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HEADER HYDROLASE 30-OCT-03 1R9N
TITLE CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV IN
TITLE 2 COMPLEX WITH A DECAPEPTIDE (TNPY) AT 2.3 ANG. RESOLUTION
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;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NEUROPEPTIDE Y;
COMPND 10 CHAIN: E, F, G, H;
COMPND 11 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: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTB;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: SEQUENCE IS THE SAME AS IN THE NATURAL
SOURCE 12 SOURCE
KEYWDS ALPHA/BETA HYDROLASE, EIGHT-BLADED BETA PROPELLER, SERINE
KEYWDS 2 PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.AERTGEERTS,S.YE,M.G.TENNANT,B.COLLINS,J.ROGERS,B.-C.SANG,
AUTHOR 2 R.SKENE,D.R.WEBB,G.S.PRASAD
REVDAT 1 29-MAR-05 1R9N 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. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 153134
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8078
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11373
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 625
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 25627
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.14000
REMARK 3 B22 (A**2) : 3.08000
REMARK 3 B33 (A**2) : -0.93000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.351
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.241
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.198
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.164
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25120 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34193 ; 1.276 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2924 ; 6.406 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1240 ;34.607 ;23.944
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4014 ;17.555 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;18.533 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3640 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19254 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 10795 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 16762 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1125 ; 0.140 ; 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): 129 ; 0.175 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 38 ; 0.140 ; 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): 14976 ; 0.445 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23698 ; 0.769 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11911 ; 1.090 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10495 ; 1.708 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 1 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7113 0.6408 19.2922
REMARK 3 T TENSOR
REMARK 3 T11: -0.1526 T22: -0.1272
REMARK 3 T33: -0.1571 T12: -0.0072
REMARK 3 T13: 0.0040 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 1.2864 L22: 0.6428
REMARK 3 L33: 0.8407 L12: 0.1148
REMARK 3 L13: 0.0501 L23: -0.0989
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: -0.1218 S13: 0.1489
REMARK 3 S21: 0.1446 S22: -0.0179 S23: 0.1703
REMARK 3 S31: -0.0085 S32: -0.2956 S33: 0.0224
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 67.5772 7.0220 20.6110
REMARK 3 T TENSOR
REMARK 3 T11: -0.1451 T22: -0.1816
REMARK 3 T33: -0.0945 T12: -0.0020
REMARK 3 T13: -0.0433 T23: -0.0675
REMARK 3 L TENSOR
REMARK 3 L11: 1.4448 L22: 0.3480
REMARK 3 L33: 0.8065 L12: 0.0309
REMARK 3 L13: 0.0893 L23: -0.0720
REMARK 3 S TENSOR
REMARK 3 S11: -0.0275 S12: 0.0004 S13: 0.1493
REMARK 3 S21: 0.0401 S22: 0.0394 S23: -0.1656
REMARK 3 S31: 0.0553 S32: 0.1918 S33: -0.0118
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 : C 1 C 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1316 61.3325 33.8005
REMARK 3 T TENSOR
REMARK 3 T11: -0.1009 T22: -0.0345
REMARK 3 T33: -0.1460 T12: 0.0233
REMARK 3 T13: -0.0162 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 2.1043 L22: 0.6208
REMARK 3 L33: 0.7480 L12: 0.2434
REMARK 3 L13: -0.3377 L23: 0.0796
REMARK 3 S TENSOR
REMARK 3 S11: 0.0885 S12: -0.2519 S13: -0.1428
REMARK 3 S21: 0.1257 S22: -0.0444 S23: -0.2156
REMARK 3 S31: 0.1036 S32: 0.4106 S33: -0.0441
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 92.8819 63.0120 47.2912
REMARK 3 T TENSOR
REMARK 3 T11: -0.0214 T22: 0.0323
REMARK 3 T33: 0.0168 T12: -0.0474
REMARK 3 T13: 0.0458 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 1.2786 L22: 0.7211
REMARK 3 L33: 1.0778 L12: 0.1115
REMARK 3 L13: -0.2687 L23: 0.2599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0581 S12: -0.2515 S13: 0.1515
REMARK 3 S21: 0.1363 S22: -0.0811 S23: 0.4004
REMARK 3 S31: -0.0948 S32: -0.3935 S33: 0.0230
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1R9N COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-2004.
REMARK 100 THE RCSB ID CODE IS RCSB020609.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-2003
REMARK 200 TEMPERATURE (KELVIN) : 173.0
REMARK 200 PH : 8.25
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 161260
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 23270.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : 0.05400
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.42900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY: 1R9M
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: PEG 2000, BICINE, PH 8.25, VAPOR
REMARK 280 DIFFUSION, 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 61.35050
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 8 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, E, B, F, I, J
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, G, D, H, K, L
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 ALA A 28
REMARK 465 ASP A 29
REMARK 465 PRO A 30
REMARK 465 GLY A 31
REMARK 465 GLY A 32
REMARK 465 SER 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 PRO E 1005
REMARK 465 ASP E 1006
REMARK 465 ASN E 1007
REMARK 465 PRO E 1008
REMARK 465 GLY E 1009
REMARK 465 GLU E 1010
REMARK 465 ALA B 28
REMARK 465 ASP B 29
REMARK 465 PRO B 30
REMARK 465 GLY B 31
REMARK 465 GLY B 32
REMARK 465 SER B 33
REMARK 465 HIS B 34
REMARK 465 HIS B 35
REMARK 465 ASN F 1007
REMARK 465 PRO F 1008
REMARK 465 GLY F 1009
REMARK 465 GLU F 1010
REMARK 465 ALA C 28
REMARK 465 ASP C 29
REMARK 465 PRO C 30
REMARK 465 GLY C 31
REMARK 465 GLY C 32
REMARK 465 SER 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 PRO G 1005
REMARK 465 ASP G 1006
REMARK 465 ASN G 1007
REMARK 465 PRO G 1008
REMARK 465 GLY G 1009
REMARK 465 GLU G 1010
REMARK 465 ALA D 28
REMARK 465 ASP D 29
REMARK 465 PRO D 30
REMARK 465 GLY D 31
REMARK 465 GLY D 32
REMARK 465 SER 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 465 ASP H 1006
REMARK 465 ASN H 1007
REMARK 465 PRO H 1008
REMARK 465 GLY H 1009
REMARK 465 GLU H 1010
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 N GLY B 599 OE2 GLU B 602 2.08
REMARK 500 OG SER A 458 NH1 ARG A 471 2.15
REMARK 500 ND1 HIS A 704 OG SER A 716 2.19
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 ASP A 192 CG ASP A 192 OD2 0.070
REMARK 500 VAL A 262 CA VAL A 262 CB 0.065
REMARK 500 VAL A 665 CA VAL A 665 CB 0.061
REMARK 500 VAL A 688 CA VAL A 688 CB 0.069
REMARK 500 VAL A 728 CA VAL A 728 CB 0.062
REMARK 500 ASP B 192 CG ASP B 192 OD2 0.082
REMARK 500 ASN C 179 CG ASN C 179 ND2 0.060
REMARK 500 ASP C 192 CG ASP C 192 OD2 0.078
REMARK 500 VAL C 262 CA VAL C 262 CB 0.069
REMARK 500 ILE C 594 CA ILE C 594 CB 0.081
REMARK 500 PRO C 655 CB PRO C 655 CG -0.065
REMARK 500 VAL C 728 CA VAL C 728 CB 0.061
REMARK 500 ASP D 192 CG ASP D 192 OD2 0.077
REMARK 500 VAL D 688 CA VAL D 688 CB 0.072
REMARK 500 VAL D 728 CA VAL D 728 CB 0.065
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 LEU A 55 CA - CB - CG ANGL. DEV. = 10.0 DEGREES
REMARK 500 LEU A 142 CA - CB - CG ANGL. DEV. = 7.7 DEGREES
REMARK 500 VAL A 262 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 LEU A 313 CA - CB - CG ANGL. DEV. = 8.9 DEGREES
REMARK 500 LEU A 316 CA - CB - CG ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU A 366 CA - CB - CG ANGL. DEV. = 7.9 DEGREES
REMARK 500 LEU A 514 CA - CB - CG ANGL. DEV. = 9.8 DEGREES
REMARK 500 VAL A 711 CB - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU B 55 CA - CB - CG ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU B 164 CA - CB - CG ANGL. DEV. = 11.0 DEGREES
REMARK 500 TRP B 402 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 LEU B 482 CA - CB - CG ANGL. DEV. = 7.4 DEGREES
REMARK 500 LEU B 514 CA - CB - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 VAL B 711 CB - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU C 57 CA - CB - CG ANGL. DEV. = 7.4 DEGREES
REMARK 500 LEU C 60 CA - CB - CG ANGL. DEV. = 8.2 DEGREES
REMARK 500 LEU C 142 CA - CB - CG ANGL. DEV. = 7.9 DEGREES
REMARK 500 LEU C 214 CA - CB - CG ANGL. DEV. = 7.8 DEGREES
REMARK 500 LEU C 316 CA - CB - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 TRP C 402 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 LEU C 514 CA - CB - CG ANGL. DEV. = 9.3 DEGREES
REMARK 500 VAL C 656 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 VAL C 711 CB - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU D 55 CA - CB - CG ANGL. DEV. = 7.5 DEGREES
REMARK 500 LEU D 57 CA - CB - CG ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP D 297 N - CA - CB ANGL. DEV. = 9.0 DEGREES
REMARK 500 CYS D 454 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 LEU D 514 CA - CB - CG ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG D 658 N - CA - C ANGL. DEV. = -7.8 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 -108.45 72.11
REMARK 500 SER B 630 -114.30 70.30
REMARK 500 SER C 630 -110.80 69.08
REMARK 500 SER D 630 -106.82 71.65
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 165 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH 180 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH 196 DISTANCE = 5.55 ANGSTROMS
REMARK 525 HOH 211 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH 251 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH 254 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH 266 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH 298 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH 299 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH 301 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH 323 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH 390 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH 391 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH 395 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH 403 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH 408 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH 415 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH 423 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH 429 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH 434 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH 440 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH 457 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH 458 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH 477 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH 480 DISTANCE = 8.00 ANGSTROMS
REMARK 525 HOH 494 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH 499 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH 503 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH 504 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH 535 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH 536 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH 540 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH 544 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH 546 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH 559 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH 572 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH 573 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH 581 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH 583 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH 584 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH 603 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH 609 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH 610 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH 612 DISTANCE = 7.63 ANGSTROMS
REMARK 525 HOH 639 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH 647 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH 652 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH 656 DISTANCE = 8.11 ANGSTROMS
REMARK 525 HOH 659 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH 669 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH 683 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH 692 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH 701 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH 703 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH 705 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH 707 DISTANCE = 8.23 ANGSTROMS
REMARK 525 HOH 708 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH 712 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH 720 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH 721 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH 726 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH 729 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH 736 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH 743 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH 745 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH 747 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH 754 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH 758 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH 763 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH 764 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH 765 DISTANCE = 8.56 ANGSTROMS
REMARK 525 HOH 773 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH 777 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH 778 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH 779 DISTANCE = 8.06 ANGSTROMS
REMARK 525 HOH 782 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH 784 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH 785 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH 796 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH 801 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH 803 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH 860 DISTANCE = 7.64 ANGSTROMS
REMARK 525 HOH 863 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH 872 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH 875 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH 878 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH 885 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH 888 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH 889 DISTANCE = 10.38 ANGSTROMS
REMARK 525 HOH 890 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH 896 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH 902 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH 903 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH 907 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH 912 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH 914 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH 916 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH 918 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH 921 DISTANCE = 9.24 ANGSTROMS
REMARK 525 HOH 933 DISTANCE = 9.51 ANGSTROMS
REMARK 525 HOH 938 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH 941 DISTANCE = 10.70 ANGSTROMS
REMARK 525 HOH 943 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH 945 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH 947 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH 948 DISTANCE = 5.68 ANGSTROMS
REMARK 525 HOH 949 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH 950 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH 952 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH 953 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH 957 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH 964 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH 966 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH 970 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH 972 DISTANCE = 10.41 ANGSTROMS
REMARK 525 HOH 976 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH 987 DISTANCE = 13.19 ANGSTROMS
REMARK 525 HOH 989 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH 990 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH 991 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH 997 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH 1000 DISTANCE = 9.06 ANGSTROMS
REMARK 525 HOH 1002 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH 1003 DISTANCE = 9.62 ANGSTROMS
REMARK 525 HOH 1004 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH 1009 DISTANCE = 7.55 ANGSTROMS
REMARK 525 HOH 1014 DISTANCE = 12.92 ANGSTROMS
REMARK 525 HOH 1015 DISTANCE = 7.62 ANGSTROMS
REMARK 525 HOH 1025 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH 1032 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH 1033 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH 1036 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH 1040 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH 1041 DISTANCE = 9.25 ANGSTROMS
REMARK 525 HOH 1043 DISTANCE = 8.26 ANGSTROMS
REMARK 525 HOH 1046 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH 1047 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH 1053 DISTANCE = 9.59 ANGSTROMS
REMARK 525 HOH 1056 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH 1062 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH 1063 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH 1066 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH 1068 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH 1069 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH 1071 DISTANCE = 10.14 ANGSTROMS
REMARK 525 HOH 1080 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH 1082 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH 1085 DISTANCE = 10.98 ANGSTROMS
REMARK 525 HOH 1088 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH 1090 DISTANCE = 9.40 ANGSTROMS
REMARK 525 HOH 1091 DISTANCE = 8.91 ANGSTROMS
REMARK 525 HOH 1094 DISTANCE = 8.82 ANGSTROMS
REMARK 525 HOH 1095 DISTANCE = 12.48 ANGSTROMS
REMARK 525 HOH 1103 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH 1104 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH 1105 DISTANCE = 8.98 ANGSTROMS
REMARK 525 HOH 1106 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH 1111 DISTANCE = 8.82 ANGSTROMS
REMARK 525 HOH 1113 DISTANCE = 9.06 ANGSTROMS
REMARK 525 HOH 1115 DISTANCE = 5.58 ANGSTROMS
REMARK 525 HOH 1117 DISTANCE = 9.25 ANGSTROMS
REMARK 525 HOH 1119 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH 1122 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH 1123 DISTANCE = 7.98 ANGSTROMS
REMARK 525 HOH 1124 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH 1125 DISTANCE = 7.68 ANGSTROMS
REMARK 525 HOH 1127 DISTANCE = 8.01 ANGSTROMS
REMARK 525 HOH 1128 DISTANCE = 8.70 ANGSTROMS
REMARK 525 HOH 1129 DISTANCE = 9.97 ANGSTROMS
REMARK 525 HOH 1130 DISTANCE = 8.54 ANGSTROMS
REMARK 525 HOH 1132 DISTANCE = 9.54 ANGSTROMS
REMARK 525 HOH 1134 DISTANCE = 10.40 ANGSTROMS
REMARK 525 HOH 1135 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH 1136 DISTANCE = 8.60 ANGSTROMS
REMARK 525 HOH 1139 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH 1140 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH 1142 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH 1144 DISTANCE = 9.65 ANGSTROMS
REMARK 525 HOH 1145 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH 1146 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH 1152 DISTANCE = 8.49 ANGSTROMS
REMARK 525 HOH 1154 DISTANCE = 8.05 ANGSTROMS
REMARK 525 HOH 1156 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH 1157 DISTANCE = 8.83 ANGSTROMS
REMARK 525 HOH 1158 DISTANCE = 7.51 ANGSTROMS
REMARK 525 HOH 1159 DISTANCE = 10.26 ANGSTROMS
REMARK 525 HOH 1161 DISTANCE = 7.28 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R9M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV AT 2.1
REMARK 900 ANG. RESOLUTION.
DBREF 1R9N A 39 766 SWS P27487 DPP4_HUMAN 39 766
DBREF 1R9N B 39 766 SWS P27487 DPP4_HUMAN 39 766
DBREF 1R9N C 39 766 SWS P27487 DPP4_HUMAN 39 766
DBREF 1R9N D 39 766 SWS P27487 DPP4_HUMAN 39 766
DBREF 1R9N E 1001 1010 SWS Q9XSW6 NPY_MACMU 29 38
DBREF 1R9N F 1001 1010 SWS Q9XSW6 NPY_MACMU 29 38
DBREF 1R9N G 1001 1010 SWS Q9XSW6 NPY_MACMU 29 38
DBREF 1R9N H 1001 1010 SWS Q9XSW6 NPY_MACMU 29 38
SEQADV 1R9N ALA A 28 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N ASP A 29 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N PRO A 30 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N GLY A 31 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N GLY A 32 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N SER A 33 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N HIS A 34 SWS P27487 HIS TAG
SEQADV 1R9N HIS A 35 SWS P27487 HIS TAG
SEQADV 1R9N HIS A 36 SWS P27487 HIS TAG
SEQADV 1R9N HIS A 37 SWS P27487 HIS TAG
SEQADV 1R9N HIS A 38 SWS P27487 HIS TAG
SEQADV 1R9N ALA B 28 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N ASP B 29 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N PRO B 30 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N GLY B 31 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N GLY B 32 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N SER B 33 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N HIS B 34 SWS P27487 HIS TAG
SEQADV 1R9N HIS B 35 SWS P27487 HIS TAG
SEQADV 1R9N HIS B 36 SWS P27487 HIS TAG
SEQADV 1R9N HIS B 37 SWS P27487 HIS TAG
SEQADV 1R9N HIS B 38 SWS P27487 HIS TAG
SEQADV 1R9N ALA C 28 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N ASP C 29 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N PRO C 30 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N GLY C 31 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N GLY C 32 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N SER C 33 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N HIS C 34 SWS P27487 HIS TAG
SEQADV 1R9N HIS C 35 SWS P27487 HIS TAG
SEQADV 1R9N HIS C 36 SWS P27487 HIS TAG
SEQADV 1R9N HIS C 37 SWS P27487 HIS TAG
SEQADV 1R9N HIS C 38 SWS P27487 HIS TAG
SEQADV 1R9N ALA D 28 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N ASP D 29 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N PRO D 30 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N GLY D 31 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N GLY D 32 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N SER D 33 SWS P27487 CLONING ARTIFACT
SEQADV 1R9N HIS D 34 SWS P27487 HIS TAG
SEQADV 1R9N HIS D 35 SWS P27487 HIS TAG
SEQADV 1R9N HIS D 36 SWS P27487 HIS TAG
SEQADV 1R9N HIS D 37 SWS P27487 HIS TAG
SEQADV 1R9N HIS D 38 SWS P27487 HIS TAG
SEQRES 1 A 739 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS SER ARG
SEQRES 2 A 739 LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR
SEQRES 3 A 739 ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS
SEQRES 4 A 739 GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE
SEQRES 5 A 739 ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN
SEQRES 6 A 739 SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR
SEQRES 7 A 739 SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR
SEQRES 8 A 739 ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER
SEQRES 9 A 739 TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR
SEQRES 10 A 739 GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP
SEQRES 11 A 739 SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN
SEQRES 12 A 739 ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR
SEQRES 13 A 739 ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN
SEQRES 14 A 739 GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER
SEQRES 15 A 739 ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE
SEQRES 16 A 739 LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU
SEQRES 17 A 739 ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR
SEQRES 18 A 739 PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA
SEQRES 19 A 739 VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP
SEQRES 20 A 739 SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE
SEQRES 21 A 739 THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU
SEQRES 22 A 739 CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU
SEQRES 23 A 739 GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP
SEQRES 24 A 739 ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS
SEQRES 25 A 739 LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY
SEQRES 26 A 739 TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR
SEQRES 27 A 739 LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU
SEQRES 28 A 739 GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS
SEQRES 29 A 739 LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL
SEQRES 30 A 739 ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR
SEQRES 31 A 739 ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN
SEQRES 32 A 739 LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR
SEQRES 33 A 739 CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR
SEQRES 34 A 739 TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN
SEQRES 35 A 739 LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU
SEQRES 36 A 739 HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU
SEQRES 37 A 739 ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN
SEQRES 38 A 739 MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU
SEQRES 39 A 739 THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE
SEQRES 40 A 739 ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR
SEQRES 41 A 739 ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG
SEQRES 42 A 739 LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE
SEQRES 43 A 739 ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN
SEQRES 44 A 739 GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY
SEQRES 45 A 739 THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN
SEQRES 46 A 739 PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA
SEQRES 47 A 739 ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET
SEQRES 48 A 739 VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE
SEQRES 49 A 739 ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER
SEQRES 50 A 739 VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU
SEQRES 51 A 739 ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER
SEQRES 52 A 739 ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE
SEQRES 53 A 739 HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER
SEQRES 54 A 739 ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP
SEQRES 55 A 739 PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE
SEQRES 56 A 739 ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET
SEQRES 57 A 739 SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 E 10 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU
SEQRES 1 B 739 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS SER ARG
SEQRES 2 B 739 LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR
SEQRES 3 B 739 ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS
SEQRES 4 B 739 GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE
SEQRES 5 B 739 ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN
SEQRES 6 B 739 SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR
SEQRES 7 B 739 SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR
SEQRES 8 B 739 ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER
SEQRES 9 B 739 TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR
SEQRES 10 B 739 GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP
SEQRES 11 B 739 SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN
SEQRES 12 B 739 ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR
SEQRES 13 B 739 ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN
SEQRES 14 B 739 GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER
SEQRES 15 B 739 ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE
SEQRES 16 B 739 LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU
SEQRES 17 B 739 ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR
SEQRES 18 B 739 PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA
SEQRES 19 B 739 VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP
SEQRES 20 B 739 SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE
SEQRES 21 B 739 THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU
SEQRES 22 B 739 CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU
SEQRES 23 B 739 GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP
SEQRES 24 B 739 ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS
SEQRES 25 B 739 LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY
SEQRES 26 B 739 TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR
SEQRES 27 B 739 LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU
SEQRES 28 B 739 GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS
SEQRES 29 B 739 LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL
SEQRES 30 B 739 ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR
SEQRES 31 B 739 ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN
SEQRES 32 B 739 LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR
SEQRES 33 B 739 CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR
SEQRES 34 B 739 TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN
SEQRES 35 B 739 LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU
SEQRES 36 B 739 HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU
SEQRES 37 B 739 ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN
SEQRES 38 B 739 MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU
SEQRES 39 B 739 THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE
SEQRES 40 B 739 ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR
SEQRES 41 B 739 ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG
SEQRES 42 B 739 LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE
SEQRES 43 B 739 ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN
SEQRES 44 B 739 GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY
SEQRES 45 B 739 THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN
SEQRES 46 B 739 PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA
SEQRES 47 B 739 ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET
SEQRES 48 B 739 VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE
SEQRES 49 B 739 ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER
SEQRES 50 B 739 VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU
SEQRES 51 B 739 ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER
SEQRES 52 B 739 ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE
SEQRES 53 B 739 HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER
SEQRES 54 B 739 ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP
SEQRES 55 B 739 PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE
SEQRES 56 B 739 ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET
SEQRES 57 B 739 SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 F 10 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU
SEQRES 1 C 739 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS SER ARG
SEQRES 2 C 739 LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR
SEQRES 3 C 739 ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS
SEQRES 4 C 739 GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE
SEQRES 5 C 739 ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN
SEQRES 6 C 739 SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR
SEQRES 7 C 739 SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR
SEQRES 8 C 739 ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER
SEQRES 9 C 739 TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR
SEQRES 10 C 739 GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP
SEQRES 11 C 739 SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN
SEQRES 12 C 739 ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR
SEQRES 13 C 739 ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN
SEQRES 14 C 739 GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER
SEQRES 15 C 739 ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE
SEQRES 16 C 739 LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU
SEQRES 17 C 739 ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR
SEQRES 18 C 739 PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA
SEQRES 19 C 739 VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP
SEQRES 20 C 739 SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE
SEQRES 21 C 739 THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU
SEQRES 22 C 739 CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU
SEQRES 23 C 739 GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP
SEQRES 24 C 739 ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS
SEQRES 25 C 739 LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY
SEQRES 26 C 739 TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR
SEQRES 27 C 739 LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU
SEQRES 28 C 739 GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS
SEQRES 29 C 739 LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL
SEQRES 30 C 739 ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR
SEQRES 31 C 739 ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN
SEQRES 32 C 739 LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR
SEQRES 33 C 739 CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR
SEQRES 34 C 739 TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN
SEQRES 35 C 739 LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU
SEQRES 36 C 739 HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU
SEQRES 37 C 739 ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN
SEQRES 38 C 739 MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU
SEQRES 39 C 739 THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE
SEQRES 40 C 739 ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR
SEQRES 41 C 739 ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG
SEQRES 42 C 739 LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE
SEQRES 43 C 739 ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN
SEQRES 44 C 739 GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY
SEQRES 45 C 739 THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN
SEQRES 46 C 739 PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA
SEQRES 47 C 739 ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET
SEQRES 48 C 739 VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE
SEQRES 49 C 739 ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER
SEQRES 50 C 739 VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU
SEQRES 51 C 739 ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER
SEQRES 52 C 739 ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE
SEQRES 53 C 739 HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER
SEQRES 54 C 739 ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP
SEQRES 55 C 739 PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE
SEQRES 56 C 739 ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET
SEQRES 57 C 739 SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 G 10 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU
SEQRES 1 D 739 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS SER ARG
SEQRES 2 D 739 LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR
SEQRES 3 D 739 ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS
SEQRES 4 D 739 GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE
SEQRES 5 D 739 ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN
SEQRES 6 D 739 SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR
SEQRES 7 D 739 SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR
SEQRES 8 D 739 ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER
SEQRES 9 D 739 TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR
SEQRES 10 D 739 GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP
SEQRES 11 D 739 SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN
SEQRES 12 D 739 ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR
SEQRES 13 D 739 ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN
SEQRES 14 D 739 GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER
SEQRES 15 D 739 ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE
SEQRES 16 D 739 LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU
SEQRES 17 D 739 ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR
SEQRES 18 D 739 PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA
SEQRES 19 D 739 VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP
SEQRES 20 D 739 SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE
SEQRES 21 D 739 THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU
SEQRES 22 D 739 CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU
SEQRES 23 D 739 GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP
SEQRES 24 D 739 ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS
SEQRES 25 D 739 LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY
SEQRES 26 D 739 TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR
SEQRES 27 D 739 LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU
SEQRES 28 D 739 GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS
SEQRES 29 D 739 LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL
SEQRES 30 D 739 ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR
SEQRES 31 D 739 ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN
SEQRES 32 D 739 LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR
SEQRES 33 D 739 CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR
SEQRES 34 D 739 TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN
SEQRES 35 D 739 LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU
SEQRES 36 D 739 HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU
SEQRES 37 D 739 ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN
SEQRES 38 D 739 MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU
SEQRES 39 D 739 THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE
SEQRES 40 D 739 ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR
SEQRES 41 D 739 ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG
SEQRES 42 D 739 LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE
SEQRES 43 D 739 ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN
SEQRES 44 D 739 GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY
SEQRES 45 D 739 THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN
SEQRES 46 D 739 PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA
SEQRES 47 D 739 ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET
SEQRES 48 D 739 VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE
SEQRES 49 D 739 ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER
SEQRES 50 D 739 VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU
SEQRES 51 D 739 ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER
SEQRES 52 D 739 ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE
SEQRES 53 D 739 HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER
SEQRES 54 D 739 ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP
SEQRES 55 D 739 PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE
SEQRES 56 D 739 ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET
SEQRES 57 D 739 SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 H 10 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU
MODRES 1R9N ASN A 85 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN A 150 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN A 219 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN A 229 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN A 281 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN A 321 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN A 685 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN B 85 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN B 150 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN B 219 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN B 229 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN B 281 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN B 321 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN C 219 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN C 229 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN C 281 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN C 321 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN C 520 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN D 219 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN D 229 ASN GLYCOSYLATION SITE
MODRES 1R9N ASN D 281 ASN GLYCOSYLATION SITE
HET NAG A 851 14
HET NAG A1501 14
HET NAG A2191 14
HET NAG I2291 14
HET NAG I2292 14
HET NAG A2811 14
HET NAG A3211 14
HET NAG A6851 14
HET NAG B 851 14
HET NAG B1501 14
HET NAG B2191 14
HET NAG J2291 14
HET NAG J2292 14
HET NAG B2811 14
HET NAG B3211 14
HET NAG C2191 14
HET NAG K2291 14
HET NAG K2292 14
HET NAG C2811 14
HET NAG C3211 14
HET NAG C5201 14
HET NAG D2191 14
HET NAG L2291 14
HET NAG L2292 14
HET NAG D2811 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 9 NAG 25(C8 H15 N1 O6)
FORMUL 30 HOH *1249(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 ASP A 274 LEU A 276 5 3
HELIX 5 5 PRO A 290 ILE A 295 1 6
HELIX 6 6 VAL A 341 GLN A 344 5 4
HELIX 7 7 GLU A 421 MET A 425 5 5
HELIX 8 8 ASN A 497 GLN A 505 1 9
HELIX 9 9 ASN A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 LYS A 615 1 16
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 ARG A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 SER A 686 1 8
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 PHE A 713 VAL A 726 1 14
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 THR B 44 ASN B 51 1 8
HELIX 21 21 PHE B 95 GLY B 99 5 5
HELIX 22 22 ASP B 200 VAL B 207 1 8
HELIX 23 23 PRO B 290 ILE B 295 1 6
HELIX 24 24 VAL B 341 GLN B 344 5 4
HELIX 25 25 GLU B 421 MET B 425 5 5
HELIX 26 26 ASN B 497 LEU B 504 1 8
HELIX 27 27 ASN B 562 THR B 570 1 9
HELIX 28 28 GLY B 587 HIS B 592 1 6
HELIX 29 29 ALA B 593 ASN B 595 5 3
HELIX 30 30 THR B 600 LYS B 615 1 16
HELIX 31 31 SER B 630 GLY B 641 1 12
HELIX 32 32 ARG B 658 TYR B 662 5 5
HELIX 33 33 ASP B 663 GLY B 672 1 10
HELIX 34 34 ASN B 679 SER B 686 1 8
HELIX 35 35 VAL B 688 VAL B 698 5 11
HELIX 36 36 HIS B 712 VAL B 726 1 15
HELIX 37 37 SER B 744 PHE B 763 1 20
HELIX 38 38 THR C 44 ASN C 51 1 8
HELIX 39 39 ASP C 200 GLU C 206 1 7
HELIX 40 40 PRO C 290 ILE C 295 1 6
HELIX 41 41 VAL C 341 GLN C 344 5 4
HELIX 42 42 GLU C 421 MET C 425 5 5
HELIX 43 43 ASN C 497 GLN C 505 1 9
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 GLU D 91 ASP D 96 5 6
HELIX 57 57 ASP D 200 GLU D 206 1 7
HELIX 58 58 PRO D 290 ILE D 295 1 6
HELIX 59 59 GLU D 421 MET D 425 5 5
HELIX 60 60 ASN D 497 LEU D 504 1 8
HELIX 61 61 ASN D 562 ASN D 572 1 11
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 GLY D 727 1 16
HELIX 71 71 SER D 744 SER D 764 1 21
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 ARG A 61 TRP A 62 0
SHEET 2 B 4 GLU A 67 LYS A 71 -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 LEU A 90 N ILE A 76
SHEET 1 C 4 ILE A 102 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 SER A 131 N TYR A 118
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 TRP A 154 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
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 GLN A 286 -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 ARG A 336 N ASP A 331
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 LYS A 391 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 THR A 481 N LEU A 470
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 LEU A 530 N SER A 511
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 ARG B 61 TRP B 62 0
SHEET 2 O 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ASN B 75 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 ASP B 104 ILE B 107 0
SHEET 2 P 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 P 4 TYR B 128 ASP B 136 -1 O ASP B 133 N LEU B 116
SHEET 4 P 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 Q 4 THR B 152 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 PHE B 269 N TYR B 225
SHEET 4 S 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O 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 ASP B 326 N LEU B 313
SHEET 4 U 4 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 1 V 4 HIS B 298 THR B 307 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 V 4 TYR B 322 ASP B 331 -1 O ASP B 326 N LEU B 313
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 LEU B 479 N CYS B 472
SHEET 4 Y 4 LYS B 489 GLU B 495 -1 O LEU B 491 N LEU B 482
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Z 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Z 8 TYR B 540 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 2 LYS C 41 THR C 42 0
SHEET 2 AA 2 VAL C 507 GLN C 508 1 O GLN C 508 N LYS C 41
SHEET 1 AB 4 LEU C 60 TRP C 62 0
SHEET 2 AB 4 GLU C 67 LYS C 71 -1 O LEU C 69 N ARG C 61
SHEET 3 AB 4 ILE C 76 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 4 AB 4 SER C 87 LEU C 90 -1 O LEU C 90 N ILE C 76
SHEET 1 AC 4 ASP C 104 ILE C 107 0
SHEET 2 AC 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AC 4 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 4 AC 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AD 4 TRP C 154 TRP C 157 0
SHEET 2 AD 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AD 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AD 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AE 3 ILE C 194 ASN C 196 0
SHEET 2 AE 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AE 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AF 4 ILE C 194 ASN C 196 0
SHEET 2 AF 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AF 4 THR C 265 ASN C 272 -1 O VAL C 271 N LEU C 223
SHEET 4 AF 4 SER C 284 ILE C 287 -1 O ILE C 287 N PHE C 268
SHEET 1 AG 2 LEU C 235 PHE C 240 0
SHEET 2 AG 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AH 4 HIS C 298 TRP C 305 0
SHEET 2 AH 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AH 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AH 4 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 1 AI 4 HIS C 298 TRP C 305 0
SHEET 2 AI 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AI 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AI 4 HIS C 345 MET C 348 -1 O HIS C 345 N MET C 325
SHEET 1 AJ 4 HIS C 363 PHE C 364 0
SHEET 2 AJ 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AJ 4 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AJ 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AK 4 VAL C 404 LEU C 410 0
SHEET 2 AK 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AK 4 ASN C 430 GLN C 435 -1 O ILE C 434 N LEU C 415
SHEET 4 AK 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AL 4 TYR C 457 PHE C 461 0
SHEET 2 AL 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AL 4 LEU C 479 SER C 484 -1 O THR C 481 N LEU C 470
SHEET 4 AL 4 LYS C 489 GLU C 495 -1 O ARG C 492 N LEU C 482
SHEET 1 AM 8 SER C 511 LEU C 519 0
SHEET 2 AM 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AM 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AM 8 TYR C 540 ASP C 545 1 N ASP C 545 O ALA C 576
SHEET 5 AM 8 VAL C 619 TRP C 629 1 O ASP C 620 N TYR C 540
SHEET 6 AM 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AM 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AM 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AN 2 LYS D 41 THR D 42 0
SHEET 2 AN 2 VAL D 507 GLN D 508 1 O GLN D 508 N LYS D 41
SHEET 1 AO 3 GLU D 67 LYS D 71 0
SHEET 2 AO 3 ILE D 76 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 3 AO 3 SER D 86 VAL D 88 -1 O SER D 87 N VAL D 78
SHEET 1 AP 4 ASP D 104 ILE D 107 0
SHEET 2 AP 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AP 4 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 4 AP 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AQ 4 THR D 152 TRP D 157 0
SHEET 2 AQ 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
SHEET 3 AQ 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AQ 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AR 3 ILE D 194 ASN D 196 0
SHEET 2 AR 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AR 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AS 4 ILE D 194 ASN D 196 0
SHEET 2 AS 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AS 4 THR D 265 ASN D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AS 4 ILE D 285 ILE D 287 -1 O ILE D 285 N VAL D 270
SHEET 1 AT 2 LEU D 235 PHE D 240 0
SHEET 2 AT 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AU 4 HIS D 298 TRP D 305 0
SHEET 2 AU 4 ARG D 310 ARG D 317 -1 O LEU D 316 N TYR D 299
SHEET 3 AU 4 TYR D 322 ASP D 331 -1 O CYS D 328 N ILE D 311
SHEET 4 AU 4 ARG D 336 MET D 348 -1 O ASN D 338 N ASP D 329
SHEET 1 AV 4 HIS D 363 PHE D 364 0
SHEET 2 AV 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AV 4 ARG D 382 GLN D 388 -1 O HIS D 383 N ILE D 375
SHEET 4 AV 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 AW 4 VAL D 404 LEU D 410 0
SHEET 2 AW 4 TYR D 414 SER D 419 -1 O ILE D 418 N ILE D 405
SHEET 3 AW 4 ASN D 430 GLN D 435 -1 O ILE D 434 N LEU D 415
SHEET 4 AW 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AX 4 TYR D 457 PHE D 461 0
SHEET 2 AX 4 TYR D 467 CYS D 472 -1 O ARG D 471 N SER D 458
SHEET 3 AX 4 LEU D 479 SER D 484 -1 O HIS D 483 N TYR D 468
SHEET 4 AX 4 LYS D 489 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AY 8 SER D 511 ILE D 518 0
SHEET 2 AY 8 LYS D 523 LEU D 530 -1 O TYR D 526 N ASP D 515
SHEET 3 AY 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AY 8 TYR D 540 ASP D 545 1 N LEU D 543 O ILE D 574
SHEET 5 AY 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 544
SHEET 6 AY 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AY 8 GLU D 699 GLY D 705 1 O ILE D 703 N ALA D 652
SHEET 8 AY 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 339 CYS A 328
SSBOND 2 CYS A 394 CYS A 385
SSBOND 3 CYS A 447 CYS A 444
SSBOND 4 CYS A 472 CYS A 454
SSBOND 5 CYS A 762 CYS A 649
SSBOND 6 CYS B 339 CYS B 328
SSBOND 7 CYS B 394 CYS B 385
SSBOND 8 CYS B 447 CYS B 444
SSBOND 9 CYS B 472 CYS B 454
SSBOND 10 CYS B 762 CYS B 649
SSBOND 11 CYS C 339 CYS C 328
SSBOND 12 CYS C 394 CYS C 385
SSBOND 13 CYS C 447 CYS C 444
SSBOND 14 CYS C 472 CYS C 454
SSBOND 15 CYS C 762 CYS C 649
SSBOND 16 CYS D 339 CYS D 328
SSBOND 17 CYS D 394 CYS D 385
SSBOND 18 CYS D 447 CYS D 444
SSBOND 19 CYS D 472 CYS D 454
SSBOND 20 CYS D 762 CYS D 649
LINK ND2 ASN A 85 C1 NAG A 851
LINK ND2 ASN A 150 C1 NAG A1501
LINK ND2 ASN A 219 C1 NAG A2191
LINK ND2 ASN A 229 C1 NAG I2291
LINK ND2 ASN A 281 C1 NAG A2811
LINK ND2 ASN A 321 C1 NAG A3211
LINK ND2 ASN A 685 C1 NAG A6851
LINK ND2 ASN B 85 C1 NAG B 851
LINK ND2 ASN B 150 C1 NAG B1501
LINK ND2 ASN B 219 C1 NAG B2191
LINK ND2 ASN B 229 C1 NAG J2291
LINK ND2 ASN B 281 C1 NAG B2811
LINK ND2 ASN B 321 C1 NAG B3211
LINK ND2 ASN C 219 C1 NAG C2191
LINK ND2 ASN C 229 C1 NAG K2291
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 219 C1 NAG D2191
LINK ND2 ASN D 229 C1 NAG L2291
LINK ND2 ASN D 281 C1 NAG D2811
LINK O4 NAG I2291 C1 NAG I2292
LINK O4 NAG J2291 C1 NAG J2292
LINK O4 NAG K2291 C1 NAG K2292
LINK O4 NAG L2291 C1 NAG L2292
CISPEP 1 GLY A 474 PRO A 475 0 9.43
CISPEP 2 GLY B 474 PRO B 475 0 13.04
CISPEP 3 GLY C 474 PRO C 475 0 4.04
CISPEP 4 GLY D 474 PRO D 475 0 9.24
CRYST1 122.606 122.701 145.405 90.00 114.88 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 0.008156 0.000000 0.003783 0.00000
SCALE2 0.000000 0.008150 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007581 0.00000
TER 5964 PRO A 766
TER 5999 LYS E1004
TER 11993 PRO B 766
TER 12043 ASP F1006
TER 18001 PRO C 766
TER 18036 LYS G1004
TER 23994 PRO D 766
TER 24036 PRO H1005
MASTER 665 0 25 71 199 0 0 625627 8 411 232
END |