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HEADER HYDROLASE 27-JAN-09 3G0B
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH
TITLE 2 TAK-322
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 39-766;
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION
COMPND 6 ANTIGEN CD26, TP103, ADENOSINE DEAMINASE COMPLEXING PROTEIN
COMPND 7 2, ADABP, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL
COMPND 8 PEPTIDASE IV MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE
COMPND 9 FORM, DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 10 EC: 3.4.14.5;
COMPND 11 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: 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,
KEYWDS 2 CELL MEMBRANE, GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE,
KEYWDS 3 SECRETED, SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ZHANG,M.B.WALLACE,J.FENG,J.A.STAFFORD,S.W.KALDOR,L.SHI,
AUTHOR 2 R.J.SKENE,K.AERTGEERTS,B.LEE,A.JENNINGS,R.XU,D.KASSEL,
AUTHOR 3 D.R.WEBB,S.L.GWALTNEY
REVDAT 1 16-FEB-10 3G0B 0
JRNL AUTH Z.ZHANG,M.B.WALLACE,J.FENG,J.A.STAFFORD,S.W.KALDOR,
JRNL AUTH 2 L.SHI,R.J.SKENE,K.AERTGEERTS,B.LEE,A.JENNINGS,R.XU,
JRNL AUTH 3 D.KASSEL,D.R.WEBB,S.L.GWALTNEY
JRNL TITL THE DESIGN AND SYNTHESIS OF PYRIMIDINONE AND
JRNL TITL 2 PYRIMIDINEDIONE INHIBITORS OF DIPEPTIDYL PEPTIDASE
JRNL TITL 3 IV
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 168006
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8857
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9868
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 530
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23873
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 562
REMARK 3 SOLVENT ATOMS : 557
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.98000
REMARK 3 B22 (A**2) : 2.55000
REMARK 3 B33 (A**2) : -0.38000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.288
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.215
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.178
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.970
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25170 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34266 ; 1.284 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2909 ; 6.339 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1236 ;33.639 ;23.956
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3987 ;16.974 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 119 ;18.000 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3661 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19257 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 11938 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 16953 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1293 ; 0.129 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 68 ; 0.201 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.129 ; 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): 14863 ; 0.435 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23540 ; 0.742 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12148 ; 1.089 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10725 ; 1.678 ; 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): 56.1361 34.5376 28.6239
REMARK 3 T TENSOR
REMARK 3 T11: -0.1249 T22: 0.0292
REMARK 3 T33: -0.0959 T12: 0.0524
REMARK 3 T13: -0.0652 T23: 0.0804
REMARK 3 L TENSOR
REMARK 3 L11: 1.9655 L22: 0.7186
REMARK 3 L33: 1.4753 L12: 0.1617
REMARK 3 L13: -0.3807 L23: 0.2729
REMARK 3 S TENSOR
REMARK 3 S11: -0.0686 S12: -0.5252 S13: -0.3363
REMARK 3 S21: 0.2772 S22: 0.0395 S23: -0.3226
REMARK 3 S31: 0.0712 S32: 0.4460 S33: 0.0291
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 800
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4114 29.8991 3.4946
REMARK 3 T TENSOR
REMARK 3 T11: -0.2405 T22: -0.2436
REMARK 3 T33: -0.2182 T12: 0.0113
REMARK 3 T13: 0.0365 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 2.2349 L22: 1.0433
REMARK 3 L33: 1.2091 L12: 0.2167
REMARK 3 L13: -0.2866 L23: 0.0327
REMARK 3 S TENSOR
REMARK 3 S11: -0.1164 S12: 0.2348 S13: -0.2934
REMARK 3 S21: -0.1658 S22: 0.0957 S23: -0.0720
REMARK 3 S31: 0.0155 S32: 0.0874 S33: 0.0207
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): -13.5903 32.9603 26.8222
REMARK 3 T TENSOR
REMARK 3 T11: -0.1423 T22: -0.0278
REMARK 3 T33: -0.0957 T12: 0.1154
REMARK 3 T13: 0.0568 T23: 0.0918
REMARK 3 L TENSOR
REMARK 3 L11: 2.2831 L22: 0.7932
REMARK 3 L33: 0.9223 L12: 0.5387
REMARK 3 L13: -0.0350 L23: 0.3475
REMARK 3 S TENSOR
REMARK 3 S11: -0.1017 S12: -0.3340 S13: 0.1375
REMARK 3 S21: -0.0342 S22: 0.0735 S23: 0.3038
REMARK 3 S31: -0.2366 S32: -0.3312 S33: 0.0283
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 800
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4870 13.0143 12.6316
REMARK 3 T TENSOR
REMARK 3 T11: -0.2223 T22: -0.2498
REMARK 3 T33: 0.0123 T12: 0.0156
REMARK 3 T13: 0.0717 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 2.1793 L22: 0.8201
REMARK 3 L33: 1.1678 L12: 0.2992
REMARK 3 L13: 0.0861 L23: -0.1399
REMARK 3 S TENSOR
REMARK 3 S11: -0.1134 S12: 0.0068 S13: -0.6614
REMARK 3 S21: -0.0683 S22: 0.0942 S23: 0.0344
REMARK 3 S31: 0.2186 S32: -0.0790 S33: 0.0192
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): 95.8698 -38.9092 52.5781
REMARK 3 T TENSOR
REMARK 3 T11: 0.0178 T22: 0.3209
REMARK 3 T33: 0.2313 T12: -0.0076
REMARK 3 T13: -0.1717 T23: 0.3439
REMARK 3 L TENSOR
REMARK 3 L11: 2.9328 L22: 1.8952
REMARK 3 L33: 1.2476 L12: 1.0086
REMARK 3 L13: 0.1830 L23: -0.5380
REMARK 3 S TENSOR
REMARK 3 S11: 0.2044 S12: -0.5404 S13: -0.6695
REMARK 3 S21: 0.2406 S22: -0.4405 S23: -0.9312
REMARK 3 S31: 0.1536 S32: 0.7736 S33: 0.2361
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 800
REMARK 3 ORIGIN FOR THE GROUP (A): 81.7377 -14.5662 39.5712
REMARK 3 T TENSOR
REMARK 3 T11: -0.0805 T22: -0.2136
REMARK 3 T33: -0.0724 T12: -0.0776
REMARK 3 T13: 0.0020 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 2.9604 L22: 1.7087
REMARK 3 L33: 1.3372 L12: 0.8943
REMARK 3 L13: 0.0481 L23: -0.2844
REMARK 3 S TENSOR
REMARK 3 S11: 0.1655 S12: -0.2027 S13: 0.5119
REMARK 3 S21: 0.1252 S22: -0.1962 S23: -0.2521
REMARK 3 S31: -0.3272 S32: 0.2998 S33: 0.0307
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): 27.1107 -32.0791 41.0177
REMARK 3 T TENSOR
REMARK 3 T11: -0.0937 T22: 0.1415
REMARK 3 T33: -0.1533 T12: 0.0076
REMARK 3 T13: 0.0749 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 3.0185 L22: 0.5145
REMARK 3 L33: 1.3204 L12: -0.0989
REMARK 3 L13: 0.8748 L23: -0.3882
REMARK 3 S TENSOR
REMARK 3 S11: 0.0982 S12: -0.6859 S13: 0.1153
REMARK 3 S21: 0.1935 S22: -0.0095 S23: 0.2366
REMARK 3 S31: -0.1256 S32: -0.6184 S33: -0.0887
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 800
REMARK 3 ORIGIN FOR THE GROUP (A): 50.0148 -24.9261 21.1233
REMARK 3 T TENSOR
REMARK 3 T11: -0.1598 T22: -0.1822
REMARK 3 T33: -0.2270 T12: 0.0912
REMARK 3 T13: 0.0398 T23: 0.0921
REMARK 3 L TENSOR
REMARK 3 L11: 2.6572 L22: 0.9192
REMARK 3 L33: 1.3191 L12: 0.2021
REMARK 3 L13: 0.3995 L23: -0.1127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0576 S12: 0.4288 S13: 0.3522
REMARK 3 S21: -0.1535 S22: -0.0440 S23: 0.0459
REMARK 3 S31: -0.1756 S32: -0.1325 S33: -0.0136
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: NULL
REMARK 4
REMARK 4 3G0B COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051261.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 182012
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG MME 2000, 0.06M NP_BICINE_
REMARK 280 NA, 0.04M BICINE, VAPOR DIFFUSION, TEMPERATURE 298K
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 61.19900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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: 57720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.5 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: 2
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: 4450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.3 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 ARG C 40
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 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 ND2 ASN A 229 C1 NAG A 805 1.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU C 177 CD GLU C 177 OE1 0.129
REMARK 500 GLU C 177 CD GLU C 177 OE2 0.148
REMARK 500 ASP C 274 CG ASP C 274 OD1 0.223
REMARK 500 ASP C 274 CG ASP C 274 OD2 0.204
REMARK 500 GLU C 309 CG GLU C 309 CD 0.159
REMARK 500 ASP C 329 CG ASP C 329 OD1 0.405
REMARK 500 ASP C 329 CG ASP C 329 OD2 0.260
REMARK 500 ASP C 331 CB ASP C 331 CG 0.165
REMARK 500 ASP C 331 CG ASP C 331 OD2 0.156
REMARK 500 GLU C 332 CD GLU C 332 OE1 0.083
REMARK 500 GLU C 332 CD GLU C 332 OE2 0.069
REMARK 500 TRP C 337 C TRP C 337 O 0.132
REMARK 500 ASN C 338 CB ASN C 338 CG 0.151
REMARK 500 ASN C 338 CG ASN C 338 ND2 0.562
REMARK 500 ARG C 343 CD ARG C 343 NE 0.184
REMARK 500 ARG C 343 NE ARG C 343 CZ 0.093
REMARK 500 ARG C 343 CZ ARG C 343 NH1 0.124
REMARK 500 ARG C 343 CZ ARG C 343 NH2 0.224
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP C 274 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP C 329 OD1 - CG - OD2 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP C 329 CB - CG - OD1 ANGL. DEV. = -17.6 DEGREES
REMARK 500 ARG C 343 NE - CZ - NH1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 LEU D 415 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 64 -159.66 -148.08
REMARK 500 GLN A 72 73.11 -68.37
REMARK 500 GLU A 73 -107.47 64.52
REMARK 500 SER A 106 107.58 -160.75
REMARK 500 GLN A 123 -104.40 -108.87
REMARK 500 TRP A 124 -147.74 -84.73
REMARK 500 HIS A 162 33.35 -144.07
REMARK 500 ILE A 193 -62.13 -127.95
REMARK 500 SER A 242 -161.04 62.82
REMARK 500 GLN A 320 39.11 -83.53
REMARK 500 ASN A 377 -169.95 -75.49
REMARK 500 ASP A 438 99.79 -169.90
REMARK 500 ASN A 450 79.72 -151.61
REMARK 500 ASP A 488 18.33 59.75
REMARK 500 GLN A 508 93.73 -68.10
REMARK 500 TYR A 547 -75.14 -118.27
REMARK 500 ARG A 597 47.66 -141.12
REMARK 500 THR A 600 -93.22 -124.82
REMARK 500 LYS A 615 0.96 -69.43
REMARK 500 SER A 630 -119.00 63.11
REMARK 500 ASP A 678 -97.69 -114.69
REMARK 500 ASN A 710 -72.28 -100.77
REMARK 500 GLN A 714 -46.94 -29.28
REMARK 500 ASP A 739 -162.48 -105.69
REMARK 500 HIS B 66 -10.95 -142.40
REMARK 500 GLN B 72 -68.83 -91.49
REMARK 500 ASN B 74 -12.67 67.73
REMARK 500 SER B 93 52.99 -90.81
REMARK 500 GLN B 123 -97.87 -105.46
REMARK 500 TRP B 124 -148.52 -94.41
REMARK 500 HIS B 162 35.02 -146.76
REMARK 500 ILE B 193 -58.78 -123.99
REMARK 500 SER B 242 -161.68 72.52
REMARK 500 GLN B 320 36.46 -87.60
REMARK 500 LYS B 423 16.67 56.69
REMARK 500 ASP B 488 24.32 49.68
REMARK 500 GLU B 521 29.34 44.12
REMARK 500 TYR B 547 -71.89 -121.88
REMARK 500 ARG B 597 48.26 -150.84
REMARK 500 THR B 600 -104.73 -123.94
REMARK 500 SER B 630 -118.92 62.24
REMARK 500 ASP B 678 -94.42 -106.51
REMARK 500 ALA B 707 31.63 -95.94
REMARK 500 ASN B 710 -71.57 -102.60
REMARK 500 ASP B 739 -156.86 -99.71
REMARK 500 ILE B 742 54.18 35.10
REMARK 500 GLU C 73 -82.65 64.30
REMARK 500 SER C 93 70.57 -153.59
REMARK 500 GLN C 123 -101.05 -103.70
REMARK 500 TRP C 124 -150.13 -92.52
REMARK 500
REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASN C 338 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 575 23.5 L L OUTSIDE RANGE
REMARK 500 VAL B 665 23.2 L L OUTSIDE RANGE
REMARK 500 VAL D 665 24.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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 801
REMARK 610 NAG A 804
REMARK 610 NAG A 811
REMARK 610 NAG A 812
REMARK 610 NAG B 801
REMARK 610 NAG B 802
REMARK 610 NAG B 807
REMARK 610 NAG B 808
REMARK 610 NAG C 802
REMARK 610 NAG C 805
REMARK 610 NAG C 807
REMARK 610 NAG D 803
REMARK 610 NAG D 808
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T22 A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T22 B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T22 C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T22 D 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3G0C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH A PYRIMIDINEDIONE INHIBITOR 1
REMARK 900 RELATED ID: 3G0D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH A PYRIMIDINEDIONE INHIBITOR 2
REMARK 900 RELATED ID: 3G0G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH A PYRIMIDINEDIONE INHIBITOR 3
DBREF 3G0B A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3G0B B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3G0B C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3G0B D 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 3G0B ALA A 27 UNP P27487 EXPRESSION TAG
SEQADV 3G0B ASP A 28 UNP P27487 EXPRESSION TAG
SEQADV 3G0B PRO A 29 UNP P27487 EXPRESSION TAG
SEQADV 3G0B GLY A 30 UNP P27487 EXPRESSION TAG
SEQADV 3G0B GLY A 31 UNP P27487 EXPRESSION TAG
SEQADV 3G0B SER A 32 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS A 33 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS A 34 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS A 35 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS A 36 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS A 37 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS A 38 UNP P27487 EXPRESSION TAG
SEQADV 3G0B ALA B 27 UNP P27487 EXPRESSION TAG
SEQADV 3G0B ASP B 28 UNP P27487 EXPRESSION TAG
SEQADV 3G0B PRO B 29 UNP P27487 EXPRESSION TAG
SEQADV 3G0B GLY B 30 UNP P27487 EXPRESSION TAG
SEQADV 3G0B GLY B 31 UNP P27487 EXPRESSION TAG
SEQADV 3G0B SER B 32 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS B 33 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS B 34 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS B 35 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS B 36 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS B 37 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS B 38 UNP P27487 EXPRESSION TAG
SEQADV 3G0B ALA C 27 UNP P27487 EXPRESSION TAG
SEQADV 3G0B ASP C 28 UNP P27487 EXPRESSION TAG
SEQADV 3G0B PRO C 29 UNP P27487 EXPRESSION TAG
SEQADV 3G0B GLY C 30 UNP P27487 EXPRESSION TAG
SEQADV 3G0B GLY C 31 UNP P27487 EXPRESSION TAG
SEQADV 3G0B SER C 32 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS C 33 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS C 34 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS C 35 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS C 36 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS C 37 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS C 38 UNP P27487 EXPRESSION TAG
SEQADV 3G0B ALA D 27 UNP P27487 EXPRESSION TAG
SEQADV 3G0B ASP D 28 UNP P27487 EXPRESSION TAG
SEQADV 3G0B PRO D 29 UNP P27487 EXPRESSION TAG
SEQADV 3G0B GLY D 30 UNP P27487 EXPRESSION TAG
SEQADV 3G0B GLY D 31 UNP P27487 EXPRESSION TAG
SEQADV 3G0B SER D 32 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS D 33 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS D 34 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS D 35 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS D 36 UNP P27487 EXPRESSION TAG
SEQADV 3G0B HIS D 37 UNP P27487 EXPRESSION TAG
SEQADV 3G0B 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 3G0B ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3G0B ASN C 321 ASN GLYCOSYLATION SITE
MODRES 3G0B ASN D 150 ASN GLYCOSYLATION SITE
MODRES 3G0B ASN D 281 ASN GLYCOSYLATION SITE
MODRES 3G0B ASN D 520 ASN GLYCOSYLATION SITE
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET NAG A 807 14
HET NAG A 808 14
HET NAG A 809 14
HET NAG A 810 14
HET NAG A 811 14
HET NAG A 812 14
HET T22 A 800 25
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 805 14
HET NAG B 806 14
HET NAG B 807 14
HET NAG B 808 14
HET T22 B 800 25
HET NAG C 802 14
HET NAG C 803 14
HET NAG C 804 14
HET NAG C 805 14
HET NAG C 806 14
HET NAG C 807 14
HET T22 C 800 25
HET NAG D 802 14
HET NAG D 803 14
HET NAG D 804 14
HET NAG D 805 14
HET NAG D 806 14
HET NAG D 807 14
HET NAG D 808 14
HET T22 D 800 25
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM T22 2-({6-[(3R)-3-AMINOPIPERIDIN-1-YL]-3-METHYL-2,4-DIOXO-
HETNAM 2 T22 3,4-DIHYDROPYRIMIDIN-1(2H)-YL}METHYL)BENZONITRILE
HETSYN NAG NAG
FORMUL 5 NAG 33(C8 H15 N O6)
FORMUL 13 T22 4(C18 H21 N5 O2)
FORMUL 34 HOH *557(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 PHE A 95 GLY A 99 5 5
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 VAL A 341 GLN A 344 5 4
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 GLN A 505 1 9
HELIX 8 8 ASN A 562 ASN A 572 1 11
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 VAL A 726 1 15
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 ASP B 200 VAL B 207 1 8
HELIX 21 21 ASP B 274 LEU B 276 5 3
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 GLN B 505 1 9
HELIX 26 26 ASN B 562 THR B 570 1 9
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 ARG B 658 TYR B 662 5 5
HELIX 32 32 ASP B 663 GLY B 672 1 10
HELIX 33 33 ASN B 679 SER B 686 1 8
HELIX 34 34 VAL B 688 VAL B 698 5 11
HELIX 35 35 PHE B 713 VAL B 726 1 14
HELIX 36 36 SER B 744 PHE B 763 1 20
HELIX 37 37 THR C 44 ASN C 51 1 8
HELIX 38 38 ASP C 200 VAL C 207 1 8
HELIX 39 39 PRO C 290 ILE C 295 1 6
HELIX 40 40 GLU C 421 MET C 425 5 5
HELIX 41 41 ASN C 497 LEU C 504 1 8
HELIX 42 42 ASN C 562 THR C 570 1 9
HELIX 43 43 GLY C 587 HIS C 592 1 6
HELIX 44 44 ALA C 593 ASN C 595 5 3
HELIX 45 45 THR C 600 MET C 616 1 17
HELIX 46 46 SER C 630 GLY C 641 1 12
HELIX 47 47 ARG C 658 TYR C 662 5 5
HELIX 48 48 ASP C 663 GLY C 672 1 10
HELIX 49 49 ASN C 679 SER C 686 1 8
HELIX 50 50 VAL C 688 VAL C 698 5 11
HELIX 51 51 HIS C 712 GLY C 727 1 16
HELIX 52 52 SER C 744 PHE C 763 1 20
HELIX 53 53 THR D 44 ASN D 51 1 8
HELIX 54 54 ASP D 200 VAL D 207 1 8
HELIX 55 55 PRO D 290 ILE D 295 1 6
HELIX 56 56 VAL D 341 GLN D 344 5 4
HELIX 57 57 GLU D 421 MET D 425 5 5
HELIX 58 58 ASN D 497 GLN D 505 1 9
HELIX 59 59 ASN D 562 THR D 570 1 9
HELIX 60 60 GLY D 587 HIS D 592 1 6
HELIX 61 61 ALA D 593 ASN D 595 5 3
HELIX 62 62 THR D 600 MET D 616 1 17
HELIX 63 63 SER D 630 GLY D 641 1 12
HELIX 64 64 ARG D 658 TYR D 662 5 5
HELIX 65 65 ASP D 663 GLY D 672 1 10
HELIX 66 66 ASN D 679 SER D 686 1 8
HELIX 67 67 VAL D 688 VAL D 698 5 11
HELIX 68 68 PHE D 713 GLY D 727 1 15
HELIX 69 69 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 LEU A 60 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 ILE A 76 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 B 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 C 4 ASP A 104 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
SHEET 4 C 4 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 ALA A 165 N THR A 156
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 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 H 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 ARG A 336 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 TRP A 305 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 I 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 I 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
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 LEU A 479 N CYS A 472
SHEET 4 L 4 GLY A 490 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 LEU A 543 O ILE A 574
SHEET 5 M 8 VAL A 619 TRP A 629 1 O TRP A 627 N VAL A 546
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 ILE A 703 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 LEU B 90 N ILE B 76
SHEET 1 P 4 ILE B 102 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 LYS B 175 N LEU B 164
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 LYS B 267 N GLN B 227
SHEET 4 S 4 SER B 284 ILE B 287 -1 O ILE B 287 N PHE B 268
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 U 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 U 4 ARG B 336 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 V 4 HIS B 298 THR B 307 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 V 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
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 GLN B 469 N SER B 460
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 Y 4 GLY B 490 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 ASP B 545 1 N LEU B 543 O ILE B 574
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
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 3 GLU C 67 GLN C 72 0
SHEET 2 AA 3 ASN C 75 ASN C 80 -1 O ASN C 75 N GLN C 72
SHEET 3 AA 3 SER C 86 LEU C 90 -1 O SER C 87 N VAL C 78
SHEET 1 AB 3 ASP C 104 ILE C 107 0
SHEET 2 AB 3 PHE C 113 LYS C 122 -1 O GLU C 117 N ASP C 104
SHEET 3 AB 3 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 1 AC 4 THR C 152 TRP C 157 0
SHEET 2 AC 4 LEU C 164 TRP C 168 -1 O VAL C 167 N GLN C 153
SHEET 3 AC 4 ASP C 171 LYS C 175 -1 O TYR C 173 N TYR C 166
SHEET 4 AC 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AD 3 ILE C 194 ASN C 196 0
SHEET 2 AD 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AE 4 ILE C 194 ASN C 196 0
SHEET 2 AE 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AE 4 THR C 265 ASN C 272 -1 O LYS C 267 N GLN C 227
SHEET 4 AE 4 ILE C 285 ILE C 287 -1 O ILE C 285 N VAL C 270
SHEET 1 AF 2 LEU C 235 PHE C 240 0
SHEET 2 AF 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AG 4 HIS C 298 THR C 307 0
SHEET 2 AG 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 AG 4 TYR C 322 TYR C 330 -1 O CYS C 328 N ILE C 311
SHEET 4 AG 4 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 1 AH 4 HIS C 298 THR C 307 0
SHEET 2 AH 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 AH 4 TYR C 322 TYR C 330 -1 O CYS C 328 N ILE C 311
SHEET 4 AH 4 HIS C 345 MET C 348 -1 O HIS C 345 N MET C 325
SHEET 1 AI 4 HIS C 363 PHE C 364 0
SHEET 2 AI 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AI 4 ARG C 382 GLN C 388 -1 O HIS C 383 N ILE C 375
SHEET 4 AI 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AJ 4 VAL C 404 LEU C 410 0
SHEET 2 AJ 4 TYR C 414 SER C 419 -1 O ILE C 418 N ILE C 405
SHEET 3 AJ 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AJ 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AK 4 TYR C 457 PHE C 461 0
SHEET 2 AK 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AK 4 LEU C 479 SER C 484 -1 O LEU C 479 N CYS C 472
SHEET 4 AK 4 GLY C 490 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AL 8 SER C 511 LEU C 519 0
SHEET 2 AL 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AL 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AL 8 TYR C 540 VAL C 546 1 N ASP C 545 O ALA C 576
SHEET 5 AL 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 544
SHEET 6 AL 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AL 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AL 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AM 4 LEU D 60 TRP D 62 0
SHEET 2 AM 4 GLU D 67 LYS D 71 -1 O LEU D 69 N ARG D 61
SHEET 3 AM 4 ILE D 76 ASN D 80 -1 O PHE D 79 N TYR D 68
SHEET 4 AM 4 SER D 86 LEU D 90 -1 O LEU D 90 N ILE D 76
SHEET 1 AN 4 ASP D 104 ILE D 107 0
SHEET 2 AN 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AN 4 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 4 AN 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AO 4 THR D 152 TRP D 157 0
SHEET 2 AO 4 LEU D 164 TRP D 168 -1 O VAL D 167 N TRP D 154
SHEET 3 AO 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AO 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AP 3 ILE D 194 ASN D 196 0
SHEET 2 AP 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AP 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AQ 4 ILE D 194 ASN D 196 0
SHEET 2 AQ 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AQ 4 THR D 265 ASN D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AQ 4 ILE D 285 ILE D 287 -1 O ILE D 287 N PHE D 268
SHEET 1 AR 2 LEU D 235 PHE D 240 0
SHEET 2 AR 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AS 4 HIS D 298 TRP D 305 0
SHEET 2 AS 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AS 4 TYR D 322 ASP D 331 -1 O CYS D 328 N ILE D 311
SHEET 4 AS 4 ARG D 336 CYS D 339 -1 O ASN D 338 N ASP D 329
SHEET 1 AT 4 HIS D 298 TRP D 305 0
SHEET 2 AT 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AT 4 TYR D 322 ASP D 331 -1 O CYS D 328 N ILE D 311
SHEET 4 AT 4 HIS D 345 MET D 348 -1 O HIS D 345 N MET D 325
SHEET 1 AU 4 HIS D 363 PHE D 364 0
SHEET 2 AU 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AU 4 ARG D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AU 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 AV 4 VAL D 404 LEU D 410 0
SHEET 2 AV 4 TYR D 414 SER D 419 -1 O TYR D 416 N ALA D 409
SHEET 3 AV 4 ASN D 430 GLN D 435 -1 O ILE D 434 N LEU D 415
SHEET 4 AV 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AW 4 CYS D 454 PHE D 461 0
SHEET 2 AW 4 TYR D 467 PRO D 475 -1 O GLY D 474 N GLN D 455
SHEET 3 AW 4 LEU D 479 SER D 484 -1 O LEU D 479 N CYS D 472
SHEET 4 AW 4 GLY D 490 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AX 8 SER D 511 LEU D 519 0
SHEET 2 AX 8 THR D 522 LEU D 530 -1 O LEU D 530 N SER D 511
SHEET 3 AX 8 ILE D 574 ASP D 579 -1 O VAL D 575 N ILE D 529
SHEET 4 AX 8 TYR D 540 VAL D 546 1 N ASP D 545 O ALA D 576
SHEET 5 AX 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 542
SHEET 6 AX 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AX 8 GLU D 699 GLY D 705 1 O ILE D 703 N ALA D 652
SHEET 8 AX 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 2.03
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 2.05
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.04
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.02
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.04
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.04
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.04
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.04
SSBOND 13 CYS C 444 CYS C 447 1555 1555 2.04
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.04
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.04
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.04
SSBOND 17 CYS D 385 CYS D 394 1555 1555 2.03
SSBOND 18 CYS D 444 CYS D 447 1555 1555 2.03
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.06
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.03
LINK ND2 ASN A 150 C1 NAG A 802 1555 1555 1.45
LINK ND2 ASN C 321 C1 NAG C 806 1555 1555 1.45
LINK ND2 ASN D 150 C1 NAG D 802 1555 1555 1.39
LINK ND2 ASN D 281 C1 NAG D 806 1555 1555 1.45
LINK ND2 ASN D 520 C1 NAG D 807 1555 1555 1.45
LINK O4 NAG A 802 C1 NAG A 803 1555 1555 1.45
LINK O4 NAG A 805 C1 NAG A 806 1555 1555 1.44
LINK O4 NAG A 807 C1 NAG A 808 1555 1555 1.45
LINK O4 NAG A 809 C1 NAG A 810 1555 1555 1.45
LINK O4 NAG B 803 C1 NAG B 804 1555 1555 1.45
LINK O4 NAG B 805 C1 NAG B 806 1555 1555 1.44
LINK O4 NAG C 803 C1 NAG C 804 1555 1555 1.44
LINK O4 NAG D 804 C1 NAG D 805 1555 1555 1.44
LINK ND2 ASN D 150 O5 NAG D 802 1555 1555 1.51
CISPEP 1 GLY A 474 PRO A 475 0 8.26
CISPEP 2 GLY B 474 PRO B 475 0 8.30
CISPEP 3 GLY C 474 PRO C 475 0 9.84
CISPEP 4 GLY D 474 PRO D 475 0 5.88
SITE 1 AC1 4 ASN A 80 ASN A 85 SER A 86 SER A 87
SITE 1 AC2 4 ARG A 147 ILE A 148 ASN A 150 NAG A 803
SITE 1 AC3 1 NAG A 802
SITE 1 AC4 3 ASN A 219 THR A 221 GLU A 309
SITE 1 AC5 4 ILE A 194 ASN A 229 THR A 231 NAG A 806
SITE 1 AC6 2 GLU A 232 NAG A 805
SITE 1 AC7 3 TRP A 187 ASN A 281 NAG A 808
SITE 1 AC8 1 NAG A 807
SITE 1 AC9 4 ASN A 321 SER A 349 ARG A 596 NAG A 810
SITE 1 BC1 1 NAG A 809
SITE 1 BC2 6 LEU A 519 ASN A 520 PHE A 524 ARG A 581
SITE 2 BC2 6 ASP A 605 HOH B 944
SITE 1 BC3 3 ASP A 681 ARG A 684 ASN A 685
SITE 1 BC4 6 GLU B 67 VAL B 78 ASN B 80 ASN B 85
SITE 2 BC4 6 SER B 87 HOH B1253
SITE 1 BC5 1 ASN B 150
SITE 1 BC6 5 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC6 5 NAG B 804
SITE 1 BC7 3 ASN B 272 GLU B 332 NAG B 803
SITE 1 BC8 5 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 BC8 5 NAG B 806
SITE 1 BC9 1 NAG B 805
SITE 1 CC1 2 TRP B 187 ASN B 281
SITE 1 CC2 2 ASN B 321 SER B 349
SITE 1 CC3 1 ASN C 150
SITE 1 CC4 4 ASN C 229 THR C 231 GLU C 232 NAG C 804
SITE 1 CC5 1 NAG C 803
SITE 1 CC6 2 TRP C 187 ASN C 281
SITE 1 CC7 4 ASN C 321 MET C 348 SER C 349 THR C 350
SITE 1 CC8 6 LEU C 519 ASN C 520 PHE C 524 ARG C 581
SITE 2 CC8 6 ASP C 605 GLU C 608
SITE 1 CC9 1 ASN D 150
SITE 1 DC1 4 ASN D 219 THR D 221 GLN D 308 GLU D 309
SITE 1 DC2 6 ILE D 194 ASN D 229 THR D 231 GLU D 232
SITE 2 DC2 6 LYS D 267 NAG D 805
SITE 1 DC3 1 NAG D 804
SITE 1 DC4 1 ASN D 281
SITE 1 DC5 4 LEU D 519 ASN D 520 PHE D 524 ARG D 581
SITE 1 DC6 2 ASP D 681 ASN D 685
SITE 1 DC7 12 HOH A 1 ARG A 125 GLU A 205 GLU A 206
SITE 2 DC7 12 TYR A 547 TRP A 629 SER A 630 TYR A 631
SITE 3 DC7 12 VAL A 656 TYR A 662 TYR A 666 VAL A 711
SITE 1 DC8 11 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 DC8 11 SER B 630 TYR B 631 VAL B 656 TYR B 662
SITE 3 DC8 11 TYR B 666 VAL B 711 HOH B1157
SITE 1 DC9 11 HOH B 954 ARG C 125 GLU C 205 GLU C 206
SITE 2 DC9 11 TYR C 547 SER C 630 TYR C 631 VAL C 656
SITE 3 DC9 11 TYR C 662 TYR C 666 VAL C 711
SITE 1 EC1 12 HOH B 955 ARG D 125 GLU D 205 GLU D 206
SITE 2 EC1 12 TYR D 547 TRP D 629 SER D 630 TYR D 631
SITE 3 EC1 12 VAL D 656 TYR D 662 TYR D 666 ASN D 710
CRYST1 121.686 122.398 144.010 90.00 114.72 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 0.008218 0.000000 0.003784 0.00000
SCALE2 0.000000 0.008170 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007645 0.00000
TER 5958 PRO A 766
TER 11972 PRO B 766
TER 17919 PRO C 766
TER 23877 PRO D 766
MASTER 791 0 37 69 198 0 51 624992 4 607 228
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