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HEADER HYDROLASE/HYDROLASE INHIBITOR 01-SEP-10 3OPM
TITLE CRYSTAL STRUCTURE OF HUMAN DPP4 BOUND TO TAK-294
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: DPP4;
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN
COMPND 6 CD26, TP103, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2, ADABP;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADCP2, CD26, DPP4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS PROTEASE AND 8-BLADED BETA-PROPELLER DOMAIN, AMINOPEPTIDASE, CELL
KEYWDS 2 MEMBRANE, GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE, SECRETED,
KEYWDS 3 SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE, SIGNALING PROTEIN,
KEYWDS 4 HYDROLASE-HYDROLASE INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.YANO,K.AERTGEERTS
REVDAT 1 19-OCT-11 3OPM 0
JRNL AUTH Y.BANNO,Y.MIYAMOTO,M.SASAKI,S.OI,T.ASAKAWA,O.KATAOKA,
JRNL AUTH 2 K.TAKEUCHI,N.SUZUKI,K.IKEDO,T.KOSAKA,S.TSUBOTANI,A.TANI,
JRNL AUTH 3 M.FUNAMI,M.TAWADA,Y.YAMAMOTO,K.AERTGEERTS,J.YANO,H.MAEZAKI
JRNL TITL IDENTIFICATION OF
JRNL TITL 2 3-AMINOMETHYL-1,2-DIHYDRO-4-PHENYL-1-ISOQUINOLONES: A NEW
JRNL TITL 3 CLASS OF POTENT, SELECTIVE, AND ORALLY ACTIVE NON-PEPTIDE
JRNL TITL 4 DIPEPTIDYL PEPTIDASE IV INHIBITORS THAT FORM A UNIQUE
JRNL TITL 5 INTERACTION WITH LYS554.
JRNL REF BIOORG.MED.CHEM. V. 19 4953 2011
JRNL REFN ISSN 0968-0896
JRNL PMID 21764322
JRNL DOI 10.1016/J.BMC.2011.06.059
REMARK 2
REMARK 2 RESOLUTION. 2.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 95647
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5038
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6015
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 311
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23857
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 350
REMARK 3 SOLVENT ATOMS : 506
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.53000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : -0.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.361
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.277
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.408
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24927 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 16594 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 33920 ; 1.217 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 40110 ; 0.844 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2907 ; 6.647 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1234 ;33.889 ;23.955
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3984 ;16.362 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 119 ;17.476 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3588 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 27646 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5443 ; 0.002 ; 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): 1018 ; 0.154 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.055 ; 0.200
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): 28 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 46 ; 0.206 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.182 ; 0.200
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): 14503 ; 0.292 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5872 ; 0.053 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23528 ; 0.556 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10424 ; 0.847 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10392 ; 1.374 ; 4.500
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 : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 61 A 495
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7010 -34.7340 28.6610
REMARK 3 T TENSOR
REMARK 3 T11: 0.1955 T22: 0.4517
REMARK 3 T33: 0.2234 T12: 0.0437
REMARK 3 T13: 0.1052 T23: -0.0900
REMARK 3 L TENSOR
REMARK 3 L11: 2.2088 L22: 0.5909
REMARK 3 L33: 1.5177 L12: 0.2151
REMARK 3 L13: 0.4927 L23: -0.2082
REMARK 3 S TENSOR
REMARK 3 S11: -0.0288 S12: -0.4949 S13: 0.3783
REMARK 3 S21: 0.3017 S22: -0.0031 S23: 0.2982
REMARK 3 S31: -0.0920 S32: -0.4682 S33: 0.0319
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 497 A 766
REMARK 3 RESIDUE RANGE : A 1 A 1
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2940 -30.0070 3.2350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0456 T22: 0.2070
REMARK 3 T33: 0.0732 T12: 0.0102
REMARK 3 T13: -0.0287 T23: 0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 2.3039 L22: 1.0001
REMARK 3 L33: 1.4754 L12: 0.2823
REMARK 3 L13: 0.3927 L23: 0.0772
REMARK 3 S TENSOR
REMARK 3 S11: -0.1074 S12: 0.2286 S13: 0.3463
REMARK 3 S21: -0.1931 S22: 0.0851 S23: 0.0856
REMARK 3 S31: -0.0040 S32: -0.0845 S33: 0.0222
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 61 B 495
REMARK 3 ORIGIN FOR THE GROUP (A): 74.3630 -32.9120 26.9600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1737 T22: 0.4174
REMARK 3 T33: 0.2620 T12: 0.1137
REMARK 3 T13: -0.0734 T23: -0.1541
REMARK 3 L TENSOR
REMARK 3 L11: 2.3571 L22: 0.6788
REMARK 3 L33: 1.0716 L12: 0.4765
REMARK 3 L13: 0.1375 L23: -0.5643
REMARK 3 S TENSOR
REMARK 3 S11: -0.1121 S12: -0.2473 S13: -0.1337
REMARK 3 S21: -0.1006 S22: 0.0563 S23: -0.3069
REMARK 3 S31: 0.3082 S32: 0.2065 S33: 0.0558
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 497 B 766
REMARK 3 RESIDUE RANGE : B 1 B 1
REMARK 3 ORIGIN FOR THE GROUP (A): 55.3710 -12.6850 12.6180
REMARK 3 T TENSOR
REMARK 3 T11: 0.0559 T22: 0.1731
REMARK 3 T33: 0.3105 T12: 0.0071
REMARK 3 T13: -0.0480 T23: -0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 2.0709 L22: 1.2392
REMARK 3 L33: 1.2526 L12: 0.2665
REMARK 3 L13: -0.1820 L23: 0.0463
REMARK 3 S TENSOR
REMARK 3 S11: -0.1051 S12: -0.0113 S13: 0.6605
REMARK 3 S21: -0.0733 S22: 0.0995 S23: -0.0237
REMARK 3 S31: -0.2286 S32: 0.0626 S33: 0.0056
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 61 C 495
REMARK 3 ORIGIN FOR THE GROUP (A): -34.9750 38.8030 52.7500
REMARK 3 T TENSOR
REMARK 3 T11: 0.3225 T22: 0.7758
REMARK 3 T33: 0.5006 T12: -0.0501
REMARK 3 T13: 0.1825 T23: -0.3108
REMARK 3 L TENSOR
REMARK 3 L11: 2.5916 L22: 1.6543
REMARK 3 L33: 0.9510 L12: 0.6959
REMARK 3 L13: -0.2664 L23: 0.4350
REMARK 3 S TENSOR
REMARK 3 S11: 0.1872 S12: -0.5148 S13: 0.5246
REMARK 3 S21: 0.2400 S22: -0.3842 S23: 0.8512
REMARK 3 S31: -0.1492 S32: -0.6330 S33: 0.1970
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 497 C 766
REMARK 3 RESIDUE RANGE : C 1 C 1
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9620 14.2570 39.5610
REMARK 3 T TENSOR
REMARK 3 T11: 0.2210 T22: 0.2308
REMARK 3 T33: 0.2767 T12: -0.0903
REMARK 3 T13: -0.0003 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 2.8681 L22: 1.7572
REMARK 3 L33: 1.1750 L12: 0.9631
REMARK 3 L13: -0.0701 L23: 0.1674
REMARK 3 S TENSOR
REMARK 3 S11: 0.2415 S12: -0.1891 S13: -0.5489
REMARK 3 S21: 0.1808 S22: -0.2338 S23: 0.2044
REMARK 3 S31: 0.3471 S32: -0.2682 S33: -0.0077
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 61 D 495
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8100 32.2490 40.9050
REMARK 3 T TENSOR
REMARK 3 T11: 0.2172 T22: 0.6186
REMARK 3 T33: 0.1691 T12: -0.0011
REMARK 3 T13: -0.0969 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 3.3888 L22: 0.4232
REMARK 3 L33: 1.3649 L12: -0.0719
REMARK 3 L13: -0.8621 L23: 0.4911
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: -0.7191 S13: -0.1989
REMARK 3 S21: 0.2276 S22: 0.0297 S23: -0.1982
REMARK 3 S31: 0.1887 S32: 0.6189 S33: -0.0947
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 497 D 766
REMARK 3 RESIDUE RANGE : D 1 D 1
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9300 24.9000 20.7160
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.2563
REMARK 3 T33: 0.0789 T12: 0.0941
REMARK 3 T13: -0.0308 T23: -0.1040
REMARK 3 L TENSOR
REMARK 3 L11: 2.8271 L22: 0.7690
REMARK 3 L33: 1.4883 L12: 0.1676
REMARK 3 L13: -0.2990 L23: 0.1793
REMARK 3 S TENSOR
REMARK 3 S11: 0.0936 S12: 0.4561 S13: -0.4255
REMARK 3 S21: -0.1236 S22: -0.0774 S23: -0.0178
REMARK 3 S31: 0.2041 S32: 0.1282 S33: -0.0163
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OPM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 92
REMARK 200 PH : 8-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
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 : SI (220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100745
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.720
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 (%) : 97.5
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
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 (%): 56.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23.6% PEG MME 2000, 100 MM BICINE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 61.27850
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, 3
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 117390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 40.0 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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 60.60250
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -61.27850
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 131.17627
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 ALA A 27
REMARK 465 ASP A 28
REMARK 465 PRO A 29
REMARK 465 GLY A 30
REMARK 465 GLY A 31
REMARK 465 SER A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 HIS A 37
REMARK 465 HIS A 38
REMARK 465 SER A 39
REMARK 465 ALA B 27
REMARK 465 ASP B 28
REMARK 465 PRO B 29
REMARK 465 GLY B 30
REMARK 465 GLY B 31
REMARK 465 SER B 32
REMARK 465 HIS B 33
REMARK 465 ALA C 27
REMARK 465 ASP C 28
REMARK 465 PRO C 29
REMARK 465 GLY C 30
REMARK 465 GLY C 31
REMARK 465 SER C 32
REMARK 465 HIS C 33
REMARK 465 HIS C 34
REMARK 465 HIS C 35
REMARK 465 HIS C 36
REMARK 465 HIS C 37
REMARK 465 HIS C 38
REMARK 465 SER C 39
REMARK 465 GLU C 97
REMARK 465 PHE C 98
REMARK 465 ALA D 27
REMARK 465 ASP D 28
REMARK 465 PRO D 29
REMARK 465 GLY D 30
REMARK 465 GLY D 31
REMARK 465 SER D 32
REMARK 465 HIS D 33
REMARK 465 HIS D 34
REMARK 465 HIS D 35
REMARK 465 HIS D 36
REMARK 465 HIS D 37
REMARK 465 HIS D 38
REMARK 465 SER D 39
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 ARG A 40 N CG CD NE CZ NH1 NH2
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 OE2 GLU A 82 OH TYR A 467 1.93
REMARK 500 OE1 GLU A 347 NZ LYS A 373 2.18
REMARK 500 OG SER C 630 NE2 HIS C 740 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 64 -156.26 -144.10
REMARK 500 HIS A 66 26.74 -145.53
REMARK 500 GLN A 72 65.99 -57.50
REMARK 500 GLU A 73 -75.94 34.34
REMARK 500 ASN A 74 44.90 -93.10
REMARK 500 VAL A 88 99.27 -59.91
REMARK 500 ASN A 92 -69.49 -13.32
REMARK 500 SER A 106 117.57 -165.01
REMARK 500 GLN A 123 -108.75 -112.47
REMARK 500 TRP A 124 -148.91 -84.76
REMARK 500 ILE A 193 -60.09 -127.58
REMARK 500 VAL A 207 -62.41 -99.85
REMARK 500 SER A 209 47.23 36.33
REMARK 500 SER A 242 -169.52 66.30
REMARK 500 GLN A 320 46.59 -81.07
REMARK 500 GLU A 332 -71.71 -44.73
REMARK 500 THR A 401 66.08 -102.26
REMARK 500 ASN A 420 46.17 -102.60
REMARK 500 ASN A 450 73.04 -173.11
REMARK 500 LEU A 491 -62.48 -17.98
REMARK 500 ASN A 520 50.98 39.13
REMARK 500 TYR A 547 -69.88 -121.76
REMARK 500 ARG A 597 46.44 -147.82
REMARK 500 THR A 600 -93.51 -130.34
REMARK 500 SER A 630 -129.07 61.25
REMARK 500 ASP A 678 -98.38 -124.57
REMARK 500 ASN A 710 -69.55 -90.77
REMARK 500 GLN A 714 -52.13 -25.12
REMARK 500 ASP A 739 -151.60 -91.05
REMARK 500 SER B 64 -168.65 -128.58
REMARK 500 ASN B 74 -20.98 68.38
REMARK 500 PHE B 95 -156.30 -103.51
REMARK 500 ASP B 96 8.28 49.92
REMARK 500 SER B 106 118.72 -162.06
REMARK 500 GLN B 123 -100.67 -123.38
REMARK 500 TRP B 124 -148.52 -93.10
REMARK 500 ARG B 140 71.86 45.85
REMARK 500 HIS B 162 41.53 -159.14
REMARK 500 ILE B 193 -61.32 -133.09
REMARK 500 VAL B 207 -64.57 -97.92
REMARK 500 SER B 209 46.61 33.74
REMARK 500 SER B 242 -156.34 58.33
REMARK 500 GLU B 244 -6.97 -53.46
REMARK 500 GLN B 320 41.84 -84.47
REMARK 500 LYS B 423 27.67 49.16
REMARK 500 ASN B 450 74.15 -156.72
REMARK 500 ASN B 487 29.98 -147.44
REMARK 500 ASP B 488 45.58 38.35
REMARK 500 LEU B 491 -60.43 -96.17
REMARK 500 TYR B 547 -75.00 -117.17
REMARK 500
REMARK 500 THIS ENTRY HAS 125 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 96 GLU B 97 138.44
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 795 DISTANCE = 5.80 ANGSTROMS
REMARK 525 HOH A 811 DISTANCE = 8.95 ANGSTROMS
REMARK 525 HOH A 820 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH A 834 DISTANCE = 8.93 ANGSTROMS
REMARK 525 HOH A 886 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH B 797 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH C 782 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C 801 DISTANCE = 9.14 ANGSTROMS
REMARK 525 HOH C 806 DISTANCE = 7.19 ANGSTROMS
REMARK 525 HOH C 815 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH C 830 DISTANCE = 14.01 ANGSTROMS
REMARK 525 HOH C 844 DISTANCE = 9.41 ANGSTROMS
REMARK 525 HOH C 846 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH D 787 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH D 813 DISTANCE = 5.16 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 2292
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUI A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUI B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3211
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUI C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUI D 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2811
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O9V RELATED DB: PDB
REMARK 900 RELATED ID: 3O95 RELATED DB: PDB
DBREF 3OPM A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3OPM B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3OPM C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3OPM D 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 3OPM ALA A 27 UNP P27487 EXPRESSION TAG
SEQADV 3OPM ASP A 28 UNP P27487 EXPRESSION TAG
SEQADV 3OPM PRO A 29 UNP P27487 EXPRESSION TAG
SEQADV 3OPM GLY A 30 UNP P27487 EXPRESSION TAG
SEQADV 3OPM GLY A 31 UNP P27487 EXPRESSION TAG
SEQADV 3OPM SER A 32 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS A 33 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS A 34 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS A 35 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS A 36 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS A 37 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS A 38 UNP P27487 EXPRESSION TAG
SEQADV 3OPM ALA B 27 UNP P27487 EXPRESSION TAG
SEQADV 3OPM ASP B 28 UNP P27487 EXPRESSION TAG
SEQADV 3OPM PRO B 29 UNP P27487 EXPRESSION TAG
SEQADV 3OPM GLY B 30 UNP P27487 EXPRESSION TAG
SEQADV 3OPM GLY B 31 UNP P27487 EXPRESSION TAG
SEQADV 3OPM SER B 32 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS B 33 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS B 34 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS B 35 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS B 36 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS B 37 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS B 38 UNP P27487 EXPRESSION TAG
SEQADV 3OPM ALA C 27 UNP P27487 EXPRESSION TAG
SEQADV 3OPM ASP C 28 UNP P27487 EXPRESSION TAG
SEQADV 3OPM PRO C 29 UNP P27487 EXPRESSION TAG
SEQADV 3OPM GLY C 30 UNP P27487 EXPRESSION TAG
SEQADV 3OPM GLY C 31 UNP P27487 EXPRESSION TAG
SEQADV 3OPM SER C 32 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS C 33 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS C 34 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS C 35 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS C 36 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS C 37 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS C 38 UNP P27487 EXPRESSION TAG
SEQADV 3OPM ALA D 27 UNP P27487 EXPRESSION TAG
SEQADV 3OPM ASP D 28 UNP P27487 EXPRESSION TAG
SEQADV 3OPM PRO D 29 UNP P27487 EXPRESSION TAG
SEQADV 3OPM GLY D 30 UNP P27487 EXPRESSION TAG
SEQADV 3OPM GLY D 31 UNP P27487 EXPRESSION TAG
SEQADV 3OPM SER D 32 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS D 33 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS D 34 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS D 35 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS D 36 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS D 37 UNP P27487 EXPRESSION TAG
SEQADV 3OPM HIS D 38 UNP P27487 EXPRESSION TAG
SEQRES 1 A 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 A 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 A 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 A 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 A 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 A 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 A 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 A 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 A 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 A 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 A 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 A 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 A 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 A 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 A 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 A 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 A 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 A 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 A 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 A 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 A 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 A 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 A 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 A 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 A 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 A 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 A 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 A 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 A 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 A 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 A 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 A 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 A 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 A 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 A 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 A 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 A 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 A 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 A 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 A 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 A 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 A 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 A 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 A 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 A 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 A 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 A 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 A 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 A 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 A 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 A 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 A 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 A 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 A 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 A 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 A 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 B 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 B 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 B 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 B 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 B 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 B 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 B 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 B 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 B 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 B 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 B 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 B 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 B 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 B 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 B 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 B 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 B 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 B 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 B 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 B 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 B 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 B 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 B 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 B 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 B 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 B 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 B 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 B 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 B 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 B 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 B 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 B 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 B 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 B 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 B 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 B 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 B 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 B 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 B 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 B 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 B 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 B 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 B 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 B 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 B 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 B 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 B 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 B 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 B 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 B 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 B 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 B 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 B 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 B 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 B 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 B 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 C 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 C 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 C 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 C 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 C 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 C 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 C 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 C 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 C 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 C 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 C 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 C 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 C 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 C 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 C 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 C 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 C 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 C 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 C 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 C 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 C 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 C 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 C 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 C 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 C 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 C 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 C 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 C 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 C 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 C 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 C 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 C 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 C 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 C 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 C 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 C 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 C 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 C 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 C 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 C 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 C 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 C 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 C 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 C 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 C 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 C 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 C 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 C 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 C 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 C 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 C 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 C 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 C 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 C 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 C 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 C 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 D 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 D 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 D 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 D 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 D 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 D 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 D 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 D 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 D 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 D 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 D 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 D 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 D 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 D 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 D 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 D 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 D 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 D 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 D 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 D 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 D 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 D 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 D 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 D 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 D 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 D 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 D 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 D 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 D 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 D 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 D 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 D 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 D 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 D 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 D 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 D 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 D 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 D 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 D 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 D 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 D 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 D 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 D 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 D 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 D 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 D 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 D 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 D 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 D 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 D 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 D 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 D 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 D 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 D 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 D 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 D 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
MODRES 3OPM ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN D 150 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN B 321 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN A 321 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN A 281 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN D 229 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN B 281 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN D 219 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN D 281 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3OPM ASN C 229 ASN GLYCOSYLATION SITE
HET LUI A 800 28
HET NAG A1501 14
HET NAG A2191 14
HET NAG A2291 14
HET NAG A2292 14
HET NAG A2811 14
HET NAG A3211 14
HET LUI B 800 28
HET NAG B 901 14
HET NAG B1501 14
HET NAG B2291 14
HET NAG B2811 14
HET NAG B3211 14
HET LUI C 800 28
HET NAG C2291 14
HET NAG C2292 14
HET LUI D 800 28
HET NAG D1501 14
HET NAG D2191 14
HET NAG D2291 14
HET NAG D2811 14
HETNAM LUI 2-{[3-(AMINOMETHYL)-2-(2-METHYLPROPYL)-1-OXO-4-PHENYL-
HETNAM 2 LUI 1,2-DIHYDROISOQUINOLIN-6-YL]OXY}ACETAMIDE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN LUI TAK-285
FORMUL 5 LUI 4(C22 H25 N3 O3)
FORMUL 6 NAG 17(C8 H15 N O6)
FORMUL 26 HOH *506(H2 O)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 SER A 93 PHE A 95 5 3
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 LEU A 340 GLN A 344 5 5
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 LEU A 504 1 8
HELIX 8 8 ASN A 562 THR A 570 1 9
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
HELIX 11 11 THR A 600 LYS A 615 1 16
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 ARG A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 GLY A 672 1 10
HELIX 15 15 ASN A 679 SER A 686 1 8
HELIX 16 16 VAL A 688 VAL A 698 5 11
HELIX 17 17 HIS A 712 GLY A 727 1 16
HELIX 18 18 SER A 744 PHE A 763 1 20
HELIX 19 19 THR B 44 ASN B 51 1 8
HELIX 20 20 GLU B 91 PHE B 95 5 5
HELIX 21 21 ASP B 200 VAL B 207 1 8
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 VAL B 341 GLN B 344 5 4
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 ASN B 497 LEU B 504 1 8
HELIX 26 26 ASN B 562 ASN B 572 1 11
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 MET B 616 1 17
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ASP B 663 GLY B 672 1 10
HELIX 32 32 ASN B 679 SER B 686 1 8
HELIX 33 33 VAL B 688 VAL B 698 5 11
HELIX 34 34 HIS B 712 VAL B 726 1 15
HELIX 35 35 SER B 744 PHE B 763 1 20
HELIX 36 36 THR C 44 ASN C 51 1 8
HELIX 37 37 ASP C 200 VAL C 207 1 8
HELIX 38 38 PRO C 290 ILE C 295 1 6
HELIX 39 39 GLU C 421 MET C 425 5 5
HELIX 40 40 ASN C 497 GLN C 505 1 9
HELIX 41 41 ASN C 562 ASN C 572 1 11
HELIX 42 42 GLY C 587 HIS C 592 1 6
HELIX 43 43 ALA C 593 ASN C 595 5 3
HELIX 44 44 THR C 600 MET C 616 1 17
HELIX 45 45 SER C 630 GLY C 641 1 12
HELIX 46 46 ASP C 663 GLY C 672 1 10
HELIX 47 47 ASN C 679 SER C 686 1 8
HELIX 48 48 THR C 687 VAL C 698 5 12
HELIX 49 49 HIS C 712 GLY C 727 1 16
HELIX 50 50 SER C 744 PHE C 763 1 20
HELIX 51 51 THR D 44 ASN D 51 1 8
HELIX 52 52 ASP D 200 GLU D 206 1 7
HELIX 53 53 PRO D 290 ILE D 295 1 6
HELIX 54 54 LEU D 340 GLN D 344 5 5
HELIX 55 55 GLU D 421 MET D 425 5 5
HELIX 56 56 ASN D 497 GLN D 505 1 9
HELIX 57 57 ASN D 562 THR D 570 1 9
HELIX 58 58 GLY D 587 HIS D 592 1 6
HELIX 59 59 ALA D 593 ASN D 595 5 3
HELIX 60 60 THR D 600 MET D 616 1 17
HELIX 61 61 TYR D 631 GLY D 641 1 11
HELIX 62 62 ARG D 658 TYR D 662 5 5
HELIX 63 63 ASP D 663 GLY D 672 1 10
HELIX 64 64 ASN D 679 SER D 686 1 8
HELIX 65 65 VAL D 688 VAL D 698 5 11
HELIX 66 66 PHE D 713 VAL D 726 1 14
HELIX 67 67 SER D 744 PHE D 763 1 20
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 ARG A 61 TRP A 62 0
SHEET 2 B 4 GLU A 67 TYR A 70 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ASN A 75 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 B 4 SER A 86 GLU A 91 -1 O SER A 87 N VAL A 78
SHEET 1 C 3 PHE A 113 LYS A 122 0
SHEET 2 C 3 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 3 C 3 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 THR A 152 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N GLN A 153
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 F 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O GLN A 314 N CYS A 301
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 THR A 307 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O GLN A 314 N CYS A 301
SHEET 3 I 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 I 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 L 4 LEU A 479 SER A 484 -1 O HIS A 483 N TYR A 468
SHEET 4 L 4 ARG A 492 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 ARG B 61 TRP B 62 0
SHEET 2 O 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ILE B 76 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 O 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 P 4 ASP B 104 ILE B 107 0
SHEET 2 P 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 P 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 P 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 Q 4 TRP B 154 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 Q 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 S 4 SER B 284 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 U 4 TYR B 322 ASP B 331 -1 O VAL B 324 N TRP B 315
SHEET 4 U 4 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 1 V 4 HIS B 298 THR B 307 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 V 4 TYR B 322 ASP B 331 -1 O VAL B 324 N TRP B 315
SHEET 4 V 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 W 4 HIS B 363 PHE B 364 0
SHEET 2 W 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 W 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 W 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 X 4 VAL B 404 LEU B 410 0
SHEET 2 X 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 X 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 X 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 Y 4 TYR B 457 PHE B 461 0
SHEET 2 Y 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 Y 4 LYS B 489 GLU B 495 -1 O LEU B 491 N LEU B 482
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Z 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Z 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O TRP B 627 N VAL B 546
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Z 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AA 4 ARG C 61 TRP C 62 0
SHEET 2 AA 4 GLU C 67 GLN C 72 -1 O LEU C 69 N ARG C 61
SHEET 3 AA 4 ASN C 75 ASN C 80 -1 O ASN C 75 N GLN C 72
SHEET 4 AA 4 VAL C 88 GLU C 91 -1 O PHE C 89 N ILE C 76
SHEET 1 AB 4 ASP C 104 ILE C 107 0
SHEET 2 AB 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AB 4 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 4 AB 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AC 4 ASP C 104 ILE C 107 0
SHEET 2 AC 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AC 4 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 4 AC 4 ILE C 148 THR C 152 -1 O THR C 152 N ALA C 130
SHEET 1 AD 4 TRP C 154 TRP C 157 0
SHEET 2 AD 4 LEU C 164 TRP C 168 -1 O ALA C 165 N THR C 156
SHEET 3 AD 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AD 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AE 3 ILE C 194 ASN C 196 0
SHEET 2 AE 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AE 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AF 4 ILE C 194 ASN C 196 0
SHEET 2 AF 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AF 4 THR C 265 ASN C 272 -1 O PHE C 269 N TYR C 225
SHEET 4 AF 4 ILE C 285 ILE C 287 -1 O ILE C 285 N VAL C 270
SHEET 1 AG 2 LEU C 235 PHE C 240 0
SHEET 2 AG 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AH 4 HIS C 298 TRP C 305 0
SHEET 2 AH 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AH 4 TYR C 322 TYR C 330 -1 O CYS C 328 N ILE C 311
SHEET 4 AH 4 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 1 AI 4 HIS C 298 TRP C 305 0
SHEET 2 AI 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AI 4 TYR C 322 TYR C 330 -1 O CYS C 328 N ILE C 311
SHEET 4 AI 4 HIS C 345 MET C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AJ 4 HIS C 363 PHE C 364 0
SHEET 2 AJ 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AJ 4 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AJ 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AK 4 VAL C 404 LEU C 410 0
SHEET 2 AK 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AK 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AK 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AL 4 TYR C 457 PHE C 461 0
SHEET 2 AL 4 TYR C 467 CYS C 472 -1 O GLN C 469 N SER C 460
SHEET 3 AL 4 LEU C 479 SER C 484 -1 O HIS C 483 N TYR C 468
SHEET 4 AL 4 LYS C 489 GLU C 495 -1 O ARG C 492 N LEU C 482
SHEET 1 AM 8 SER C 511 LEU C 519 0
SHEET 2 AM 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AM 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AM 8 TYR C 540 VAL C 546 1 N ASP C 545 O ALA C 576
SHEET 5 AM 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 542
SHEET 6 AM 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AM 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 652
SHEET 8 AM 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AN 2 LYS D 41 THR D 42 0
SHEET 2 AN 2 VAL D 507 GLN D 508 1 O GLN D 508 N LYS D 41
SHEET 1 AO 4 ARG D 61 TRP D 62 0
SHEET 2 AO 4 GLU D 67 LYS D 71 -1 O LEU D 69 N ARG D 61
SHEET 3 AO 4 ILE D 76 ASN D 80 -1 O PHE D 79 N TYR D 68
SHEET 4 AO 4 VAL D 88 LEU D 90 -1 O LEU D 90 N ILE D 76
SHEET 1 AP 3 ASP D 104 ILE D 107 0
SHEET 2 AP 3 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AP 3 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 1 AQ 4 TRP D 154 TRP D 157 0
SHEET 2 AQ 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
SHEET 3 AQ 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AQ 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AR 3 ILE D 194 ASN D 196 0
SHEET 2 AR 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AR 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AS 4 ILE D 194 ASN D 196 0
SHEET 2 AS 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AS 4 THR D 265 ASN D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AS 4 ILE D 285 GLN D 286 -1 O ILE D 285 N VAL D 270
SHEET 1 AT 2 LEU D 235 PHE D 240 0
SHEET 2 AT 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AU 4 HIS D 298 TRP D 305 0
SHEET 2 AU 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AU 4 TYR D 322 ASP D 331 -1 O CYS D 328 N ILE D 311
SHEET 4 AU 4 ARG D 336 ASN D 338 -1 O ARG D 336 N ASP D 331
SHEET 1 AV 4 HIS D 298 TRP D 305 0
SHEET 2 AV 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AV 4 TYR D 322 ASP D 331 -1 O CYS D 328 N ILE D 311
SHEET 4 AV 4 HIS D 345 MET D 348 -1 O GLU D 347 N SER D 323
SHEET 1 AW 4 HIS D 363 PHE D 364 0
SHEET 2 AW 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AW 4 ARG D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AW 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 AX 4 VAL D 404 LEU D 410 0
SHEET 2 AX 4 TYR D 414 SER D 419 -1 O TYR D 416 N ALA D 409
SHEET 3 AX 4 ASN D 430 GLN D 435 -1 O ILE D 434 N LEU D 415
SHEET 4 AX 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AY 4 CYS D 454 PHE D 461 0
SHEET 2 AY 4 TYR D 467 PRO D 475 -1 O GLY D 474 N GLN D 455
SHEET 3 AY 4 LEU D 479 SER D 484 -1 O THR D 481 N LEU D 470
SHEET 4 AY 4 GLY D 490 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AZ 8 SER D 511 LEU D 519 0
SHEET 2 AZ 8 THR D 522 LEU D 530 -1 O LEU D 530 N SER D 511
SHEET 3 AZ 8 ILE D 574 ASP D 579 -1 O VAL D 575 N ILE D 529
SHEET 4 AZ 8 TYR D 540 VAL D 546 1 N ASP D 545 O ALA D 576
SHEET 5 AZ 8 VAL D 619 SER D 630 1 O ALA D 625 N LEU D 542
SHEET 6 AZ 8 CYS D 649 PRO D 655 1 O VAL D 653 N GLY D 628
SHEET 7 AZ 8 GLU D 699 GLY D 705 1 O ILE D 703 N ALA D 654
SHEET 8 AZ 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.04
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.06
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.07
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.06
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.06
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.08
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.06
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.05
SSBOND 13 CYS C 444 CYS C 447 1555 1555 2.05
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.06
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.07
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.04
SSBOND 17 CYS D 385 CYS D 394 1555 1555 2.04
SSBOND 18 CYS D 444 CYS D 447 1555 1555 2.03
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.08
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.05
LINK ND2 ASN A 229 C1 NAG A2291 1555 1555 1.61
LINK ND2 ASN D 150 C1 NAG D1501 1555 1555 1.65
LINK ND2 ASN A 150 C1 NAG A1501 1555 1555 1.65
LINK ND2 ASN B 321 C1 NAG B3211 1555 1555 1.66
LINK ND2 ASN A 321 C1 NAG A3211 1555 1555 1.71
LINK ND2 ASN B 85 C1 NAG B 901 1555 1555 1.71
LINK ND2 ASN A 281 C1 NAG A2811 1555 1555 1.75
LINK ND2 ASN B 229 C1 NAG B2291 1555 1555 1.76
LINK ND2 ASN B 150 C1 NAG B1501 1555 1555 1.83
LINK ND2 ASN D 229 C1 NAG D2291 1555 1555 1.87
LINK ND2 ASN B 281 C1 NAG B2811 1555 1555 2.00
LINK ND2 ASN D 219 C1 NAG D2191 1555 1555 2.04
LINK ND2 ASN D 281 C1 NAG D2811 1555 1555 2.11
LINK ND2 ASN A 219 C1 NAG A2191 1555 1555 1.63
LINK ND2 ASN C 229 C1 NAG C2291 1555 1555 1.89
LINK O4 NAG C2291 C1 NAG C2292 1555 1555 2.03
CISPEP 1 GLY A 474 PRO A 475 0 -0.54
CISPEP 2 GLY B 474 PRO B 475 0 8.04
CISPEP 3 GLY C 474 PRO C 475 0 8.10
CISPEP 4 GLY D 474 PRO D 475 0 7.63
SITE 1 AC1 10 HOH A 1 ARG A 125 GLU A 205 GLU A 206
SITE 2 AC1 10 PHE A 357 TYR A 547 TRP A 629 TYR A 662
SITE 3 AC1 10 TYR A 666 HOH A 789
SITE 1 AC2 3 ASN A 150 HOH A 816 HOH A 840
SITE 1 AC3 5 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 2 AC3 5 HOH A 889
SITE 1 AC4 5 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC4 5 NAG A2292
SITE 1 AC5 4 THR A 231 GLU A 232 HOH A 836 NAG A2291
SITE 1 AC6 2 ASN A 281 HOH A 866
SITE 1 AC7 6 ILE A 319 ASN A 321 SER A 349 THR A 350
SITE 2 AC7 6 ARG A 596 HOH A 869
SITE 1 AC8 14 HOH B 22 GLU B 205 GLU B 206 SER B 209
SITE 2 AC8 14 PHE B 357 TYR B 547 LYS B 554 TRP B 629
SITE 3 AC8 14 SER B 630 TYR B 631 TYR B 662 TYR B 666
SITE 4 AC8 14 HOH B 814 HOH B 815
SITE 1 AC9 3 ASN B 85 HOH B 818 HOH B 874
SITE 1 BC1 6 ARG B 147 ILE B 148 ASN B 150 HOH B 826
SITE 2 BC1 6 HOH B 827 HOH B 834
SITE 1 BC2 4 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 1 BC3 4 TRP B 187 ASN B 281 HOH B 821 HOH B 891
SITE 1 BC4 6 ILE B 319 ASN B 321 TYR B 322 ARG B 596
SITE 2 BC4 6 HOH B 792 HOH B 883
SITE 1 BC5 10 GLU C 205 GLU C 206 SER C 209 PHE C 357
SITE 2 BC5 10 TYR C 547 LYS C 554 TRP C 629 TYR C 662
SITE 3 BC5 10 TYR C 666 HOH C 794
SITE 1 BC6 4 ASN C 229 THR C 231 GLU C 232 NAG C2292
SITE 1 BC7 1 NAG C2291
SITE 1 BC8 9 GLU D 205 GLU D 206 PHE D 357 TYR D 547
SITE 2 BC8 9 LYS D 554 TRP D 629 TYR D 662 TYR D 666
SITE 3 BC8 9 HOH D 890
SITE 1 BC9 4 ASN D 150 HOH D 784 HOH D 828 HOH D 835
SITE 1 CC1 5 ASN D 219 THR D 221 GLN D 308 GLU D 309
SITE 2 CC1 5 HOH D 779
SITE 1 CC2 5 ILE D 194 ASN D 229 THR D 231 GLU D 232
SITE 2 CC2 5 LYS D 267
SITE 1 CC3 3 ASN D 281 HOH D 851 HOH D 870
CRYST1 121.771 122.557 144.737 90.00 115.00 90.00 P 1 21 1 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 0.008212 0.000000 0.003829 0.00000
SCALE2 0.000000 0.008159 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007623 0.00000
TER 5951 PRO A 766
TER 11965 PRO B 766
TER 17903 PRO C 766
TER 23861 PRO D 766
MASTER 677 0 21 67 204 0 37 624713 4 405 228
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