552138
JRNL DOI 10.1107/S0907444906001314
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.133
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3349
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2002
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 249
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 ANGLE DISTANCES (A) : 0.032
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.080
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.093
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : SHELX97 DEFAULT
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE AUTHOR ASIGNED THE RFREE
REMARK 3 REFLECTIONS BY THE FOLLOWING SHELXL97 INPUT COMMAND LINE L.S. 5 -
REMARK 3 20 WHICH INDICATES 5 CYCLES OF LEAST-SQUARES CALCULATION AND
REMARK 3 IGNORE EVERY 20TH REFLECTIONS (5%) IN THE REFINEMENT FOR THE
REMARK 3 RFREE CALCULATION
REMARK 4
REMARK 4 2D4K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000024978.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 290
REMARK 200 PH : 7.6
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 : MACSCIENCE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CURVED MIRROR
REMARK 200 OPTICS : CONFOCAL MAX-FLUX OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINTPLUS, SMART V. 6000
REMARK 200 DATA SCALING SOFTWARE : SAINTPLUS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67029
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 19.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 4.140
REMARK 200 R MERGE (I) : 0.11900
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) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33600
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: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1LYS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PROTEIN, 10% SODIUM CHLORIDE, 5% 1
REMARK 280 -PROPANOL, PH 7.6, BATCH METHOD, TEMPERATURE 313K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 31.74200
REMARK 290 SMTRY3 2 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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 14 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 45 CD - NE - CZ ANGL. DEV. = 25.4 DEGREES
REMARK 500 ARG A 45 NH1 - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 68 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 73 CD - NE - CZ ANGL. DEV. = 19.3 DEGREES
REMARK 500 ARG A 73 NE - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 114 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 125 CD - NE - CZ ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 LEU A 129 C - N - CA ANGL. DEV. = 16.5 DEGREES
REMARK 500 ARG N 214 CD - NE - CZ ANGL. DEV. = 28.6 DEGREES
REMARK 500 ARG N 214 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP N 218 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG N 221 CD - NE - CZ ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG N 245 CD - NE - CZ ANGL. DEV. = 26.6 DEGREES
REMARK 500 ARG N 245 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG N 261 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG N 268 CD - NE - CZ ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG N 314 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP N 319 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG N 325 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG N 328 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
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 ASP A 101 10.75 -67.84
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 A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 60 O
REMARK 620 2 CYS A 64 O 85.8
REMARK 620 3 SER A 72 OG 117.5 136.6
REMARK 620 4 ARG A 73 O 117.2 99.5 100.5
REMARK 620 5 HOH A 402 O 165.9 93.5 54.9 76.9
REMARK 620 6 HOH A 403 O 85.2 81.1 66.3 157.6 80.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA N 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER N 260 O
REMARK 620 2 CYS N 264 O 90.6
REMARK 620 3 SER N 272 OG 90.2 160.7
REMARK 620 4 ARG N 273 O 98.1 94.0 105.0
REMARK 620 5 HOH N 407 O 96.8 86.8 74.0 165.0
REMARK 620 6 HOH N 408 O 170.5 97.3 80.6 86.6 78.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA N 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 411
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2D4I RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG-WHITE LYSOZYME CRYSTALLIZED FROM A HEAVY WATER
REMARK 900 SOLUTION AT PD 4.5
REMARK 900 RELATED ID: 2D4J RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG-WHITE LYSOZYME CRYSTALLIZED FROM A HEAVY WATER
REMARK 900 SOLUTION AT PD 4.5
DBREF 2D4K A 1 129 UNP P00698 LYSC_CHICK 19 147
DBREF 2D4K N 201 329 UNP P00698 LYSC_CHICK 19 147
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 N 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 N 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 N 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 N 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 N 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 N 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 N 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 N 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 N 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 N 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
HET NA A 401 1
HET CL A 405 1
HET NA N 406 1
HET CL N 409 1
HET CL N 410 1
HET CL N 411 1
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 NA 2(NA 1+)
FORMUL 4 CL 4(CL 1-)
FORMUL 9 HOH *249(H2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 ASN A 19 TYR A 23 5 5
HELIX 3 3 SER A 24 ASN A 37 1 14
HELIX 4 4 PRO A 79 SER A 85 5 7
HELIX 5 5 ILE A 88 ASP A 101 1 14
HELIX 6 6 GLY A 102 ALA A 107 5 6
HELIX 7 7 TRP A 108 CYS A 115 1 8
HELIX 8 8 ASP A 119 ARG A 125 5 7
HELIX 9 9 GLY N 204 HIS N 215 1 12
HELIX 10 10 ASN N 219 TYR N 223 5 5
HELIX 11 11 SER N 224 ASN N 237 1 14
HELIX 12 12 PRO N 279 SER N 285 5 7
HELIX 13 13 ILE N 288 SER N 300 1 13
HELIX 14 14 ASN N 303 ALA N 307 5 5
HELIX 15 15 TRP N 308 CYS N 315 1 8
HELIX 16 16 ASP N 319 ARG N 325 5 7
SHEET 1 A 3 THR A 43 ARG A 45 0
SHEET 2 A 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 A 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SHEET 1 B 3 THR N 243 ARG N 245 0
SHEET 2 B 3 THR N 251 TYR N 253 -1 O ASP N 252 N ASN N 244
SHEET 3 B 3 ILE N 258 ASN N 259 -1 O ILE N 258 N TYR N 253
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.03
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.01
SSBOND 3 CYS A 64 CYS A 80 1555 1555 1.99
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.05
SSBOND 5 CYS N 206 CYS N 327 1555 1555 2.03
SSBOND 6 CYS N 230 CYS N 315 1555 1555 2.03
SSBOND 7 CYS N 264 CYS N 280 1555 1555 1.99
SSBOND 8 CYS N 276 CYS N 294 1555 1555 2.03
LINK O SER A 60 NA NA A 401 1555 1555 2.29
LINK O CYS A 64 NA NA A 401 1555 1555 2.31
LINK OG SER A 72 NA NA A 401 1555 1555 2.26
LINK O ARG A 73 NA NA A 401 1555 1555 2.36
LINK NA NA A 401 O HOH A 402 1555 1555 2.68
LINK NA NA A 401 O AHOH A 403 1555 1555 2.60
LINK O SER N 260 NA NA N 406 1555 1555 2.35
LINK O CYS N 264 NA NA N 406 1555 1555 2.34
LINK OG SER N 272 NA NA N 406 1555 1555 2.48
LINK O ARG N 273 NA NA N 406 1555 1555 2.43
LINK NA NA N 406 O HOH N 407 1555 1555 2.56
LINK NA NA N 406 O HOH N 408 1555 1555 2.49
SITE 1 AC1 6 SER A 60 CYS A 64 SER A 72 ARG A 73
SITE 2 AC1 6 HOH A 402 HOH A 403
SITE 1 AC2 4 ASN A 65 ASP A 66 GLY A 67 SER A 72
SITE 1 AC3 6 SER N 260 CYS N 264 SER N 272 ARG N 273
SITE 2 AC3 6 HOH N 407 HOH N 408
SITE 1 AC4 6 ASN N 265 GLY N 267 ARG N 268 THR N 269
SITE 2 AC4 6 SER N 272 HOH N 407
SITE 1 AC5 1 TRP N 263
SITE 1 AC6 2 SER N 224 GLY N 226
CRYST1 27.217 63.484 59.189 90.00 92.93 90.00 P 1 21 1 4
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 0.036742 0.000000 0.001881 0.00000
SCALE2 0.000000 0.015752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016917 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
