HEADER OXIDOREDUCTASE 22-DEC-16 5UCA
TITLE CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-2 IN COMPLEX WITH LAURATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEME OXYGENASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 30-242;
COMPND 5 SYNONYM: HO-2;
COMPND 6 EC: 1.14.14.18;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HMOX2, HO2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HEME OXYGENASE, LAURIC ACID, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LUO,L.TONG
REVDAT 4 04-OCT-23 5UCA 1 REMARK
REVDAT 3 22-NOV-17 5UCA 1 REMARK
REVDAT 2 22-FEB-17 5UCA 1 JRNL
REVDAT 1 15-FEB-17 5UCA 0
JRNL AUTH Y.ZHU,S.LUO,Y.SABO,C.WANG,L.TONG,S.P.GOFF
JRNL TITL HEME OXYGENASE 2 BINDS MYRISTATE TO REGULATE RETROVIRUS
JRNL TITL 2 ASSEMBLY AND TLR4 SIGNALING.
JRNL REF CELL HOST MICROBE V. 21 220 2017
JRNL REFN ESSN 1934-6069
JRNL PMID 28132836
JRNL DOI 10.1016/J.CHOM.2017.01.002
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 51395
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.810
REMARK 3 FREE R VALUE TEST SET COUNT : 1445
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 24.6518 - 4.5522 0.96 5115 149 0.1634 0.2066
REMARK 3 2 4.5522 - 3.6169 1.00 5114 147 0.1630 0.1979
REMARK 3 3 3.6169 - 3.1607 1.00 5062 150 0.1969 0.2582
REMARK 3 4 3.1607 - 2.8722 1.00 5029 144 0.2169 0.2700
REMARK 3 5 2.8722 - 2.6666 1.00 5022 147 0.2183 0.2793
REMARK 3 6 2.6666 - 2.5096 1.00 5010 143 0.2181 0.2898
REMARK 3 7 2.5096 - 2.3840 1.00 5008 149 0.2144 0.3131
REMARK 3 8 2.3840 - 2.2803 1.00 4967 132 0.2117 0.3092
REMARK 3 9 2.2803 - 2.1926 1.00 4997 147 0.2385 0.2962
REMARK 3 10 2.1926 - 2.1169 0.93 4626 137 0.2531 0.3331
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.72
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 : 0.007 7098
REMARK 3 ANGLE : 0.797 9528
REMARK 3 CHIRALITY : 0.043 983
REMARK 3 PLANARITY : 0.005 1254
REMARK 3 DIHEDRAL : 19.404 4327
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 5UCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225646.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-16
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 : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97921
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : LR-DESIGN DETECTOR POSITIONER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51449
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.38500
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: PHENIX
REMARK 200 STARTING MODEL: 5UC8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS (PH 6.5) AND 24% (W/V)
REMARK 280 PEG 2000 MONOMETHYL ETHER, VAPOR DIFFUSION, TEMPERATURE 293K
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 38.68150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.14850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.96000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.14850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.68150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.96000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 HIS A 21
REMARK 465 HIS A 22
REMARK 465 HIS A 23
REMARK 465 HIS A 24
REMARK 465 HIS A 25
REMARK 465 HIS A 26
REMARK 465 SER A 27
REMARK 465 SER A 28
REMARK 465 GLY A 29
REMARK 465 MET A 30
REMARK 465 ALA A 240
REMARK 465 GLY A 241
REMARK 465 SER A 242
REMARK 465 MET B 17
REMARK 465 GLY B 18
REMARK 465 SER B 19
REMARK 465 SER B 20
REMARK 465 HIS B 21
REMARK 465 HIS B 22
REMARK 465 HIS B 23
REMARK 465 HIS B 24
REMARK 465 HIS B 25
REMARK 465 HIS B 26
REMARK 465 SER B 27
REMARK 465 SER B 28
REMARK 465 GLY B 29
REMARK 465 MET B 30
REMARK 465 GLY B 241
REMARK 465 SER B 242
REMARK 465 MET C 17
REMARK 465 GLY C 18
REMARK 465 SER C 19
REMARK 465 SER C 20
REMARK 465 HIS C 21
REMARK 465 HIS C 22
REMARK 465 HIS C 23
REMARK 465 HIS C 24
REMARK 465 HIS C 25
REMARK 465 HIS C 26
REMARK 465 SER C 27
REMARK 465 SER C 28
REMARK 465 GLY C 29
REMARK 465 MET C 30
REMARK 465 GLY C 241
REMARK 465 SER C 242
REMARK 465 MET D 17
REMARK 465 GLY D 18
REMARK 465 SER D 19
REMARK 465 SER D 20
REMARK 465 HIS D 21
REMARK 465 HIS D 22
REMARK 465 HIS D 23
REMARK 465 HIS D 24
REMARK 465 HIS D 25
REMARK 465 HIS D 26
REMARK 465 SER D 27
REMARK 465 SER D 28
REMARK 465 GLY D 29
REMARK 465 MET D 30
REMARK 465 GLY D 241
REMARK 465 SER D 242
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 NH2 ARG D 47 OE2 GLU D 228 2.12
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 D 455 O HOH D 490 4555 2.19
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 61 58.17 -105.92
REMARK 500 PHE A 94 -27.32 -141.19
REMARK 500 ASN A 120 36.78 -91.10
REMARK 500 ARG A 156 -63.34 -92.80
REMARK 500 PHE A 189 79.15 -102.78
REMARK 500 ASN B 61 48.10 -99.57
REMARK 500 PHE B 94 -30.03 -130.57
REMARK 500 ASN B 120 31.16 -89.51
REMARK 500 ASN B 144 -26.81 -140.28
REMARK 500 GLN B 239 1.32 -69.81
REMARK 500 ARG C 156 -60.27 -90.17
REMARK 500 ASN D 61 49.77 -102.52
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 DAO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UC8 RELATED DB: PDB
REMARK 900 RELATED ID: 5UC9 RELATED DB: PDB
DBREF 5UCA A 30 242 UNP P30519 HMOX2_HUMAN 1 213
DBREF 5UCA B 30 242 UNP P30519 HMOX2_HUMAN 1 213
DBREF 5UCA C 30 242 UNP P30519 HMOX2_HUMAN 1 213
DBREF 5UCA D 30 242 UNP P30519 HMOX2_HUMAN 1 213
SEQADV 5UCA MET A 17 UNP P30519 INITIATING METHIONINE
SEQADV 5UCA GLY A 18 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER A 19 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER A 20 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS A 21 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS A 22 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS A 23 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS A 24 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS A 25 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS A 26 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER A 27 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER A 28 UNP P30519 EXPRESSION TAG
SEQADV 5UCA GLY A 29 UNP P30519 EXPRESSION TAG
SEQADV 5UCA MET B 17 UNP P30519 INITIATING METHIONINE
SEQADV 5UCA GLY B 18 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER B 19 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER B 20 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS B 21 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS B 22 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS B 23 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS B 24 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS B 25 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS B 26 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER B 27 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER B 28 UNP P30519 EXPRESSION TAG
SEQADV 5UCA GLY B 29 UNP P30519 EXPRESSION TAG
SEQADV 5UCA MET C 17 UNP P30519 INITIATING METHIONINE
SEQADV 5UCA GLY C 18 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER C 19 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER C 20 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS C 21 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS C 22 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS C 23 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS C 24 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS C 25 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS C 26 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER C 27 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER C 28 UNP P30519 EXPRESSION TAG
SEQADV 5UCA GLY C 29 UNP P30519 EXPRESSION TAG
SEQADV 5UCA MET D 17 UNP P30519 INITIATING METHIONINE
SEQADV 5UCA GLY D 18 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER D 19 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER D 20 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS D 21 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS D 22 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS D 23 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS D 24 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS D 25 UNP P30519 EXPRESSION TAG
SEQADV 5UCA HIS D 26 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER D 27 UNP P30519 EXPRESSION TAG
SEQADV 5UCA SER D 28 UNP P30519 EXPRESSION TAG
SEQADV 5UCA GLY D 29 UNP P30519 EXPRESSION TAG
SEQRES 1 A 226 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 226 MET ALA ASP LEU SER GLU LEU LEU LYS GLU GLY THR LYS
SEQRES 3 A 226 GLU ALA HIS ASP ARG ALA GLU ASN THR GLN PHE VAL LYS
SEQRES 4 A 226 ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU LEU PHE LYS
SEQRES 5 A 226 LEU ALA THR THR ALA LEU TYR PHE THR TYR SER ALA LEU
SEQRES 6 A 226 GLU GLU GLU MET GLU ARG ASN LYS ASP HIS PRO ALA PHE
SEQRES 7 A 226 ALA PRO LEU TYR PHE PRO MET GLU LEU HIS ARG LYS GLU
SEQRES 8 A 226 ALA LEU THR LYS ASP MET GLU TYR PHE PHE GLY GLU ASN
SEQRES 9 A 226 TRP GLU GLU GLN VAL GLN CYS PRO LYS ALA ALA GLN LYS
SEQRES 10 A 226 TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN ASN GLU PRO
SEQRES 11 A 226 GLU LEU LEU VAL ALA HIS ALA TYR THR ARG TYR MET GLY
SEQRES 12 A 226 ASP LEU SER GLY GLY GLN VAL LEU LYS LYS VAL ALA GLN
SEQRES 13 A 226 ARG ALA LEU LYS LEU PRO SER THR GLY GLU GLY THR GLN
SEQRES 14 A 226 PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA GLN GLN PHE
SEQRES 15 A 226 LYS GLN LEU TYR ARG ALA ARG MET ASN ALA LEU ASP LEU
SEQRES 16 A 226 ASN MET LYS THR LYS GLU ARG ILE VAL GLU GLU ALA ASN
SEQRES 17 A 226 LYS ALA PHE GLU TYR ASN MET GLN ILE PHE ASN GLU LEU
SEQRES 18 A 226 ASP GLN ALA GLY SER
SEQRES 1 B 226 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 226 MET ALA ASP LEU SER GLU LEU LEU LYS GLU GLY THR LYS
SEQRES 3 B 226 GLU ALA HIS ASP ARG ALA GLU ASN THR GLN PHE VAL LYS
SEQRES 4 B 226 ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU LEU PHE LYS
SEQRES 5 B 226 LEU ALA THR THR ALA LEU TYR PHE THR TYR SER ALA LEU
SEQRES 6 B 226 GLU GLU GLU MET GLU ARG ASN LYS ASP HIS PRO ALA PHE
SEQRES 7 B 226 ALA PRO LEU TYR PHE PRO MET GLU LEU HIS ARG LYS GLU
SEQRES 8 B 226 ALA LEU THR LYS ASP MET GLU TYR PHE PHE GLY GLU ASN
SEQRES 9 B 226 TRP GLU GLU GLN VAL GLN CYS PRO LYS ALA ALA GLN LYS
SEQRES 10 B 226 TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN ASN GLU PRO
SEQRES 11 B 226 GLU LEU LEU VAL ALA HIS ALA TYR THR ARG TYR MET GLY
SEQRES 12 B 226 ASP LEU SER GLY GLY GLN VAL LEU LYS LYS VAL ALA GLN
SEQRES 13 B 226 ARG ALA LEU LYS LEU PRO SER THR GLY GLU GLY THR GLN
SEQRES 14 B 226 PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA GLN GLN PHE
SEQRES 15 B 226 LYS GLN LEU TYR ARG ALA ARG MET ASN ALA LEU ASP LEU
SEQRES 16 B 226 ASN MET LYS THR LYS GLU ARG ILE VAL GLU GLU ALA ASN
SEQRES 17 B 226 LYS ALA PHE GLU TYR ASN MET GLN ILE PHE ASN GLU LEU
SEQRES 18 B 226 ASP GLN ALA GLY SER
SEQRES 1 C 226 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 226 MET ALA ASP LEU SER GLU LEU LEU LYS GLU GLY THR LYS
SEQRES 3 C 226 GLU ALA HIS ASP ARG ALA GLU ASN THR GLN PHE VAL LYS
SEQRES 4 C 226 ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU LEU PHE LYS
SEQRES 5 C 226 LEU ALA THR THR ALA LEU TYR PHE THR TYR SER ALA LEU
SEQRES 6 C 226 GLU GLU GLU MET GLU ARG ASN LYS ASP HIS PRO ALA PHE
SEQRES 7 C 226 ALA PRO LEU TYR PHE PRO MET GLU LEU HIS ARG LYS GLU
SEQRES 8 C 226 ALA LEU THR LYS ASP MET GLU TYR PHE PHE GLY GLU ASN
SEQRES 9 C 226 TRP GLU GLU GLN VAL GLN CYS PRO LYS ALA ALA GLN LYS
SEQRES 10 C 226 TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN ASN GLU PRO
SEQRES 11 C 226 GLU LEU LEU VAL ALA HIS ALA TYR THR ARG TYR MET GLY
SEQRES 12 C 226 ASP LEU SER GLY GLY GLN VAL LEU LYS LYS VAL ALA GLN
SEQRES 13 C 226 ARG ALA LEU LYS LEU PRO SER THR GLY GLU GLY THR GLN
SEQRES 14 C 226 PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA GLN GLN PHE
SEQRES 15 C 226 LYS GLN LEU TYR ARG ALA ARG MET ASN ALA LEU ASP LEU
SEQRES 16 C 226 ASN MET LYS THR LYS GLU ARG ILE VAL GLU GLU ALA ASN
SEQRES 17 C 226 LYS ALA PHE GLU TYR ASN MET GLN ILE PHE ASN GLU LEU
SEQRES 18 C 226 ASP GLN ALA GLY SER
SEQRES 1 D 226 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 226 MET ALA ASP LEU SER GLU LEU LEU LYS GLU GLY THR LYS
SEQRES 3 D 226 GLU ALA HIS ASP ARG ALA GLU ASN THR GLN PHE VAL LYS
SEQRES 4 D 226 ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU LEU PHE LYS
SEQRES 5 D 226 LEU ALA THR THR ALA LEU TYR PHE THR TYR SER ALA LEU
SEQRES 6 D 226 GLU GLU GLU MET GLU ARG ASN LYS ASP HIS PRO ALA PHE
SEQRES 7 D 226 ALA PRO LEU TYR PHE PRO MET GLU LEU HIS ARG LYS GLU
SEQRES 8 D 226 ALA LEU THR LYS ASP MET GLU TYR PHE PHE GLY GLU ASN
SEQRES 9 D 226 TRP GLU GLU GLN VAL GLN CYS PRO LYS ALA ALA GLN LYS
SEQRES 10 D 226 TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN ASN GLU PRO
SEQRES 11 D 226 GLU LEU LEU VAL ALA HIS ALA TYR THR ARG TYR MET GLY
SEQRES 12 D 226 ASP LEU SER GLY GLY GLN VAL LEU LYS LYS VAL ALA GLN
SEQRES 13 D 226 ARG ALA LEU LYS LEU PRO SER THR GLY GLU GLY THR GLN
SEQRES 14 D 226 PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA GLN GLN PHE
SEQRES 15 D 226 LYS GLN LEU TYR ARG ALA ARG MET ASN ALA LEU ASP LEU
SEQRES 16 D 226 ASN MET LYS THR LYS GLU ARG ILE VAL GLU GLU ALA ASN
SEQRES 17 D 226 LYS ALA PHE GLU TYR ASN MET GLN ILE PHE ASN GLU LEU
SEQRES 18 D 226 ASP GLN ALA GLY SER
HET DAO B 301 14
HET DAO C 301 14
HET DAO D 301 14
HETNAM DAO LAURIC ACID
FORMUL 5 DAO 3(C12 H24 O2)
FORMUL 8 HOH *414(H2 O)
HELIX 1 AA1 ASP A 32 THR A 41 1 10
HELIX 2 AA2 THR A 41 ASN A 50 1 10
HELIX 3 AA3 THR A 51 LYS A 59 1 9
HELIX 4 AA4 LYS A 63 ASN A 88 1 26
HELIX 5 AA5 PHE A 94 TYR A 98 5 5
HELIX 6 AA6 PHE A 99 HIS A 104 1 6
HELIX 7 AA7 ARG A 105 GLY A 118 1 14
HELIX 8 AA8 ASN A 120 VAL A 125 1 6
HELIX 9 AA9 PRO A 128 GLU A 145 1 18
HELIX 10 AB1 LEU A 148 LEU A 175 1 28
HELIX 11 AB2 THR A 184 LEU A 188 5 5
HELIX 12 AB3 ASN A 194 ALA A 208 1 15
HELIX 13 AB4 ASN A 212 GLN A 239 1 28
HELIX 14 AB5 ASP B 32 THR B 41 1 10
HELIX 15 AB6 THR B 41 ASN B 50 1 10
HELIX 16 AB7 THR B 51 GLY B 60 1 10
HELIX 17 AB8 LYS B 63 ASN B 88 1 26
HELIX 18 AB9 PHE B 94 TYR B 98 5 5
HELIX 19 AC1 PHE B 99 HIS B 104 1 6
HELIX 20 AC2 ARG B 105 GLY B 118 1 14
HELIX 21 AC3 ASN B 120 VAL B 125 1 6
HELIX 22 AC4 PRO B 128 GLU B 145 1 18
HELIX 23 AC5 LEU B 148 LYS B 176 1 29
HELIX 24 AC6 THR B 184 LEU B 188 5 5
HELIX 25 AC7 ASN B 194 LEU B 209 1 16
HELIX 26 AC8 ASN B 212 GLN B 239 1 28
HELIX 27 AC9 ASP C 32 THR C 41 1 10
HELIX 28 AD1 THR C 41 ASN C 50 1 10
HELIX 29 AD2 THR C 51 GLY C 60 1 10
HELIX 30 AD3 LYS C 63 ASN C 88 1 26
HELIX 31 AD4 PHE C 94 TYR C 98 5 5
HELIX 32 AD5 PHE C 99 HIS C 104 1 6
HELIX 33 AD6 ARG C 105 GLY C 118 1 14
HELIX 34 AD7 ASN C 120 VAL C 125 1 6
HELIX 35 AD8 PRO C 128 GLU C 145 1 18
HELIX 36 AD9 LEU C 148 LYS C 176 1 29
HELIX 37 AE1 THR C 184 LEU C 188 5 5
HELIX 38 AE2 ASN C 194 LEU C 209 1 16
HELIX 39 AE3 ASN C 212 ALA C 240 1 29
HELIX 40 AE4 ASP D 32 THR D 41 1 10
HELIX 41 AE5 THR D 41 ASN D 50 1 10
HELIX 42 AE6 THR D 51 LYS D 59 1 9
HELIX 43 AE7 LYS D 63 ASN D 88 1 26
HELIX 44 AE8 PHE D 94 TYR D 98 5 5
HELIX 45 AE9 PHE D 99 HIS D 104 1 6
HELIX 46 AF1 ARG D 105 GLY D 118 1 14
HELIX 47 AF2 ASN D 120 VAL D 125 1 6
HELIX 48 AF3 PRO D 128 GLU D 145 1 18
HELIX 49 AF4 LEU D 148 LEU D 175 1 28
HELIX 50 AF5 THR D 184 LEU D 188 5 5
HELIX 51 AF6 ASN D 194 LEU D 209 1 16
HELIX 52 AF7 ASN D 212 ALA D 240 1 29
SITE 1 AC1 5 GLU B 49 LEU B 74 ARG B 156 TYR B 187
SITE 2 AC1 5 PHE B 234
SITE 1 AC2 4 GLU C 49 VAL C 54 LEU C 74 ARG C 156
SITE 1 AC3 8 VAL D 54 ALA D 70 THR D 77 ARG D 156
SITE 2 AC3 8 TYR D 187 ASN D 230 PHE D 234 HOH D 404
CRYST1 77.363 83.920 138.297 90.00 90.00 90.00 P 21 21 21 16
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 0.012926 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011916 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007231 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
