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HEADER HYDROLASE 04-MAY-21 7OEX
TITLE CRYSTAL STRUCTURE OF RBBP9 IN COMPLEX WITH PHENYLALANINE
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 HYDROLASE, RETINOBLASTOMA-BINDING PROTEIN 9
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FIEDLER,S.TANG,J.W.CHIN
REVDAT 1 22-DEC-21 7OEX 0
JRNL AUTH S.TANG,M.FIEDLER,J.W.CHIN
JRNL TITL CRYSTAL STRUCTURE OF RBBP9 IN COMPLEX WITH PHENYLALANINE:
JRNL TITL 2 AMINOPEPTIDASE ACTIVITY WITH PREFERENCE FOR AROMATIC
JRNL TITL 3 RESIDUES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 47250
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2383
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.51
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2829
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 154
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3006
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 292
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.688
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3121 ; 0.011 ; 0.018
REMARK 3 BOND LENGTHS OTHERS (A): 2852 ; 0.001 ; 0.019
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4241 ; 1.433 ; 1.842
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6605 ; 1.163 ; 2.735
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 374 ; 5.923 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 156 ;35.257 ;23.013
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 509 ;10.442 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.363 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 451 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3492 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 704 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7OEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAY-21.
REMARK 100 THE DEPOSITION ID IS D_1292114603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-20
REMARK 200 TEMPERATURE (KELVIN) : 130
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49673
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 29.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.66900
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: 2QS9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/V PEG 4K, 0.1 M MES SODIUM SALT
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 65.06350
REMARK 290 SMTRY3 2 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 HIS A 194
REMARK 465 MET B 1
REMARK 465 ALA B 186
REMARK 465 LEU B 187
REMARK 465 GLU B 188
REMARK 465 HIS B 189
REMARK 465 HIS B 190
REMARK 465 HIS B 191
REMARK 465 HIS B 192
REMARK 465 HIS B 193
REMARK 465 HIS B 194
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 OG1 THR A 20 O HOH A 301 2.17
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 MET B 82 CG - SD - CE ANGL. DEV. = -11.6 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 -114.69 57.31
REMARK 500 ASP A 162 20.48 -140.13
REMARK 500 PHE A 171 71.09 -154.30
REMARK 500 VAL A 184 69.33 61.33
REMARK 500 SER B 75 -115.67 61.64
REMARK 500 SER B 97 62.37 64.49
REMARK 500 ASP B 162 20.09 -140.31
REMARK 500 PHE B 171 71.83 -159.37
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 PHE A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHE B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QS9 RELATED DB: PDB
REMARK 900 RBBP9 WITHOUT LIGAND
DBREF 7OEX A 1 186 UNP O75884 RBBP9_HUMAN 1 186
DBREF 7OEX B 1 186 UNP O75884 RBBP9_HUMAN 1 186
SEQADV 7OEX LEU A 187 UNP O75884 EXPRESSION TAG
SEQADV 7OEX GLU A 188 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS A 189 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS A 190 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS A 191 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS A 192 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS A 193 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS A 194 UNP O75884 EXPRESSION TAG
SEQADV 7OEX LEU B 187 UNP O75884 EXPRESSION TAG
SEQADV 7OEX GLU B 188 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS B 189 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS B 190 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS B 191 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS B 192 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS B 193 UNP O75884 EXPRESSION TAG
SEQADV 7OEX HIS B 194 UNP O75884 EXPRESSION TAG
SEQRES 1 A 194 MET ALA SER PRO SER LYS ALA VAL ILE VAL PRO GLY ASN
SEQRES 2 A 194 GLY GLY GLY ASP VAL THR THR HIS GLY TRP TYR GLY TRP
SEQRES 3 A 194 VAL LYS LYS GLU LEU GLU LYS ILE PRO GLY PHE GLN CYS
SEQRES 4 A 194 LEU ALA LYS ASN MET PRO ASP PRO ILE THR ALA ARG GLU
SEQRES 5 A 194 SER ILE TRP LEU PRO PHE MET GLU THR GLU LEU HIS CYS
SEQRES 6 A 194 ASP GLU LYS THR ILE ILE ILE GLY HIS SER SER GLY ALA
SEQRES 7 A 194 ILE ALA ALA MET ARG TYR ALA GLU THR HIS ARG VAL TYR
SEQRES 8 A 194 ALA ILE VAL LEU VAL SER ALA TYR THR SER ASP LEU GLY
SEQRES 9 A 194 ASP GLU ASN GLU ARG ALA SER GLY TYR PHE THR ARG PRO
SEQRES 10 A 194 TRP GLN TRP GLU LYS ILE LYS ALA ASN CYS PRO TYR ILE
SEQRES 11 A 194 VAL GLN PHE GLY SER THR ASP ASP PRO PHE LEU PRO TRP
SEQRES 12 A 194 LYS GLU GLN GLN GLU VAL ALA ASP ARG LEU GLU THR LYS
SEQRES 13 A 194 LEU HIS LYS PHE THR ASP CYS GLY HIS PHE GLN ASN THR
SEQRES 14 A 194 GLU PHE HIS GLU LEU ILE THR VAL VAL LYS SER LEU LEU
SEQRES 15 A 194 LYS VAL PRO ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 194 MET ALA SER PRO SER LYS ALA VAL ILE VAL PRO GLY ASN
SEQRES 2 B 194 GLY GLY GLY ASP VAL THR THR HIS GLY TRP TYR GLY TRP
SEQRES 3 B 194 VAL LYS LYS GLU LEU GLU LYS ILE PRO GLY PHE GLN CYS
SEQRES 4 B 194 LEU ALA LYS ASN MET PRO ASP PRO ILE THR ALA ARG GLU
SEQRES 5 B 194 SER ILE TRP LEU PRO PHE MET GLU THR GLU LEU HIS CYS
SEQRES 6 B 194 ASP GLU LYS THR ILE ILE ILE GLY HIS SER SER GLY ALA
SEQRES 7 B 194 ILE ALA ALA MET ARG TYR ALA GLU THR HIS ARG VAL TYR
SEQRES 8 B 194 ALA ILE VAL LEU VAL SER ALA TYR THR SER ASP LEU GLY
SEQRES 9 B 194 ASP GLU ASN GLU ARG ALA SER GLY TYR PHE THR ARG PRO
SEQRES 10 B 194 TRP GLN TRP GLU LYS ILE LYS ALA ASN CYS PRO TYR ILE
SEQRES 11 B 194 VAL GLN PHE GLY SER THR ASP ASP PRO PHE LEU PRO TRP
SEQRES 12 B 194 LYS GLU GLN GLN GLU VAL ALA ASP ARG LEU GLU THR LYS
SEQRES 13 B 194 LEU HIS LYS PHE THR ASP CYS GLY HIS PHE GLN ASN THR
SEQRES 14 B 194 GLU PHE HIS GLU LEU ILE THR VAL VAL LYS SER LEU LEU
SEQRES 15 B 194 LYS VAL PRO ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET PHE A 201 12
HET PHE B 201 12
HETNAM PHE PHENYLALANINE
FORMUL 3 PHE 2(C9 H11 N O2)
FORMUL 5 HOH *292(H2 O)
HELIX 1 AA1 TRP A 23 LYS A 33 1 11
HELIX 2 AA2 ARG A 51 GLU A 62 1 12
HELIX 3 AA3 SER A 75 HIS A 88 1 14
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 LEU A 182 1 12
HELIX 8 AA8 TRP B 23 LYS B 33 1 11
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 SER B 111 1 7
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 ILE A 9 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 96 N GLY A 73
SHEET 5 AA1 6 TYR A 129 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 96 N GLY B 73
SHEET 5 AA2 6 TYR B 129 SER B 135 1 O PHE B 133 N LEU B 95
SHEET 6 AA2 6 LYS B 156 PHE B 160 1 O HIS B 158 N GLN B 132
SITE 1 AC1 8 GLY A 12 ASN A 13 SER A 75 SER A 76
SITE 2 AC1 8 TYR A 99 GLU A 108 PHE A 140 HIS A 165
SITE 1 AC2 8 GLY B 12 ASN B 13 SER B 75 SER B 76
SITE 2 AC2 8 TYR B 99 GLU B 108 HIS B 165 HOH B 328
CRYST1 36.956 130.127 38.993 90.00 115.24 90.00 P 1 21 1 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 0.027059 0.000000 0.012756 0.00000
SCALE2 0.000000 0.007685 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028352 0.00000
TER 1540 HIS A 193
TER 3008 PRO B 185
MASTER 319 0 2 14 12 0 4 6 3322 2 0 30
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