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HEADER HYDROLASE 18-APR-07 2PKY
TITLE THE EFFECT OF DEUTERATION ON PROTEIN STRUCTURE A HIGH
TITLE 2 RESOLUTION COMPARISON OF HYDROGENOUS AND PERDEUTERATED
TITLE 3 HALOALKANE DEHALOGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: X;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOBACTER AUTOTROPHICUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: GJ10;
SOURCE 5 GENE: DHLA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCHC109
KEYWDS PROTEIN DEUTERATION, HALOALKANE DEHALOGENASE, HIGH
KEYWDS 2 RESOLUTION STRUCTURE, CATALYTIC MECHANISM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LIU,L.HANSON,P.LANGAN,R.E.VIOLA
REVDAT 1 04-SEP-07 2PKY 0
JRNL AUTH X.LIU,L.HANSON,P.LANGAN,R.E.VIOLA
JRNL TITL THE EFFECT OF DEUTERATION ON PROTEIN STRUCTURE A
JRNL TITL 2 HIGH RESOLUTION COMPARISON OF HYDROGENOUS AND
JRNL TITL 3 PERDEUTERATED HALOALKANE DEHALOGENASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 36432
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1959
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1769
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE SET COUNT : 93
REMARK 3 BIN FREE R VALUE : 0.4560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2875
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.54000
REMARK 3 B22 (A**2) : -0.85000
REMARK 3 B33 (A**2) : 0.31000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.148
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.104
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.895
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2658 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3629 ; 1.198 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 318 ; 5.505 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;36.995 ;24.420
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 441 ;12.793 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;11.428 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 391 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2087 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1348 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1823 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 259 ; 0.127 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 71 ; 0.218 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 36 ; 0.107 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1640 ; 1.074 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2604 ; 1.621 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1169 ; 3.111 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1023 ; 3.603 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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 4
REMARK 4 2PKY COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB042491.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41347
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 28.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.1
REMARK 200 DATA REDUNDANCY : 3.520
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 16.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.35200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RIGID BODY REFINEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1B6G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.6M AMMONIUM SULFATE, 0.1M SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 1/2-X,1/2+Y,-Z
REMARK 290 4555 1/2+X,1/2-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 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 47.18150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.54650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.18150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.54650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET X 1
REMARK 465 GLU X 310
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 PRO X 57 59.56 -104.09
REMARK 500 THR X 58 -158.62 -110.94
REMARK 500 ASP X 124 -140.56 52.56
REMARK 500 ASP X 137 73.51 -159.01
REMARK 500 ASN X 148 94.25 -10.86
REMARK 500 LEU X 262 -69.38 -94.62
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2PKY X 1 310 UNP P22643 DHLA_XANAU 1 310
SEQRES 1 X 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER
SEQRES 2 X 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP
SEQRES 3 X 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU
SEQRES 4 X 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS
SEQRES 5 X 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS
SEQRES 6 X 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE
SEQRES 7 X 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO
SEQRES 8 X 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN
SEQRES 9 X 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN
SEQRES 10 X 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY
SEQRES 11 X 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG
SEQRES 12 X 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL
SEQRES 13 X 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA
SEQRES 14 X 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO
SEQRES 15 X 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA
SEQRES 16 X 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA
SEQRES 17 X 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS
SEQRES 18 X 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE
SEQRES 19 X 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP
SEQRES 20 X 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP
SEQRES 21 X 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA
SEQRES 22 X 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP
SEQRES 23 X 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA
SEQRES 24 X 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU
FORMUL 2 HOH *296(H2 O)
HELIX 1 1 PRO X 8 SER X 13 5 6
HELIX 2 2 TRP X 59 ARG X 64 5 6
HELIX 3 3 MET X 66 SER X 73 1 8
HELIX 4 4 ASP X 93 TYR X 97 5 5
HELIX 5 5 THR X 98 ASP X 114 1 17
HELIX 6 6 GLN X 123 LEU X 131 1 9
HELIX 7 7 THR X 132 SER X 139 5 8
HELIX 8 8 PRO X 159 PHE X 164 1 6
HELIX 9 9 GLY X 171 THR X 181 1 11
HELIX 10 10 ARG X 186 ALA X 195 1 10
HELIX 11 11 THR X 199 ALA X 208 1 10
HELIX 12 12 ASP X 212 TYR X 215 5 4
HELIX 13 13 GLN X 216 GLN X 228 1 13
HELIX 14 14 ASP X 230 ASP X 247 1 18
HELIX 15 15 GLY X 264 ILE X 275 1 12
HELIX 16 16 PHE X 290 GLU X 293 5 4
HELIX 17 17 PHE X 294 THR X 309 1 16
SHEET 1 A 2 ALA X 4 ILE X 5 0
SHEET 2 A 2 LYS X 90 PRO X 91 -1 O LYS X 90 N ILE X 5
SHEET 1 B 8 ASN X 23 LEU X 25 0
SHEET 2 B 8 ALA X 36 GLU X 41 -1 O TYR X 38 N ASN X 23
SHEET 3 B 8 ARG X 76 PRO X 80 -1 O VAL X 77 N GLU X 41
SHEET 4 B 8 VAL X 49 LEU X 53 1 N PHE X 50 O ILE X 78
SHEET 5 B 8 ILE X 118 VAL X 122 1 O THR X 119 N VAL X 49
SHEET 6 B 8 PHE X 141 MET X 147 1 O ILE X 145 N LEU X 120
SHEET 7 B 8 GLN X 251 GLY X 257 1 O ALA X 255 N ILE X 146
SHEET 8 B 8 LEU X 282 ILE X 284 1 O LEU X 282 N MET X 254
CISPEP 1 GLU X 56 PRO X 57 0 -15.71
CISPEP 2 GLN X 167 PRO X 168 0 -2.08
CRYST1 94.363 71.093 40.035 90.00 90.00 90.00 P 21 21 2 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 0.010597 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014066 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024978 0.00000
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