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HEADER HYDROLASE/IMMUNE SYSTEM, INHIBITOR 01-JUN-12 4FFV
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPP4, DPP-IV, CD26) IN
TITLE 2 COMPLEX WITH 11A19 FAB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BILE CANALICULUS DOMAIN-SPECIFIC MEMBRANE GLYCOPROTEIN,
COMPND 5 DIPEPTIDYL PEPTIDASE IV, DPP IV, GP110 GLYCOPROTEIN, T-CELL
COMPND 6 ACTIVATION ANTIGEN CD26, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM,
COMPND 7 DIPEPTIDYL PEPTIDASE IV MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE
COMPND 8 FORM, DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM, DIPEPTIDYL PEPTIDASE 4 60
COMPND 9 KDA SOLUBLE FORM, DIPEPTIDYL PEPTIDASE IV 60 KDA SOLUBLE FORM;
COMPND 10 EC: 3.4.14.5;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: 11A19 FAB LIGHT CHAIN;
COMPND 14 CHAIN: C, L;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: 11A19 FAB HEAVY CHAIN;
COMPND 17 CHAIN: D, H
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: DPP4, CD26;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HEK293 6E;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 16 ORGANISM_COMMON: MOUSE;
SOURCE 17 ORGANISM_TAXID: 10090
KEYWDS HYDROLASE, HYDROLASE-IMMUNE SYSTEM, INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WANG,A.SUDOM,N.P.WALKER,X.MIN
REVDAT 1 12-DEC-12 4FFV 0
JRNL AUTH J.TANG,J.MAJETI,A.SUDOM,Y.XIONG,M.LU,Q.LIU,J.HIGBEE,Y.ZHANG,
JRNL AUTH 2 Y.WANG,W.WANG,P.CAO,Z.XIA,S.JOHNSTONE,X.YANG,T.YU,N.SHARKOV,
JRNL AUTH 3 N.WALKER,H.TU,W.SHEN,Z.WANG,X.MIN
JRNL TITL AN INHIBITORY ANTIBODY AGAINST DPP IV IMPROVES GLUCOSE
JRNL TITL 2 TOLERANCE IN VIVO - VALIDATION OF LARGE MOLECULE APPROACH
JRNL TITL 3 FOR DPP IV INHIBITION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 136244
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) : 0.272
REMARK 3 R VALUE (WORKING SET) : 0.271
REMARK 3 FREE R VALUE : 0.301
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7181
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9908
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.3610
REMARK 3 BIN FREE R VALUE SET COUNT : 534
REMARK 3 BIN FREE R VALUE : 0.3770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18210
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 213
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : -0.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.361
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.272
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.238
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.199
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.886
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.858
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 18725 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 17012 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 25495 ; 0.992 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): 39219 ; 0.706 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2277 ; 5.978 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 849 ;34.402 ;24.205
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3020 ;16.068 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 75 ;15.869 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2767 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 21226 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4465 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 11455 ; 0.859 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18603 ; 1.582 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7354 ; 2.373 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7008 ; 3.623 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4FFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB072849.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI (111)
REMARK 200 OPTICS : 3X3 CCD ARRAY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 100.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09700
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.54400
REMARK 200 R SYM FOR SHELL (I) : 0.54400
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2-2.7 M AMMONIUM SULFATE, 0.1 M TRIS
REMARK 280 7.5-7.9, VAPOR DIFFUSION, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 100.86000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, L, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG A 38
REMARK 465 LEU A 766
REMARK 465 ARG A 767
REMARK 465 ARG B 38
REMARK 465 ARG C 154
REMARK 465 GLN C 155
REMARK 465 ASN C 156
REMARK 465 VAL D 131
REMARK 465 CYS D 132
REMARK 465 GLY D 133
REMARK 465 GLY D 134
REMARK 465 THR D 135
REMARK 465 THR D 136
REMARK 465 GLY D 137
REMARK 465 SER D 138
REMARK 465 ARG L 154
REMARK 465 GLN L 155
REMARK 465 ASN L 156
REMARK 465 CYS H 132
REMARK 465 GLY H 133
REMARK 465 GLY H 134
REMARK 465 THR H 135
REMARK 465 THR H 136
REMARK 465 GLY H 137
REMARK 465 SER H 138
REMARK 465 LEU H 163
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 ASN A 49 47.98 70.00
REMARK 500 SER A 62 -169.60 -129.59
REMARK 500 GLN A 70 -93.46 -97.64
REMARK 500 GLU A 71 60.88 -115.17
REMARK 500 HIS A 81 -156.26 -104.62
REMARK 500 GLN A 121 -99.59 -117.69
REMARK 500 TRP A 122 -147.21 -93.37
REMARK 500 ASN A 148 153.37 -46.65
REMARK 500 HIS A 160 37.94 -149.39
REMARK 500 VAL A 191 -63.44 -125.71
REMARK 500 SER A 240 -166.91 60.87
REMARK 500 GLN A 318 43.45 -90.81
REMARK 500 ASN A 442 80.45 -69.54
REMARK 500 ASN A 451 88.37 -155.91
REMARK 500 GLN A 489 46.26 -75.68
REMARK 500 TYR A 548 -67.73 -125.53
REMARK 500 ARG A 598 57.54 -140.07
REMARK 500 THR A 601 -91.00 -123.74
REMARK 500 SER A 631 -115.75 63.00
REMARK 500 ASP A 679 -110.50 -117.85
REMARK 500 ASN A 711 -72.38 -99.92
REMARK 500 ILE A 743 47.98 39.42
REMARK 500 SER B 55 -169.81 -129.88
REMARK 500 HIS B 81 -149.16 -105.68
REMARK 500 GLN B 121 -95.95 -110.77
REMARK 500 TRP B 122 -148.28 -96.86
REMARK 500 ASN B 148 148.83 -38.18
REMARK 500 GLU B 189 -68.69 -17.94
REMARK 500 VAL B 191 -60.31 -135.05
REMARK 500 ILE B 205 -68.87 -100.40
REMARK 500 SER B 240 -167.12 61.20
REMARK 500 GLN B 318 42.07 -91.36
REMARK 500 PRO B 391 -77.93 -36.87
REMARK 500 GLN B 393 84.08 -60.83
REMARK 500 LYS B 424 23.65 46.44
REMARK 500 ASN B 451 81.67 -162.96
REMARK 500 MET B 504 -44.45 93.13
REMARK 500 TYR B 548 -65.74 -122.69
REMARK 500 LYS B 597 8.52 55.75
REMARK 500 THR B 601 -70.06 -129.75
REMARK 500 SER B 631 -120.52 62.06
REMARK 500 ASP B 679 -103.75 -112.75
REMARK 500 ASN B 711 -75.84 -91.78
REMARK 500 TRP C 46 -64.34 -102.56
REMARK 500 SER C 69 95.72 -164.08
REMARK 500 ALA C 82 101.09 -49.74
REMARK 500 ALA C 83 -169.52 -161.72
REMARK 500 TRP C 90 45.12 -151.50
REMARK 500 LEU C 103 87.57 -67.69
REMARK 500 ASN C 136 -97.66 -68.57
REMARK 500
REMARK 500 THIS ENTRY HAS 87 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY C 99 GLY C 100 -148.04
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4FFV A 38 767 UNP P14740 DPP4_RAT 38 767
DBREF 4FFV B 38 767 UNP P14740 DPP4_RAT 38 767
DBREF 4FFV C 1 210 PDB 4FFV 4FFV 1 210
DBREF 4FFV L 1 210 PDB 4FFV 4FFV 1 210
DBREF 4FFV D 1 217 PDB 4FFV 4FFV 1 217
DBREF 4FFV H 1 217 PDB 4FFV 4FFV 1 217
SEQRES 1 A 730 ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN THR
SEQRES 2 A 730 PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER ASP
SEQRES 3 A 730 SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 4 A 730 PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU GLU
SEQRES 5 A 730 ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER ASP
SEQRES 6 A 730 TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU GLU
SEQRES 7 A 730 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 A 730 SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 A 730 THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 10 A 730 TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP LYS
SEQRES 11 A 730 ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO SER
SEQRES 12 A 730 HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE PHE
SEQRES 13 A 730 ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE PHE
SEQRES 14 A 730 GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 A 730 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL PRO
SEQRES 16 A 730 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 A 730 TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA GLY
SEQRES 18 A 730 ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN THR
SEQRES 19 A 730 ASP SER LEU SER SER THR THR THR THR ILE PRO MET GLN
SEQRES 20 A 730 ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS TYR
SEQRES 21 A 730 LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE SER
SEQRES 22 A 730 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 A 730 ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP ASN
SEQRES 24 A 730 CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA THR
SEQRES 25 A 730 GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE
SEQRES 26 A 730 THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER ASP
SEQRES 27 A 730 LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS ASP
SEQRES 28 A 730 ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS GLY
SEQRES 29 A 730 ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER ASP
SEQRES 30 A 730 TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET PRO
SEQRES 31 A 730 GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP HIS
SEQRES 32 A 730 THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO GLU
SEQRES 33 A 730 ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU ALA
SEQRES 34 A 730 LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU PRO
SEQRES 35 A 730 LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU LEU
SEQRES 36 A 730 ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU
SEQRES 37 A 730 GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE
SEQRES 38 A 730 VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE LEU
SEQRES 39 A 730 PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU
SEQRES 40 A 730 ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP
SEQRES 41 A 730 ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER
SEQRES 42 A 730 THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY
SEQRES 43 A 730 SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN
SEQRES 44 A 730 LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE GLU
SEQRES 45 A 730 ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP SER
SEQRES 46 A 730 LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY TYR
SEQRES 47 A 730 VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE
SEQRES 48 A 730 LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU
SEQRES 49 A 730 TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU
SEQRES 50 A 730 PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER
SEQRES 51 A 730 THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU
SEQRES 52 A 730 TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS
SEQRES 53 A 730 PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP
SEQRES 54 A 730 ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU
SEQRES 55 A 730 ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE
SEQRES 56 A 730 TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE SER
SEQRES 57 A 730 LEU ARG
SEQRES 1 B 730 ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN THR
SEQRES 2 B 730 PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER ASP
SEQRES 3 B 730 SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 4 B 730 PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU GLU
SEQRES 5 B 730 ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER ASP
SEQRES 6 B 730 TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU GLU
SEQRES 7 B 730 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 B 730 SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 B 730 THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 10 B 730 TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP LYS
SEQRES 11 B 730 ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO SER
SEQRES 12 B 730 HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE PHE
SEQRES 13 B 730 ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE PHE
SEQRES 14 B 730 GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 B 730 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL PRO
SEQRES 16 B 730 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 B 730 TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA GLY
SEQRES 18 B 730 ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN THR
SEQRES 19 B 730 ASP SER LEU SER SER THR THR THR THR ILE PRO MET GLN
SEQRES 20 B 730 ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS TYR
SEQRES 21 B 730 LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE SER
SEQRES 22 B 730 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 B 730 ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP ASN
SEQRES 24 B 730 CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA THR
SEQRES 25 B 730 GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE
SEQRES 26 B 730 THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER ASP
SEQRES 27 B 730 LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS ASP
SEQRES 28 B 730 ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS GLY
SEQRES 29 B 730 ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER ASP
SEQRES 30 B 730 TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET PRO
SEQRES 31 B 730 GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP HIS
SEQRES 32 B 730 THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO GLU
SEQRES 33 B 730 ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU ALA
SEQRES 34 B 730 LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU PRO
SEQRES 35 B 730 LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU LEU
SEQRES 36 B 730 ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU
SEQRES 37 B 730 GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE
SEQRES 38 B 730 VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE LEU
SEQRES 39 B 730 PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU
SEQRES 40 B 730 ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP
SEQRES 41 B 730 ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER
SEQRES 42 B 730 THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY
SEQRES 43 B 730 SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN
SEQRES 44 B 730 LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE GLU
SEQRES 45 B 730 ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP SER
SEQRES 46 B 730 LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY TYR
SEQRES 47 B 730 VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE
SEQRES 48 B 730 LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU
SEQRES 49 B 730 TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU
SEQRES 50 B 730 PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER
SEQRES 51 B 730 THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU
SEQRES 52 B 730 TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS
SEQRES 53 B 730 PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP
SEQRES 54 B 730 ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU
SEQRES 55 B 730 ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE
SEQRES 56 B 730 TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE SER
SEQRES 57 B 730 LEU ARG
SEQRES 1 C 210 GLN ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA
SEQRES 2 C 210 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER
SEQRES 3 C 210 SER SER VAL ASN ASN MET HIS TRP TYR GLN GLN LYS PRO
SEQRES 4 C 210 GLY SER SER PRO LYS PRO TRP LEU HIS GLY THR SER ASN
SEQRES 5 C 210 LEU ALA SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY
SEQRES 6 C 210 SER GLY THR SER PHE SER LEU THR ILE SER ARG VAL GLU
SEQRES 7 C 210 ALA GLU ASP ALA ALA THR TYR PHE CYS GLN GLN TRP SER
SEQRES 8 C 210 ASN HIS PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 C 210 ILE ASP ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 C 210 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 C 210 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 C 210 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 C 210 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 C 210 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 C 210 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 C 210 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 C 210 ASN ARG
SEQRES 1 D 217 GLU PHE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 D 217 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 D 217 TYR SER PHE THR ASP TYR ASN ILE ASN TRP MET LYS GLN
SEQRES 4 D 217 SER ASN GLY LYS SER LEU GLU TRP ILE GLY VAL VAL ILE
SEQRES 5 D 217 PRO LYS TYR GLY THR THR ASN TYR ASN GLN LYS PHE GLN
SEQRES 6 D 217 GLY LYS ALA THR LEU THR VAL ASP GLN SER SER SER THR
SEQRES 7 D 217 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER
SEQRES 8 D 217 ALA VAL TYR TYR CYS THR ARG PHE ARG ASP VAL PHE PHE
SEQRES 9 D 217 ASP VAL TRP GLY THR GLY THR THR VAL THR VAL SER SER
SEQRES 10 D 217 ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA PRO
SEQRES 11 D 217 VAL CYS GLY GLY THR THR GLY SER SER VAL THR LEU GLY
SEQRES 12 D 217 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR LEU
SEQRES 13 D 217 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR
SEQRES 14 D 217 PHE PRO ALA LEU LEU GLN SER GLY LEU TYR THR LEU SER
SEQRES 15 D 217 SER SER VAL THR VAL THR SER ASN THR TRP PRO SER GLN
SEQRES 16 D 217 THR ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR
SEQRES 17 D 217 LYS VAL ASP LYS LYS ILE VAL PRO ARG
SEQRES 1 L 210 GLN ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA
SEQRES 2 L 210 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER
SEQRES 3 L 210 SER SER VAL ASN ASN MET HIS TRP TYR GLN GLN LYS PRO
SEQRES 4 L 210 GLY SER SER PRO LYS PRO TRP LEU HIS GLY THR SER ASN
SEQRES 5 L 210 LEU ALA SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY
SEQRES 6 L 210 SER GLY THR SER PHE SER LEU THR ILE SER ARG VAL GLU
SEQRES 7 L 210 ALA GLU ASP ALA ALA THR TYR PHE CYS GLN GLN TRP SER
SEQRES 8 L 210 ASN HIS PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 L 210 ILE ASP ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 L 210 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 L 210 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 L 210 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 L 210 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 L 210 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 L 210 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 L 210 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 L 210 ASN ARG
SEQRES 1 H 217 GLU PHE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 H 217 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 H 217 TYR SER PHE THR ASP TYR ASN ILE ASN TRP MET LYS GLN
SEQRES 4 H 217 SER ASN GLY LYS SER LEU GLU TRP ILE GLY VAL VAL ILE
SEQRES 5 H 217 PRO LYS TYR GLY THR THR ASN TYR ASN GLN LYS PHE GLN
SEQRES 6 H 217 GLY LYS ALA THR LEU THR VAL ASP GLN SER SER SER THR
SEQRES 7 H 217 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER
SEQRES 8 H 217 ALA VAL TYR TYR CYS THR ARG PHE ARG ASP VAL PHE PHE
SEQRES 9 H 217 ASP VAL TRP GLY THR GLY THR THR VAL THR VAL SER SER
SEQRES 10 H 217 ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA PRO
SEQRES 11 H 217 VAL CYS GLY GLY THR THR GLY SER SER VAL THR LEU GLY
SEQRES 12 H 217 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR LEU
SEQRES 13 H 217 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR
SEQRES 14 H 217 PHE PRO ALA LEU LEU GLN SER GLY LEU TYR THR LEU SER
SEQRES 15 H 217 SER SER VAL THR VAL THR SER ASN THR TRP PRO SER GLN
SEQRES 16 H 217 THR ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR
SEQRES 17 H 217 LYS VAL ASP LYS LYS ILE VAL PRO ARG
FORMUL 7 HOH *213(H2 O)
HELIX 1 1 THR A 42 ASN A 49 1 8
HELIX 2 2 GLU A 89 GLU A 94 1 6
HELIX 3 3 ASP A 198 ILE A 205 1 8
HELIX 4 4 PRO A 338 THR A 340 5 3
HELIX 5 5 GLU A 422 MET A 426 5 5
HELIX 6 6 ASN A 498 LEU A 505 1 8
HELIX 7 7 GLN A 506 VAL A 508 5 3
HELIX 8 8 ASN A 563 THR A 571 1 9
HELIX 9 9 GLY A 588 HIS A 593 1 6
HELIX 10 10 ALA A 594 ASN A 596 5 3
HELIX 11 11 THR A 601 MET A 617 1 17
HELIX 12 12 SER A 631 GLY A 642 1 12
HELIX 13 13 ARG A 659 TYR A 663 5 5
HELIX 14 14 ASP A 664 GLY A 673 1 10
HELIX 15 15 ASN A 680 SER A 687 1 8
HELIX 16 16 VAL A 689 VAL A 699 5 11
HELIX 17 17 HIS A 713 ALA A 727 1 15
HELIX 18 18 SER A 745 SER A 765 1 21
HELIX 19 19 THR B 42 ASN B 49 1 8
HELIX 20 20 GLU B 89 ILE B 95 1 7
HELIX 21 21 ASP B 198 ILE B 205 1 8
HELIX 22 22 PRO B 288 THR B 293 1 6
HELIX 23 23 PRO B 338 THR B 340 5 3
HELIX 24 24 GLU B 422 MET B 426 5 5
HELIX 25 25 ASN B 498 LYS B 503 1 6
HELIX 26 26 MET B 504 VAL B 508 5 5
HELIX 27 27 ASN B 563 THR B 571 1 9
HELIX 28 28 GLY B 588 HIS B 593 1 6
HELIX 29 29 ALA B 594 ASN B 596 5 3
HELIX 30 30 THR B 601 MET B 617 1 17
HELIX 31 31 SER B 631 GLY B 642 1 12
HELIX 32 32 ARG B 659 TYR B 663 5 5
HELIX 33 33 ASP B 664 MET B 672 1 9
HELIX 34 34 ASN B 680 SER B 687 1 8
HELIX 35 35 VAL B 689 VAL B 699 5 11
HELIX 36 36 HIS B 713 ALA B 727 1 15
HELIX 37 37 SER B 745 SER B 765 1 21
HELIX 38 38 SER C 120 THR C 125 1 6
HELIX 39 39 LYS C 182 GLU C 186 1 5
HELIX 40 40 SER D 28 TYR D 32 5 5
HELIX 41 41 GLN D 62 GLN D 65 5 4
HELIX 42 42 THR D 87 SER D 91 5 5
HELIX 43 43 PRO D 204 SER D 207 5 4
HELIX 44 44 SER L 120 THR L 125 1 6
HELIX 45 45 LYS L 182 GLU L 186 1 5
HELIX 46 46 SER H 28 TYR H 32 5 5
HELIX 47 47 GLN H 62 GLN H 65 5 4
HELIX 48 48 THR H 87 SER H 91 5 5
SHEET 1 A 4 ARG A 59 TRP A 60 0
SHEET 2 A 4 GLU A 65 LYS A 69 -1 O LEU A 67 N ARG A 59
SHEET 3 A 4 ILE A 74 ASN A 78 -1 O PHE A 77 N TYR A 66
SHEET 4 A 4 SER A 84 LEU A 88 -1 O SER A 85 N LEU A 76
SHEET 1 B 4 ILE A 100 VAL A 105 0
SHEET 2 B 4 PHE A 111 LYS A 120 -1 O LEU A 113 N SER A 104
SHEET 3 B 4 TYR A 126 ASP A 134 -1 O SER A 129 N TYR A 116
SHEET 4 B 4 GLN A 139 LEU A 140 -1 O GLN A 139 N ASP A 134
SHEET 1 C 4 TRP A 152 TRP A 155 0
SHEET 2 C 4 LEU A 162 TRP A 166 -1 O VAL A 165 N TRP A 152
SHEET 3 C 4 ASP A 169 LYS A 173 -1 O LYS A 173 N LEU A 162
SHEET 4 C 4 HIS A 181 ARG A 182 -1 O HIS A 181 N VAL A 172
SHEET 1 D 3 ILE A 192 ASN A 194 0
SHEET 2 D 3 PHE A 220 ASN A 227 -1 O PHE A 226 N PHE A 193
SHEET 3 D 3 LEU A 212 TRP A 214 -1 N TRP A 213 O ALA A 222
SHEET 1 E 4 ILE A 192 ASN A 194 0
SHEET 2 E 4 PHE A 220 ASN A 227 -1 O PHE A 226 N PHE A 193
SHEET 3 E 4 THR A 263 ASN A 270 -1 O PHE A 267 N TYR A 223
SHEET 4 E 4 MET A 283 GLN A 284 -1 O MET A 283 N ILE A 268
SHEET 1 F 2 LEU A 233 PHE A 238 0
SHEET 2 F 2 LYS A 248 PRO A 253 -1 O LYS A 248 N PHE A 238
SHEET 1 G 4 HIS A 296 SER A 305 0
SHEET 2 G 4 ARG A 308 ARG A 315 -1 O LEU A 314 N TYR A 297
SHEET 3 G 4 TYR A 320 ASP A 329 -1 O CYS A 326 N ILE A 309
SHEET 4 G 4 VAL A 334 ASN A 336 -1 O ASN A 336 N ASP A 327
SHEET 1 H 4 HIS A 296 SER A 305 0
SHEET 2 H 4 ARG A 308 ARG A 315 -1 O LEU A 314 N TYR A 297
SHEET 3 H 4 TYR A 320 ASP A 329 -1 O CYS A 326 N ILE A 309
SHEET 4 H 4 GLU A 342 THR A 346 -1 O HIS A 343 N MET A 323
SHEET 1 I 4 HIS A 361 PHE A 362 0
SHEET 2 I 4 SER A 368 SER A 374 -1 O TYR A 370 N HIS A 361
SHEET 3 I 4 LYS A 380 GLN A 386 -1 O PHE A 385 N PHE A 369
SHEET 4 I 4 THR A 396 PHE A 397 -1 O THR A 396 N GLN A 384
SHEET 1 J 4 VAL A 405 LEU A 411 0
SHEET 2 J 4 TYR A 415 SER A 420 -1 O ILE A 419 N ILE A 406
SHEET 3 J 4 ASN A 431 GLN A 436 -1 O ILE A 435 N LEU A 416
SHEET 4 J 4 LYS A 443 CYS A 445 -1 O LYS A 444 N LYS A 434
SHEET 1 K 4 TYR A 458 LEU A 462 0
SHEET 2 K 4 TYR A 468 CYS A 473 -1 O GLY A 472 N SER A 459
SHEET 3 K 4 LEU A 480 ARG A 485 -1 O LEU A 480 N CYS A 473
SHEET 4 K 4 GLU A 491 GLU A 496 -1 O GLU A 496 N TYR A 481
SHEET 1 L 8 SER A 512 LEU A 520 0
SHEET 2 L 8 THR A 523 LEU A 531 -1 O TYR A 527 N ASP A 516
SHEET 3 L 8 ILE A 575 PHE A 579 -1 O VAL A 576 N ILE A 530
SHEET 4 L 8 TYR A 541 VAL A 547 1 N ASP A 546 O ALA A 577
SHEET 5 L 8 VAL A 620 TRP A 630 1 O ALA A 626 N ILE A 545
SHEET 6 L 8 CYS A 650 VAL A 654 1 O VAL A 654 N GLY A 629
SHEET 7 L 8 GLU A 700 GLY A 706 1 O LEU A 702 N ALA A 653
SHEET 8 L 8 GLN A 732 TYR A 736 1 O GLN A 732 N TYR A 701
SHEET 1 M 4 LEU B 58 TRP B 60 0
SHEET 2 M 4 GLU B 65 GLN B 70 -1 O LEU B 67 N ARG B 59
SHEET 3 M 4 ASN B 73 ASN B 78 -1 O LEU B 75 N TYR B 68
SHEET 4 M 4 SER B 84 LEU B 88 -1 O SER B 85 N LEU B 76
SHEET 1 N 4 ILE B 100 VAL B 105 0
SHEET 2 N 4 PHE B 111 LYS B 120 -1 O LEU B 113 N SER B 104
SHEET 3 N 4 TYR B 126 ASP B 134 -1 O SER B 129 N TYR B 116
SHEET 4 N 4 GLN B 139 LEU B 140 -1 O GLN B 139 N ASP B 134
SHEET 1 O 4 TRP B 152 TRP B 155 0
SHEET 2 O 4 LEU B 162 TRP B 166 -1 O VAL B 165 N TRP B 152
SHEET 3 O 4 ASP B 169 LYS B 173 -1 O LYS B 173 N LEU B 162
SHEET 4 O 4 HIS B 181 ARG B 182 -1 O HIS B 181 N VAL B 172
SHEET 1 P 3 ILE B 192 ASN B 194 0
SHEET 2 P 3 PHE B 220 ASN B 227 -1 O PHE B 226 N PHE B 193
SHEET 3 P 3 LEU B 212 TRP B 214 -1 N TRP B 213 O ALA B 222
SHEET 1 Q 4 ILE B 192 ASN B 194 0
SHEET 2 Q 4 PHE B 220 ASN B 227 -1 O PHE B 226 N PHE B 193
SHEET 3 Q 4 THR B 263 ASN B 270 -1 O VAL B 269 N LEU B 221
SHEET 4 Q 4 MET B 283 ILE B 285 -1 O MET B 283 N ILE B 268
SHEET 1 R 2 LEU B 233 PHE B 238 0
SHEET 2 R 2 LYS B 248 PRO B 253 -1 O LYS B 248 N PHE B 238
SHEET 1 S 4 HIS B 296 SER B 305 0
SHEET 2 S 4 ARG B 308 ARG B 315 -1 O LEU B 314 N TYR B 297
SHEET 3 S 4 TYR B 320 ASP B 329 -1 O CYS B 326 N ILE B 309
SHEET 4 S 4 VAL B 334 ASN B 336 -1 O ASN B 336 N ASP B 327
SHEET 1 T 4 HIS B 296 SER B 305 0
SHEET 2 T 4 ARG B 308 ARG B 315 -1 O LEU B 314 N TYR B 297
SHEET 3 T 4 TYR B 320 ASP B 329 -1 O CYS B 326 N ILE B 309
SHEET 4 T 4 GLU B 342 THR B 346 -1 O HIS B 343 N MET B 323
SHEET 1 U 4 PRO B 360 PHE B 362 0
SHEET 2 U 4 SER B 368 SER B 374 -1 O TYR B 370 N HIS B 361
SHEET 3 U 4 LYS B 380 GLN B 386 -1 O HIS B 381 N VAL B 373
SHEET 4 U 4 THR B 396 PHE B 397 -1 O THR B 396 N GLN B 384
SHEET 1 V 4 VAL B 405 LEU B 411 0
SHEET 2 V 4 TYR B 415 SER B 420 -1 O TYR B 417 N ALA B 410
SHEET 3 V 4 ASN B 431 GLN B 436 -1 O TYR B 433 N TYR B 418
SHEET 4 V 4 LYS B 443 CYS B 445 -1 O LYS B 444 N LYS B 434
SHEET 1 W 4 TYR B 458 LEU B 462 0
SHEET 2 W 4 TYR B 468 CYS B 473 -1 O GLY B 472 N SER B 459
SHEET 3 W 4 LEU B 480 ARG B 485 -1 O HIS B 484 N TYR B 469
SHEET 4 W 4 GLU B 491 GLU B 496 -1 O LEU B 492 N LEU B 483
SHEET 1 X 8 SER B 512 LEU B 520 0
SHEET 2 X 8 THR B 523 LEU B 531 -1 O TYR B 527 N ASP B 516
SHEET 3 X 8 ILE B 575 PHE B 579 -1 O VAL B 576 N ILE B 530
SHEET 4 X 8 TYR B 541 ASP B 546 1 N ASP B 546 O ALA B 577
SHEET 5 X 8 VAL B 620 TRP B 630 1 O ASP B 621 N TYR B 541
SHEET 6 X 8 CYS B 650 VAL B 654 1 O VAL B 654 N GLY B 629
SHEET 7 X 8 GLU B 700 GLY B 706 1 O ILE B 704 N ALA B 653
SHEET 8 X 8 GLN B 732 TYR B 736 1 O GLN B 732 N TYR B 701
SHEET 1 Y 4 SER C 5 SER C 7 0
SHEET 2 Y 4 VAL C 19 ARG C 24 -1 O ARG C 24 N SER C 5
SHEET 3 Y 4 SER C 69 ILE C 74 -1 O ILE C 74 N VAL C 19
SHEET 4 Y 4 PHE C 61 SER C 66 -1 N SER C 62 O THR C 73
SHEET 1 Z 6 ILE C 10 ALA C 13 0
SHEET 2 Z 6 THR C 101 ILE C 105 1 O GLU C 104 N ALA C 13
SHEET 3 Z 6 ALA C 83 GLN C 89 -1 N TYR C 85 O THR C 101
SHEET 4 Z 6 MET C 32 GLN C 37 -1 N GLN C 37 O THR C 84
SHEET 5 Z 6 LYS C 44 HIS C 48 -1 O LYS C 44 N GLN C 36
SHEET 6 Z 6 ASN C 52 LEU C 53 -1 O ASN C 52 N HIS C 48
SHEET 1 AA 4 ILE C 10 ALA C 13 0
SHEET 2 AA 4 THR C 101 ILE C 105 1 O GLU C 104 N ALA C 13
SHEET 3 AA 4 ALA C 83 GLN C 89 -1 N TYR C 85 O THR C 101
SHEET 4 AA 4 THR C 96 PHE C 97 -1 O THR C 96 N GLN C 89
SHEET 1 AB 3 GLY C 128 PHE C 138 0
SHEET 2 AB 3 TYR C 172 THR C 181 -1 O LEU C 178 N VAL C 131
SHEET 3 AB 3 VAL C 158 THR C 163 -1 N LEU C 159 O THR C 177
SHEET 1 AC 3 ASN C 144 ILE C 149 0
SHEET 2 AC 3 SER C 190 THR C 196 -1 O GLU C 194 N LYS C 146
SHEET 3 AC 3 LYS C 206 ASN C 209 -1 O PHE C 208 N TYR C 191
SHEET 1 AD 4 GLN D 3 GLN D 6 0
SHEET 2 AD 4 VAL D 18 SER D 25 -1 O LYS D 23 N GLN D 5
SHEET 3 AD 4 THR D 78 LEU D 83 -1 O LEU D 83 N VAL D 18
SHEET 4 AD 4 ALA D 68 ASP D 73 -1 N ASP D 73 O THR D 78
SHEET 1 AE 6 GLU D 10 VAL D 12 0
SHEET 2 AE 6 THR D 111 VAL D 115 1 O THR D 114 N GLU D 10
SHEET 3 AE 6 ALA D 92 PHE D 99 -1 N ALA D 92 O VAL D 113
SHEET 4 AE 6 ASN D 33 GLN D 39 -1 N ASN D 35 O THR D 97
SHEET 5 AE 6 LEU D 45 VAL D 51 -1 O VAL D 51 N ILE D 34
SHEET 6 AE 6 THR D 58 TYR D 60 -1 O ASN D 59 N VAL D 50
SHEET 1 AF 4 GLU D 10 VAL D 12 0
SHEET 2 AF 4 THR D 111 VAL D 115 1 O THR D 114 N GLU D 10
SHEET 3 AF 4 ALA D 92 PHE D 99 -1 N ALA D 92 O VAL D 113
SHEET 4 AF 4 VAL D 106 TRP D 107 -1 O VAL D 106 N ARG D 98
SHEET 1 AG 4 SER D 124 TYR D 126 0
SHEET 2 AG 4 LEU D 145 TYR D 149 -1 O LYS D 147 N SER D 124
SHEET 3 AG 4 LEU D 178 LEU D 181 -1 O LEU D 181 N VAL D 146
SHEET 4 AG 4 LEU D 173 GLN D 175 -1 N GLN D 175 O LEU D 178
SHEET 1 AH 2 THR D 141 GLY D 143 0
SHEET 2 AH 2 SER D 184 THR D 186 -1 O VAL D 185 N LEU D 142
SHEET 1 AI 3 THR D 155 TRP D 158 0
SHEET 2 AI 3 THR D 198 HIS D 203 -1 O ASN D 200 N THR D 157
SHEET 3 AI 3 THR D 208 LYS D 213 -1 O VAL D 210 N VAL D 201
SHEET 1 AJ 4 LEU L 4 SER L 7 0
SHEET 2 AJ 4 VAL L 19 ALA L 25 -1 O ARG L 24 N SER L 5
SHEET 3 AJ 4 SER L 69 ILE L 74 -1 O ILE L 74 N VAL L 19
SHEET 4 AJ 4 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73
SHEET 1 AK 5 ILE L 10 SER L 12 0
SHEET 2 AK 5 THR L 101 GLU L 104 1 O GLU L 104 N LEU L 11
SHEET 3 AK 5 ALA L 83 GLN L 89 -1 N TYR L 85 O THR L 101
SHEET 4 AK 5 MET L 32 GLN L 37 -1 N GLN L 37 O THR L 84
SHEET 5 AK 5 LYS L 44 LEU L 47 -1 O LYS L 44 N GLN L 36
SHEET 1 AL 4 ILE L 10 SER L 12 0
SHEET 2 AL 4 THR L 101 GLU L 104 1 O GLU L 104 N LEU L 11
SHEET 3 AL 4 ALA L 83 GLN L 89 -1 N TYR L 85 O THR L 101
SHEET 4 AL 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 89
SHEET 1 AM 4 VAL L 114 PHE L 117 0
SHEET 2 AM 4 GLY L 128 PHE L 138 -1 O VAL L 132 N PHE L 117
SHEET 3 AM 4 TYR L 172 THR L 181 -1 O LEU L 180 N ALA L 129
SHEET 4 AM 4 VAL L 158 TRP L 162 -1 N LEU L 159 O THR L 177
SHEET 1 AN 2 SER L 190 THR L 192 0
SHEET 2 AN 2 SER L 207 ASN L 209 -1 O PHE L 208 N TYR L 191
SHEET 1 AO 4 GLN H 3 GLN H 6 0
SHEET 2 AO 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5
SHEET 3 AO 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18
SHEET 4 AO 4 ALA H 68 ASP H 73 -1 N THR H 69 O GLN H 82
SHEET 1 AP 6 GLU H 10 VAL H 12 0
SHEET 2 AP 6 THR H 111 VAL H 115 1 O THR H 114 N GLU H 10
SHEET 3 AP 6 ALA H 92 PHE H 99 -1 N ALA H 92 O VAL H 113
SHEET 4 AP 6 ASN H 33 GLN H 39 -1 N ASN H 35 O THR H 97
SHEET 5 AP 6 LEU H 45 ILE H 52 -1 O ILE H 48 N TRP H 36
SHEET 6 AP 6 THR H 57 TYR H 60 -1 O THR H 57 N ILE H 52
SHEET 1 AQ 4 SER H 124 LEU H 128 0
SHEET 2 AQ 4 GLY H 143 TYR H 149 -1 O LEU H 145 N TYR H 126
SHEET 3 AQ 4 LEU H 178 LEU H 181 -1 O TYR H 179 N TYR H 149
SHEET 4 AQ 4 LEU H 173 GLN H 175 -1 N GLN H 175 O LEU H 178
SHEET 1 AR 2 VAL H 140 THR H 141 0
SHEET 2 AR 2 THR H 186 VAL H 187 -1 O VAL H 187 N VAL H 140
SHEET 1 AS 3 LEU H 156 TRP H 158 0
SHEET 2 AS 3 THR H 198 HIS H 203 -1 O ASN H 200 N THR H 157
SHEET 3 AS 3 THR H 208 LYS H 213 -1 O LYS H 212 N CYS H 199
SSBOND 1 CYS A 326 CYS A 337 1555 1555 2.04
SSBOND 2 CYS A 383 CYS A 395 1555 1555 2.03
SSBOND 3 CYS A 445 CYS A 448 1555 1555 2.03
SSBOND 4 CYS A 455 CYS A 473 1555 1555 2.05
SSBOND 5 CYS A 650 CYS A 763 1555 1555 2.05
SSBOND 6 CYS B 326 CYS B 337 1555 1555 2.04
SSBOND 7 CYS B 383 CYS B 395 1555 1555 2.05
SSBOND 8 CYS B 445 CYS B 448 1555 1555 2.03
SSBOND 9 CYS B 455 CYS B 473 1555 1555 2.05
SSBOND 10 CYS B 650 CYS B 763 1555 1555 2.05
SSBOND 11 CYS C 23 CYS C 87 1555 1555 2.05
SSBOND 12 CYS C 133 CYS C 193 1555 1555 2.03
SSBOND 13 CYS D 22 CYS D 96 1555 1555 2.04
SSBOND 14 CYS D 144 CYS D 199 1555 1555 2.03
SSBOND 15 CYS L 23 CYS L 87 1555 1555 2.04
SSBOND 16 CYS L 133 CYS L 193 1555 1555 2.03
SSBOND 17 CYS H 22 CYS H 96 1555 1555 2.04
SSBOND 18 CYS H 144 CYS H 199 1555 1555 2.03
CISPEP 1 GLY A 475 PRO A 476 0 4.39
CISPEP 2 GLY B 475 PRO B 476 0 5.75
CISPEP 3 SER C 7 PRO C 8 0 -5.04
CISPEP 4 HIS C 93 PRO C 94 0 -2.32
CISPEP 5 PRO D 153 VAL D 154 0 -0.78
CISPEP 6 SER L 7 PRO L 8 0 -5.59
CISPEP 7 HIS L 93 PRO L 94 0 0.51
CRYST1 97.260 201.720 97.280 90.00 93.71 90.00 P 1 21 1 4
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 0.010282 0.000000 0.000667 0.00000
SCALE2 0.000000 0.004957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010301 0.00000
TER 5922 SER A 765
TER 11863 ARG B 767
TER 13443 ARG C 210
TER 15040 ARG D 217
TER 16620 ARG L 210
TER 18216 ARG H 217
MASTER 334 0 0 48 179 0 0 618423 6 36 182
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