HEADER DE NOVO PROTEIN 23-SEP-11 4A29
TITLE STRUCTURE OF THE ENGINEERED RETRO-ALDOLASE RA95.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENGINEERED RETRO-ALDOL ENZYME RA95.0;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TIM-BARREL FOLD, RESIDUES 1-258;
COMPND 5 EC: 4.1.1.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: ARTIFICIAL GENE. THE SEQUENCE WAS COMPUTATIONALLY
COMPND 8 DESIGNED BASED ON INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE NATURALLY
COMPND 9 FOUND IN SULFOLOBUS SOLFATARICUS.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: GOLD;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-29B(PLUS)
KEYWDS DE NOVO PROTEIN, ENGINEERED ENZYME, RETRO-ALDOLASE, DIRECTED
KEYWDS 2 EVOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR L.GIGER,S.CANER,P.KAST,D.BAKER,N.BAN,D.HILVERT
REVDAT 6 20-DEC-23 4A29 1 REMARK LINK
REVDAT 5 15-MAY-19 4A29 1 JRNL REMARK LINK
REVDAT 4 31-JUL-13 4A29 1 JRNL
REVDAT 3 19-JUN-13 4A29 1 JRNL
REVDAT 2 12-JUN-13 4A29 1 JRNL
REVDAT 1 07-NOV-12 4A29 0
JRNL AUTH L.GIGER,S.CANER,R.OBEXER,P.KAST,D.BAKER,N.BAN,D.HILVERT
JRNL TITL EVOLUTION OF A DESIGNED RETRO-ALDOLASE LEADS TO COMPLETE
JRNL TITL 2 ACTIVE SITE REMODELING.
JRNL REF NAT.CHEM.BIOL. V. 9 494 2013
JRNL REFN ESSN 1552-4469
JRNL PMID 23748672
JRNL DOI 10.1038/NCHEMBIO.1276
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 100713
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.120
REMARK 3 R VALUE (WORKING SET) : 0.120
REMARK 3 FREE R VALUE : 0.137
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2030
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 7.9812 - 2.6217 0.98 7889 162 0.1462 0.1410
REMARK 3 2 2.6217 - 2.0933 0.99 7717 161 0.1154 0.1483
REMARK 3 3 2.0933 - 1.8324 0.98 7615 155 0.1048 0.1282
REMARK 3 4 1.8324 - 1.6665 0.99 7587 156 0.0974 0.1220
REMARK 3 5 1.6665 - 1.5480 0.98 7519 155 0.0912 0.1316
REMARK 3 6 1.5480 - 1.4573 0.98 7468 155 0.0925 0.1184
REMARK 3 7 1.4573 - 1.3847 0.97 7428 155 0.0968 0.1187
REMARK 3 8 1.3847 - 1.3247 0.97 7471 148 0.0993 0.1245
REMARK 3 9 1.3247 - 1.2739 0.97 7389 153 0.1090 0.1379
REMARK 3 10 1.2739 - 1.2301 0.97 7369 147 0.1161 0.1367
REMARK 3 11 1.2301 - 1.1918 0.95 7261 150 0.1227 0.1399
REMARK 3 12 1.1918 - 1.1578 0.84 6404 128 0.1232 0.1542
REMARK 3 13 1.1578 - 1.1274 0.69 5226 130 0.1377 0.1545
REMARK 3 14 1.1274 - 1.1000 0.57 4340 75 0.1581 0.1877
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.10
REMARK 3 SHRINKAGE RADIUS : 0.00
REMARK 3 K_SOL : 0.60
REMARK 3 B_SOL : 96.57
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.740
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) : 0.90320
REMARK 3 B22 (A**2) : -1.85220
REMARK 3 B33 (A**2) : 0.94900
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 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 : 0.009 2404
REMARK 3 ANGLE : 1.297 3288
REMARK 3 CHIRALITY : 0.070 370
REMARK 3 PLANARITY : 0.007 438
REMARK 3 DIHEDRAL : 0.000 0
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 4A29 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1290049766.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101040
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.02000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.210
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 1LBL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M DL-MALIC ACID PH 7.0, 20% W/V
REMARK 280 PEG 3350, 28 DEGREES CELSIUS., VAPOR DIFFUSION, TEMPERATURE 301K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 26.97000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.90500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.29500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.90500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.97000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.29500
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/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 MET A 1
REMARK 465 GLY A 249
REMARK 465 SER A 250
REMARK 465 LEU A 251
REMARK 465 GLU A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
REMARK 465 HIS A 255
REMARK 465 HIS A 256
REMARK 465 HIS A 257
REMARK 465 HIS A 258
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 HD22 ASN A 190 OD1 ASN A 193 1.50
REMARK 500 OE1 GLN A 27 O HOH A 2097 2.04
REMARK 500 ND2 ASN A 190 OD1 ASN A 193 2.10
REMARK 500
REMARK 500 REMARK: NULL
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 64 NE - CZ - NH2 ANGL. DEV. = -4.3 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 111 -168.79 -166.00
REMARK 500 SER A 233 -84.05 -117.21
REMARK 500 SER A 233 -87.17 -103.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3NK A 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLT A 300
DBREF 4A29 A 1 258 PDB 4A29 4A29 1 258
SEQRES 1 A 258 MET PRO ARG TYR LEU LYS GLY TRP LEU GLU ASP VAL VAL
SEQRES 2 A 258 GLN LEU SER LEU ARG ARG PRO SER VAL ARG ALA SER ARG
SEQRES 3 A 258 GLN ARG PRO ILE ILE SER LEU ASN GLU ARG ILE LEU GLU
SEQRES 4 A 258 PHE ASN LYS ARG ASN ILE THR ALA ILE ILE ALA VAL TYR
SEQRES 5 A 258 GLU ARG LYS SER PRO SER GLY LEU ASP VAL GLU ARG ASP
SEQRES 6 A 258 PRO ILE GLU TYR ALA LYS PHE MET GLU ARG TYR ALA VAL
SEQRES 7 A 258 GLY LEU SER ILE THR THR GLU GLU LYS TYR PHE ASN GLY
SEQRES 8 A 258 SER TYR GLU THR LEU ARG LYS ILE ALA SER SER VAL SER
SEQRES 9 A 258 ILE PRO ILE LEU MET SER ASP PHE ILE VAL LYS GLU SER
SEQRES 10 A 258 GLN ILE ASP ASP ALA TYR ASN LEU GLY ALA ASP THR VAL
SEQRES 11 A 258 LEU LEU ILE VAL LYS ILE LEU THR GLU ARG GLU LEU GLU
SEQRES 12 A 258 SER LEU LEU GLU TYR ALA ARG SER TYR GLY MET GLU PRO
SEQRES 13 A 258 LEU ILE LEU ILE ASN ASP GLU ASN ASP LEU ASP ILE ALA
SEQRES 14 A 258 LEU ARG ILE GLY ALA ARG PHE ILE GLY ILE MET SER ARG
SEQRES 15 A 258 ASP PHE GLU THR GLY GLU ILE ASN LYS GLU ASN GLN ARG
SEQRES 16 A 258 LYS LEU ILE SER MET ILE PRO SER ASN VAL VAL LYS VAL
SEQRES 17 A 258 ALA LYS LEU GLY ILE SER GLU ARG ASN GLU ILE GLU GLU
SEQRES 18 A 258 LEU ARG LYS LEU GLY VAL ASN ALA PHE LEU ILE SER SER
SEQRES 19 A 258 SER LEU MET ARG ASN PRO GLU LYS ILE LYS GLU LEU ILE
SEQRES 20 A 258 GLU GLY SER LEU GLU HIS HIS HIS HIS HIS HIS
HET 3NK A 299 31
HET MLT A 300 13
HETNAM 3NK 1-(6-METHOXYNAPHTHALEN-2-YL)BUTANE-1,3-DIONE
HETNAM MLT D-MALATE
HETSYN MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID
FORMUL 2 3NK C15 H14 O3
FORMUL 3 MLT C4 H6 O5
FORMUL 4 HOH *369(H2 O)
HELIX 1 1 LYS A 6 ARG A 18 1 13
HELIX 2 2 SER A 32 ARG A 43 1 12
HELIX 3 3 ASP A 65 GLU A 74 1 10
HELIX 4 4 SER A 92 SER A 101 1 10
HELIX 5 5 LYS A 115 GLY A 126 1 12
HELIX 6 6 LYS A 135 LEU A 137 5 3
HELIX 7 7 THR A 138 TYR A 152 1 15
HELIX 8 8 ASP A 162 ILE A 172 1 11
HELIX 9 9 ASN A 190 SER A 199 1 10
HELIX 10 10 GLU A 215 LEU A 225 1 11
HELIX 11 11 SER A 233 ASN A 239 1 7
HELIX 12 12 GLU A 241 GLU A 248 1 8
SHEET 1 AA 9 ILE A 48 TYR A 52 0
SHEET 2 AA 9 ALA A 229 ILE A 232 1 O PHE A 230 N ILE A 49
SHEET 3 AA 9 VAL A 206 LEU A 211 1 O ALA A 209 N LEU A 231
SHEET 4 AA 9 PHE A 176 ILE A 179 1 O ILE A 177 N VAL A 208
SHEET 5 AA 9 LEU A 157 ILE A 160 1 O ILE A 158 N GLY A 178
SHEET 6 AA 9 THR A 129 ILE A 133 1 O VAL A 130 N LEU A 157
SHEET 7 AA 9 ILE A 107 SER A 110 1 O MET A 109 N LEU A 131
SHEET 8 AA 9 GLY A 79 THR A 83 1 O LEU A 80 N LEU A 108
SHEET 9 AA 9 ILE A 48 TYR A 52 1 O ALA A 50 N SER A 81
LINK NZ LYS A 210 C13 3NK A 299 1555 1555 1.34
SITE 1 AC1 8 MET A 180 ARG A 182 ASP A 183 GLY A 187
SITE 2 AC1 8 LYS A 210 MLT A 300 HOH A2303 HOH A2340
SITE 1 AC2 12 GLU A 53 SER A 56 SER A 58 PHE A 89
SITE 2 AC2 12 ARG A 182 GLY A 212 SER A 233 SER A 234
SITE 3 AC2 12 3NK A 299 HOH A2160 HOH A2175 HOH A2304
CRYST1 53.940 62.590 79.810 90.00 90.00 90.00 P 21 21 21 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 0.018539 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015977 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012530 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
