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HEADER HYDROLASE 23-JAN-07 2ONC
TITLE CRYSTAL STRUCTURE OF HUMAN DPP-4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE, DPP IV, T-CELL ACTIVATION
COMPND 5 ANTIGEN CD26, TP103, ADENOSINE DEAMINASE COMPLEXING
COMPND 6 PROTEIN 2, ADABP;
COMPND 7 EC: 3.4.14.5;
COMPND 8 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_STRAIN: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSXB9
KEYWDS DPP4 PROTEIN-INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.FENG,Z.ZHANG,M.B.WALLACE,J.A.STAFFORD,S.W.KALDOR,
AUTHOR 2 D.B.KASSEL,M.NAVRE,L.SHI,R.J.SKENE,T.ASAKAWA,K.TAKEUCHI,
AUTHOR 3 R.XU,D.R.WEBB,S.L.GWALTNEY
REVDAT 1 04-MAR-08 2ONC 0
JRNL AUTH J.FENG,Z.ZHANG,M.B.WALLACE,J.A.STAFFORD,S.W.KALDOR,
JRNL AUTH 2 D.B.KASSEL,M.NAVRE,L.SHI,R.J.SKENE,T.ASAKAWA,
JRNL AUTH 3 K.TAKEUCHI,R.XU,D.R.WEBB,S.L.GWALTNEY
JRNL TITL THE DISCOVERY OF ALOGLIPTIN (SYR-322), A POTENT
JRNL TITL 2 SELECTIVE, BIOAVAILABLE AND EFFICACIOUS INHIBITOR
JRNL TITL 3 OF DIPEPTIDYL PEPTIDASE IV
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.55 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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 118367
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5942
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4937
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 226
REMARK 3 BIN FREE R VALUE : 0.4350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 25016
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.33000
REMARK 3 B22 (A**2) : 2.64000
REMARK 3 B33 (A**2) : 1.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.39000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.741
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.318
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.225
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.136
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25026 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34080 ; 1.198 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2887 ; 4.987 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1218 ;33.490 ;23.941
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3945 ;15.694 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 116 ;15.647 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3608 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19140 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 10938 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 16943 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1170 ; 0.128 ; 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): 101 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.143 ; 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): 14777 ; 0.993 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23395 ; 1.660 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12185 ; 0.887 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10685 ; 1.399 ; 3.000
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 40 A 801
REMARK 3 ORIGIN FOR THE GROUP (A): -49.5289 -17.2730 19.1433
REMARK 3 T TENSOR
REMARK 3 T11: -0.0192 T22: -0.0434
REMARK 3 T33: -0.0325 T12: 0.0371
REMARK 3 T13: 0.0084 T23: -0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 0.7728 L22: 0.4476
REMARK 3 L33: 0.3974 L12: 0.1803
REMARK 3 L13: 0.0137 L23: -0.0345
REMARK 3 S TENSOR
REMARK 3 S11: -0.0487 S12: -0.1005 S13: 0.1871
REMARK 3 S21: 0.0245 S22: 0.0209 S23: 0.1013
REMARK 3 S31: 0.0271 S32: -0.0699 S33: 0.0278
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 36 B 801
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1476 -10.4145 20.9940
REMARK 3 T TENSOR
REMARK 3 T11: -0.0590 T22: -0.0603
REMARK 3 T33: -0.0201 T12: 0.0403
REMARK 3 T13: -0.0214 T23: -0.1141
REMARK 3 L TENSOR
REMARK 3 L11: 1.0781 L22: 0.4474
REMARK 3 L33: 0.3274 L12: 0.0523
REMARK 3 L13: 0.1349 L23: -0.0709
REMARK 3 S TENSOR
REMARK 3 S11: -0.0605 S12: -0.1769 S13: 0.1992
REMARK 3 S21: -0.0186 S22: 0.0908 S23: -0.1057
REMARK 3 S31: 0.0310 S32: 0.0667 S33: -0.0303
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 40 C 801
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2724 -17.3124 -33.6940
REMARK 3 T TENSOR
REMARK 3 T11: 0.0078 T22: -0.0255
REMARK 3 T33: -0.0996 T12: -0.0403
REMARK 3 T13: -0.0148 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.3355 L22: 0.2745
REMARK 3 L33: 0.3784 L12: -0.0030
REMARK 3 L13: -0.2572 L23: -0.0953
REMARK 3 S TENSOR
REMARK 3 S11: 0.0864 S12: 0.1348 S13: -0.1221
REMARK 3 S21: -0.0143 S22: -0.0371 S23: 0.0182
REMARK 3 S31: 0.0413 S32: -0.1465 S33: -0.0493
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 40 D 801
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4648 45.6662 47.2933
REMARK 3 T TENSOR
REMARK 3 T11: -0.0289 T22: 0.0193
REMARK 3 T33: -0.0477 T12: -0.0384
REMARK 3 T13: 0.0674 T23: -0.0722
REMARK 3 L TENSOR
REMARK 3 L11: 1.0578 L22: 0.6341
REMARK 3 L33: 0.5515 L12: 0.1117
REMARK 3 L13: 0.0990 L23: 0.2736
REMARK 3 S TENSOR
REMARK 3 S11: 0.0797 S12: -0.2489 S13: -0.0282
REMARK 3 S21: 0.0426 S22: -0.1571 S23: 0.2028
REMARK 3 S31: 0.0194 S32: -0.2376 S33: 0.0773
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ONC COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB041349.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118392
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.38900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG2000MME, 0.1M BICINE, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 61.85100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300
REMARK 300 REMARK: BIOLOGICAL ASSEMBLY
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 122.35700
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -61.85100
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 -1.000000 0.000000 0.000000 122.35700
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 61.85100
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 HIS A 36
REMARK 465 HIS A 37
REMARK 465 ALA A 38
REMARK 465 SER A 39
REMARK 465 GLN A 72
REMARK 465 GLU A 73
REMARK 465 ASN A 74
REMARK 465 GLN B 72
REMARK 465 GLU B 73
REMARK 465 ASN B 74
REMARK 465 HIS C 36
REMARK 465 HIS C 37
REMARK 465 ALA C 38
REMARK 465 SER C 39
REMARK 465 GLN C 72
REMARK 465 GLU C 73
REMARK 465 LYS C 392
REMARK 465 ASP C 393
REMARK 465 HIS D 36
REMARK 465 HIS D 37
REMARK 465 ALA D 38
REMARK 465 SER D 39
REMARK 465 GLN D 72
REMARK 465 GLU D 73
REMARK 465 ASN D 74
REMARK 465 LYS D 391
REMARK 465 LYS D 392
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 64 -157.28 -138.58
REMARK 500 ASN A 85 -133.44 -76.32
REMARK 500 SER A 86 -143.00 54.59
REMARK 500 SER A 87 -102.50 -162.52
REMARK 500 PHE A 95 30.55 -92.54
REMARK 500 GLU A 97 43.29 -89.70
REMARK 500 GLN A 123 -102.92 -108.83
REMARK 500 TRP A 124 -149.68 -87.94
REMARK 500 HIS A 162 31.73 -141.31
REMARK 500 ILE A 193 -51.96 -128.72
REMARK 500 SER A 242 -164.60 65.83
REMARK 500 ALA A 259 129.22 -39.01
REMARK 500 GLN A 320 38.24 -80.00
REMARK 500 ASP A 390 47.81 -108.57
REMARK 500 ASN A 450 76.95 -171.40
REMARK 500 TYR A 547 -78.03 -123.84
REMARK 500 ARG A 597 42.08 -140.89
REMARK 500 THR A 600 -96.51 -124.46
REMARK 500 SER A 630 -122.93 56.30
REMARK 500 PRO A 674 48.73 -84.96
REMARK 500 ASP A 678 -97.47 -122.41
REMARK 500 ASN A 710 -68.33 -95.42
REMARK 500 ASP A 739 -156.31 -108.84
REMARK 500 HIS B 66 6.43 -150.92
REMARK 500 GLU B 82 -83.90 -75.00
REMARK 500 TYR B 83 -83.57 -70.17
REMARK 500 ASN B 85 93.93 -65.49
REMARK 500 GLN B 123 -107.05 -107.12
REMARK 500 TRP B 124 -148.76 -85.48
REMARK 500 LEU B 137 0.65 -68.56
REMARK 500 TRP B 154 135.45 -170.29
REMARK 500 HIS B 162 41.74 -143.65
REMARK 500 ASP B 192 -3.03 71.05
REMARK 500 ILE B 193 -56.36 -121.24
REMARK 500 SER B 242 -165.20 67.44
REMARK 500 GLN B 320 38.55 -78.78
REMARK 500 ASP B 390 62.69 -105.35
REMARK 500 LYS B 392 -73.05 -105.57
REMARK 500 THR B 401 58.82 -93.89
REMARK 500 ALA B 409 149.06 -171.89
REMARK 500 LYS B 423 18.95 59.52
REMARK 500 ASN B 450 84.14 -156.50
REMARK 500 LYS B 463 -28.80 -38.43
REMARK 500 ASP B 488 -4.67 58.64
REMARK 500 GLN B 508 86.91 -69.40
REMARK 500 TYR B 547 -75.48 -124.06
REMARK 500 THR B 600 -89.07 -110.95
REMARK 500 SER B 630 -112.72 58.11
REMARK 500 PRO B 674 46.00 -80.23
REMARK 500 ASP B 678 -98.08 -116.51
REMARK 500 ASN B 710 -73.41 -90.45
REMARK 500 PHE B 713 -36.88 -39.70
REMARK 500 ASP B 739 -159.25 -105.56
REMARK 500 ASN C 51 46.43 70.15
REMARK 500 SER C 64 -163.89 -112.22
REMARK 500 TYR C 83 -74.10 -121.31
REMARK 500 GLN C 123 -97.60 -98.23
REMARK 500 TRP C 124 -144.07 -93.54
REMARK 500 ASN C 138 -70.37 -64.50
REMARK 500 TRP C 154 140.06 -170.41
REMARK 500 HIS C 162 25.50 -152.15
REMARK 500 ILE C 193 -62.13 -130.70
REMARK 500 SER C 242 -152.26 59.78
REMARK 500 GLN C 320 37.02 -79.25
REMARK 500 ASP C 390 40.74 -104.03
REMARK 500 LYS C 423 22.18 49.63
REMARK 500 ASP C 438 88.01 -160.61
REMARK 500 ASN C 450 93.27 -161.21
REMARK 500 GLU C 521 18.82 57.35
REMARK 500 LYS C 536 -17.99 -46.35
REMARK 500 TYR C 547 -70.19 -122.53
REMARK 500 THR C 600 -92.85 -128.37
REMARK 500 SER C 630 -117.62 63.95
REMARK 500 ASP C 678 -94.17 -129.11
REMARK 500 ASN C 710 -72.19 -86.17
REMARK 500 MET C 733 116.57 -163.82
REMARK 500 ASP C 739 -159.54 -103.39
REMARK 500 ILE C 742 56.91 37.73
REMARK 500 TYR D 58 79.75 -115.27
REMARK 500 SER D 64 -167.91 -129.94
REMARK 500 GLU D 82 -73.58 -63.51
REMARK 500 PHE D 89 -85.62 -97.31
REMARK 500 PHE D 98 -30.27 -134.32
REMARK 500 PRO D 109 -34.08 -37.68
REMARK 500 GLN D 123 -98.88 -103.25
REMARK 500 TRP D 124 -147.76 -98.89
REMARK 500 ILE D 193 -54.38 -130.05
REMARK 500 ALA D 213 44.80 -140.68
REMARK 500 SER D 242 -169.50 68.97
REMARK 500 SER D 275 33.72 -95.22
REMARK 500 ALA D 306 -67.28 -91.07
REMARK 500 THR D 307 -156.72 -122.11
REMARK 500 GLN D 320 44.00 -89.76
REMARK 500 ARG D 343 24.16 -77.28
REMARK 500 LEU D 366 -39.64 -38.55
REMARK 500 GLU D 408 -63.48 -90.47
REMARK 500 SER D 462 -161.11 -75.90
REMARK 500 ASN D 487 -4.41 -148.20
REMARK 500 ALA D 548 16.02 59.49
REMARK 500 ASP D 579 79.93 -104.96
REMARK 500 THR D 600 -96.07 -119.88
REMARK 500 ASN D 621 1.11 -67.99
REMARK 500 SER D 630 -121.50 57.29
REMARK 500 PRO D 674 35.26 -86.54
REMARK 500 ASP D 678 -85.07 -120.41
REMARK 500 ASN D 679 24.80 -145.57
REMARK 500 ASN D 710 -74.24 -81.60
REMARK 500 ASP D 739 -159.22 -108.01
REMARK 500 ILE D 742 57.78 28.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 861 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH B 892 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH C 911 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH A 941 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH B 989 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B 995 DISTANCE = 5.12 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 802
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 803
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 804
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 805
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 806
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 807
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 808
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 809
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 802
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 804
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 805
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE C 802
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE C 803
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE C 804
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE C 805
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE C 807
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE D 802
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE D 803
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE D 804
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: SY1 BINDING SITE FOR RESIDUE A 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: SY1 BINDING SITE FOR RESIDUE A 801
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: SY1 BINDING SITE FOR RESIDUE B 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: SY1 BINDING SITE FOR RESIDUE B 801
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: SY1 BINDING SITE FOR RESIDUE C 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: SY1 BINDING SITE FOR RESIDUE C 801
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: SY1 BINDING SITE FOR RESIDUE D 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 SITE_DESCRIPTION: SY1 BINDING SITE FOR RESIDUE D 801
DBREF 2ONC A 41 766 UNP P27487 DPP4_HUMAN 41 766
DBREF 2ONC B 41 766 UNP P27487 DPP4_HUMAN 41 766
DBREF 2ONC C 41 766 UNP P27487 DPP4_HUMAN 41 766
DBREF 2ONC D 41 766 UNP P27487 DPP4_HUMAN 41 766
SEQADV 2ONC HIS A 36 UNP P27487 EXPRESSION TAG
SEQADV 2ONC HIS A 37 UNP P27487 EXPRESSION TAG
SEQADV 2ONC ALA A 38 UNP P27487 EXPRESSION TAG
SEQADV 2ONC SER A 39 UNP P27487 EXPRESSION TAG
SEQADV 2ONC ALA A 40 UNP P27487 EXPRESSION TAG
SEQADV 2ONC HIS B 36 UNP P27487 EXPRESSION TAG
SEQADV 2ONC HIS B 37 UNP P27487 EXPRESSION TAG
SEQADV 2ONC ALA B 38 UNP P27487 EXPRESSION TAG
SEQADV 2ONC SER B 39 UNP P27487 EXPRESSION TAG
SEQADV 2ONC ALA B 40 UNP P27487 EXPRESSION TAG
SEQADV 2ONC HIS C 36 UNP P27487 EXPRESSION TAG
SEQADV 2ONC HIS C 37 UNP P27487 EXPRESSION TAG
SEQADV 2ONC ALA C 38 UNP P27487 EXPRESSION TAG
SEQADV 2ONC SER C 39 UNP P27487 EXPRESSION TAG
SEQADV 2ONC ALA C 40 UNP P27487 EXPRESSION TAG
SEQADV 2ONC HIS D 36 UNP P27487 EXPRESSION TAG
SEQADV 2ONC HIS D 37 UNP P27487 EXPRESSION TAG
SEQADV 2ONC ALA D 38 UNP P27487 EXPRESSION TAG
SEQADV 2ONC SER D 39 UNP P27487 EXPRESSION TAG
SEQADV 2ONC ALA D 40 UNP P27487 EXPRESSION TAG
SEQRES 1 A 731 HIS HIS ALA SER ALA LYS THR TYR THR LEU THR ASP TYR
SEQRES 2 A 731 LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG
SEQRES 3 A 731 TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN
SEQRES 4 A 731 ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER
SEQRES 5 A 731 VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS
SEQRES 6 A 731 SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE
SEQRES 7 A 731 ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS
SEQRES 8 A 731 SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS
SEQRES 9 A 731 ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR
SEQRES 10 A 731 GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA
SEQRES 11 A 731 TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO
SEQRES 12 A 731 ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU
SEQRES 13 A 731 ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU
SEQRES 14 A 731 GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER
SEQRES 15 A 731 PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP
SEQRES 16 A 731 THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP
SEQRES 17 A 731 GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR
SEQRES 18 A 731 PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE
SEQRES 19 A 731 VAL VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA
SEQRES 20 A 731 THR SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE
SEQRES 21 A 731 GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN
SEQRES 22 A 731 GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN
SEQRES 23 A 731 TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER
SEQRES 24 A 731 GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU
SEQRES 25 A 731 MET SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER
SEQRES 26 A 731 GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS
SEQRES 27 A 731 ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR
SEQRES 28 A 731 PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS
SEQRES 29 A 731 GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER
SEQRES 30 A 731 ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET
SEQRES 31 A 731 PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP
SEQRES 32 A 731 TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO
SEQRES 33 A 731 GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU
SEQRES 34 A 731 ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU
SEQRES 35 A 731 PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY
SEQRES 36 A 731 LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET
SEQRES 37 A 731 LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE
SEQRES 38 A 731 ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE
SEQRES 39 A 731 LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU
SEQRES 40 A 731 LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA
SEQRES 41 A 731 ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA
SEQRES 42 A 731 SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG
SEQRES 43 A 731 GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE
SEQRES 44 A 731 ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE
SEQRES 45 A 731 GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP
SEQRES 46 A 731 ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY
SEQRES 47 A 731 TYR VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL
SEQRES 48 A 731 PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP
SEQRES 49 A 731 GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY
SEQRES 50 A 731 LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN
SEQRES 51 A 731 SER THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL
SEQRES 52 A 731 GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL
SEQRES 53 A 731 HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL
SEQRES 54 A 731 ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP
SEQRES 55 A 731 GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS
SEQRES 56 A 731 ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE
SEQRES 57 A 731 SER LEU PRO
SEQRES 1 B 731 HIS HIS ALA SER ALA LYS THR TYR THR LEU THR ASP TYR
SEQRES 2 B 731 LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG
SEQRES 3 B 731 TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN
SEQRES 4 B 731 ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER
SEQRES 5 B 731 VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS
SEQRES 6 B 731 SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE
SEQRES 7 B 731 ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS
SEQRES 8 B 731 SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS
SEQRES 9 B 731 ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR
SEQRES 10 B 731 GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA
SEQRES 11 B 731 TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO
SEQRES 12 B 731 ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU
SEQRES 13 B 731 ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU
SEQRES 14 B 731 GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER
SEQRES 15 B 731 PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP
SEQRES 16 B 731 THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP
SEQRES 17 B 731 GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR
SEQRES 18 B 731 PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE
SEQRES 19 B 731 VAL VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA
SEQRES 20 B 731 THR SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE
SEQRES 21 B 731 GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN
SEQRES 22 B 731 GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN
SEQRES 23 B 731 TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER
SEQRES 24 B 731 GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU
SEQRES 25 B 731 MET SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER
SEQRES 26 B 731 GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS
SEQRES 27 B 731 ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR
SEQRES 28 B 731 PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS
SEQRES 29 B 731 GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER
SEQRES 30 B 731 ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET
SEQRES 31 B 731 PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP
SEQRES 32 B 731 TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO
SEQRES 33 B 731 GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU
SEQRES 34 B 731 ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU
SEQRES 35 B 731 PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY
SEQRES 36 B 731 LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET
SEQRES 37 B 731 LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE
SEQRES 38 B 731 ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE
SEQRES 39 B 731 LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU
SEQRES 40 B 731 LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA
SEQRES 41 B 731 ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA
SEQRES 42 B 731 SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG
SEQRES 43 B 731 GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE
SEQRES 44 B 731 ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE
SEQRES 45 B 731 GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP
SEQRES 46 B 731 ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY
SEQRES 47 B 731 TYR VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL
SEQRES 48 B 731 PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP
SEQRES 49 B 731 GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY
SEQRES 50 B 731 LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN
SEQRES 51 B 731 SER THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL
SEQRES 52 B 731 GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL
SEQRES 53 B 731 HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL
SEQRES 54 B 731 ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP
SEQRES 55 B 731 GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS
SEQRES 56 B 731 ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE
SEQRES 57 B 731 SER LEU PRO
SEQRES 1 C 731 HIS HIS ALA SER ALA LYS THR TYR THR LEU THR ASP TYR
SEQRES 2 C 731 LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG
SEQRES 3 C 731 TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN
SEQRES 4 C 731 ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER
SEQRES 5 C 731 VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS
SEQRES 6 C 731 SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE
SEQRES 7 C 731 ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS
SEQRES 8 C 731 SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS
SEQRES 9 C 731 ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR
SEQRES 10 C 731 GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA
SEQRES 11 C 731 TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO
SEQRES 12 C 731 ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU
SEQRES 13 C 731 ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU
SEQRES 14 C 731 GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER
SEQRES 15 C 731 PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP
SEQRES 16 C 731 THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP
SEQRES 17 C 731 GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR
SEQRES 18 C 731 PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE
SEQRES 19 C 731 VAL VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA
SEQRES 20 C 731 THR SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE
SEQRES 21 C 731 GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN
SEQRES 22 C 731 GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN
SEQRES 23 C 731 TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER
SEQRES 24 C 731 GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU
SEQRES 25 C 731 MET SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER
SEQRES 26 C 731 GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS
SEQRES 27 C 731 ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR
SEQRES 28 C 731 PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS
SEQRES 29 C 731 GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER
SEQRES 30 C 731 ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET
SEQRES 31 C 731 PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP
SEQRES 32 C 731 TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO
SEQRES 33 C 731 GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU
SEQRES 34 C 731 ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU
SEQRES 35 C 731 PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY
SEQRES 36 C 731 LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET
SEQRES 37 C 731 LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE
SEQRES 38 C 731 ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE
SEQRES 39 C 731 LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU
SEQRES 40 C 731 LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA
SEQRES 41 C 731 ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA
SEQRES 42 C 731 SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG
SEQRES 43 C 731 GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE
SEQRES 44 C 731 ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE
SEQRES 45 C 731 GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP
SEQRES 46 C 731 ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY
SEQRES 47 C 731 TYR VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL
SEQRES 48 C 731 PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP
SEQRES 49 C 731 GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY
SEQRES 50 C 731 LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN
SEQRES 51 C 731 SER THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL
SEQRES 52 C 731 GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL
SEQRES 53 C 731 HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL
SEQRES 54 C 731 ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP
SEQRES 55 C 731 GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS
SEQRES 56 C 731 ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE
SEQRES 57 C 731 SER LEU PRO
SEQRES 1 D 731 HIS HIS ALA SER ALA LYS THR TYR THR LEU THR ASP TYR
SEQRES 2 D 731 LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG
SEQRES 3 D 731 TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN
SEQRES 4 D 731 ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER
SEQRES 5 D 731 VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS
SEQRES 6 D 731 SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE
SEQRES 7 D 731 ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS
SEQRES 8 D 731 SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS
SEQRES 9 D 731 ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR
SEQRES 10 D 731 GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA
SEQRES 11 D 731 TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO
SEQRES 12 D 731 ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU
SEQRES 13 D 731 ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU
SEQRES 14 D 731 GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER
SEQRES 15 D 731 PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP
SEQRES 16 D 731 THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP
SEQRES 17 D 731 GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR
SEQRES 18 D 731 PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE
SEQRES 19 D 731 VAL VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA
SEQRES 20 D 731 THR SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE
SEQRES 21 D 731 GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN
SEQRES 22 D 731 GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN
SEQRES 23 D 731 TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER
SEQRES 24 D 731 GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU
SEQRES 25 D 731 MET SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER
SEQRES 26 D 731 GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS
SEQRES 27 D 731 ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR
SEQRES 28 D 731 PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS
SEQRES 29 D 731 GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER
SEQRES 30 D 731 ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET
SEQRES 31 D 731 PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP
SEQRES 32 D 731 TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO
SEQRES 33 D 731 GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU
SEQRES 34 D 731 ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU
SEQRES 35 D 731 PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY
SEQRES 36 D 731 LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET
SEQRES 37 D 731 LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE
SEQRES 38 D 731 ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE
SEQRES 39 D 731 LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU
SEQRES 40 D 731 LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA
SEQRES 41 D 731 ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA
SEQRES 42 D 731 SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG
SEQRES 43 D 731 GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE
SEQRES 44 D 731 ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE
SEQRES 45 D 731 GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP
SEQRES 46 D 731 ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY
SEQRES 47 D 731 TYR VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL
SEQRES 48 D 731 PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP
SEQRES 49 D 731 GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY
SEQRES 50 D 731 LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN
SEQRES 51 D 731 SER THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL
SEQRES 52 D 731 GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL
SEQRES 53 D 731 HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL
SEQRES 54 D 731 ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP
SEQRES 55 D 731 GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS
SEQRES 56 D 731 ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE
SEQRES 57 D 731 SER LEU PRO
MODRES 2ONC ASN A 85 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN A 150 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN A 219 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN A 229 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN A 321 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN B 85 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN B 150 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN B 219 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN B 229 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN B 281 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN C 150 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN C 219 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN C 229 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN C 281 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN C 321 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN D 150 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN D 229 ASN GLYCOSYLATION SITE
MODRES 2ONC ASN D 281 ASN GLYCOSYLATION SITE
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET NAG A 807 14
HET NAG A 808 14
HET NAG A 809 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 807 14
HET NAG B 805 14
HET NAG B 806 14
HET NAG C 802 14
HET NAG C 803 14
HET NAG C 806 14
HET NAG C 807 14
HET NAG D 802 14
HET NAG C 804 14
HET NAG C 805 14
HET NAG D 805 14
HET NAG D 803 14
HET NAG D 804 14
HET SY1 A 800 27
HET SY1 A 801 27
HET SY1 B 800 27
HET SY1 B 801 27
HET SY1 C 800 27
HET SY1 C 801 27
HET SY1 D 800 27
HET SY1 D 801 27
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SY1 2-({2-[(3R)-3-AMINOPIPERIDIN-1-YL]-4-OXOQUINAZOLIN-
HETNAM 2 SY1 3(4H)-YL}METHYL)BENZONITRILE
HETSYN NAG NAG
FORMUL 5 NAG 24(C8 H15 N O6)
FORMUL 24 SY1 8(C21 H21 N5 O)
FORMUL 32 HOH *756(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 THR A 94 GLY A 99 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 LEU A 504 1 8
HELIX 8 8 ASN A 562 THR A 570 1 9
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
HELIX 11 11 THR A 600 LYS A 615 1 16
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 ARG A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 GLY A 672 1 10
HELIX 15 15 ASN A 679 SER A 686 1 8
HELIX 16 16 VAL A 688 VAL A 698 5 11
HELIX 17 17 PHE A 713 VAL A 726 1 14
HELIX 18 18 SER A 744 PHE A 763 1 20
HELIX 19 19 THR B 44 ASN B 51 1 8
HELIX 20 20 GLU B 91 GLY B 99 5 9
HELIX 21 21 ASP B 200 VAL B 207 1 8
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 VAL B 341 GLN B 344 5 4
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 ASN B 497 GLN B 505 1 9
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 MET B 616 1 17
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ASP B 663 GLY B 672 1 10
HELIX 32 32 ASN B 679 SER B 686 1 8
HELIX 33 33 VAL B 688 VAL B 698 5 11
HELIX 34 34 PHE B 713 VAL B 726 1 14
HELIX 35 35 SER B 744 PHE B 763 1 20
HELIX 36 36 THR C 44 ASN C 51 1 8
HELIX 37 37 ASP C 200 VAL C 207 1 8
HELIX 38 38 PRO C 290 ILE C 295 1 6
HELIX 39 39 LEU C 340 GLN C 344 5 5
HELIX 40 40 GLU C 421 MET C 425 5 5
HELIX 41 41 ASN C 497 VAL C 507 1 11
HELIX 42 42 ASN C 562 THR C 570 1 9
HELIX 43 43 GLY C 587 HIS C 592 1 6
HELIX 44 44 ALA C 593 ASN C 595 5 3
HELIX 45 45 THR C 600 LYS C 615 1 16
HELIX 46 46 SER C 630 GLY C 641 1 12
HELIX 47 47 ARG C 658 TYR C 662 5 5
HELIX 48 48 ASP C 663 GLY C 672 1 10
HELIX 49 49 ASN C 679 SER C 686 1 8
HELIX 50 50 VAL C 688 VAL C 698 5 11
HELIX 51 51 HIS C 712 VAL C 726 1 15
HELIX 52 52 SER C 744 PHE C 763 1 20
HELIX 53 53 THR D 44 LYS D 50 1 7
HELIX 54 54 ASN D 92 ASP D 96 5 5
HELIX 55 55 ASP D 200 VAL D 207 1 8
HELIX 56 56 PRO D 290 ILE D 295 1 6
HELIX 57 57 GLU D 421 MET D 425 5 5
HELIX 58 58 ASN D 497 LEU D 504 1 8
HELIX 59 59 ASN D 562 THR D 570 1 9
HELIX 60 60 GLY D 587 HIS D 592 1 6
HELIX 61 61 ALA D 593 ASN D 595 5 3
HELIX 62 62 THR D 600 MET D 616 1 17
HELIX 63 63 SER D 630 GLY D 641 1 12
HELIX 64 64 ARG D 658 TYR D 662 5 5
HELIX 65 65 ASP D 663 GLY D 672 1 10
HELIX 66 66 ASN D 679 SER D 686 1 8
HELIX 67 67 ARG D 691 VAL D 698 5 8
HELIX 68 68 HIS D 712 VAL D 726 1 15
HELIX 69 69 SER D 744 PHE D 763 1 20
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 ARG A 61 TRP A 62 0
SHEET 2 B 4 GLU A 67 TYR A 70 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ILE A 76 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 B 4 VAL A 88 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 C 4 ASP A 104 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O 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 LYS A 267 N GLN A 227
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 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 TRP A 305 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 I 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 I 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 ASP A 438 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 GLN A 469 N SER A 460
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 ILE A 518 0
SHEET 2 M 8 LYS A 523 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 4 ARG B 61 TRP B 62 0
SHEET 2 N 4 GLU B 67 TYR B 70 -1 O LEU B 69 N ARG B 61
SHEET 3 N 4 ILE B 76 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 N 4 VAL B 88 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 GLU B 117 N ASP B 104
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 THR B 265 N ASN B 229
SHEET 4 R 4 ILE B 285 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 LYS B 250 N PHE B 240
SHEET 1 T 4 HIS B 298 TRP B 305 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 T 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 T 4 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 1 U 4 HIS B 298 TRP B 305 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 U 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
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 ASP B 438 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 THR B 522 N LEU B 519
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 VAL B 546 1 N ASP B 545 O ALA B 576
SHEET 5 Y 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
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 TYR C 70 -1 O LEU C 69 N ARG C 61
SHEET 3 Z 4 ILE C 76 ASN C 80 -1 O PHE C 79 N TYR C 68
SHEET 4 Z 4 SER C 86 LEU C 90 -1 O SER C 87 N VAL C 78
SHEET 1 AA 3 ASP C 104 ILE C 107 0
SHEET 2 AA 3 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AA 3 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 1 AB 4 TRP C 154 TRP C 157 0
SHEET 2 AB 4 LEU C 164 TRP C 168 -1 O ALA C 165 N THR C 156
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 287 N PHE C 268
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 TRP C 305 0
SHEET 2 AF 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AF 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AF 4 TRP C 337 ASN C 338 -1 O ASN C 338 N ASP C 329
SHEET 1 AG 4 HIS C 298 TRP C 305 0
SHEET 2 AG 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AG 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AG 4 HIS C 345 MET C 348 -1 O GLU C 347 N SER C 323
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 ILE C 434 N LEU C 415
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 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
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 VAL C 546 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 542
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 ILE C 703 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 4 ARG D 61 TRP D 62 0
SHEET 2 AL 4 GLU D 67 TYR D 70 -1 O LEU D 69 N ARG D 61
SHEET 3 AL 4 LEU D 77 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 4 AL 4 SER D 86 VAL D 88 -1 O SER D 87 N VAL D 78
SHEET 1 AM 4 ASP D 104 ILE D 107 0
SHEET 2 AM 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AM 4 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 4 AM 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AN 4 THR D 152 TRP D 157 0
SHEET 2 AN 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
SHEET 3 AN 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AN 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AO 3 ILE D 194 ASN D 196 0
SHEET 2 AO 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AO 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AP 4 ILE D 194 ASN D 196 0
SHEET 2 AP 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AP 4 THR D 265 ASN D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AP 4 ILE D 285 ILE D 287 -1 O ILE D 285 N VAL D 270
SHEET 1 AQ 2 LEU D 235 PHE D 240 0
SHEET 2 AQ 2 LYS D 250 PRO D 255 -1 O VAL D 252 N TYR D 238
SHEET 1 AR 4 HIS D 298 TRP D 305 0
SHEET 2 AR 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AR 4 TYR D 322 TYR D 330 -1 O VAL D 324 N TRP D 315
SHEET 4 AR 4 TRP D 337 CYS D 339 -1 O ASN D 338 N ASP D 329
SHEET 1 AS 4 HIS D 298 TRP D 305 0
SHEET 2 AS 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AS 4 TYR D 322 TYR D 330 -1 O VAL D 324 N TRP D 315
SHEET 4 AS 4 HIS D 345 MET D 348 -1 O HIS D 345 N MET D 325
SHEET 1 AT 4 HIS D 363 PHE D 364 0
SHEET 2 AT 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AT 4 ARG D 382 GLN D 388 -1 O HIS D 383 N ILE D 375
SHEET 4 AT 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 AU 4 VAL D 404 LEU D 410 0
SHEET 2 AU 4 TYR D 414 SER D 419 -1 O ILE D 418 N ILE D 405
SHEET 3 AU 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AU 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AV 4 TYR D 457 PHE D 461 0
SHEET 2 AV 4 TYR D 467 CYS D 472 -1 O GLN D 469 N SER D 460
SHEET 3 AV 4 LEU D 479 SER D 484 -1 O HIS D 483 N TYR D 468
SHEET 4 AV 4 LYS D 489 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AW 8 SER D 511 LEU D 519 0
SHEET 2 AW 8 THR D 522 LEU D 530 -1 O TYR D 526 N ASP D 515
SHEET 3 AW 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AW 8 TYR D 540 ASP D 545 1 N LEU D 543 O ILE D 574
SHEET 5 AW 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 544
SHEET 6 AW 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AW 8 GLU D 699 GLY D 705 1 O LEU D 701 N ALA D 652
SHEET 8 AW 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.04
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.04
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.04
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.04
SSBOND 13 CYS C 444 CYS C 447 1555 1555 2.05
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.06
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.05
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.04
SSBOND 17 CYS D 385 CYS D 394 1555 1555 2.05
SSBOND 18 CYS D 444 CYS D 447 1555 1555 2.03
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.04
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.04
LINK ND2 ASN A 85 C1 NAG A 802 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A 803 1555 1555 1.46
LINK ND2 ASN A 219 C1 NAG A 804 1555 1555 1.45
LINK ND2 ASN A 321 C1 NAG A 807 1555 1555 1.45
LINK ND2 ASN B 85 C1 NAG B 802 1555 1555 1.45
LINK ND2 ASN B 150 C1 NAG B 803 1555 1555 1.45
LINK ND2 ASN B 219 C1 NAG B 804 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG B 807 1555 1555 1.45
LINK ND2 ASN C 150 C1 NAG C 802 1555 1555 1.45
LINK ND2 ASN C 219 C1 NAG C 803 1555 1555 1.44
LINK ND2 ASN C 281 C1 NAG C 806 1555 1555 1.46
LINK ND2 ASN C 321 C1 NAG C 807 1555 1555 1.45
LINK ND2 ASN D 150 C1 NAG D 802 1555 1555 1.45
LINK ND2 ASN D 281 C1 NAG D 805 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG A 808 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG B 805 1555 1555 1.45
LINK ND2 ASN C 229 C1 NAG C 804 1555 1555 1.45
LINK ND2 ASN D 229 C1 NAG D 803 1555 1555 1.45
LINK O4 NAG A 805 C1 NAG A 806 1555 1555 1.45
LINK O4 NAG A 808 C1 NAG A 809 1555 1555 1.44
LINK O4 NAG B 805 C1 NAG B 806 1555 1555 1.45
LINK O4 NAG C 804 C1 NAG C 805 1555 1555 1.44
LINK O4 NAG D 803 C1 NAG D 804 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 4.15
CISPEP 2 GLY B 474 PRO B 475 0 5.56
CISPEP 3 GLY C 474 PRO C 475 0 5.01
CISPEP 4 GLY D 474 PRO D 475 0 0.59
SITE 1 AC1 2 ASN A 85 SER A 86
SITE 1 AC2 2 ASN A 150 HOH A1006
SITE 1 AC3 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC4 1 ASN A 281
SITE 1 AC5 1 GLN C 141
SITE 1 AC6 3 ILE A 319 ASN A 321 SER A 349
SITE 1 AC7 4 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 1 AC8 1 THR A 231
SITE 1 AC9 2 TYR B 83 ASN B 85
SITE 1 BC1 4 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 1 BC2 4 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 1 BC3 2 ASN C 150 HOH C1015
SITE 1 BC4 4 ASN C 219 THR C 221 GLN C 308 GLU C 309
SITE 1 BC5 5 ILE C 194 ASN C 229 THR C 231 GLU C 232
SITE 2 BC5 5 HOH C1026
SITE 1 BC6 1 GLU C 232
SITE 1 BC7 6 ILE C 319 ASN C 321 SER C 349 THR C 350
SITE 2 BC7 6 ARG C 596 HOH C1019
SITE 1 BC8 4 ILE D 148 ASN D 150 HOH D 879 HOH D 900
SITE 1 BC9 4 ILE D 194 ASN D 229 THR D 231 GLU D 232
SITE 1 CC1 1 GLU D 232
SITE 1 CC2 8 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 CC2 8 SER A 630 TYR A 631 TYR A 662 TYR A 666
SITE 1 CC3 6 GLN A 123 GLU A 191 ASP A 192 LYS A 250
SITE 2 CC3 6 THR A 251 ARG A 253
SITE 1 CC4 10 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 CC4 10 TRP B 629 SER B 630 TYR B 631 TYR B 662
SITE 3 CC4 10 TYR B 666 HOH B 908
SITE 1 CC5 5 GLN B 123 GLU B 191 ASP B 192 LYS B 250
SITE 2 CC5 5 ARG B 253
SITE 1 CC6 10 ARG C 125 GLU C 205 GLU C 206 TYR C 547
SITE 2 CC6 10 TRP C 629 SER C 630 TYR C 631 TYR C 662
SITE 3 CC6 10 TYR C 666 HOH C 856
SITE 1 CC7 5 GLN C 123 ASP C 192 PHE C 240 LYS C 250
SITE 2 CC7 5 ARG C 253
SITE 1 CC8 9 ARG D 125 GLU D 205 GLU D 206 TYR D 547
SITE 2 CC8 9 SER D 630 TYR D 631 TYR D 662 TYR D 666
SITE 3 CC8 9 HOH D 858
SITE 1 CC9 4 GLN D 123 ASP D 192 LYS D 250 ARG D 253
CRYST1 122.357 123.702 145.358 90.00 114.89 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 0.008173 0.000000 0.003792 0.00000
SCALE2 0.000000 0.008084 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007584 0.00000
TER 5926 PRO A 766
TER 11885 PRO B 766
TER 17804 PRO C 766
TER 23712 PRO D 766
MASTER 547 0 32 69 197 0 39 625016 4 610 228
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