HEADER LYASE 16-FEB-13 4J9J
TITLE STRUCTURE OF DESIGNED HISF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEE REMARK 999;
COMPND 5 SYNONYM: IGP SYNTHASE CYCLASE SUBUNIT, IGP SYNTHASE SUBUNIT HISF,
COMPND 6 IMGP SYNTHASE SUBUNIT HISF, IGPS SUBUNIT HISF;
COMPND 7 EC: 4.1.3.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 STRAIN: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
SOURCE 5 GENE: HISF, TM_1036;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS BETA BARREL, PROTEIN ENGINEERING, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.STERNER,C.RAJENDRAN,J.SPERL
REVDAT 4 20-SEP-23 4J9J 1 SEQADV
REVDAT 3 26-JUL-17 4J9J 1 SOURCE
REVDAT 2 11-SEP-13 4J9J 1 JRNL
REVDAT 1 17-JUL-13 4J9J 0
JRNL AUTH J.M.SPERL,B.ROHWEDER,C.RAJENDRAN,R.STERNER
JRNL TITL ESTABLISHING CATALYTIC ACTIVITY ON AN ARTIFICIAL ( BETA
JRNL TITL 2 ALPHA )8-BARREL PROTEIN DESIGNED FROM IDENTICAL
JRNL TITL 3 HALF-BARRELS.
JRNL REF FEBS LETT. V. 587 2798 2013
JRNL REFN ISSN 0014-5793
JRNL PMID 23806364
JRNL DOI 10.1016/J.FEBSLET.2013.06.022
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 10542
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 528
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.7191 - 3.6506 0.94 2473 131 0.2105 0.2532
REMARK 3 2 3.6506 - 2.8978 0.96 2486 131 0.2478 0.2998
REMARK 3 3 2.8978 - 2.5316 0.97 2491 131 0.2901 0.3394
REMARK 3 4 2.5316 - 2.3001 0.99 2564 135 0.2544 0.3634
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 1731
REMARK 3 ANGLE : 0.655 2343
REMARK 3 CHIRALITY : 0.043 282
REMARK 3 PLANARITY : 0.002 297
REMARK 3 DIHEDRAL : 11.207 615
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4J9J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000077766.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.7
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10548
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.805
REMARK 200 RESOLUTION RANGE LOW (A) : 41.712
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PDB ENTRY 3OG3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 31.57100
REMARK 290 SMTRY3 2 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/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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 ILE A 77
REMARK 465 ASP A 78
REMARK 465 ARG A 79
REMARK 465 GLY A 80
REMARK 465 GLY A 81
REMARK 465 THR A 82
REMARK 465 LYS A 83
REMARK 465 SER A 84
REMARK 465 VAL A 201
REMARK 465 GLY A 202
REMARK 465 THR A 203
REMARK 465 LYS A 204
REMARK 465 SER A 205
REMARK 465 LEU A 240
REMARK 465 ALA A 241
REMARK 465 GLY A 242
REMARK 465 ALA A 243
REMARK 465 ASP A 244
REMARK 465 ALA A 245
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 A 110 CG CD CE NZ
REMARK 470 ARG A 200 CG CD NE CZ NH1 NH2
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 O HOH A 425 O HOH A 440 1.85
REMARK 500 O HOH A 357 O HOH A 375 1.96
REMARK 500 O HOH A 423 O HOH A 436 2.01
REMARK 500 N GLY A 40 O HOH A 401 2.02
REMARK 500 NH1 ARG A 92 O HOH A 367 2.04
REMARK 500 N LEU A 0 O HOH A 363 2.04
REMARK 500 O PRO A 96 O HOH A 332 2.04
REMARK 500 O GLY A 191 O HOH A 342 2.07
REMARK 500 OE2 GLU A 210 O HOH A 369 2.09
REMARK 500 O HOH A 387 O HOH A 397 2.11
REMARK 500 OE2 GLU A 116 O HOH A 405 2.12
REMARK 500 O HOH A 337 O HOH A 361 2.12
REMARK 500 O HOH A 369 O HOH A 383 2.14
REMARK 500 N LEU A 0 O HOH A 426 2.15
REMARK 500 O HOH A 357 O HOH A 397 2.18
REMARK 500 O HOH A 365 O HOH A 442 2.18
REMARK 500 O PHE A 45 O HOH A 354 2.18
REMARK 500 O HOH A 349 O HOH A 442 2.18
REMARK 500 O HOH A 413 O HOH A 437 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLY A 206 O HOH A 338 2557 1.95
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 ASN A 7 -86.02 -144.25
REMARK 500 ASN A 13 86.90 -162.82
REMARK 500 TYR A 86 130.73 68.67
REMARK 500 ASN A 128 -83.48 -143.34
REMARK 500 TYR A 207 112.68 44.17
REMARK 500 ASP A 208 83.72 -65.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PROTEIN IS AN ENGINEERED CONSTRUCT COMPRISING UNP RESIDUES 97-216
REMARK 999 COUPLED TO UNP RESIDUES 96-220 (Q9X0C6).
DBREF 4J9J A 1 120 UNP Q9X0C6 HIS6_THEMA 97 216
DBREF 4J9J A 121 245 UNP Q9X0C6 HIS6_THEMA 96 220
SEQADV 4J9J LEU A 0 UNP Q9X0C6 EXPRESSION TAG
SEQADV 4J9J ILE A 5 UNP Q9X0C6 SER 101 ENGINEERED MUTATION
SEQADV 4J9J ALA A 44 UNP Q9X0C6 VAL 140 ENGINEERED MUTATION
SEQADV 4J9J ALA A 75 UNP Q9X0C6 THR 171 ENGINEERED MUTATION
SEQADV 4J9J GLY A 80 UNP Q9X0C6 ASP 176 ENGINEERED MUTATION
SEQADV 4J9J VAL A 155 UNP Q9X0C6 ASP 130 ENGINEERED MUTATION
SEQADV 4J9J VAL A 201 UNP Q9X0C6 ASP 176 ENGINEERED MUTATION
SEQRES 1 A 246 LEU ALA ASP LYS VAL ILE ILE ASN THR ALA ALA VAL GLU
SEQRES 2 A 246 ASN PRO SER LEU ILE THR GLN ILE ALA GLN THR PHE GLY
SEQRES 3 A 246 SER GLN ALA VAL VAL VAL ALA ILE ASP ALA LYS ARG VAL
SEQRES 4 A 246 ASP GLY GLU PHE MET ALA PHE THR TYR SER GLY LYS LYS
SEQRES 5 A 246 ASN THR GLY ILE LEU LEU ARG ASP TRP VAL VAL GLU VAL
SEQRES 6 A 246 GLU LYS ARG GLY ALA GLY GLU ILE LEU LEU ALA SER ILE
SEQRES 7 A 246 ASP ARG GLY GLY THR LYS SER GLY TYR ASP THR GLU MET
SEQRES 8 A 246 ILE ARG PHE VAL ARG PRO LEU THR THR LEU PRO ILE ILE
SEQRES 9 A 246 ALA SER GLY GLY ALA GLY LYS MET GLU HIS PHE LEU GLU
SEQRES 10 A 246 ALA PHE LEU ALA GLY ALA ASP LYS VAL SER ILE ASN THR
SEQRES 11 A 246 ALA ALA VAL GLU ASN PRO SER LEU ILE THR GLN ILE ALA
SEQRES 12 A 246 GLN THR PHE GLY SER GLN ALA VAL VAL VAL ALA ILE VAL
SEQRES 13 A 246 ALA LYS ARG VAL ASP GLY GLU PHE MET VAL PHE THR TYR
SEQRES 14 A 246 SER GLY LYS LYS ASN THR GLY ILE LEU LEU ARG ASP TRP
SEQRES 15 A 246 VAL VAL GLU VAL GLU LYS ARG GLY ALA GLY GLU ILE LEU
SEQRES 16 A 246 LEU THR SER ILE ASP ARG VAL GLY THR LYS SER GLY TYR
SEQRES 17 A 246 ASP THR GLU MET ILE ARG PHE VAL ARG PRO LEU THR THR
SEQRES 18 A 246 LEU PRO ILE ILE ALA SER GLY GLY ALA GLY LYS MET GLU
SEQRES 19 A 246 HIS PHE LEU GLU ALA PHE LEU ALA GLY ALA ASP ALA
FORMUL 2 HOH *147(H2 O)
HELIX 1 1 ASN A 7 GLU A 12 1 6
HELIX 2 2 PRO A 14 GLY A 25 1 12
HELIX 3 3 LEU A 57 GLY A 68 1 12
HELIX 4 4 ASP A 87 ARG A 95 1 9
HELIX 5 5 PRO A 96 THR A 98 5 3
HELIX 6 6 LYS A 110 GLY A 121 1 12
HELIX 7 7 ASN A 128 ASN A 134 1 7
HELIX 8 8 PRO A 135 PHE A 145 1 11
HELIX 9 9 GLY A 146 GLN A 148 5 3
HELIX 10 10 LEU A 178 GLY A 189 1 12
HELIX 11 11 ASP A 208 ARG A 216 1 9
HELIX 12 12 PRO A 217 THR A 219 5 3
HELIX 13 13 HIS A 234 PHE A 239 1 6
SHEET 1 A 9 LYS A 51 LEU A 56 0
SHEET 2 A 9 GLU A 41 THR A 46 -1 N ALA A 44 O ILE A 55
SHEET 3 A 9 VAL A 29 VAL A 38 -1 N VAL A 38 O GLU A 41
SHEET 4 A 9 LYS A 3 ILE A 6 1 N ILE A 6 O ALA A 32
SHEET 5 A 9 ILE A 223 ALA A 225 1 O ALA A 225 N LYS A 3
SHEET 6 A 9 GLU A 192 SER A 197 1 N ILE A 193 O ILE A 224
SHEET 7 A 9 VAL A 150 VAL A 159 1 N ILE A 154 O LEU A 194
SHEET 8 A 9 GLU A 162 THR A 167 -1 O PHE A 166 N VAL A 155
SHEET 9 A 9 LYS A 172 LEU A 177 -1 O ILE A 176 N VAL A 165
SHEET 1 B 9 LYS A 51 LEU A 56 0
SHEET 2 B 9 GLU A 41 THR A 46 -1 N ALA A 44 O ILE A 55
SHEET 3 B 9 VAL A 29 VAL A 38 -1 N VAL A 38 O GLU A 41
SHEET 4 B 9 GLU A 71 ALA A 75 1 O LEU A 73 N ILE A 33
SHEET 5 B 9 ILE A 102 SER A 105 1 O ILE A 103 N ILE A 72
SHEET 6 B 9 LYS A 124 ILE A 127 1 O LYS A 124 N ALA A 104
SHEET 7 B 9 VAL A 150 VAL A 159 1 O ALA A 153 N ILE A 127
SHEET 8 B 9 GLU A 162 THR A 167 -1 O PHE A 166 N VAL A 155
SHEET 9 B 9 LYS A 172 LEU A 177 -1 O ILE A 176 N VAL A 165
CRYST1 35.212 63.142 56.260 90.00 99.03 90.00 P 1 21 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 0.028399 0.000000 0.004513 0.00000
SCALE2 0.000000 0.015837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017998 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
