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HEADER HYDROLASE 12-APR-22 7UOC
TITLE CRYSTAL STRUCTURE OF OROBANCHE MINOR KAI2D4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KAI2D4;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OROBANCHE MINOR;
SOURCE 3 ORGANISM_TAXID: 36748;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS STRIGOLACTONE RECEPTOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BURGER,J.CHORY
REVDAT 1 19-APR-23 7UOC 0
JRNL AUTH M.BURGER
JRNL TITL CRYSTAL STRUCTURE OF OROBANCHE MINOR KAI2D4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20_4459
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 32311
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.220
REMARK 3 FREE R VALUE TEST SET COUNT : 1688
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 48.7200 - 5.2600 1.00 2761 156 0.1800 0.2322
REMARK 3 2 5.2600 - 4.1800 1.00 2617 131 0.1344 0.1834
REMARK 3 3 4.1800 - 3.6500 1.00 2580 143 0.1432 0.1829
REMARK 3 4 3.6500 - 3.3200 1.00 2544 146 0.1525 0.1987
REMARK 3 5 3.3200 - 3.0800 1.00 2535 139 0.1817 0.2364
REMARK 3 6 3.0800 - 2.9000 1.00 2527 144 0.1972 0.2080
REMARK 3 7 2.9000 - 2.7500 1.00 2528 137 0.1956 0.2867
REMARK 3 8 2.7500 - 2.6300 1.00 2506 139 0.2031 0.2769
REMARK 3 9 2.6300 - 2.5300 1.00 2516 145 0.2048 0.3219
REMARK 3 10 2.5300 - 2.4400 1.00 2502 131 0.2172 0.3044
REMARK 3 11 2.4400 - 2.3700 1.00 2497 143 0.2064 0.2600
REMARK 3 12 2.3700 - 2.3000 1.00 2510 134 0.2167 0.2877
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.263
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.95
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 : 0.004 4358
REMARK 3 ANGLE : 0.645 5936
REMARK 3 CHIRALITY : 0.047 666
REMARK 3 PLANARITY : 0.006 762
REMARK 3 DIHEDRAL : 11.377 1600
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 7UOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1000264553.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-20
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 : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32317
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 48.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 20.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: 4JYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5, 0.8 M DI
REMARK 280 -AMMONIUM PHOSPHATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 73.83400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.72400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.72400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 110.75100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.72400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.72400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.91700
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.72400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.72400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 110.75100
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.72400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.72400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.91700
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 73.83400
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 GLY A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 ALA A 272
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 SER B 3
REMARK 465 MET B 167
REMARK 465 ASP B 168
REMARK 465 ASP B 271
REMARK 465 ALA B 272
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 TYR B 245 CG CD1 CD2 CE1 CE2 CZ OH
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 NH1 ARG A 124 O HOH A 401 2.14
REMARK 500 O HOH A 488 O HOH A 589 2.15
REMARK 500 O HOH B 407 O HOH B 530 2.17
REMARK 500 O HOH A 484 O HOH A 554 2.18
REMARK 500 O HOH B 514 O HOH B 578 2.19
REMARK 500 O HOH A 442 O HOH A 589 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 SER A 96 -111.89 55.98
REMARK 500 ARG A 124 127.09 -174.51
REMARK 500 PRO A 219 0.35 -69.32
REMARK 500 SER B 96 -112.23 55.59
REMARK 500 ARG B 124 122.71 -170.69
REMARK 500 ASN B 150 73.72 -118.70
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7UOC A 1 272 UNP A0A2U8XQU6_OROMI
DBREF2 7UOC A A0A2U8XQU6 1 272
DBREF1 7UOC B 1 272 UNP A0A2U8XQU6_OROMI
DBREF2 7UOC B A0A2U8XQU6 1 272
SEQADV 7UOC GLY A -1 UNP A0A2U8XQU EXPRESSION TAG
SEQADV 7UOC PRO A 0 UNP A0A2U8XQU EXPRESSION TAG
SEQADV 7UOC GLY B -1 UNP A0A2U8XQU EXPRESSION TAG
SEQADV 7UOC PRO B 0 UNP A0A2U8XQU EXPRESSION TAG
SEQRES 1 A 274 GLY PRO MET ASN SER LYS VAL GLY SER ALA HIS ASN VAL
SEQRES 2 A 274 ARG VAL LEU GLY SER GLY GLY THR THR VAL VAL LEU GLY
SEQRES 3 A 274 HIS GLY PHE GLY CYS GLU GLN SER VAL TRP ARG HIS LEU
SEQRES 4 A 274 VAL PRO HIS LEU VAL ASP GLU TYR ARG VAL LEU LEU TYR
SEQRES 5 A 274 ASP VAL MET GLY ALA GLY SER THR ASN PRO ASP TYR TYR
SEQRES 6 A 274 ASP PHE VAL ARG TYR SER THR LEU GLU GLY HIS ALA HIS
SEQRES 7 A 274 ASP LEU LEU ALA ILE LEU GLU GLU PHE THR ILE GLY LYS
SEQRES 8 A 274 CYS ILE PHE VAL GLY HIS SER LEU SER SER MET VAL GLY
SEQRES 9 A 274 ALA MET ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS
SEQRES 10 A 274 LEU VAL MET ILE SER ALA SER PRO ARG VAL LEU ASN SER
SEQRES 11 A 274 PRO GLY TYR HIS GLY GLY LEU ASP GLN LYS ASP LEU ASP
SEQRES 12 A 274 GLN PHE LEU VAL ALA MET GLU THR ASN TYR LYS SER PHE
SEQRES 13 A 274 LEU SER GLY MET ALA PRO LEU VAL ILE GLY CYS ASP MET
SEQRES 14 A 274 ASP SER PRO ALA PHE GLN GLU TYR SER ARG THR LEU PHE
SEQRES 15 A 274 ASN MET ARG PRO ASP ILE SER LEU SER MET ALA ARG THR
SEQRES 16 A 274 ILE ASN THR TYR ASP MET ARG PRO PHE LEU GLY HIS VAL
SEQRES 17 A 274 THR VAL PRO CYS HIS ILE ILE TYR SER ARG GLU ASP PRO
SEQRES 18 A 274 ILE VAL PRO VAL LYS LEU ALA GLU TYR LEU HIS GLN ASN
SEQRES 19 A 274 LEU GLY GLY LYS SER ILE VAL GLU GLY MET SER THR TYR
SEQRES 20 A 274 GLY HIS LEU PRO HIS LEU SER ALA PRO GLU VAL THR ILE
SEQRES 21 A 274 PRO VAL LEU LEU ARG HIS ILE ARG GLN ASP ILE VAL ASP
SEQRES 22 A 274 ALA
SEQRES 1 B 274 GLY PRO MET ASN SER LYS VAL GLY SER ALA HIS ASN VAL
SEQRES 2 B 274 ARG VAL LEU GLY SER GLY GLY THR THR VAL VAL LEU GLY
SEQRES 3 B 274 HIS GLY PHE GLY CYS GLU GLN SER VAL TRP ARG HIS LEU
SEQRES 4 B 274 VAL PRO HIS LEU VAL ASP GLU TYR ARG VAL LEU LEU TYR
SEQRES 5 B 274 ASP VAL MET GLY ALA GLY SER THR ASN PRO ASP TYR TYR
SEQRES 6 B 274 ASP PHE VAL ARG TYR SER THR LEU GLU GLY HIS ALA HIS
SEQRES 7 B 274 ASP LEU LEU ALA ILE LEU GLU GLU PHE THR ILE GLY LYS
SEQRES 8 B 274 CYS ILE PHE VAL GLY HIS SER LEU SER SER MET VAL GLY
SEQRES 9 B 274 ALA MET ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS
SEQRES 10 B 274 LEU VAL MET ILE SER ALA SER PRO ARG VAL LEU ASN SER
SEQRES 11 B 274 PRO GLY TYR HIS GLY GLY LEU ASP GLN LYS ASP LEU ASP
SEQRES 12 B 274 GLN PHE LEU VAL ALA MET GLU THR ASN TYR LYS SER PHE
SEQRES 13 B 274 LEU SER GLY MET ALA PRO LEU VAL ILE GLY CYS ASP MET
SEQRES 14 B 274 ASP SER PRO ALA PHE GLN GLU TYR SER ARG THR LEU PHE
SEQRES 15 B 274 ASN MET ARG PRO ASP ILE SER LEU SER MET ALA ARG THR
SEQRES 16 B 274 ILE ASN THR TYR ASP MET ARG PRO PHE LEU GLY HIS VAL
SEQRES 17 B 274 THR VAL PRO CYS HIS ILE ILE TYR SER ARG GLU ASP PRO
SEQRES 18 B 274 ILE VAL PRO VAL LYS LEU ALA GLU TYR LEU HIS GLN ASN
SEQRES 19 B 274 LEU GLY GLY LYS SER ILE VAL GLU GLY MET SER THR TYR
SEQRES 20 B 274 GLY HIS LEU PRO HIS LEU SER ALA PRO GLU VAL THR ILE
SEQRES 21 B 274 PRO VAL LEU LEU ARG HIS ILE ARG GLN ASP ILE VAL ASP
SEQRES 22 B 274 ALA
HET CL A 301 1
HET CL B 301 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *407(H2 O)
HELIX 1 AA1 SER A 3 HIS A 9 1 7
HELIX 2 AA2 GLU A 30 ARG A 35 5 6
HELIX 3 AA3 LEU A 37 LEU A 41 5 5
HELIX 4 AA4 ASN A 59 TYR A 63 5 5
HELIX 5 AA5 VAL A 66 SER A 69 5 4
HELIX 6 AA6 THR A 70 THR A 86 1 17
HELIX 7 AA7 SER A 96 ARG A 109 1 14
HELIX 8 AA8 ASP A 136 ASN A 150 1 15
HELIX 9 AA9 ASN A 150 GLY A 164 1 15
HELIX 10 AB1 SER A 169 MET A 182 1 14
HELIX 11 AB2 ARG A 183 ASN A 195 1 13
HELIX 12 AB3 MET A 199 VAL A 206 5 8
HELIX 13 AB4 PRO A 222 LEU A 233 1 12
HELIX 14 AB5 LEU A 248 ALA A 253 1 6
HELIX 15 AB6 ALA A 253 GLN A 267 1 15
HELIX 16 AB7 VAL B 5 HIS B 9 1 5
HELIX 17 AB8 GLU B 30 ARG B 35 5 6
HELIX 18 AB9 LEU B 37 LEU B 41 5 5
HELIX 19 AC1 ASN B 59 TYR B 63 5 5
HELIX 20 AC2 VAL B 66 SER B 69 5 4
HELIX 21 AC3 THR B 70 THR B 86 1 17
HELIX 22 AC4 SER B 96 ARG B 109 1 14
HELIX 23 AC5 ASP B 136 ASN B 150 1 15
HELIX 24 AC6 ASN B 150 GLY B 164 1 15
HELIX 25 AC7 SER B 169 ALA B 171 5 3
HELIX 26 AC8 PHE B 172 PHE B 180 1 9
HELIX 27 AC9 ARG B 183 ASN B 195 1 13
HELIX 28 AD1 MET B 199 VAL B 206 5 8
HELIX 29 AD2 VAL B 223 LEU B 233 1 11
HELIX 30 AD3 LEU B 248 ALA B 253 1 6
HELIX 31 AD4 ALA B 253 GLN B 267 1 15
SHEET 1 AA1 7 ARG A 12 GLY A 15 0
SHEET 2 AA1 7 ARG A 46 LEU A 49 -1 O LEU A 49 N ARG A 12
SHEET 3 AA1 7 THR A 20 GLY A 24 1 N VAL A 21 O ARG A 46
SHEET 4 AA1 7 CYS A 90 HIS A 95 1 O VAL A 93 N VAL A 22
SHEET 5 AA1 7 PHE A 113 ILE A 119 1 O HIS A 114 N CYS A 90
SHEET 6 AA1 7 CYS A 210 GLU A 217 1 O HIS A 211 N LEU A 116
SHEET 7 AA1 7 SER A 237 TYR A 245 1 O ILE A 238 N ILE A 212
SHEET 1 AA2 7 ARG B 12 GLY B 15 0
SHEET 2 AA2 7 ARG B 46 LEU B 49 -1 O VAL B 47 N LEU B 14
SHEET 3 AA2 7 THR B 20 GLY B 24 1 N VAL B 21 O ARG B 46
SHEET 4 AA2 7 CYS B 90 HIS B 95 1 O VAL B 93 N VAL B 22
SHEET 5 AA2 7 PHE B 113 ILE B 119 1 O HIS B 114 N CYS B 90
SHEET 6 AA2 7 CYS B 210 GLU B 217 1 O HIS B 211 N LEU B 116
SHEET 7 AA2 7 SER B 237 TYR B 245 1 O ILE B 238 N ILE B 212
CRYST1 97.448 97.448 147.668 90.00 90.00 90.00 P 43 21 2 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 0.010262 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010262 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006772 0.00000
TER 2128 ASP A 271
TER 4226 VAL B 270
MASTER 284 0 2 31 14 0 0 6 4570 2 0 44
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