HEADER ELECTRON TRANSPORT 07-FEB-14 4OXX
TITLE CRYSTAL STRUCTURE OF CINDOXIN, SURFACE ENTROPY REDUCTION MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CINDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CDX, FMN-CONTAINING REDOX PARTNER;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CITROBACTER BRAAKII;
SOURCE 3 ORGANISM_TAXID: 57706;
SOURCE 4 GENE: CINC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS FLAVOPROTEIN, FMN, CINDOXIN, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.MADRONA,T.L.POULOS
REVDAT 5 27-DEC-23 4OXX 1 REMARK
REVDAT 4 25-DEC-19 4OXX 1 REMARK
REVDAT 3 20-SEP-17 4OXX 1 SOURCE JRNL REMARK
REVDAT 2 01-OCT-14 4OXX 1 JRNL
REVDAT 1 16-APR-14 4OXX 0
JRNL AUTH Y.MADRONA,S.A.HOLLINGSWORTH,S.TRIPATHI,J.B.FIELDS,
JRNL AUTH 2 J.C.RWIGEMA,D.J.TOBIAS,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURE OF CINDOXIN, THE P450CIN REDOX PARTNER.
JRNL REF BIOCHEMISTRY V. 53 1435 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 24533927
JRNL DOI 10.1021/BI500010M
REMARK 2
REMARK 2 RESOLUTION. 1.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 1.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 43762
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2213
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 32.8640 - 3.0438 0.96 2649 136 0.1705 0.1856
REMARK 3 2 3.0438 - 2.4162 1.00 2655 136 0.1671 0.1839
REMARK 3 3 2.4162 - 2.1109 0.94 2504 132 0.1383 0.1467
REMARK 3 4 2.1109 - 1.9179 0.98 2568 134 0.1277 0.1459
REMARK 3 5 1.9179 - 1.7804 0.99 2613 131 0.1253 0.1466
REMARK 3 6 1.7804 - 1.6755 0.99 2578 151 0.1197 0.1496
REMARK 3 7 1.6755 - 1.5916 1.00 2636 137 0.1052 0.1338
REMARK 3 8 1.5916 - 1.5223 1.00 2609 128 0.1029 0.1155
REMARK 3 9 1.5223 - 1.4637 1.00 2586 162 0.1035 0.1281
REMARK 3 10 1.4637 - 1.4132 1.00 2600 124 0.1034 0.1115
REMARK 3 11 1.4132 - 1.3690 1.00 2562 143 0.1085 0.1269
REMARK 3 12 1.3690 - 1.3298 1.00 2654 153 0.1056 0.1342
REMARK 3 13 1.3298 - 1.2948 1.00 2608 125 0.1195 0.1797
REMARK 3 14 1.2948 - 1.2632 1.00 2577 145 0.1275 0.1730
REMARK 3 15 1.2632 - 1.2345 1.00 2596 123 0.1470 0.1923
REMARK 3 16 1.2345 - 1.2100 0.98 2554 153 0.1766 0.2120
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.30
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.230
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 : 0.014 1163
REMARK 3 ANGLE : 1.576 1594
REMARK 3 CHIRALITY : 0.084 188
REMARK 3 PLANARITY : 0.012 205
REMARK 3 DIHEDRAL : 14.030 386
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 4OXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000200214.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43778
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.210
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.8000
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, PH 7, 1.7-2.1M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, TEMPERATURE 298K
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 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 24.69467
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 12.34733
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 12.34733
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 24.69467
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 320 LIES ON A SPECIAL POSITION.
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 A 154
REMARK 465 LEU A 155
REMARK 465 GLU A 156
REMARK 465 HIS A 157
REMARK 465 HIS A 158
REMARK 465 HIS A 159
REMARK 465 HIS A 160
REMARK 465 HIS A 161
REMARK 465 HIS A 162
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 329 O HOH A 400 1.72
REMARK 500 O HOH A 322 O HOH A 367 1.86
REMARK 500 OG1 THR A 56 O HOH A 478 1.95
REMARK 500 O HOH A 390 O HOH A 429 2.07
REMARK 500 O HOH A 464 O HOH A 517 2.08
REMARK 500 OD2 ASP A 38 O HOH A 301 2.10
REMARK 500 O HOH A 344 O HOH A 390 2.13
REMARK 500 O HOH A 329 O HOH A 408 2.13
REMARK 500 NH1 ARG A 142 O HOH A 302 2.15
REMARK 500 O HOH A 334 O HOH A 408 2.15
REMARK 500 O HOH A 322 O HOH A 516 2.15
REMARK 500 OD2 ASP A 38 O HOH A 301 2.18
REMARK 500 O HOH A 303 O HOH A 305 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 HOH A 400 O HOH A 412 3545 1.78
REMARK 500 O HOH A 305 O HOH A 317 3545 1.96
REMARK 500 O HOH A 387 O HOH A 387 6554 2.08
REMARK 500 O HOH A 330 O HOH A 376 5445 2.11
REMARK 500 O HOH A 375 O HOH A 380 3545 2.18
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 FMN A 200
DBREF 4OXX A 1 154 UNP Q8VQF4 CINC_CITBR 1 154
SEQADV 4OXX ALA A 134 UNP Q8VQF4 GLU 134 ENGINEERED MUTATION
SEQADV 4OXX ALA A 135 UNP Q8VQF4 GLU 135 ENGINEERED MUTATION
SEQADV 4OXX ALA A 138 UNP Q8VQF4 GLU 138 ENGINEERED MUTATION
SEQADV 4OXX LEU A 155 UNP Q8VQF4 EXPRESSION TAG
SEQADV 4OXX GLU A 156 UNP Q8VQF4 EXPRESSION TAG
SEQADV 4OXX HIS A 157 UNP Q8VQF4 EXPRESSION TAG
SEQADV 4OXX HIS A 158 UNP Q8VQF4 EXPRESSION TAG
SEQADV 4OXX HIS A 159 UNP Q8VQF4 EXPRESSION TAG
SEQADV 4OXX HIS A 160 UNP Q8VQF4 EXPRESSION TAG
SEQADV 4OXX HIS A 161 UNP Q8VQF4 EXPRESSION TAG
SEQADV 4OXX HIS A 162 UNP Q8VQF4 EXPRESSION TAG
SEQRES 1 A 162 MET ASN ALA LEU ILE LEU TYR GLY THR GLU THR GLY ASN
SEQRES 2 A 162 ALA GLU ALA CYS ALA THR THR ILE SER GLN VAL LEU ALA
SEQRES 3 A 162 ASP THR VAL ASP THR LYS VAL HIS ASP LEU ALA ASP MET
SEQRES 4 A 162 THR PRO ARG ALA MET LEU ASP SER GLY ALA ASP LEU ILE
SEQRES 5 A 162 VAL PHE ALA THR ALA THR TYR GLY GLU GLY GLU PHE ALA
SEQRES 6 A 162 GLY GLY GLY ALA ALA PHE PHE GLU THR LEU ARG GLU THR
SEQRES 7 A 162 LYS PRO ASP LEU SER GLY LEU ARG PHE ALA VAL PHE GLY
SEQRES 8 A 162 LEU GLY ASP SER TYR TYR THR THR PHE ASN GLN ALA GLY
SEQRES 9 A 162 ALA THR ALA ALA THR ILE LEU ALA SER LEU GLY GLY THR
SEQRES 10 A 162 GLN VAL GLY ASP THR ALA ARG HIS ASP THR SER SER GLY
SEQRES 11 A 162 ASP ASP PRO ALA ALA THR ALA ALA GLU TRP ALA ARG GLU
SEQRES 12 A 162 ILE LEU THR ALA LEU ALA THR PRO ALA VAL SER LEU GLU
SEQRES 13 A 162 HIS HIS HIS HIS HIS HIS
HET FMN A 200 31
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 FMN C17 H21 N4 O9 P
FORMUL 3 HOH *228(H2 O)
HELIX 1 AA1 GLY A 12 ALA A 26 1 15
HELIX 2 AA2 ALA A 37 MET A 39 5 3
HELIX 3 AA3 THR A 40 SER A 47 1 8
HELIX 4 AA4 GLY A 67 LYS A 79 1 13
HELIX 5 AA5 ASN A 101 LEU A 114 1 14
HELIX 6 AA6 SER A 128 GLY A 130 5 3
HELIX 7 AA7 ASP A 132 ALA A 149 1 18
SHEET 1 AA1 5 ASP A 30 ASP A 35 0
SHEET 2 AA1 5 ASN A 2 GLY A 8 1 N ALA A 3 O ASP A 30
SHEET 3 AA1 5 LEU A 51 TYR A 59 1 O VAL A 53 N LEU A 6
SHEET 4 AA1 5 ARG A 86 GLY A 93 1 O PHE A 90 N PHE A 54
SHEET 5 AA1 5 THR A 117 GLN A 118 1 O THR A 117 N PHE A 87
SHEET 1 AA2 4 GLU A 63 PHE A 64 0
SHEET 2 AA2 4 LEU A 51 TYR A 59 -1 N TYR A 59 O GLU A 63
SHEET 3 AA2 4 ARG A 86 GLY A 93 1 O PHE A 90 N PHE A 54
SHEET 4 AA2 4 ALA A 123 ASP A 126 1 O HIS A 125 N GLY A 91
SITE 1 AC1 24 THR A 9 GLU A 10 THR A 11 GLY A 12
SITE 2 AC1 24 ASN A 13 ALA A 14 ALA A 57 THR A 58
SITE 3 AC1 24 TYR A 59 GLY A 60 GLY A 93 ASP A 94
SITE 4 AC1 24 TYR A 97 THR A 98 THR A 99 PHE A 100
SITE 5 AC1 24 ASN A 101 THR A 109 THR A 127 HOH A 433
SITE 6 AC1 24 HOH A 436 HOH A 443 HOH A 447 HOH A 463
CRYST1 82.109 82.109 37.042 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 0.012179 0.007032 0.000000 0.00000
SCALE2 0.000000 0.014063 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026996 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
