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HEADER CELL CYCLE 15-MAY-24 9FCR
TITLE CRYSTAL STRUCTURE OF RBBP9 WITH SPACEGROUP P212121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE HYDROLASE RBBP9;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: B5T-OVEREXPRESSED GENE PROTEIN,PROTEIN BOG,RETINOBLASTOMA-
COMPND 5 BINDING PROTEIN 10,RBBP-10,RETINOBLASTOMA-BINDING PROTEIN 9,RBBP-9;
COMPND 6 EC: 3.-.-.-;
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: RBBP9, BOG, RBBP10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS REGULATION OF CELL PROLIFERATION AND DIFFERENTIATION, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.GORREC,D.BELLINI
REVDAT 1 11-SEP-24 9FCR 0
JRNL AUTH F.GORREC,D.BELLINI
JRNL TITL CRYSTAL STRUCTURE OF RBBP9 WITH SPACEGROUP P212121
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 62575
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 3077
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 44.3800 - 3.8400 0.99 3213 165 0.1559 0.1836
REMARK 3 2 3.8400 - 3.0500 1.00 3077 154 0.1619 0.1976
REMARK 3 3 3.0500 - 2.6600 1.00 3068 154 0.1861 0.2255
REMARK 3 4 2.6600 - 2.4200 1.00 3019 177 0.1953 0.2228
REMARK 3 5 2.4200 - 2.2500 1.00 3032 152 0.1994 0.1980
REMARK 3 6 2.2400 - 2.1100 1.00 3028 146 0.1930 0.2699
REMARK 3 7 2.1100 - 2.0100 1.00 3051 141 0.2039 0.2220
REMARK 3 8 2.0100 - 1.9200 1.00 3009 157 0.2138 0.2414
REMARK 3 9 1.9200 - 1.8500 1.00 2982 162 0.2357 0.2502
REMARK 3 10 1.8500 - 1.7800 1.00 3008 142 0.2290 0.2754
REMARK 3 11 1.7800 - 1.7300 1.00 3034 131 0.2360 0.2952
REMARK 3 12 1.7300 - 1.6800 1.00 2998 152 0.2440 0.2858
REMARK 3 13 1.6800 - 1.6300 1.00 3005 142 0.2543 0.2838
REMARK 3 14 1.6300 - 1.5900 0.99 2964 152 0.2642 0.3182
REMARK 3 15 1.5900 - 1.5600 0.99 2974 158 0.2722 0.2730
REMARK 3 16 1.5600 - 1.5200 0.97 2865 159 0.2990 0.3410
REMARK 3 17 1.5200 - 1.4900 0.91 2734 159 0.3301 0.3591
REMARK 3 18 1.4900 - 1.4600 0.84 2481 131 0.3746 0.3763
REMARK 3 19 1.4600 - 1.4400 0.73 2177 120 0.4018 0.3849
REMARK 3 20 1.4400 - 1.4100 0.62 1840 105 0.4230 0.4130
REMARK 3 21 1.4100 - 1.3900 0.38 1124 63 0.4586 0.4223
REMARK 3 22 1.3900 - 1.3700 0.28 815 55 0.4992 0.5030
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) : 0.205
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.309
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.39
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 : 0.006 3007
REMARK 3 ANGLE : 0.817 4087
REMARK 3 CHIRALITY : 0.075 438
REMARK 3 PLANARITY : 0.006 521
REMARK 3 DIHEDRAL : 10.726 388
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 9FCR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1292138672.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-24
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 : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65671
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 44.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.95000
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350/PEG 1K/MPD (1:1:1) 37.5%, 0.1
REMARK 280 M MES/IMIDAZOLE PH 6.5, 4MM MORPHEUS II ALKALIS, 2.5% (W/V)
REMARK 280 MORPHEUS FUSION CRYOPOLYOLS, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
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 33.87000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.37000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.27500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.37000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.87000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.27500
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
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 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 ALA A 2
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 PRO B 185
REMARK 465 ALA B 186
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 372 O HOH A 378 1.83
REMARK 500 O HOH A 276 O HOH A 366 1.93
REMARK 500 O HOH A 214 O HOH A 348 1.93
REMARK 500 O HOH B 318 O HOH B 340 1.98
REMARK 500 O HOH A 204 O HOH A 378 2.00
REMARK 500 O HOH A 338 O HOH A 391 2.01
REMARK 500 OE1 GLU B 32 O HOH B 201 2.01
REMARK 500 N SER A 3 O HOH A 201 2.03
REMARK 500 O HOH B 202 O HOH B 316 2.08
REMARK 500 O HOH A 379 O HOH A 388 2.08
REMARK 500 O HOH A 217 O HOH A 315 2.13
REMARK 500 O HOH B 280 O HOH B 333 2.16
REMARK 500 O HOH A 279 O HOH A 360 2.16
REMARK 500 O HOH A 324 O HOH B 212 2.16
REMARK 500 OE1 GLU A 106 O HOH A 202 2.18
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 312 O HOH A 316 4445 1.83
REMARK 500 O HOH A 368 O HOH B 231 4545 1.84
REMARK 500 O HOH A 204 O HOH B 278 4555 2.01
REMARK 500 O HOH A 373 O HOH B 261 4555 2.03
REMARK 500 O HOH A 249 O HOH B 361 4545 2.06
REMARK 500 O HOH A 372 O HOH B 298 4555 2.15
REMARK 500 O HOH A 272 O HOH B 222 3544 2.16
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 B 152 NE - CZ - NH2 ANGL. DEV. = 3.1 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 SER A 75 -115.83 58.06
REMARK 500 SER A 97 61.81 63.11
REMARK 500 LEU A 103 16.25 59.91
REMARK 500 ASP A 162 21.44 -141.18
REMARK 500 PHE A 171 69.45 -154.85
REMARK 500 SER B 75 -113.64 57.38
REMARK 500 SER B 97 65.99 66.24
REMARK 500 ASP B 162 21.37 -142.28
REMARK 500 PHE B 171 66.41 -156.52
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9FCR A 1 186 UNP O75884 RBBP9_HUMAN 1 186
DBREF 9FCR B 1 186 UNP O75884 RBBP9_HUMAN 1 186
SEQRES 1 A 186 MET ALA SER PRO SER LYS ALA VAL ILE VAL PRO GLY ASN
SEQRES 2 A 186 GLY GLY GLY ASP VAL THR THR HIS GLY TRP TYR GLY TRP
SEQRES 3 A 186 VAL LYS LYS GLU LEU GLU LYS ILE PRO GLY PHE GLN CYS
SEQRES 4 A 186 LEU ALA LYS ASN MET PRO ASP PRO ILE THR ALA ARG GLU
SEQRES 5 A 186 SER ILE TRP LEU PRO PHE MET GLU THR GLU LEU HIS CYS
SEQRES 6 A 186 ASP GLU LYS THR ILE ILE ILE GLY HIS SER SER GLY ALA
SEQRES 7 A 186 ILE ALA ALA MET ARG TYR ALA GLU THR HIS ARG VAL TYR
SEQRES 8 A 186 ALA ILE VAL LEU VAL SER ALA TYR THR SER ASP LEU GLY
SEQRES 9 A 186 ASP GLU ASN GLU ARG ALA SER GLY TYR PHE THR ARG PRO
SEQRES 10 A 186 TRP GLN TRP GLU LYS ILE LYS ALA ASN CYS PRO TYR ILE
SEQRES 11 A 186 VAL GLN PHE GLY SER THR ASP ASP PRO PHE LEU PRO TRP
SEQRES 12 A 186 LYS GLU GLN GLN GLU VAL ALA ASP ARG LEU GLU THR LYS
SEQRES 13 A 186 LEU HIS LYS PHE THR ASP CYS GLY HIS PHE GLN ASN THR
SEQRES 14 A 186 GLU PHE HIS GLU LEU ILE THR VAL VAL LYS SER LEU LEU
SEQRES 15 A 186 LYS VAL PRO ALA
SEQRES 1 B 186 MET ALA SER PRO SER LYS ALA VAL ILE VAL PRO GLY ASN
SEQRES 2 B 186 GLY GLY GLY ASP VAL THR THR HIS GLY TRP TYR GLY TRP
SEQRES 3 B 186 VAL LYS LYS GLU LEU GLU LYS ILE PRO GLY PHE GLN CYS
SEQRES 4 B 186 LEU ALA LYS ASN MET PRO ASP PRO ILE THR ALA ARG GLU
SEQRES 5 B 186 SER ILE TRP LEU PRO PHE MET GLU THR GLU LEU HIS CYS
SEQRES 6 B 186 ASP GLU LYS THR ILE ILE ILE GLY HIS SER SER GLY ALA
SEQRES 7 B 186 ILE ALA ALA MET ARG TYR ALA GLU THR HIS ARG VAL TYR
SEQRES 8 B 186 ALA ILE VAL LEU VAL SER ALA TYR THR SER ASP LEU GLY
SEQRES 9 B 186 ASP GLU ASN GLU ARG ALA SER GLY TYR PHE THR ARG PRO
SEQRES 10 B 186 TRP GLN TRP GLU LYS ILE LYS ALA ASN CYS PRO TYR ILE
SEQRES 11 B 186 VAL GLN PHE GLY SER THR ASP ASP PRO PHE LEU PRO TRP
SEQRES 12 B 186 LYS GLU GLN GLN GLU VAL ALA ASP ARG LEU GLU THR LYS
SEQRES 13 B 186 LEU HIS LYS PHE THR ASP CYS GLY HIS PHE GLN ASN THR
SEQRES 14 B 186 GLU PHE HIS GLU LEU ILE THR VAL VAL LYS SER LEU LEU
SEQRES 15 B 186 LYS VAL PRO ALA
FORMUL 3 HOH *385(H2 O)
HELIX 1 AA1 TRP A 23 GLU A 32 1 10
HELIX 2 AA2 ARG A 51 GLU A 62 1 12
HELIX 3 AA3 SER A 75 ALA A 85 1 11
HELIX 4 AA4 ASP A 105 SER A 111 1 7
HELIX 5 AA5 GLN A 119 CYS A 127 1 9
HELIX 6 AA6 PRO A 142 GLU A 154 1 13
HELIX 7 AA7 PHE A 171 LYS A 183 1 13
HELIX 8 AA8 TRP B 23 GLU B 32 1 10
HELIX 9 AA9 ARG B 51 GLU B 62 1 12
HELIX 10 AB1 SER B 75 HIS B 88 1 14
HELIX 11 AB2 ASP B 105 GLY B 112 1 8
HELIX 12 AB3 GLN B 119 CYS B 127 1 9
HELIX 13 AB4 PRO B 142 GLU B 154 1 13
HELIX 14 AB5 PHE B 171 LYS B 183 1 13
SHEET 1 AA1 6 GLN A 38 ALA A 41 0
SHEET 2 AA1 6 LYS A 6 VAL A 10 1 N ALA A 7 O LEU A 40
SHEET 3 AA1 6 THR A 69 HIS A 74 1 O ILE A 72 N VAL A 8
SHEET 4 AA1 6 ALA A 92 VAL A 96 1 O VAL A 94 N ILE A 71
SHEET 5 AA1 6 ILE A 130 SER A 135 1 O VAL A 131 N LEU A 95
SHEET 6 AA1 6 LYS A 156 PHE A 160 1 O HIS A 158 N GLN A 132
SHEET 1 AA2 6 GLN B 38 ALA B 41 0
SHEET 2 AA2 6 LYS B 6 VAL B 10 1 N ILE B 9 O LEU B 40
SHEET 3 AA2 6 THR B 69 HIS B 74 1 O ILE B 72 N VAL B 8
SHEET 4 AA2 6 ALA B 92 VAL B 96 1 O VAL B 94 N ILE B 71
SHEET 5 AA2 6 TYR B 129 SER B 135 1 O VAL B 131 N LEU B 95
SHEET 6 AA2 6 LYS B 156 PHE B 160 1 O PHE B 160 N GLY B 134
CRYST1 67.740 82.550 58.740 90.00 90.00 90.00 P 21 21 21 8
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 0.014762 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012114 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017024 0.00000
TER 1468 ALA A 186
TER 2924 VAL B 184
MASTER 324 0 0 14 12 0 0 6 3307 2 0 30
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