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HEADER HYDROLASE 27-MAY-03 1PFQ
TITLE CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL PEPTIDASE IV /
TITLE 2 CD26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26, TP103,
COMPND 5 ADENOSINE DEAMINASE COMPLEXING PROTEIN-2, ADABP;
COMPND 6 EC: 3.4.14.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DPP4 OR ADCP2 OR CD26;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: YEAST;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: KM71;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PICZ
KEYWDS MCH_1
EXPDTA X-RAY DIFFRACTION
AUTHOR C.OEFNER,A.D'ARCY,A.MAC SWEENEY,S.PIERAU,R.GARDINER,G.E.DALE
REVDAT 1 01-JUL-03 1PFQ 0
JRNL AUTH C.OEFNER,A.D'ARCY,A.MAC SWEENEY,S.PIERAU,
JRNL AUTH 2 R.GARDINER,G.E.DALE
JRNL TITL HIGH-RESOLUTION STRUCTURE OF HUMAN APO DIPEPTIDYL
JRNL TITL 2 PEPTIDASE IV/CD26 AND ITS COMPLEX WITH
JRNL TITL 3 1-[({2-[5-IODOPYRIDIN-2-YL)AMINO]-ETHYL}AMINO)-
JRNL TITL 4 ACETYL]-2-CYANO-(S)-PYRROLIDINE
JRNL REF ACTA CRYSTALLOGR., SECT.D V. 59 1206 2003
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 115106
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) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.254
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6101
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15551
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 829
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 12418
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : -1.04000
REMARK 3 B33 (A**2) : 1.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.215
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.241
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.242
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12307 ; 0.004 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 10515 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16745 ; 0.649 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): 24479 ; 0.527 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1450 ; 8.085 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2064 ;21.363 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1771 ; 0.043 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13690 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2658 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2806 ; 0.256 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 11100 ; 0.255 ; 0.300
REMARK 3 NON-BONDED TORSION OTHERS (A): 4 ; 0.747 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 748 ; 0.214 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 17 ; 0.184 ; 0.500
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 55 ; 0.501 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 102 ; 0.489 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.483 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7239 ; 0.616 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11741 ; 1.141 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5068 ; 0.621 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5004 ; 0.889 ; 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 : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. REFLECTION FILE CONTAINS FRIEDEL'S PAIRS
REMARK 4
REMARK 4 1PFQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-2003.
REMARK 100 THE RCSB ID CODE IS RCSB019296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122631
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12600
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+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 35.51550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.29150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.07100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 92.29150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.51550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.07100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR A 36
REMARK 465 ALA A 37
REMARK 465 ASP A 38
REMARK 465 SER B 93
REMARK 465 THR B 94
REMARK 465 PHE B 95
REMARK 465 ASP B 96
REMARK 465 GLU B 97
REMARK 465 PHE B 98
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS B 100 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 101 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 ND2 ASN A 150 O HOH 399 1.71
REMARK 500 O HOH 428 O HOH 453 1.74
REMARK 500 OD2 ASP A 620 NH1 ARG A 623 1.77
REMARK 500 O ALA B 81 NH2 ARG B 492 1.81
REMARK 500 O HOH 212 O HOH 213 1.86
REMARK 500 OE2 GLU B 244 O HOH 24 1.88
REMARK 500 OD1 ASP A 65 O HOH 411 1.94
REMARK 500 OD2 ASP B 243 O HOH 466 1.96
REMARK 500 OE2 GLU A 660 O HOH 167 1.97
REMARK 500 OD1 ASP A 678 O HOH 371 1.97
REMARK 500 NE2 GLN B 749 O HOH 184 1.97
REMARK 500 O HOH 470 O HOH 471 1.97
REMARK 500 OD2 ASP B 329 NH1 ARG B 343 1.98
REMARK 500 ND2 ASN A 103 OE1 GLU A 117 1.99
REMARK 500 ND2 ASN B 685 O HOH 409 1.99
REMARK 500 OD2 ASP B 65 O LYS B 463 2.00
REMARK 500 O TYR B 83 CZ ARG B 492 2.00
REMARK 500 OG SER A 131 OD1 ASN A 150 2.01
REMARK 500 CG2 VAL A 160 O ASN A 219 2.01
REMARK 500 OD2 ASP A 367 O HOH 214 2.02
REMARK 500 NE2 GLN B 731 O HOH 113 2.02
REMARK 500 NZ LYS A 441 O HOH 210 2.09
REMARK 500 O TYR B 83 NH1 ARG B 492 2.09
REMARK 500 OG SER B 158 O VAL B 160 2.09
REMARK 500 OE2 GLU A 602 OH TYR A 631 2.11
REMARK 500 NE ARG A 596 O HOH 165 2.12
REMARK 500 O LYS B 139 N GLN B 141 2.12
REMARK 500 OD1 ASP B 243 O HOH 466 2.12
REMARK 500 O LEU A 57 O HOH 225 2.13
REMARK 500 OE2 GLU A 244 O HOH 462 2.13
REMARK 500 O VAL A 493 O HOH 230 2.13
REMARK 500 OE2 GLU A 571 O HOH 75 2.14
REMARK 500 NZ LYS B 250 O HOH 253 2.14
REMARK 500 O GLY A 584 NE2 GLN A 586 2.15
REMARK 500 OE1 GLN B 314 NZ LYS B 373 2.15
REMARK 500 O3 NAG B 855 O HOH 404 2.19
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 450 O HOH 461 3555 1.53
REMARK 500 CZ PHE A 98 CZ3 TRP B 168 1455 1.81
REMARK 500 CD1 TYR A 83 OE1 GLU A 677 1455 1.89
REMARK 500 O SER B 642 O HOH 404 1455 1.91
REMARK 500 CZ PHE A 98 CH2 TRP B 168 1455 2.12
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR A 94 CA THR A 94 CB -0.030
REMARK 500 THR A 94 CB THR A 94 OG1 0.026
REMARK 500 THR A 94 CB THR A 94 CG2 0.037
REMARK 500 PHE A 95 CG PHE A 95 CD2 0.025
REMARK 500 PHE A 95 CG PHE A 95 CD1 0.025
REMARK 500 PHE A 95 CD1 PHE A 95 CE1 -0.049
REMARK 500 PHE A 95 CE1 PHE A 95 CZ -0.052
REMARK 500 PHE A 95 CZ PHE A 95 CE2 0.029
REMARK 500 ASP A 96 CG ASP A 96 OD1 0.026
REMARK 500 ASP A 96 CG ASP A 96 OD2 0.030
REMARK 500 MET A 293 SD MET A 293 CE -0.032
REMARK 500 MET A 509 SD MET A 509 CE -0.025
REMARK 500 CYS A 551 CA CYS A 551 CB 0.028
REMARK 500 CYS A 551 CB CYS A 551 SG 0.040
REMARK 500 CYS A 551 CA CYS A 551 C 0.035
REMARK 500 MET A 616 SD MET A 616 CE 0.026
REMARK 500 MET A 638 SD MET A 638 CE 0.030
REMARK 500 THR A 753 CA THR A 753 CB 0.026
REMARK 500 ILE B 134 CB ILE B 134 CG2 -0.035
REMARK 500 PRO B 181 CB PRO B 181 CG 0.028
REMARK 500 MET B 509 SD MET B 509 CE -0.028
REMARK 500 CYS B 551 CA CYS B 551 CB 0.036
REMARK 500 CYS B 551 CB CYS B 551 SG 0.049
REMARK 500 CYS B 551 CA CYS B 551 C 0.036
REMARK 500 THR B 746 CB THR B 746 CG2 -0.024
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR A 144 OG1 - CB - CG2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 THR A 152 OG1 - CB - CG2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 THR A 199 OG1 - CB - CG2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 THR A 288 OG1 - CB - CG2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 LEU A 449 CA - CB - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 THR A 570 OG1 - CB - CG2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 THR A 636 OG1 - CB - CG2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 THR B 42 OG1 - CB - CG2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 THR B 44 OG1 - CB - CG2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 THR B 46 OG1 - CB - CG2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 THR B 152 OG1 - CB - CG2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 THR B 199 OG1 - CB - CG2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 THR B 231 OG1 - CB - CG2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 THR B 288 OG1 - CB - CG2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 THR B 304 OG1 - CB - CG2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 THR B 365 OG1 - CB - CG2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 THR B 411 OG1 - CB - CG2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 LEU B 449 CA - CB - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP B 545 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 CYS B 551 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 THR B 687 OG1 - CB - CG2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 THR B 753 OG1 - CB - CG2 ANGL. DEV. = -6.1 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 73 -73.30 61.31
REMARK 500 SER A 630 -116.28 69.85
REMARK 500 GLU B 73 -100.96 58.42
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 ARG B 581 GLY B 582 -52.64
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 207 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH 208 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH 219 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH 289 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH 296 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH 301 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH 302 DISTANCE = 7.86 ANGSTROMS
REMARK 525 HOH 345 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH 351 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH 385 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH 451 DISTANCE = 6.93 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ORW RELATED DB: PDB
REMARK 900 RELATED ID: 1ORV RELATED DB: PDB
REMARK 900 RELATED ID: 1N1M RELATED DB: PDB
DBREF 1PFQ A 36 766 SWS P27487 DPP4_HUMAN 36 766
DBREF 1PFQ B 36 766 SWS P27487 DPP4_HUMAN 36 766
SEQRES 1 A 731 THR ALA ASP SER ARG 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 THR ALA ASP SER ARG 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
MODRES 1PFQ ASN A 85 ASN GLYCOSYLATION SITE
MODRES 1PFQ ASN A 229 ASN GLYCOSYLATION SITE
MODRES 1PFQ ASN B 85 ASN GLYCOSYLATION SITE
MODRES 1PFQ ASN B 229 ASN GLYCOSYLATION SITE
HET NAG B 852 14
HET NAG A 851 14
HET NAG A 853 14
HET NAG B 855 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 NAG 4(C8 H15 N1 O6)
FORMUL 7 HOH *472(H2 O1)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 ASP A 200 GLU A 206 1 7
HELIX 3 3 ASP A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 LEU A 340 GLN A 344 5 5
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 LYS A 463 ALA A 465 5 3
HELIX 8 8 ASN A 497 GLN A 505 1 9
HELIX 9 9 ASN A 562 ASN A 572 1 11
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 LYS A 615 1 16
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 ARG A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 SER A 686 1 8
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 PHE A 713 VAL A 726 1 14
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 THR B 44 ASN B 51 1 8
HELIX 21 21 ASP B 200 GLU B 206 1 7
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 GLU B 421 MET B 425 5 5
HELIX 24 24 LYS B 463 ALA B 465 5 3
HELIX 25 25 ASN B 497 GLN B 505 1 9
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 MET B 616 1 17
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ARG B 658 TYR B 662 5 5
HELIX 32 32 ASP B 663 GLY B 672 1 10
HELIX 33 33 ASN B 679 SER B 686 1 8
HELIX 34 34 VAL B 688 VAL B 698 5 11
HELIX 35 35 HIS B 712 GLY B 727 1 16
HELIX 36 36 SER B 744 PHE B 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 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 B 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 C 3 ASP A 104 ILE A 107 0
SHEET 2 C 3 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 3 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 1 D 4 THR A 152 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 F 4 SER A 284 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 VAL A 252 N TYR A 238
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 THR A 307 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 I 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
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 CYS A 385 N LYS A 373
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 L 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 L 4 LYS A 489 GLU A 495 -1 O LEU A 491 N LEU A 482
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O PHE A 524 N ILE A 517
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
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 LEU A 702
SHEET 1 N 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 LEU B 60 TRP B 62 0
SHEET 2 O 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 O 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 P 3 ASP B 104 ILE B 107 0
SHEET 2 P 3 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 P 3 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 1 Q 4 THR B 152 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 Q 4 SER B 182 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O LYS B 267 N GLN B 227
SHEET 4 S 4 ILE B 285 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 U 4 HIS B 298 THR B 307 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 ASP B 326 N LEU B 313
SHEET 4 U 4 ARG B 336 ASN B 338 -1 O ASN B 338 N ASP B 329
SHEET 1 V 4 HIS B 298 THR B 307 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 V 4 TYR B 322 ASP B 331 -1 O ASP B 326 N LEU B 313
SHEET 4 V 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 W 4 HIS B 363 PHE B 364 0
SHEET 2 W 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 W 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 W 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 X 4 VAL B 404 LEU B 410 0
SHEET 2 X 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 X 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 X 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 Y 4 TYR B 457 PHE B 461 0
SHEET 2 Y 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 Y 4 LYS B 489 GLU B 495 -1 O ARG B 492 N LEU B 482
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O PHE B 524 N ILE B 517
SHEET 3 Z 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Z 8 TYR B 540 ASP B 545 1 N LEU B 543 O ILE B 574
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Z 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
SSBOND 1 CYS A 328 CYS A 339
SSBOND 2 CYS A 385 CYS A 394
SSBOND 3 CYS A 444 CYS A 447
SSBOND 4 CYS A 454 CYS A 472
SSBOND 5 CYS A 649 CYS A 762
SSBOND 6 CYS B 328 CYS B 339
SSBOND 7 CYS B 385 CYS B 394
SSBOND 8 CYS B 444 CYS B 447
SSBOND 9 CYS B 454 CYS B 472
SSBOND 10 CYS B 649 CYS B 762
LINK ND2 ASN A 85 C1 NAG A 851
LINK ND2 ASN A 229 C1 NAG A 853
LINK ND2 ASN B 85 C1 NAG B 855
LINK ND2 ASN B 229 C1 NAG B 852
CISPEP 1 ASN A 219 GLY A 220 0 9.50
CISPEP 2 GLY A 474 PRO A 475 0 8.47
CISPEP 3 ARG A 581 GLY A 582 0 -24.61
CISPEP 4 GLY A 584 TYR A 585 0 -19.12
CISPEP 5 GLY B 474 PRO B 475 0 10.51
CRYST1 71.031 118.142 184.583 90.00 90.00 90.00 P 21 21 21 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 0.014078 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005418 0.00000
TER 5965 PRO A 766
TER 11892 PRO B 766
MASTER 429 0 4 36 100 0 0 612418 2 80 114
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