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HEADER LIPASE 02-AUG-04 1W52
TITLE CRYSTAL STRUCTURE OF A PROTEOLYZED FORM OF PANCREATIC
TITLE 2 LIPASE RELATED PROTEIN 2 FROM HORSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANCREATIC LIPASE RELATED PROTEIN 2;
COMPND 3 CHAIN: X
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGAN: PANCREAS
KEYWDS PANCREATIC LIPASE RELATED PROTEINS, DETERGENT, CLEAVED FLAP,
KEYWDS 2 LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MANCHENO,S.JAYNE,B.KERFELEC,C.CHAPUS,I.CRENON,J.A.HERMOSO
REVDAT 1 12-JUL-06 1W52 0
JRNL AUTH J.M.MANCHENO,S.JAYNE,B.KERFELEC,C.CHAPUS,I.CRENON,
JRNL AUTH 2 J.A.HERMOSO
JRNL TITL CRYSTALIZATION OF A PROTEOLYZED FORM OF THE HORSE
JRNL TITL 2 PANCREATIC LIPASE-RELATED PROTEIN 2: STRUCTURAL
JRNL TITL 3 BASIS FOR THE SPECIFIC DETERGENT REQUIREMENT.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 2107 2004
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 2.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.97
REMARK 3 NUMBER OF REFLECTIONS : 15958
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) : 0.23445
REMARK 3 R VALUE (WORKING SET) : 0.23138
REMARK 3 FREE R VALUE : 0.29378
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 847
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.990
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.067
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1155
REMARK 3 BIN R VALUE (WORKING SET) : 0.342
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.421
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3494
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.087
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02
REMARK 3 B22 (A**2) : 0.02
REMARK 3 B33 (A**2) : -0.03
REMARK 3 B12 (A**2) : 0.01
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.968
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.420
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.313
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.505
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.892
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.838
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 3611 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3129 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 4891 ; 1.993 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7337 ; 1.368 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 446 ; 7.549 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 515 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 4045 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 729 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 1012 ; 0.266 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4070 ; 0.262 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2082 ; 0.093 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 91 ; 0.194 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED (A): 1 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 7 ; 0.369 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 44 ; 0.329 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 1 ; 0.281 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 2222 ; 1.765 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 3576 ; 3.487 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 1389 ; 3.502 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1315 ; 6.163 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS :1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 3 CHAINS FROM SEVERAL SEQUENCE REGIONS FROM THE C-TERMINAL
REMARK 3 DOMAIN ARE NOT DEFINED IN THE ELECTRON DENSITY MAP
REMARK 3 THE FOLLOWING REGIONS ARE NOT DEFINED IN ELECTRON DENSITY
REMARK 3 MAP, 346-354,363-368,379-386,398-402,407-424,433-452 B-
REMARK 3 FACTORS OF THESE RESIDUES HAVE BEEN CHANGED TOP 100.00
REMARK 4
REMARK 4 1W52 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 18-AUG-2004.
REMARK 100 THE EBI ID CODE IS EBI-20635.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-2004
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE ID14-EH2
REMARK 200 BEAMLINE : ID14-EH2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16857
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.99
REMARK 200 RESOLUTION RANGE LOW (A) : 46.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.6
REMARK 200 R MERGE (I) : 0.13
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.2
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1BU8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 Y-X,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,1/3-Z
REMARK 290 6555 -X,Y-X,2/3-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 -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 57.21200
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 28.60600
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 28.60600
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 57.21200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: X
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 SER X 243
REMARK 465 PHE X 244
REMARK 465 SER X 245
REMARK 465 THR X 246
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO X 213 CB PRO X 213 CG 0.255
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 O ASP X 57 OG1 THR X 60 2.11
REMARK 500 O ILE X 61 OG SER X 64 2.12
REMARK 500 O ARG X 363 O GLY X 367 2.19
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 SER X 154 -117.39 56.87
REMARK 500 VAL X 404 155.02 124.25
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU X 212 PRO X 213 230.00
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM CA CA X 602 THE COORDINATION ANGLES ARE:
REMARK 600 1 ASP 194X OD1
REMARK 600 2 ASP 197X OD1 85.7
REMARK 600 3 GLU 189X O 101.9 145.2
REMARK 600 4 ASP 197X OD2 80.0 51.1 163.3
REMARK 600 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: DDQ BINDING SITE FOR CHAIN X
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: DDQ BINDING SITE FOR CHAIN X
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN X
DBREF 1W52 X 1 452 UNP Q95KP4 Q95KP4 1 452
SEQRES 1 X 452 LYS GLU VAL CYS TYR THR PRO LEU GLY CYS PHE SER ASP
SEQRES 2 X 452 ASP LYS PRO TRP ALA GLY THR LEU GLN ARG PRO LEU LYS
SEQRES 3 X 452 SER LEU PRO TRP SER PRO GLU GLU VAL ASN THR ARG PHE
SEQRES 4 X 452 LEU LEU TYR THR ASN LYS ASN PRO ASP SER TYR GLN LEU
SEQRES 5 X 452 ILE THR ALA ARG ASP VAL ALA THR ILE LYS SER SER ASN
SEQRES 6 X 452 PHE GLN SER SER ARG LYS THR HIS PHE VAL ILE HIS GLY
SEQRES 7 X 452 PHE ARG ASP ARG GLY GLU ASP SER TRP PRO SER ASP MET
SEQRES 8 X 452 CYS LYS LYS ILE LEU GLN VAL GLU THR THR ASN CYS ILE
SEQRES 9 X 452 SER VAL ASP TRP SER SER GLY ALA LYS ALA GLU TYR THR
SEQRES 10 X 452 GLN ALA VAL GLN ASN ILE ARG ILE VAL GLY ALA GLU THR
SEQRES 11 X 452 ALA TYR LEU ILE GLN GLN LEU LEU THR GLU LEU SER TYR
SEQRES 12 X 452 ASN PRO GLU ASN VAL HIS ILE ILE GLY HIS SER LEU GLY
SEQRES 13 X 452 ALA HIS THR ALA GLY GLU ALA GLY ARG ARG LEU GLU GLY
SEQRES 14 X 452 ARG VAL GLY ARG VAL THR GLY LEU ASP PRO ALA GLU PRO
SEQRES 15 X 452 CYS PHE GLN ASP ALA SER GLU GLU VAL ARG LEU ASP PRO
SEQRES 16 X 452 SER ASP ALA GLN PHE VAL ASP VAL ILE HIS THR ASP ALA
SEQRES 17 X 452 SER PRO MET LEU PRO SER LEU GLY PHE GLY MET SER GLN
SEQRES 18 X 452 LYS VAL GLY HIS MET ASP PHE PHE PRO ASN GLY GLY LYS
SEQRES 19 X 452 GLN MET PRO GLY CYS LYS ARG SER SER PHE SER THR PHE
SEQRES 20 X 452 ILE ASP ILE ASN GLY ILE TRP GLN GLY ALA GLN ASP TYR
SEQRES 21 X 452 LEU ALA CYS ASN HIS LEU LYS SER PHE GLU TYR TYR SER
SEQRES 22 X 452 SER SER ILE LEU ASN PRO ASP GLY PHE LEU ALA TYR PRO
SEQRES 23 X 452 CYS ASP SER TYR ASP LYS PHE GLN GLU ASN GLY CYS PHE
SEQRES 24 X 452 PRO CYS PRO ALA GLY GLY CYS PRO LYS MET GLY HIS TYR
SEQRES 25 X 452 ALA ASP GLN TYR LYS GLU LYS THR SER ALA VAL GLU GLN
SEQRES 26 X 452 THR PHE PHE LEU ASN THR GLY GLU SER GLY ASP TYR THR
SEQRES 27 X 452 SER TRP ARG TYR ARG VAL SER ILE THR LEU ALA GLY SER
SEQRES 28 X 452 GLY LYS ALA ASN GLY TYR LEU LYS VAL THR LEU ARG GLY
SEQRES 29 X 452 SER ASN GLY ASN SER LYS GLN TYR GLU ILE PHE LYS GLY
SEQRES 30 X 452 SER LEU GLN PRO ASP SER SER TYR THR LEU ASP VAL ASP
SEQRES 31 X 452 VAL ASN PHE ILE ILE GLY LYS ILE GLN GLU VAL LYS PHE
SEQRES 32 X 452 VAL TRP ASN LYS THR VAL LEU ASN LEU SER LYS PRO GLN
SEQRES 33 X 452 LEU GLY ALA SER ARG ILE THR VAL GLN SER GLY ALA ASP
SEQRES 34 X 452 GLY THR GLU TYR LYS PHE CYS GLY SER GLY THR VAL GLN
SEQRES 35 X 452 ASP ASN VAL GLU GLN SER LEU TYR PRO CYS
HET DDQ X 501 14
HET DDQ X 502 14
HET CA X 601 1
HET CA X 602 1
HETNAM DDQ DECYLAMINE-N,N-DIMETHYL-N-OXIDE
HETNAM CA CALCIUM ION
FORMUL 2 DDQ 2(C12 H27 N1 O1)
FORMUL 3 CA 2(CA1 2+)
HELIX 1 1 SER X 31 ASN X 36 1 6
HELIX 2 2 VAL X 58 SER X 63 1 6
HELIX 3 3 SER X 86 GLN X 97 1 12
HELIX 4 4 TRP X 108 LYS X 113 1 6
HELIX 5 5 GLU X 115 SER X 142 1 28
HELIX 6 6 ASN X 144 GLU X 146 5 3
HELIX 7 7 SER X 154 LEU X 167 1 14
HELIX 8 8 ASP X 194 ALA X 198 5 5
HELIX 9 9 GLY X 232 LYS X 234 5 3
HELIX 10 10 ASP X 249 ILE X 253 5 5
HELIX 11 11 GLY X 256 ASN X 278 1 23
HELIX 12 12 PRO X 279 PHE X 282 5 4
HELIX 13 13 SER X 289 GLU X 295 1 7
HELIX 14 14 GLY X 310 TYR X 316 5 7
SHEET 1 XA 2 VAL X 3 TYR X 5 0
SHEET 2 XA 2 GLY X 9 PHE X 11 -1 O GLY X 9 N TYR X 5
SHEET 1 XB10 ASN X 46 ILE X 53 0
SHEET 2 XB10 ARG X 38 THR X 43 -1 O PHE X 39 N ILE X 53
SHEET 3 XB10 ASN X 102 ASP X 107 -1 O CYS X 103 N TYR X 42
SHEET 4 XB10 THR X 72 ILE X 76 1 O HIS X 73 N ILE X 104
SHEET 5 XB10 VAL X 148 HIS X 153 1 O HIS X 149 N PHE X 74
SHEET 6 XB10 ARG X 173 LEU X 177 1 O ARG X 173 N ILE X 150
SHEET 7 XB10 VAL X 201 ILE X 204 1 O ASP X 202 N GLY X 176
SHEET 8 XB10 MET X 226 PRO X 230 1 O MET X 226 N VAL X 203
SHEET 9 XB10 GLN X 325 LEU X 329 1 O GLN X 325 N ASP X 227
SHEET 10 XB10 TYR X 285 PRO X 286 -1 O TYR X 285 N PHE X 328
SHEET 1 XC 2 TRP X 340 VAL X 344 0
SHEET 2 XC 2 LEU X 387 VAL X 391 -1 O LEU X 387 N VAL X 344
SHEET 1 XD 2 ASN X 355 GLY X 356 0
SHEET 2 XD 2 GLY X 377 SER X 378 -1 O GLY X 377 N GLY X 356
SHEET 1 XE 2 PHE X 435 CYS X 436 0
SHEET 2 XE 2 TYR X 450 PRO X 451 -1 O TYR X 450 N CYS X 436
SSBOND 1 CYS X 4 CYS X 10 1555 1555
SSBOND 2 CYS X 92 CYS X 103 1555 1555
SSBOND 3 CYS X 239 CYS X 263 1555 1555
SSBOND 4 CYS X 287 CYS X 298 1555 1555
SSBOND 5 CYS X 301 CYS X 306 1555 1555
SSBOND 6 CYS X 436 CYS X 452 1555 1555
LINK CA CA X 601 OD2 ASP X 314 1555 1555
LINK CA CA X 602 OD2 ASP X 197 1555 1555
LINK CA CA X 602 OD1 ASP X 197 1555 1555
LINK CA CA X 602 O GLU X 189 1555 1555
LINK CA CA X 602 OD1 ASP X 194 1555 1555
CISPEP 1 LYS X 15 PRO X 16 0 -10.03
CISPEP 2 PHE X 299 PRO X 300 0 -4.74
SITE 1 AC1 3 MET X 211 LEU X 215 TRP X 254
SITE 1 AC2 4 ARG X 80 ASP X 81 TYR X 116 HIS X 265
SITE 1 AC4 4 GLU X 189 ARG X 192 ASP X 194 ASP X 197
CRYST1 128.426 128.426 85.818 90.00 90.00 120.00 P 32 2 1 6
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 0.007787 0.004496 0.000000 0.00000
SCALE2 0.000000 0.008991 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011653 0.00000
TER 3495 CYS X 452
MASTER 312 0 4 14 18 0 3 6 3524 1 47 35
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