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HEADER HYDROLASE 30-OCT-03 1R9M
TITLE CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV AT 2.1
TITLE 2 ANG. RESOLUTION.
CAVEAT 1R9M CHRIALITY ERROR AT CA CENTER OF GLU C 73 AND ASN C 74
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26, TP103,
COMPND 5 ADENOSINE DEAMINASE COMPLEXING PROTEIN-2, ADABP;
COMPND 6 EC: 3.4.14.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DPP4, ADCP2, CD26;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PFASTBACHTB
KEYWDS AMINOPEPTIDASE, SERINE PROTEASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.AERTGEERTS,S.YE,M.G.TENNANT,B.COLLINS,J.ROGERS,B.C.SANG,
AUTHOR 2 R.J.SKENE,D.R.WEBB,G.S.PRASAD
REVDAT 1 29-JUN-04 1R9M 0
JRNL AUTH K.AERTGEERTS,S.YE,M.G.TENNANT,M.L.KRAUS,J.ROGERS,
JRNL AUTH 2 B.C.SANG,R.J.SKENE,D.R.WEBB,G.S.PRASAD
JRNL TITL CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV
JRNL TITL 2 IN COMPLEX WITH A DECAPEPTIDE REVEALS DETAILS ON
JRNL TITL 3 SUBSTRATE SPECIFICITY AND TETRAHEDRAL INTERMEDIATE
JRNL TITL 4 FORMATION.
JRNL REF PROTEIN SCI. V. 13 412 2004
JRNL REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 213577
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4355
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11728
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 203
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 26111
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.79000
REMARK 3 B22 (A**2) : 1.73000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.35000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.226
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.549
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25187 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34215 ; 1.457 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2910 ; 4.245 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4156 ;18.986 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3719 ; 0.158 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19225 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 11804 ; 0.233 ; 0.300
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): 2492 ; 0.146 ; 0.500
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): 40 ; 0.293 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.316 ; 0.500
REMARK 3 SYMMETRY H-BOND 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): 14514 ; 0.513 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23546 ; 0.714 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10673 ; 1.268 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10669 ; 1.588 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 40 A 766 1
REMARK 3 1 B 40 B 766 1
REMARK 3 1 C 40 C 766 1
REMARK 3 1 D 40 D 766 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 5946 ; 0.43 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 5946 ; 0.39 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 5946 ; 0.43 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 5946 ; 0.40 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 5946 ; 0.22 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 5946 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 5946 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 5946 ; 0.21 ; 0.50
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 : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 40 A 55
REMARK 3 RESIDUE RANGE : A 232 A 262
REMARK 3 RESIDUE RANGE : A 500 A 766
REMARK 3 RESIDUE RANGE : A 5201 A 6851
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2989 -0.5036 6.5209
REMARK 3 T TENSOR
REMARK 3 T11: 0.0780 T22: 0.0025
REMARK 3 T33: 0.0717 T12: 0.0124
REMARK 3 T13: 0.0054 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 1.5808 L22: 0.7988
REMARK 3 L33: 1.0837 L12: 0.2230
REMARK 3 L13: 0.3965 L23: 0.0119
REMARK 3 S TENSOR
REMARK 3 S11: -0.0911 S12: 0.1013 S13: 0.1825
REMARK 3 S21: -0.1164 S22: 0.0540 S23: 0.0933
REMARK 3 S31: 0.0074 S32: -0.0624 S33: 0.0372
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 56 A 231
REMARK 3 RESIDUE RANGE : A 263 A 499
REMARK 3 RESIDUE RANGE : A 851 A 3212
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0531 -6.1665 29.4930
REMARK 3 T TENSOR
REMARK 3 T11: 0.2021 T22: 0.2474
REMARK 3 T33: 0.2212 T12: 0.0078
REMARK 3 T13: 0.0947 T23: -0.0805
REMARK 3 L TENSOR
REMARK 3 L11: 1.5144 L22: 0.8871
REMARK 3 L33: 1.4508 L12: 0.0357
REMARK 3 L13: 0.4823 L23: -0.2830
REMARK 3 S TENSOR
REMARK 3 S11: -0.0737 S12: -0.3871 S13: 0.2624
REMARK 3 S21: 0.2622 S22: -0.0092 S23: 0.2694
REMARK 3 S31: -0.0336 S32: -0.3293 S33: 0.0829
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 34 B 55
REMARK 3 RESIDUE RANGE : B 232 B 262
REMARK 3 RESIDUE RANGE : B 500 B 766
REMARK 3 RESIDUE RANGE : B 5201 B 6851
REMARK 3 ORIGIN FOR THE GROUP (A): 54.5431 13.4337 13.1463
REMARK 3 T TENSOR
REMARK 3 T11: 0.0948 T22: 0.0530
REMARK 3 T33: 0.1632 T12: 0.0212
REMARK 3 T13: -0.0228 T23: -0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 1.3431 L22: 0.7286
REMARK 3 L33: 0.7982 L12: 0.2144
REMARK 3 L13: -0.0482 L23: -0.1037
REMARK 3 S TENSOR
REMARK 3 S11: -0.0737 S12: 0.0364 S13: 0.3101
REMARK 3 S21: -0.0062 S22: 0.0562 S23: -0.0897
REMARK 3 S31: -0.1315 S32: 0.1110 S33: 0.0175
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 56 B 231
REMARK 3 RESIDUE RANGE : B 263 B 499
REMARK 3 RESIDUE RANGE : B 851 B 3211
REMARK 3 ORIGIN FOR THE GROUP (A): 76.2286 -4.4256 27.1128
REMARK 3 T TENSOR
REMARK 3 T11: 0.1731 T22: 0.2261
REMARK 3 T33: 0.2209 T12: 0.0807
REMARK 3 T13: -0.0528 T23: -0.0990
REMARK 3 L TENSOR
REMARK 3 L11: 1.1339 L22: 0.8766
REMARK 3 L33: 1.0406 L12: 0.1284
REMARK 3 L13: -0.0771 L23: -0.4861
REMARK 3 S TENSOR
REMARK 3 S11: -0.0925 S12: -0.0809 S13: -0.0357
REMARK 3 S21: 0.0132 S22: 0.0608 S23: -0.2717
REMARK 3 S31: 0.1816 S32: 0.2056 S33: 0.0316
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 40 C 55
REMARK 3 RESIDUE RANGE : C 232 C 262
REMARK 3 RESIDUE RANGE : C 500 C 766
REMARK 3 RESIDUE RANGE : C 5201 C 5201
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4937 47.0898 39.2473
REMARK 3 T TENSOR
REMARK 3 T11: 0.1686 T22: 0.1230
REMARK 3 T33: 0.1903 T12: -0.0307
REMARK 3 T13: -0.0031 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 1.7943 L22: 1.3114
REMARK 3 L33: 0.9735 L12: 0.4609
REMARK 3 L13: -0.0276 L23: 0.2983
REMARK 3 S TENSOR
REMARK 3 S11: 0.0938 S12: -0.1330 S13: -0.3277
REMARK 3 S21: 0.0539 S22: -0.1124 S23: 0.1936
REMARK 3 S31: 0.2197 S32: -0.2128 S33: 0.0186
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 56 C 231
REMARK 3 RESIDUE RANGE : C 263 C 499
REMARK 3 RESIDUE RANGE : C 1501 C 3211
REMARK 3 ORIGIN FOR THE GROUP (A): -36.4647 69.6420 52.5143
REMARK 3 T TENSOR
REMARK 3 T11: 0.2322 T22: 0.4324
REMARK 3 T33: 0.2782 T12: 0.0658
REMARK 3 T13: 0.0483 T23: -0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 1.4308 L22: 1.4741
REMARK 3 L33: 1.0882 L12: 0.1512
REMARK 3 L13: 0.1049 L23: 0.4632
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: -0.0933 S13: 0.0596
REMARK 3 S21: 0.0362 S22: -0.1421 S23: 0.4031
REMARK 3 S31: -0.1514 S32: -0.4788 S33: 0.1256
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 39 D 55
REMARK 3 RESIDUE RANGE : D 232 D 262
REMARK 3 RESIDUE RANGE : D 500 D 766
REMARK 3 RESIDUE RANGE : D 5201 D 6851
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4835 55.0082 23.3617
REMARK 3 T TENSOR
REMARK 3 T11: 0.1212 T22: 0.0343
REMARK 3 T33: 0.0975 T12: 0.0505
REMARK 3 T13: -0.0130 T23: -0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 1.9992 L22: 0.8916
REMARK 3 L33: 1.1357 L12: 0.1193
REMARK 3 L13: -0.3203 L23: 0.2054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0561 S12: 0.1264 S13: -0.2741
REMARK 3 S21: -0.1110 S22: -0.0318 S23: -0.0542
REMARK 3 S31: 0.1141 S32: 0.1184 S33: -0.0243
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 56 D 231
REMARK 3 RESIDUE RANGE : D 263 D 499
REMARK 3 RESIDUE RANGE : D 1501 D 3211
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7547 62.0746 40.3431
REMARK 3 T TENSOR
REMARK 3 T11: 0.1923 T22: 0.4724
REMARK 3 T33: 0.1785 T12: -0.0155
REMARK 3 T13: -0.0257 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 2.0657 L22: 0.8012
REMARK 3 L33: 1.3310 L12: -0.2280
REMARK 3 L13: -0.5766 L23: 0.5814
REMARK 3 S TENSOR
REMARK 3 S11: 0.0475 S12: -0.6599 S13: -0.1086
REMARK 3 S21: 0.1849 S22: 0.0084 S23: -0.1788
REMARK 3 S31: 0.1066 S32: 0.4932 S33: -0.0559
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1R9M COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-2003.
REMARK 100 THE RCSB ID CODE IS RCSB020608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-2002
REMARK 200 TEMPERATURE (KELVIN) : 173.0
REMARK 200 PH : 7.50
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) : 1.01
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ALS-DCS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 218087
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, PH 7.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, 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,1/2+Y,-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 62.02800
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 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 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 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 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 40 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
REMARK 500 O4 MAN C 2293 O5 MAN C 2294 1.46
REMARK 500 ND2 ASN A 85 O5 NAG A 851 1.57
REMARK 500 ND2 ASN C 520 O5 NAG C 5201 1.74
REMARK 500 O4 MAN C 2293 C5 MAN C 2294 1.84
REMARK 500 O4 NAG A 3211 O5 NAG A 3212 1.92
REMARK 500 ND2 ASN A 281 O5 NAG A 2811 1.97
REMARK 500 ND2 ASN B 229 O5 NAG B 2291 1.97
REMARK 500 O4 NAG B 2291 C2 NAG B 2292 2.00
REMARK 500 NE2 GLN C 731 NE2 GLN D 731 2.03
REMARK 500 O GLN A 72 N ASN A 74 2.05
REMARK 500 N GLY B 599 OE2 GLU B 602 2.07
REMARK 500 OE2 GLU C 660 NH2 ARG C 684 2.07
REMARK 500 ND2 ASN A 520 C2 NAG A 5201 2.08
REMARK 500 NE2 GLN B 435 OG SER B 437 2.08
REMARK 500 O4 NAG B 2191 O5 NAG B 2192 2.08
REMARK 500 C4 NAG C 2292 C1 MAN C 2293 2.08
REMARK 500 O4 NAG D 2291 O5 NAG D 2292 2.09
REMARK 500 ND2 ASN D 150 O5 NAG D 1501 2.11
REMARK 500 O6 NAG B 1501 O5 FUC B 1502 2.11
REMARK 500 ND2 ASN A 685 O5 NAG A 6851 2.12
REMARK 500 ND2 ASN D 229 O5 NAG D 2291 2.12
REMARK 500 ND2 ASN A 219 C2 NAG A 2191 2.13
REMARK 500 ND2 ASN B 150 O5 NAG B 1501 2.13
REMARK 500 O4 NAG D 2291 C2 NAG D 2292 2.13
REMARK 500 ND2 ASN A 219 N2 NAG A 2191 2.15
REMARK 500 OE2 GLU A 660 NH2 ARG A 684 2.15
REMARK 500 OE2 GLU B 206 OD2 ASP B 663 2.16
REMARK 500 ND2 ASN B 520 C2 NAG B 5201 2.16
REMARK 500 O GLU A 146 NZ LYS A 175 2.17
REMARK 500 ND2 ASN B 520 O5 NAG B 5201 2.17
REMARK 500 ND2 ASN C 281 C2 NAG C 2811 2.18
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 ND1 HIS B 36 OE1 GLN D 388 2645 1.96
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 70 C LYS A 71 N -0.074
REMARK 500 GLU A 73 C ASN A 74 N 0.073
REMARK 500 ARG A 140 C GLN A 141 N 0.094
REMARK 500 VAL A 279 CA VAL A 279 C -0.052
REMARK 500 MET A 293 SD MET A 293 CE -0.092
REMARK 500 MET A 325 SD MET A 325 CE -0.102
REMARK 500 MET A 616 SD MET A 616 CE 0.053
REMARK 500 LYS B 258 CB LYS B 258 CG 0.054
REMARK 500 MET B 293 SD MET B 293 CE -0.075
REMARK 500 MET B 325 SD MET B 325 CE -0.082
REMARK 500 MET B 638 SD MET B 638 CE 0.077
REMARK 500 GLU C 73 CA GLU C 73 C -0.052
REMARK 500 ASN C 74 CA ASN C 74 CB -0.061
REMARK 500 ASN C 74 CA ASN C 74 C -0.072
REMARK 500 VAL C 279 CA VAL C 279 C -0.052
REMARK 500 MET C 638 SD MET C 638 CE 0.073
REMARK 500 MET C 689 SD MET C 689 CE -0.053
REMARK 500 MET C 733 SD MET C 733 CE 0.053
REMARK 500 THR C 736 CB THR C 736 CG2 0.052
REMARK 500 MET C 755 SD MET C 755 CE -0.066
REMARK 500 MET D 425 SD MET D 425 CE -0.051
REMARK 500 MET D 591 SD MET D 591 CE -0.081
REMARK 500 ARG D 658 CB ARG D 658 CG -0.061
REMARK 500 MET D 671 SD MET D 671 CE 0.079
REMARK 500 MET D 755 SD MET D 755 CE -0.055
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN A 74 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 GLU A 73 CA - C - N ANGL. DEV. =-16.3 DEGREES
REMARK 500 GLU A 73 O - C - N ANGL. DEV. = 10.3 DEGREES
REMARK 500 ASN A 75 N - CA - CB ANGL. DEV. = -9.5 DEGREES
REMARK 500 ASN A 75 C - N - CA ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG A 140 CA - C - O ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG A 140 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 LEU A 276 C - N - CA ANGL. DEV. =-13.4 DEGREES
REMARK 500 LEU A 276 O - C - N ANGL. DEV. =-10.5 DEGREES
REMARK 500 VAL A 279 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 VAL A 279 O - C - N ANGL. DEV. =-15.0 DEGREES
REMARK 500 LEU A 300 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 LEU A 313 CA - CB - CG ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLN A 388 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 ILE A 529 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 VAL A 656 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 GLN B 388 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 PRO B 541 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLU C 73 CB - CG - CD ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASN C 74 CB - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 ASN C 74 CA - C - O ANGL. DEV. = 18.6 DEGREES
REMARK 500 GLU C 73 O - C - N ANGL. DEV. =-10.5 DEGREES
REMARK 500 ASN C 74 C - N - CA ANGL. DEV. =-10.4 DEGREES
REMARK 500 ASN C 74 O - C - N ANGL. DEV. =-25.0 DEGREES
REMARK 500 VAL C 279 CA - C - O ANGL. DEV. = 14.5 DEGREES
REMARK 500 VAL C 279 O - C - N ANGL. DEV. =-16.3 DEGREES
REMARK 500 ILE C 319 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 LEU C 415 CA - CB - CG ANGL. DEV. = 9.5 DEGREES
REMARK 500 GLY C 617 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 VAL C 656 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 LYS D 41 O - C - N ANGL. DEV. = -9.8 DEGREES
REMARK 500 SER D 93 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 LYS D 139 CB - CA - C ANGL. DEV. =-12.2 DEGREES
REMARK 500 ARG D 140 CB - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 LEU D 300 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 ILE D 319 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 SER D 458 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 VAL D 656 N - CA - C ANGL. DEV. = -9.4 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 630 -119.65 70.29
REMARK 500 SER B 630 -118.51 66.60
REMARK 500 SER D 630 -116.11 67.52
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 GLN A 72 GLU A 73 -126.53
REMARK 500 ASN A 74 ASN A 75 -148.79
REMARK 500 SER C 278 VAL C 279 -138.93
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 359 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH 397 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH 410 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH 515 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH 533 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH 711 DISTANCE = 5.60 ANGSTROMS
REMARK 525 HOH 743 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH 753 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH 769 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH 809 DISTANCE = 9.20 ANGSTROMS
REMARK 525 HOH 850 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH 886 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH 913 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH 914 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH 915 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH 920 DISTANCE = 8.53 ANGSTROMS
REMARK 525 HOH 921 DISTANCE = 5.60 ANGSTROMS
REMARK 525 HOH 923 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH 967 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH 969 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH 987 DISTANCE = 5.80 ANGSTROMS
REMARK 525 HOH 989 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH 1015 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH 1023 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH 1053 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH 1055 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH 1056 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH 1064 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH 1065 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH 1070 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH 1094 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH 1111 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH 1131 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH 1134 DISTANCE = 9.24 ANGSTROMS
REMARK 525 HOH 1142 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH 1145 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH 1152 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH 1177 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH 1186 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH 1198 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH 1215 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH 1216 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH 1220 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH 1222 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH 1227 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH 1235 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH 1237 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH 1239 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH 1240 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH 1251 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH 1259 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH 1265 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH 1281 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH 1287 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH 1296 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH 1298 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH 1334 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH 1335 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH 1337 DISTANCE = 5.60 ANGSTROMS
REMARK 525 HOH 1339 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH 1350 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH 1361 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH 1366 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH 1378 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH 1391 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH 1403 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH 1409 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH 1411 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH 1433 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH 1440 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH 1442 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH 1444 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH 1447 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH 1450 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH 1452 DISTANCE = 8.39 ANGSTROMS
REMARK 525 HOH 1453 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH 1456 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH 1457 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH 1458 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH 1460 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH 1465 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH 1466 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH 1467 DISTANCE = 10.10 ANGSTROMS
REMARK 525 HOH 1475 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH 1480 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH 1486 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH 1489 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH 1493 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH 1495 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH 1499 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH 1502 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH 1509 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH 1510 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH 1511 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH 1512 DISTANCE = 5.78 ANGSTROMS
REMARK 525 HOH 1513 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH 1532 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH 1535 DISTANCE = 7.75 ANGSTROMS
REMARK 525 HOH 1536 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH 1541 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH 1542 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH 1548 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH 1572 DISTANCE = 8.56 ANGSTROMS
REMARK 525 HOH 1575 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH 1579 DISTANCE = 5.78 ANGSTROMS
REMARK 525 HOH 1580 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH 1581 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH 1583 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH 1587 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH 1588 DISTANCE = 8.90 ANGSTROMS
REMARK 525 HOH 1590 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH 1601 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH 1606 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH 1607 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH 1608 DISTANCE = 8.33 ANGSTROMS
REMARK 525 HOH 1610 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH 1613 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH 1629 DISTANCE = 5.72 ANGSTROMS
REMARK 525 HOH 1630 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH 1632 DISTANCE = 8.72 ANGSTROMS
REMARK 525 HOH 1634 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH 1640 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH 1642 DISTANCE = 9.16 ANGSTROMS
REMARK 525 HOH 1647 DISTANCE = 8.35 ANGSTROMS
REMARK 525 HOH 1658 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH 1662 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH 1666 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH 1669 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH 1671 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH 1677 DISTANCE = 7.17 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R9N RELATED DB: PDB
DBREF 1R9M A 39 766 SWS P27487 DPP4_HUMAN 39 766
DBREF 1R9M B 39 766 SWS P27487 DPP4_HUMAN 39 766
DBREF 1R9M C 39 766 SWS P27487 DPP4_HUMAN 39 766
DBREF 1R9M D 39 766 SWS P27487 DPP4_HUMAN 39 766
SEQADV 1R9M HIS A 34 SWS P27487 HIS TAG
SEQADV 1R9M HIS A 35 SWS P27487 HIS TAG
SEQADV 1R9M HIS A 36 SWS P27487 HIS TAG
SEQADV 1R9M HIS A 37 SWS P27487 HIS TAG
SEQADV 1R9M HIS A 38 SWS P27487 HIS TAG
SEQADV 1R9M HIS B 34 SWS P27487 HIS TAG
SEQADV 1R9M HIS B 35 SWS P27487 HIS TAG
SEQADV 1R9M HIS B 36 SWS P27487 HIS TAG
SEQADV 1R9M HIS B 37 SWS P27487 HIS TAG
SEQADV 1R9M HIS B 38 SWS P27487 HIS TAG
SEQADV 1R9M HIS C 34 SWS P27487 HIS TAG
SEQADV 1R9M HIS C 35 SWS P27487 HIS TAG
SEQADV 1R9M HIS C 36 SWS P27487 HIS TAG
SEQADV 1R9M HIS C 37 SWS P27487 HIS TAG
SEQADV 1R9M HIS C 38 SWS P27487 HIS TAG
SEQADV 1R9M HIS D 34 SWS P27487 HIS TAG
SEQADV 1R9M HIS D 35 SWS P27487 HIS TAG
SEQADV 1R9M HIS D 36 SWS P27487 HIS TAG
SEQADV 1R9M HIS D 37 SWS P27487 HIS TAG
SEQADV 1R9M HIS D 38 SWS P27487 HIS TAG
SEQRES 1 A 733 HIS HIS HIS HIS HIS SER ARG LYS THR TYR THR LEU THR
SEQRES 2 A 733 ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER
SEQRES 3 A 733 LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN
SEQRES 4 A 733 GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN
SEQRES 5 A 733 SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE
SEQRES 6 A 733 GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY
SEQRES 7 A 733 GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP
SEQRES 8 A 733 ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU
SEQRES 9 A 733 ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN
SEQRES 10 A 733 ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS
SEQRES 11 A 733 LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE
SEQRES 12 A 733 GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY
SEQRES 13 A 733 LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL
SEQRES 14 A 733 TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP
SEQRES 15 A 733 TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE
SEQRES 16 A 733 ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR
SEQRES 17 A 733 SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL
SEQRES 18 A 733 PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS
SEQRES 19 A 733 PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL THR
SEQRES 20 A 733 ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER MET
SEQRES 21 A 733 LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA
SEQRES 22 A 733 THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE
SEQRES 23 A 733 GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU
SEQRES 24 A 733 SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS
SEQRES 25 A 733 ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE ARG
SEQRES 26 A 733 PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE
SEQRES 27 A 733 TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE
SEQRES 28 A 733 CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE
SEQRES 29 A 733 THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU
SEQRES 30 A 733 THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS
SEQRES 31 A 733 GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU
SEQRES 32 A 733 SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU
SEQRES 33 A 733 ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER
SEQRES 34 A 733 LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO
SEQRES 35 A 733 GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP
SEQRES 36 A 733 LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP
SEQRES 37 A 733 LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU
SEQRES 38 A 733 ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN
SEQRES 39 A 733 MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR
SEQRES 40 A 733 PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN
SEQRES 41 A 733 LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR
SEQRES 42 A 733 LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP
SEQRES 43 A 733 GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS
SEQRES 44 A 733 ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP
SEQRES 45 A 733 GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE
SEQRES 46 A 733 VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR
SEQRES 47 A 733 GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY SER
SEQRES 48 A 733 GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER
SEQRES 49 A 733 ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR
SEQRES 50 A 733 MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR
SEQRES 51 A 733 ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE LYS
SEQRES 52 A 733 GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP
SEQRES 53 A 733 ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA
SEQRES 54 A 733 LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR
SEQRES 55 A 733 THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS
SEQRES 56 A 733 GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN
SEQRES 57 A 733 CYS PHE SER LEU PRO
SEQRES 1 B 733 HIS HIS HIS HIS HIS SER ARG LYS THR TYR THR LEU THR
SEQRES 2 B 733 ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER
SEQRES 3 B 733 LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN
SEQRES 4 B 733 GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN
SEQRES 5 B 733 SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE
SEQRES 6 B 733 GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY
SEQRES 7 B 733 GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP
SEQRES 8 B 733 ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU
SEQRES 9 B 733 ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN
SEQRES 10 B 733 ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS
SEQRES 11 B 733 LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE
SEQRES 12 B 733 GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY
SEQRES 13 B 733 LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL
SEQRES 14 B 733 TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP
SEQRES 15 B 733 TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE
SEQRES 16 B 733 ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR
SEQRES 17 B 733 SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL
SEQRES 18 B 733 PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS
SEQRES 19 B 733 PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL THR
SEQRES 20 B 733 ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER MET
SEQRES 21 B 733 LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA
SEQRES 22 B 733 THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE
SEQRES 23 B 733 GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU
SEQRES 24 B 733 SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS
SEQRES 25 B 733 ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE ARG
SEQRES 26 B 733 PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE
SEQRES 27 B 733 TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE
SEQRES 28 B 733 CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE
SEQRES 29 B 733 THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU
SEQRES 30 B 733 THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS
SEQRES 31 B 733 GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU
SEQRES 32 B 733 SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU
SEQRES 33 B 733 ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER
SEQRES 34 B 733 LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO
SEQRES 35 B 733 GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP
SEQRES 36 B 733 LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP
SEQRES 37 B 733 LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU
SEQRES 38 B 733 ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN
SEQRES 39 B 733 MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR
SEQRES 40 B 733 PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN
SEQRES 41 B 733 LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR
SEQRES 42 B 733 LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP
SEQRES 43 B 733 GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS
SEQRES 44 B 733 ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP
SEQRES 45 B 733 GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE
SEQRES 46 B 733 VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR
SEQRES 47 B 733 GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY SER
SEQRES 48 B 733 GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER
SEQRES 49 B 733 ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR
SEQRES 50 B 733 MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR
SEQRES 51 B 733 ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE LYS
SEQRES 52 B 733 GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP
SEQRES 53 B 733 ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA
SEQRES 54 B 733 LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR
SEQRES 55 B 733 THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS
SEQRES 56 B 733 GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN
SEQRES 57 B 733 CYS PHE SER LEU PRO
SEQRES 1 C 733 HIS HIS HIS HIS HIS SER ARG LYS THR TYR THR LEU THR
SEQRES 2 C 733 ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER
SEQRES 3 C 733 LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN
SEQRES 4 C 733 GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN
SEQRES 5 C 733 SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE
SEQRES 6 C 733 GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY
SEQRES 7 C 733 GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP
SEQRES 8 C 733 ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU
SEQRES 9 C 733 ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN
SEQRES 10 C 733 ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS
SEQRES 11 C 733 LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE
SEQRES 12 C 733 GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY
SEQRES 13 C 733 LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL
SEQRES 14 C 733 TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP
SEQRES 15 C 733 TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE
SEQRES 16 C 733 ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR
SEQRES 17 C 733 SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL
SEQRES 18 C 733 PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS
SEQRES 19 C 733 PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL THR
SEQRES 20 C 733 ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER MET
SEQRES 21 C 733 LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA
SEQRES 22 C 733 THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE
SEQRES 23 C 733 GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU
SEQRES 24 C 733 SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS
SEQRES 25 C 733 ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE ARG
SEQRES 26 C 733 PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE
SEQRES 27 C 733 TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE
SEQRES 28 C 733 CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE
SEQRES 29 C 733 THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU
SEQRES 30 C 733 THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS
SEQRES 31 C 733 GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU
SEQRES 32 C 733 SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU
SEQRES 33 C 733 ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER
SEQRES 34 C 733 LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO
SEQRES 35 C 733 GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP
SEQRES 36 C 733 LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP
SEQRES 37 C 733 LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU
SEQRES 38 C 733 ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN
SEQRES 39 C 733 MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR
SEQRES 40 C 733 PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN
SEQRES 41 C 733 LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR
SEQRES 42 C 733 LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP
SEQRES 43 C 733 GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS
SEQRES 44 C 733 ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP
SEQRES 45 C 733 GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE
SEQRES 46 C 733 VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR
SEQRES 47 C 733 GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY SER
SEQRES 48 C 733 GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER
SEQRES 49 C 733 ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR
SEQRES 50 C 733 MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR
SEQRES 51 C 733 ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE LYS
SEQRES 52 C 733 GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP
SEQRES 53 C 733 ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA
SEQRES 54 C 733 LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR
SEQRES 55 C 733 THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS
SEQRES 56 C 733 GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN
SEQRES 57 C 733 CYS PHE SER LEU PRO
SEQRES 1 D 733 HIS HIS HIS HIS HIS SER ARG LYS THR TYR THR LEU THR
SEQRES 2 D 733 ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER
SEQRES 3 D 733 LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN
SEQRES 4 D 733 GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN
SEQRES 5 D 733 SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE
SEQRES 6 D 733 GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY
SEQRES 7 D 733 GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP
SEQRES 8 D 733 ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU
SEQRES 9 D 733 ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN
SEQRES 10 D 733 ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS
SEQRES 11 D 733 LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE
SEQRES 12 D 733 GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY
SEQRES 13 D 733 LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL
SEQRES 14 D 733 TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP
SEQRES 15 D 733 TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE
SEQRES 16 D 733 ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR
SEQRES 17 D 733 SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL
SEQRES 18 D 733 PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS
SEQRES 19 D 733 PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL THR
SEQRES 20 D 733 ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER MET
SEQRES 21 D 733 LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA
SEQRES 22 D 733 THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE
SEQRES 23 D 733 GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU
SEQRES 24 D 733 SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS
SEQRES 25 D 733 ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE ARG
SEQRES 26 D 733 PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE
SEQRES 27 D 733 TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE
SEQRES 28 D 733 CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE
SEQRES 29 D 733 THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU
SEQRES 30 D 733 THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS
SEQRES 31 D 733 GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU
SEQRES 32 D 733 SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU
SEQRES 33 D 733 ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER
SEQRES 34 D 733 LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO
SEQRES 35 D 733 GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP
SEQRES 36 D 733 LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP
SEQRES 37 D 733 LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU
SEQRES 38 D 733 ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN
SEQRES 39 D 733 MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR
SEQRES 40 D 733 PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN
SEQRES 41 D 733 LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR
SEQRES 42 D 733 LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP
SEQRES 43 D 733 GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS
SEQRES 44 D 733 ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP
SEQRES 45 D 733 GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE
SEQRES 46 D 733 VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR
SEQRES 47 D 733 GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY SER
SEQRES 48 D 733 GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER
SEQRES 49 D 733 ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR
SEQRES 50 D 733 MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR
SEQRES 51 D 733 ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE LYS
SEQRES 52 D 733 GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP
SEQRES 53 D 733 ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA
SEQRES 54 D 733 LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR
SEQRES 55 D 733 THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS
SEQRES 56 D 733 GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN
SEQRES 57 D 733 CYS PHE SER LEU PRO
MODRES 1R9M ASN A 85 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN A 150 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN A 219 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN A 229 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN A 281 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN A 321 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN A 520 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN A 685 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN B 85 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN B 150 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN B 219 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN B 229 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN B 281 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN B 321 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN B 520 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN B 685 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN C 150 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN C 219 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN C 229 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN C 281 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN C 321 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN C 520 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN D 150 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN D 219 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN D 229 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN D 281 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN D 321 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN D 520 ASN GLYCOSYLATION SITE
MODRES 1R9M ASN D 685 ASN GLYCOSYLATION SITE
HET NAG A 851 14
HET NAG A1501 14
HET NAG A1502 14
HET NAG A2191 14
HET NAG A2291 14
HET NAG A2292 14
HET MAN A2293 11
HET NAG A2811 14
HET NAG A2812 14
HET NAG A3211 14
HET NAG A3212 14
HET NAG A5201 14
HET NAG A6851 14
HET NAG B 851 14
HET NAG B1501 14
HET FUC B1502 10
HET NAG B2191 14
HET NAG B2192 14
HET NAG B2291 14
HET NAG B2292 14
HET NAG B2811 14
HET NAG B3211 14
HET NAG B5201 14
HET NAG B6851 14
HET NAG C1501 14
HET NAG C2191 14
HET NAG C2291 14
HET NAG C2292 14
HET MAN C2293 11
HET MAN C2294 11
HET NAG C2811 14
HET NAG C3211 14
HET NAG C5201 14
HET NAG D1501 14
HET NAG D2191 14
HET NAG D2291 14
HET NAG D2292 14
HET NAG D2811 14
HET NAG D3211 14
HET NAG D5201 14
HET NAG D6851 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM FUC FUCOSE
HETSYN NAG NAG
FORMUL 5 NAG 37(C8 H15 N1 O6)
FORMUL 8 MAN 3(C6 H12 O6)
FORMUL 15 FUC C6 H12 O5
FORMUL 35 HOH *1678(H2 O1)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 GLU A 91 ASP A 96 5 6
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 VAL A 507 1 11
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 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 GLU B 206 1 7
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 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 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 HIS B 712 VAL B 726 1 15
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 GLU C 206 1 7
HELIX 39 39 PRO C 290 ILE C 295 1 6
HELIX 40 40 VAL C 341 GLN C 344 5 4
HELIX 41 41 GLU C 421 MET C 425 5 5
HELIX 42 42 ASN C 497 LEU C 504 1 8
HELIX 43 43 GLN C 505 VAL C 507 5 3
HELIX 44 44 ASN C 562 ASN C 572 1 11
HELIX 45 45 GLY C 587 HIS C 592 1 6
HELIX 46 46 ALA C 593 ASN C 595 5 3
HELIX 47 47 THR C 600 MET C 616 1 17
HELIX 48 48 SER C 630 GLY C 641 1 12
HELIX 49 49 ARG C 658 TYR C 662 5 5
HELIX 50 50 ASP C 663 GLY C 672 1 10
HELIX 51 51 ASN C 679 SER C 686 1 8
HELIX 52 52 VAL C 688 VAL C 698 5 11
HELIX 53 53 HIS C 712 VAL C 726 1 15
HELIX 54 54 SER C 744 PHE C 763 1 20
HELIX 55 55 THR D 44 LYS D 50 1 7
HELIX 56 56 ASP D 200 VAL D 207 1 8
HELIX 57 57 PRO D 290 ILE D 295 1 6
HELIX 58 58 LEU D 340 GLN D 344 5 5
HELIX 59 59 GLU D 421 MET D 425 5 5
HELIX 60 60 ASN D 497 GLN D 505 1 9
HELIX 61 61 ASN D 562 THR D 570 1 9
HELIX 62 62 GLY D 587 HIS D 592 1 6
HELIX 63 63 ALA D 593 ASN D 595 5 3
HELIX 64 64 THR D 600 LYS D 615 1 16
HELIX 65 65 SER D 630 GLY D 641 1 12
HELIX 66 66 ARG D 658 TYR D 662 5 5
HELIX 67 67 ASP D 663 GLY D 672 1 10
HELIX 68 68 ASN D 679 SER D 686 1 8
HELIX 69 69 VAL D 688 VAL D 698 5 11
HELIX 70 70 HIS D 712 VAL D 726 1 15
HELIX 71 71 SER D 744 PHE D 763 1 20
SHEET 1 A 4 ARG A 61 TRP A 62 0
SHEET 2 A 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 A 4 SER A 86 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 B 4 ILE A 102 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 B 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 THR A 152 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 C 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 D 3 ILE A 194 ASN A 196 0
SHEET 2 D 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 D 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 E 4 ILE A 194 ASN A 196 0
SHEET 2 E 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 E 4 ILE A 285 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 G 4 HIS A 298 THR A 307 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 G 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 G 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 H 4 HIS A 298 THR A 307 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 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 I 4 HIS A 363 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 J 4 VAL A 404 LEU A 410 0
SHEET 2 J 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 K 4 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 K 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 K 4 GLY A 490 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 L 8 SER A 511 LEU A 519 0
SHEET 2 L 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O SER A 577 N GLN A 527
SHEET 4 L 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 L 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 L 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 L 8 GLU A 699 GLY A 705 1 O GLU A 699 N GLY A 650
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 M 2 LYS B 41 THR B 42 0
SHEET 2 M 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 N 4 ARG B 61 TRP B 62 0
SHEET 2 N 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 N 4 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 N 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 O 4 ILE B 102 ILE B 107 0
SHEET 2 O 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 O 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 O 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 P 4 THR B 152 TRP B 157 0
SHEET 2 P 4 LEU B 164 TRP B 168 -1 O VAL B 167 N GLN B 153
SHEET 3 P 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 P 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 Q 3 ILE B 194 ASN B 196 0
SHEET 2 Q 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 R 4 ILE B 194 ASN B 196 0
SHEET 2 R 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 4 THR B 265 ASN B 272 -1 O VAL B 271 N LEU B 223
SHEET 4 R 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 S 2 LEU B 235 PHE B 240 0
SHEET 2 S 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 T 4 HIS B 298 THR B 307 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O GLN B 314 N CYS B 301
SHEET 3 T 4 TYR B 322 ASP B 331 -1 O ASP B 326 N LEU B 313
SHEET 4 T 4 ARG B 336 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O GLN B 314 N CYS B 301
SHEET 3 U 4 TYR B 322 ASP B 331 -1 O ASP B 326 N LEU B 313
SHEET 4 U 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 V 4 HIS B 363 PHE B 364 0
SHEET 2 V 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 V 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 V 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 W 4 VAL B 404 LEU B 410 0
SHEET 2 W 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 W 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 W 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 X 4 TYR B 457 PHE B 461 0
SHEET 2 X 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 X 4 LEU B 479 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 X 4 GLY B 490 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Y 8 SER B 511 LEU B 519 0
SHEET 2 Y 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Y 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Y 8 TYR B 540 ASP B 545 1 N LEU B 543 O ILE B 574
SHEET 5 Y 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 544
SHEET 6 Y 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Y 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Y 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 Z 4 LEU C 60 TRP C 62 0
SHEET 2 Z 4 GLU C 67 LYS C 71 -1 O LEU C 69 N ARG C 61
SHEET 3 Z 4 ILE C 76 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 4 Z 4 SER C 86 LEU C 90 -1 O SER C 87 N VAL C 78
SHEET 1 AA 4 ASP C 104 ILE C 107 0
SHEET 2 AA 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AA 4 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 4 AA 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AB 4 THR C 152 TRP C 157 0
SHEET 2 AB 4 LEU C 164 TRP C 168 -1 O VAL C 167 N GLN C 153
SHEET 3 AB 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AB 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AC 3 ILE C 194 ASN C 196 0
SHEET 2 AC 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AC 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AD 4 ILE C 194 ASN C 196 0
SHEET 2 AD 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD 4 THR C 265 ASN C 272 -1 O VAL C 271 N LEU C 223
SHEET 4 AD 4 ILE C 285 ILE C 287 -1 O ILE C 285 N VAL C 270
SHEET 1 AE 2 LEU C 235 PHE C 240 0
SHEET 2 AE 2 LYS C 250 PRO C 255 -1 O VAL C 252 N TYR C 238
SHEET 1 AF 4 HIS C 298 THR C 307 0
SHEET 2 AF 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 AF 4 TYR C 322 ASP C 331 -1 O ASP C 326 N LEU C 313
SHEET 4 AF 4 ARG C 336 CYS C 339 -1 O ASN C 338 N ASP C 329
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 ASP C 331 -1 O ASP C 326 N LEU C 313
SHEET 4 AG 4 HIS C 345 MET C 348 -1 O HIS C 345 N MET C 325
SHEET 1 AH 4 HIS C 363 PHE C 364 0
SHEET 2 AH 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AH 4 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AH 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AI 4 VAL C 404 LEU C 410 0
SHEET 2 AI 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AI 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AI 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AJ 4 TYR C 457 PHE C 461 0
SHEET 2 AJ 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AJ 4 LEU C 479 SER C 484 -1 O HIS C 483 N TYR C 468
SHEET 4 AJ 4 GLY C 490 GLU C 495 -1 O LEU C 491 N LEU C 482
SHEET 1 AK 8 SER C 511 LEU C 519 0
SHEET 2 AK 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AK 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AK 8 TYR C 540 ASP C 545 1 N ASP C 545 O ALA C 576
SHEET 5 AK 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 544
SHEET 6 AK 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AK 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AK 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AL 2 LYS D 41 THR D 42 0
SHEET 2 AL 2 VAL D 507 GLN D 508 1 O GLN D 508 N LYS D 41
SHEET 1 AM 4 ARG D 61 TRP D 62 0
SHEET 2 AM 4 GLU D 67 TYR D 70 -1 O LEU D 69 N ARG D 61
SHEET 3 AM 4 ILE D 76 ASN D 80 -1 O LEU D 77 N TYR D 70
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 TRP D 154 TRP D 157 0
SHEET 2 AO 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
SHEET 3 AO 4 ASP D 171 LYS D 175 -1 O TYR D 173 N TYR D 166
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 LYS D 267 N GLN D 227
SHEET 4 AQ 4 ILE D 285 ILE D 287 -1 O ILE D 285 N VAL D 270
SHEET 1 AR 2 LEU D 235 PHE D 240 0
SHEET 2 AR 2 LYS D 250 PRO D 255 -1 O VAL D 252 N TYR D 238
SHEET 1 AS 4 HIS D 298 THR D 307 0
SHEET 2 AS 4 ARG D 310 ARG D 317 -1 O ARG D 310 N ALA D 306
SHEET 3 AS 4 TYR D 322 TYR D 330 -1 O CYS D 328 N ILE D 311
SHEET 4 AS 4 TRP D 337 ASN D 338 -1 O ASN D 338 N ASP D 329
SHEET 1 AT 4 HIS D 298 THR D 307 0
SHEET 2 AT 4 ARG D 310 ARG D 317 -1 O ARG D 310 N ALA D 306
SHEET 3 AT 4 TYR D 322 TYR D 330 -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 TYR D 457 PHE D 461 0
SHEET 2 AW 4 TYR D 467 CYS D 472 -1 O ARG D 471 N SER D 458
SHEET 3 AW 4 LEU D 479 SER D 484 -1 O HIS D 483 N TYR D 468
SHEET 4 AW 4 LYS D 489 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 TYR D 526 N ASP D 515
SHEET 3 AX 8 ILE D 574 PHE D 578 -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 LEU D 701 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
SSBOND 2 CYS A 385 CYS A 394
SSBOND 3 CYS A 444 CYS A 447
SSBOND 4 CYS A 454 CYS A 472
SSBOND 5 CYS A 649 CYS A 762
SSBOND 6 CYS B 328 CYS B 339
SSBOND 7 CYS B 385 CYS B 394
SSBOND 8 CYS B 444 CYS B 447
SSBOND 9 CYS B 454 CYS B 472
SSBOND 10 CYS B 649 CYS B 762
SSBOND 11 CYS D 328 CYS D 339
SSBOND 12 CYS D 385 CYS D 394
SSBOND 13 CYS D 444 CYS D 447
SSBOND 14 CYS D 454 CYS D 472
SSBOND 15 CYS D 649 CYS D 762
SSBOND 16 CYS C 328 CYS C 339
SSBOND 17 CYS C 385 CYS C 394
SSBOND 18 CYS C 444 CYS C 447
SSBOND 19 CYS C 454 CYS C 472
SSBOND 20 CYS C 649 CYS C 762
LINK ND2 ASN A 85 C1 NAG A 851
LINK ND2 ASN A 219 C1 NAG A2191
LINK ND2 ASN A 520 C1 NAG A5201
LINK ND2 ASN A 685 C1 NAG A6851
LINK ND2 ASN B 85 C1 NAG B 851
LINK ND2 ASN B 281 C1 NAG B2811
LINK ND2 ASN B 321 C1 NAG B3211
LINK ND2 ASN B 520 C1 NAG B5201
LINK ND2 ASN B 685 C1 NAG B6851
LINK ND2 ASN C 150 C1 NAG C1501
LINK ND2 ASN C 219 C1 NAG C2191
LINK ND2 ASN C 281 C1 NAG C2811
LINK ND2 ASN C 321 C1 NAG C3211
LINK ND2 ASN C 520 C1 NAG C5201
LINK ND2 ASN D 150 C1 NAG D1501
LINK ND2 ASN D 219 C1 NAG D2191
LINK ND2 ASN D 281 C1 NAG D2811
LINK ND2 ASN D 321 C1 NAG D3211
LINK ND2 ASN D 520 C1 NAG D5201
LINK ND2 ASN D 685 C1 NAG D6851
LINK ND2 ASN A 150 C1 NAG A1501
LINK O4 NAG A1501 C1 NAG A1502
LINK ND2 ASN A 229 C1 NAG A2291
LINK O4 NAG A2291 C1 NAG A2292
LINK O4 NAG A2292 C1 MAN A2293
LINK ND2 ASN A 281 C1 NAG A2811
LINK O4 NAG A2811 C1 NAG A2812
LINK ND2 ASN A 321 C1 NAG A3211
LINK O4 NAG A3211 C1 NAG A3212
LINK ND2 ASN B 150 C1 NAG B1501
LINK O6 NAG B1501 C1 FUC B1502
LINK ND2 ASN B 219 C1 NAG B2191
LINK O4 NAG B2191 C1 NAG B2192
LINK ND2 ASN B 229 C1 NAG B2291
LINK O4 NAG B2291 C1 NAG B2292
LINK ND2 ASN C 229 C1 NAG C2291
LINK O4 NAG C2291 C1 NAG C2292
LINK O4 NAG C2292 C1 MAN C2293
LINK O4 MAN C2293 C1 MAN C2294
LINK ND2 ASN D 229 C1 NAG D2291
LINK O4 NAG D2291 C1 NAG D2292
LINK O4 NAG C2292 C2 MAN C2293
LINK O6 MAN C2293 C1 MAN C2294
CISPEP 1 GLY A 474 PRO A 475 0 4.01
CISPEP 2 GLY B 474 PRO B 475 0 7.80
CISPEP 3 GLY C 474 PRO C 475 0 3.02
CISPEP 4 GLY D 474 PRO D 475 0 4.52
CRYST1 121.823 124.056 144.491 90.00 114.71 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 0.008209 0.000000 0.003777 0.00000
SCALE2 0.000000 0.008061 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007618 0.00000
TER 5952 PRO A 766
TER 11966 PRO B 766
TER 17918 PRO C 766
TER 23876 PRO D 766
MASTER 750 0 41 71 200 0 0 626111 4 630 228
END |