| 5y7h-pdb | HEADER HYDROLASE 17-AUG-17 5Y7H
TITLE CRYSTAL STRUCTURE OF HUMAN DPP4 IN COMPLEX WITH INHIBITOR3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADABP,ADENOSINE DEAMINASE COMPLEXING PROTEIN 2,ADCP-2,
COMPND 5 DIPEPTIDYL PEPTIDASE IV,DPP IV,T-CELL ACTIVATION ANTIGEN CD26,TP103;
COMPND 6 EC: 3.4.14.5;
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: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS DPP4, INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.K.LEE,E.E.KIM
REVDAT 1 20-MAR-19 5Y7H 0
JRNL AUTH H.K.LEE,E.E.KIM
JRNL TITL CRYSTAL STRUCTURE OF HUMAN DPP4 IN COMPLEX WITH INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.560
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 32658
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1650
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 46.1779 - 6.8617 0.98 2828 172 0.2169 0.2653
REMARK 3 2 6.8617 - 5.4491 0.98 2782 150 0.2028 0.2256
REMARK 3 3 5.4491 - 4.7611 0.97 2762 143 0.1583 0.1805
REMARK 3 4 4.7611 - 4.3262 0.97 2739 136 0.1504 0.1928
REMARK 3 5 4.3262 - 4.0163 0.95 2662 146 0.1658 0.2082
REMARK 3 6 4.0163 - 3.7796 0.92 2603 133 0.1881 0.2419
REMARK 3 7 3.7796 - 3.5904 0.92 2621 148 0.2012 0.2552
REMARK 3 8 3.5904 - 3.4342 0.91 2571 132 0.2065 0.2625
REMARK 3 9 3.4342 - 3.3020 0.90 2537 146 0.2326 0.2712
REMARK 3 10 3.3020 - 3.1881 0.89 2510 130 0.2477 0.3077
REMARK 3 11 3.1881 - 3.0884 0.82 2312 117 0.2551 0.3261
REMARK 3 12 3.0884 - 3.0001 0.73 2081 97 0.2861 0.3572
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.920
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 : 0.001 12357
REMARK 3 ANGLE : 0.417 16818
REMARK 3 CHIRALITY : 0.040 1760
REMARK 3 PLANARITY : 0.002 2135
REMARK 3 DIHEDRAL : 17.707 7170
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 5Y7H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004806.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-07
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 : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35739
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
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 (%) : 91.5
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.190
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1X70
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20~28% (W/V) POLYETHYLENE GLYCOL 4000,
REMARK 280 0.1M HEPES OR TRIS PH 7.5~8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 63.21000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 SER A 39
REMARK 465 ARG A 40
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 B 40 O HOH B 901 2.17
REMARK 500 O HOH A 946 O HOH A 956 2.18
REMARK 500 OD2 ASP B 133 NH1 ARG B 147 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 HIS A 66 14.92 -145.71
REMARK 500 GLU A 73 -116.02 52.20
REMARK 500 GLU A 97 39.08 -94.14
REMARK 500 HIS A 100 -157.54 -129.64
REMARK 500 SER A 106 90.68 -160.97
REMARK 500 GLN A 123 -90.10 -118.07
REMARK 500 TRP A 124 -156.96 -101.97
REMARK 500 HIS A 162 11.16 -140.38
REMARK 500 ILE A 193 -63.52 -139.67
REMARK 500 ASP A 200 -165.86 -74.28
REMARK 500 VAL A 207 -80.59 -125.33
REMARK 500 ALA A 210 148.96 -172.10
REMARK 500 THR A 221 -69.16 -143.07
REMARK 500 SER A 242 -155.16 61.41
REMARK 500 PRO A 255 99.32 -61.37
REMARK 500 SER A 275 16.00 -145.78
REMARK 500 VAL A 279 -68.92 -90.38
REMARK 500 SER A 333 -72.70 -78.80
REMARK 500 HIS A 345 86.82 -153.23
REMARK 500 ARG A 356 -70.47 -66.66
REMARK 500 ASN A 377 -163.18 -74.56
REMARK 500 LYS A 392 22.29 -78.09
REMARK 500 ASN A 420 30.02 -89.70
REMARK 500 TYR A 439 20.62 -73.27
REMARK 500 THR A 557 32.09 -92.95
REMARK 500 THR A 600 -83.72 -127.79
REMARK 500 ASP A 620 95.55 -67.92
REMARK 500 SER A 630 -123.63 59.70
REMARK 500 ASP A 678 -89.76 -113.22
REMARK 500 ASN A 679 27.95 -142.17
REMARK 500 SER A 690 5.29 -67.24
REMARK 500 ASN A 710 -71.49 -89.44
REMARK 500 MET A 733 111.80 -169.11
REMARK 500 LEU B 57 -163.84 -125.80
REMARK 500 TYR B 58 61.87 -155.80
REMARK 500 SER B 64 -167.25 -161.07
REMARK 500 GLN B 72 -80.37 -94.22
REMARK 500 ASN B 74 -0.50 73.26
REMARK 500 SER B 87 -156.42 -107.25
REMARK 500 SER B 93 45.12 -96.97
REMARK 500 SER B 101 95.97 -69.05
REMARK 500 SER B 106 98.24 -165.79
REMARK 500 GLN B 123 -89.22 -115.89
REMARK 500 TRP B 124 -155.64 -101.58
REMARK 500 TYR B 128 166.34 179.80
REMARK 500 THR B 156 141.72 -174.07
REMARK 500 HIS B 162 32.13 -147.99
REMARK 500 ILE B 193 -62.24 -137.07
REMARK 500 ASP B 200 -168.21 -75.50
REMARK 500 VAL B 207 -85.91 -104.01
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 957 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A 958 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH A 959 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A 960 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH A 961 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH A 962 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH A 963 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH A 964 DISTANCE = 7.86 ANGSTROMS
REMARK 525 HOH A 965 DISTANCE = 7.86 ANGSTROMS
REMARK 525 HOH A 966 DISTANCE = 7.96 ANGSTROMS
REMARK 525 HOH A 967 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH A 968 DISTANCE = 8.17 ANGSTROMS
REMARK 525 HOH A 969 DISTANCE = 8.22 ANGSTROMS
REMARK 525 HOH A 970 DISTANCE = 9.59 ANGSTROMS
REMARK 525 HOH B 965 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 966 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 967 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH B 968 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH B 969 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 970 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH B 971 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH B 972 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH B 973 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH B 974 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH B 975 DISTANCE = 8.08 ANGSTROMS
REMARK 525 HOH B 976 DISTANCE = 8.60 ANGSTROMS
REMARK 525 HOH B 977 DISTANCE = 8.88 ANGSTROMS
REMARK 525 HOH B 978 DISTANCE = 9.33 ANGSTROMS
REMARK 525 HOH B 979 DISTANCE = 9.50 ANGSTROMS
REMARK 525 HOH B 980 DISTANCE = 9.59 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8O3 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8O3 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8O3 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8O3 B 802
DBREF 5Y7H A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 5Y7H B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQRES 1 A 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 B 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET 8O3 A 801 38
HET 8O3 A 802 38
HET 8O3 B 801 38
HET 8O3 B 802 38
HETNAM 8O3 (R)-4-(3-AMINO-4-(2,4,5-TRIFLUOROPHENYL)BUTANOYL)
HETNAM 2 8O3 PIPERAZIN-2-ONE
FORMUL 3 8O3 4(C14 H16 F3 N3 O2)
FORMUL 7 HOH *150(H2 O)
HELIX 1 AA1 THR A 44 ASN A 51 1 8
HELIX 2 AA2 ASP A 200 VAL A 207 1 8
HELIX 3 AA3 PRO A 290 ILE A 295 1 6
HELIX 4 AA4 VAL A 341 GLN A 344 5 4
HELIX 5 AA5 GLU A 421 MET A 425 5 5
HELIX 6 AA6 ASN A 497 LEU A 504 1 8
HELIX 7 AA7 ASN A 562 THR A 570 1 9
HELIX 8 AA8 GLY A 587 HIS A 592 1 6
HELIX 9 AA9 ALA A 593 ASN A 595 5 3
HELIX 10 AB1 THR A 600 SER A 614 1 15
HELIX 11 AB2 SER A 630 GLY A 641 1 12
HELIX 12 AB3 ASP A 663 GLY A 672 1 10
HELIX 13 AB4 ASN A 679 SER A 686 1 8
HELIX 14 AB5 VAL A 688 VAL A 698 5 11
HELIX 15 AB6 HIS A 712 ASP A 725 1 14
HELIX 16 AB7 SER A 744 SER A 764 1 21
HELIX 17 AB8 THR B 44 LYS B 50 1 7
HELIX 18 AB9 ASP B 200 GLU B 206 1 7
HELIX 19 AC1 PRO B 290 ILE B 295 1 6
HELIX 20 AC2 VAL B 341 GLN B 344 5 4
HELIX 21 AC3 GLU B 421 MET B 425 5 5
HELIX 22 AC4 ASN B 497 LEU B 504 1 8
HELIX 23 AC5 ASN B 562 THR B 570 1 9
HELIX 24 AC6 GLY B 587 HIS B 592 1 6
HELIX 25 AC7 THR B 600 LYS B 615 1 16
HELIX 26 AC8 SER B 630 SER B 642 1 13
HELIX 27 AC9 ASP B 663 GLY B 672 1 10
HELIX 28 AD1 ASN B 679 SER B 686 1 8
HELIX 29 AD2 VAL B 688 GLN B 697 5 10
HELIX 30 AD3 HIS B 712 VAL B 726 1 15
HELIX 31 AD4 SER B 744 PHE B 763 1 20
SHEET 1 AA1 4 LEU A 60 TRP A 62 0
SHEET 2 AA1 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AA1 4 ASN A 75 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 AA1 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 AA2 4 ASP A 104 ILE A 107 0
SHEET 2 AA2 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AA2 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 AA2 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AA3 4 TRP A 154 TRP A 157 0
SHEET 2 AA3 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 AA3 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 AA3 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA4 3 ILE A 194 ASN A 196 0
SHEET 2 AA4 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA4 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA5 4 ILE A 194 ASN A 196 0
SHEET 2 AA5 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 AA5 4 ILE A 285 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 AA6 2 LEU A 235 PHE A 240 0
SHEET 2 AA6 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AA7 4 HIS A 298 TRP A 305 0
SHEET 2 AA7 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA7 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 AA7 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 AA8 4 HIS A 298 TRP A 305 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA8 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 AA8 4 GLU A 347 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 AA9 4 HIS A 363 PHE A 364 0
SHEET 2 AA9 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AA9 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 AA9 4 LYS A 391 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB1 4 VAL A 404 LEU A 410 0
SHEET 2 AB1 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 AB1 4 ASN A 430 GLN A 435 -1 O ILE A 434 N LEU A 415
SHEET 4 AB1 4 ASP A 438 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB2 4 CYS A 454 PHE A 461 0
SHEET 2 AB2 4 TYR A 467 PRO A 475 -1 O ARG A 471 N SER A 458
SHEET 3 AB2 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AB2 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB3 8 SER A 511 LEU A 519 0
SHEET 2 AB3 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 AB3 8 ILE A 574 ASP A 579 -1 O VAL A 575 N ILE A 529
SHEET 4 AB3 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 AB3 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 AB3 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB3 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 AB3 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB4 4 ARG B 61 TRP B 62 0
SHEET 2 AB4 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 AB4 4 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 AB4 4 SER B 86 LEU B 90 -1 O LEU B 90 N ILE B 76
SHEET 1 AB5 3 ASP B 104 ILE B 107 0
SHEET 2 AB5 3 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 AB5 3 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 1 AB6 4 TRP B 154 TRP B 157 0
SHEET 2 AB6 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 AB6 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 AB6 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 AB7 3 ILE B 194 ASN B 196 0
SHEET 2 AB7 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB7 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AB8 4 ILE B 194 ASN B 196 0
SHEET 2 AB8 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB8 4 THR B 265 ASN B 272 -1 O LYS B 267 N GLN B 227
SHEET 4 AB8 4 ILE B 285 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 AB9 2 LEU B 235 PHE B 240 0
SHEET 2 AB9 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AC1 4 HIS B 298 TRP B 305 0
SHEET 2 AC1 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 AC1 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 AC1 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 AC2 4 HIS B 298 TRP B 305 0
SHEET 2 AC2 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 AC2 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 AC2 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 AC3 4 HIS B 363 PHE B 364 0
SHEET 2 AC3 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC3 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 AC3 4 LYS B 391 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 AC4 4 VAL B 404 LEU B 410 0
SHEET 2 AC4 4 TYR B 414 SER B 419 -1 O ILE B 418 N GLY B 406
SHEET 3 AC4 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC4 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AC5 4 CYS B 454 PHE B 461 0
SHEET 2 AC5 4 TYR B 467 PRO B 475 -1 O ARG B 471 N SER B 458
SHEET 3 AC5 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 AC5 4 GLY B 490 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AC6 8 SER B 511 LEU B 519 0
SHEET 2 AC6 8 THR B 522 LEU B 530 -1 O TYR B 526 N ASP B 515
SHEET 3 AC6 8 ILE B 574 ASP B 579 -1 O VAL B 575 N ILE B 529
SHEET 4 AC6 8 TYR B 540 VAL B 546 1 N LEU B 543 O ALA B 576
SHEET 5 AC6 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 AC6 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 AC6 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 AC6 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.03
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.03
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.03
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.03
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.03
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.03
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.03
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.03
CISPEP 1 GLY A 474 PRO A 475 0 0.38
CISPEP 2 GLY B 474 PRO B 475 0 1.03
SITE 1 AC1 14 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 AC1 14 PHE A 357 SER A 630 TYR A 631 VAL A 656
SITE 3 AC1 14 TYR A 662 TYR A 666 ASN A 710 VAL A 711
SITE 4 AC1 14 HIS A 740 8O3 A 802
SITE 1 AC2 5 ARG A 125 HIS A 126 SER A 209 TRP A 629
SITE 2 AC2 5 8O3 A 801
SITE 1 AC3 3 ARG B 125 TYR B 547 8O3 B 802
SITE 1 AC4 14 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 AC4 14 PHE B 357 SER B 630 TYR B 631 VAL B 656
SITE 3 AC4 14 TYR B 662 TYR B 666 ASN B 710 HIS B 740
SITE 4 AC4 14 8O3 B 801 HOH B 917
CRYST1 64.301 126.420 113.382 90.00 100.43 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 0.015552 0.000000 0.002862 0.00000
SCALE2 0.000000 0.007910 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008968 0.00000
TER 5948 PRO A 766
TER 11913 PRO B 766
MASTER 345 0 4 31 97 0 11 612149 2 172 112
END
|
|---|
