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HEADER HYDROLASE 23-MAR-12 4EBB
TITLE STRUCTURE OF DPP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DIPEPTIDYL PEPTIDASE 7 (UNP RESIDUES 27-492);
COMPND 5 SYNONYM: DIPEPTIDYL AMINOPEPTIDASE II, DIPEPTIDYL PEPTIDASE 7,
COMPND 6 DIPEPTIDYL PEPTIDASE II, DPP II, QUIESCENT CELL PROLINE DIPEPTIDASE;
COMPND 7 EC: 3.4.14.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP7, DPP2, QPP;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDEST
KEYWDS PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.SHEWCHUK,A.H.HASSELL,S.M.SWEITZER,T.D.SWEITZER,P.J.MCDEVITT,
AUTHOR 2 K.M.KENNEDY-WILSON,K.O.JOHANSON
REVDAT 1 19-SEP-12 4EBB 0
JRNL AUTH G.A.BEZERRA,E.DOBROVETSKY,A.DONG,A.SEITOVA,L.CROMBETT,
JRNL AUTH 2 L.M.SHEWCHUK,A.M.HASSELL,S.M.SWEITZER,T.D.SWEITZER,
JRNL AUTH 3 P.J.MCDEVITT,K.O.JOHANSON,K.M.KENNEDY-WILSON,D.COSSAR,
JRNL AUTH 4 A.BOCHKAREV,K.GRUBER,S.DHE-PAGANON
JRNL TITL STRUCTURES OF HUMAN DPP7 REVEAL THE MOLECULAR BASIS OF
JRNL TITL 2 SPECIFIC INHIBITION AND THE ARCHITECTURAL DIVERSITY OF
JRNL TITL 3 PROLINE-SPECIFIC PEPTIDASES.
JRNL REF PLOS ONE V. 7 43019 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22952628
JRNL DOI 10.1371/JOURNAL.PONE.0043019
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 72860
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3868
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5225
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 265
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 512
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : 0.00000
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): 0.179
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.204
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7249 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9876 ; 0.864 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 910 ; 4.694 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 355 ;31.368 ;23.183
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1043 ;12.032 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;15.331 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1044 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5761 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 4478 ; 0.338 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7119 ; 0.651 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2771 ; 0.983 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2750 ; 1.521 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 601 B 822
REMARK 3 RESIDUE RANGE : A 601 A 890
REMARK 3 RESIDUE RANGE : B 501 B 501
REMARK 3 RESIDUE RANGE : A 501 A 505
REMARK 3 RESIDUE RANGE : B 27 B 477
REMARK 3 RESIDUE RANGE : A 28 A 477
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5482 61.7161 78.5649
REMARK 3 T TENSOR
REMARK 3 T11: 0.0323 T22: 0.0507
REMARK 3 T33: 0.0545 T12: -0.0030
REMARK 3 T13: 0.0024 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0226 L22: 0.0195
REMARK 3 L33: 0.4496 L12: 0.0116
REMARK 3 L13: 0.0707 L23: 0.0568
REMARK 3 S TENSOR
REMARK 3 S11: -0.0312 S12: 0.0149 S13: -0.0089
REMARK 3 S21: -0.0198 S22: -0.0208 S23: 0.0034
REMARK 3 S31: -0.0751 S32: 0.0537 S33: 0.0521
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4EBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071403.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72860
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 37.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 0.05M ZINC
REMARK 280 ACETATE, 5% PEG3350, PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 30.54450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.06850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.22350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.06850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.54450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.22350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 30.54450
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 144.67050
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 192.13700
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 91.63350
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 96.44700
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 96.06850
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 PRO A 27
REMARK 465 ARG A 478
REMARK 465 GLU A 479
REMARK 465 GLN A 480
REMARK 465 GLN A 481
REMARK 465 PRO A 482
REMARK 465 ALA A 483
REMARK 465 LEU A 484
REMARK 465 ARG A 485
REMARK 465 GLY A 486
REMARK 465 GLY A 487
REMARK 465 PRO A 488
REMARK 465 ARG A 489
REMARK 465 LEU A 490
REMARK 465 SER A 491
REMARK 465 LEU A 492
REMARK 465 GLU A 493
REMARK 465 ASN A 494
REMARK 465 LEU A 495
REMARK 465 TYR A 496
REMARK 465 PHE A 497
REMARK 465 GLN A 498
REMARK 465 GLY B 67
REMARK 465 GLU B 68
REMARK 465 ARG B 478
REMARK 465 GLU B 479
REMARK 465 GLN B 480
REMARK 465 GLN B 481
REMARK 465 PRO B 482
REMARK 465 ALA B 483
REMARK 465 LEU B 484
REMARK 465 ARG B 485
REMARK 465 GLY B 486
REMARK 465 GLY B 487
REMARK 465 PRO B 488
REMARK 465 ARG B 489
REMARK 465 LEU B 490
REMARK 465 SER B 491
REMARK 465 LEU B 492
REMARK 465 GLU B 493
REMARK 465 ASN B 494
REMARK 465 LEU B 495
REMARK 465 TYR B 496
REMARK 465 PHE B 497
REMARK 465 GLN B 498
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 66 CG CD NE CZ NH1 NH2
REMARK 470 ALA A 89 CB
REMARK 470 LYS A 215 CE NZ
REMARK 470 ARG A 225 NE CZ NH1 NH2
REMARK 470 LYS A 253 CE NZ
REMARK 470 LEU A 281 CG CD1 CD2
REMARK 470 ARG A 380 NE CZ NH1 NH2
REMARK 470 ARG A 427 NE CZ NH1 NH2
REMARK 470 ARG A 477 NE CZ NH1 NH2
REMARK 470 PRO B 27 CG CD
REMARK 470 ARG B 66 CG CD NE CZ NH1 NH2
REMARK 470 ALA B 89 CB
REMARK 470 ARG B 225 NE CZ NH1 NH2
REMARK 470 GLN B 247 CG CD OE1 NE2
REMARK 470 GLU B 252 CG CD OE1 OE2
REMARK 470 LYS B 253 CG CD CE NZ
REMARK 470 LEU B 281 CG CD1 CD2
REMARK 470 THR B 340 OG1 CG2
REMARK 470 PHE B 373 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 375 CG OD1 OD2
REMARK 470 GLU B 376 CG CD OE1 OE2
REMARK 470 ARG B 380 CG CD NE CZ NH1 NH2
REMARK 470 TRP B 389 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 389 CZ3 CH2
REMARK 470 LYS B 474 CE NZ
REMARK 470 ARG B 477 CG CD NE CZ NH1 NH2
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 GLU A 68 -51.32 -128.43
REMARK 500 ASN A 77 -146.11 -110.10
REMARK 500 GLU A 78 47.65 -76.23
REMARK 500 TYR A 109 -4.49 79.35
REMARK 500 SER A 113 75.88 -102.66
REMARK 500 SER A 162 -130.35 64.67
REMARK 500 SER A 250 -25.00 -146.04
REMARK 500 PHE A 280 -71.48 -86.39
REMARK 500 ASN A 315 36.64 -143.25
REMARK 500 THR A 353 -69.00 -124.79
REMARK 500 VAL A 364 -55.28 -123.59
REMARK 500 TRP A 400 -7.80 78.81
REMARK 500 ALA A 442 -135.93 -95.59
REMARK 500 HIS A 444 53.22 39.01
REMARK 500 ASN B 77 -141.94 -112.69
REMARK 500 GLU B 78 48.01 -81.26
REMARK 500 SER B 88 58.27 -118.16
REMARK 500 TYR B 109 -3.59 80.76
REMARK 500 SER B 162 -128.75 66.72
REMARK 500 SER B 250 -43.49 -148.92
REMARK 500 ASN B 315 43.87 -140.87
REMARK 500 THR B 353 -69.72 -125.39
REMARK 500 VAL B 364 -54.82 -120.32
REMARK 500 TRP B 400 -15.02 80.79
REMARK 500 ALA B 442 -135.73 -96.48
REMARK 500 HIS B 444 57.09 36.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 453 OE1
REMARK 620 2 HIS A 451 ND1 104.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JYH RELATED DB: PDB
DBREF 4EBB A 27 492 UNP Q9UHL4 DPP2_HUMAN 27 492
DBREF 4EBB B 27 492 UNP Q9UHL4 DPP2_HUMAN 27 492
SEQADV 4EBB GLU A 493 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB ASN A 494 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB LEU A 495 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB TYR A 496 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB PHE A 497 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB GLN A 498 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB GLU B 493 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB ASN B 494 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB LEU B 495 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB TYR B 496 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB PHE B 497 UNP Q9UHL4 EXPRESSION TAG
SEQADV 4EBB GLN B 498 UNP Q9UHL4 EXPRESSION TAG
SEQRES 1 A 472 PRO ASP PRO GLY PHE GLN GLU ARG PHE PHE GLN GLN ARG
SEQRES 2 A 472 LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY ASN LYS THR
SEQRES 3 A 472 PHE PRO GLN ARG PHE LEU VAL SER ASP ARG PHE TRP VAL
SEQRES 4 A 472 ARG GLY GLU GLY PRO ILE PHE PHE TYR THR GLY ASN GLU
SEQRES 5 A 472 GLY ASP VAL TRP ALA PHE ALA ASN ASN SER ALA PHE VAL
SEQRES 6 A 472 ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU LEU VAL PHE
SEQRES 7 A 472 ALA GLU HIS ARG TYR TYR GLY LYS SER LEU PRO PHE GLY
SEQRES 8 A 472 ALA GLN SER THR GLN ARG GLY HIS THR GLU LEU LEU THR
SEQRES 9 A 472 VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU LEU LEU ARG
SEQRES 10 A 472 ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP ALA PRO ALA
SEQRES 11 A 472 ILE ALA PHE GLY GLY SER TYR GLY GLY MSE LEU SER ALA
SEQRES 12 A 472 TYR LEU ARG MSE LYS TYR PRO HIS LEU VAL ALA GLY ALA
SEQRES 13 A 472 LEU ALA ALA SER ALA PRO VAL LEU ALA VAL ALA GLY LEU
SEQRES 14 A 472 GLY ASP SER ASN GLN PHE PHE ARG ASP VAL THR ALA ASP
SEQRES 15 A 472 PHE GLU GLY GLN SER PRO LYS CYS THR GLN GLY VAL ARG
SEQRES 16 A 472 GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE LEU GLN GLY
SEQRES 17 A 472 ALA TYR ASP THR VAL ARG TRP GLU PHE GLY THR CYS GLN
SEQRES 18 A 472 PRO LEU SER ASP GLU LYS ASP LEU THR GLN LEU PHE MSE
SEQRES 19 A 472 PHE ALA ARG ASN ALA PHE THR VAL LEU ALA MSE MSE ASP
SEQRES 20 A 472 TYR PRO TYR PRO THR ASP PHE LEU GLY PRO LEU PRO ALA
SEQRES 21 A 472 ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU LEU SER GLU
SEQRES 22 A 472 ALA GLN ARG ILE THR GLY LEU ARG ALA LEU ALA GLY LEU
SEQRES 23 A 472 VAL TYR ASN ALA SER GLY SER GLU HIS CYS TYR ASP ILE
SEQRES 24 A 472 TYR ARG LEU TYR HIS SER CYS ALA ASP PRO THR GLY CYS
SEQRES 25 A 472 GLY THR GLY PRO ASP ALA ARG ALA TRP ASP TYR GLN ALA
SEQRES 26 A 472 CYS THR GLU ILE ASN LEU THR PHE ALA SER ASN ASN VAL
SEQRES 27 A 472 THR ASP MSE PHE PRO ASP LEU PRO PHE THR ASP GLU LEU
SEQRES 28 A 472 ARG GLN ARG TYR CYS LEU ASP THR TRP GLY VAL TRP PRO
SEQRES 29 A 472 ARG PRO ASP TRP LEU LEU THR SER PHE TRP GLY GLY ASP
SEQRES 30 A 472 LEU ARG ALA ALA SER ASN ILE ILE PHE SER ASN GLY ASN
SEQRES 31 A 472 LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG ARG ASN LEU
SEQRES 32 A 472 SER ALA SER VAL ILE ALA VAL THR ILE GLN GLY GLY ALA
SEQRES 33 A 472 HIS HIS LEU ASP LEU ARG ALA SER HIS PRO GLU ASP PRO
SEQRES 34 A 472 ALA SER VAL VAL GLU ALA ARG LYS LEU GLU ALA THR ILE
SEQRES 35 A 472 ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG GLU GLN GLN
SEQRES 36 A 472 PRO ALA LEU ARG GLY GLY PRO ARG LEU SER LEU GLU ASN
SEQRES 37 A 472 LEU TYR PHE GLN
SEQRES 1 B 472 PRO ASP PRO GLY PHE GLN GLU ARG PHE PHE GLN GLN ARG
SEQRES 2 B 472 LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY ASN LYS THR
SEQRES 3 B 472 PHE PRO GLN ARG PHE LEU VAL SER ASP ARG PHE TRP VAL
SEQRES 4 B 472 ARG GLY GLU GLY PRO ILE PHE PHE TYR THR GLY ASN GLU
SEQRES 5 B 472 GLY ASP VAL TRP ALA PHE ALA ASN ASN SER ALA PHE VAL
SEQRES 6 B 472 ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU LEU VAL PHE
SEQRES 7 B 472 ALA GLU HIS ARG TYR TYR GLY LYS SER LEU PRO PHE GLY
SEQRES 8 B 472 ALA GLN SER THR GLN ARG GLY HIS THR GLU LEU LEU THR
SEQRES 9 B 472 VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU LEU LEU ARG
SEQRES 10 B 472 ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP ALA PRO ALA
SEQRES 11 B 472 ILE ALA PHE GLY GLY SER TYR GLY GLY MSE LEU SER ALA
SEQRES 12 B 472 TYR LEU ARG MSE LYS TYR PRO HIS LEU VAL ALA GLY ALA
SEQRES 13 B 472 LEU ALA ALA SER ALA PRO VAL LEU ALA VAL ALA GLY LEU
SEQRES 14 B 472 GLY ASP SER ASN GLN PHE PHE ARG ASP VAL THR ALA ASP
SEQRES 15 B 472 PHE GLU GLY GLN SER PRO LYS CYS THR GLN GLY VAL ARG
SEQRES 16 B 472 GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE LEU GLN GLY
SEQRES 17 B 472 ALA TYR ASP THR VAL ARG TRP GLU PHE GLY THR CYS GLN
SEQRES 18 B 472 PRO LEU SER ASP GLU LYS ASP LEU THR GLN LEU PHE MSE
SEQRES 19 B 472 PHE ALA ARG ASN ALA PHE THR VAL LEU ALA MSE MSE ASP
SEQRES 20 B 472 TYR PRO TYR PRO THR ASP PHE LEU GLY PRO LEU PRO ALA
SEQRES 21 B 472 ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU LEU SER GLU
SEQRES 22 B 472 ALA GLN ARG ILE THR GLY LEU ARG ALA LEU ALA GLY LEU
SEQRES 23 B 472 VAL TYR ASN ALA SER GLY SER GLU HIS CYS TYR ASP ILE
SEQRES 24 B 472 TYR ARG LEU TYR HIS SER CYS ALA ASP PRO THR GLY CYS
SEQRES 25 B 472 GLY THR GLY PRO ASP ALA ARG ALA TRP ASP TYR GLN ALA
SEQRES 26 B 472 CYS THR GLU ILE ASN LEU THR PHE ALA SER ASN ASN VAL
SEQRES 27 B 472 THR ASP MSE PHE PRO ASP LEU PRO PHE THR ASP GLU LEU
SEQRES 28 B 472 ARG GLN ARG TYR CYS LEU ASP THR TRP GLY VAL TRP PRO
SEQRES 29 B 472 ARG PRO ASP TRP LEU LEU THR SER PHE TRP GLY GLY ASP
SEQRES 30 B 472 LEU ARG ALA ALA SER ASN ILE ILE PHE SER ASN GLY ASN
SEQRES 31 B 472 LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG ARG ASN LEU
SEQRES 32 B 472 SER ALA SER VAL ILE ALA VAL THR ILE GLN GLY GLY ALA
SEQRES 33 B 472 HIS HIS LEU ASP LEU ARG ALA SER HIS PRO GLU ASP PRO
SEQRES 34 B 472 ALA SER VAL VAL GLU ALA ARG LYS LEU GLU ALA THR ILE
SEQRES 35 B 472 ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG GLU GLN GLN
SEQRES 36 B 472 PRO ALA LEU ARG GLY GLY PRO ARG LEU SER LEU GLU ASN
SEQRES 37 B 472 LEU TYR PHE GLN
MODRES 4EBB ASN A 315 ASN GLYCOSYLATION SITE
MODRES 4EBB ASN A 363 ASN GLYCOSYLATION SITE
MODRES 4EBB ASN B 363 ASN GLYCOSYLATION SITE
MODRES 4EBB MSE A 166 MET SELENOMETHIONINE
MODRES 4EBB MSE A 173 MET SELENOMETHIONINE
MODRES 4EBB MSE A 260 MET SELENOMETHIONINE
MODRES 4EBB MSE A 271 MET SELENOMETHIONINE
MODRES 4EBB MSE A 272 MET SELENOMETHIONINE
MODRES 4EBB MSE A 367 MET SELENOMETHIONINE
MODRES 4EBB MSE B 166 MET SELENOMETHIONINE
MODRES 4EBB MSE B 173 MET SELENOMETHIONINE
MODRES 4EBB MSE B 260 MET SELENOMETHIONINE
MODRES 4EBB MSE B 271 MET SELENOMETHIONINE
MODRES 4EBB MSE B 272 MET SELENOMETHIONINE
MODRES 4EBB MSE B 367 MET SELENOMETHIONINE
HET MSE A 166 8
HET MSE A 173 8
HET MSE A 260 13
HET MSE A 271 8
HET MSE A 272 13
HET MSE A 367 8
HET MSE B 166 8
HET MSE B 173 8
HET MSE B 260 8
HET MSE B 271 8
HET MSE B 272 8
HET MSE B 367 8
HET NAG A 501 14
HET NAG A 502 14
HET ZN A 503 1
HET ZN A 504 1
HET ZN A 505 1
HET NAG B 501 14
HETNAM MSE SELENOMETHIONINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM ZN ZINC ION
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 5 ZN 3(ZN 2+)
FORMUL 9 HOH *512(H2 O)
HELIX 1 1 ASP A 80 SER A 88 1 9
HELIX 2 2 SER A 88 GLY A 99 1 12
HELIX 3 3 PHE A 116 GLN A 122 5 7
HELIX 4 4 THR A 130 LEU A 149 1 20
HELIX 5 5 SER A 162 TYR A 175 1 14
HELIX 6 6 LEU A 190 GLY A 194 5 5
HELIX 7 7 ASN A 199 GLY A 211 1 13
HELIX 8 8 SER A 213 GLY A 234 1 22
HELIX 9 9 ALA A 235 GLY A 244 1 10
HELIX 10 10 ASP A 251 MSE A 272 1 22
HELIX 11 11 ASN A 287 SER A 298 1 12
HELIX 12 12 GLN A 301 ASN A 315 1 15
HELIX 13 13 ASP A 324 TYR A 329 1 6
HELIX 14 14 GLY A 341 CYS A 352 1 12
HELIX 15 15 THR A 374 GLY A 387 1 14
HELIX 16 16 ASP A 393 TRP A 400 1 8
HELIX 17 17 TRP A 420 GLY A 424 5 5
HELIX 18 18 HIS A 444 ARG A 448 5 5
HELIX 19 19 PRO A 455 ARG A 477 1 23
HELIX 20 20 ASP B 80 SER B 88 1 9
HELIX 21 21 SER B 88 GLY B 99 1 12
HELIX 22 22 PHE B 116 GLN B 122 5 7
HELIX 23 23 THR B 130 LEU B 149 1 20
HELIX 24 24 SER B 162 TYR B 175 1 14
HELIX 25 25 LEU B 190 GLY B 194 5 5
HELIX 26 26 ASN B 199 SER B 213 1 15
HELIX 27 27 SER B 213 GLY B 234 1 22
HELIX 28 28 ALA B 235 GLY B 244 1 10
HELIX 29 29 ASP B 251 MSE B 272 1 22
HELIX 30 30 ASN B 287 SER B 298 1 12
HELIX 31 31 GLN B 301 ASN B 315 1 15
HELIX 32 32 ASP B 324 TYR B 329 1 6
HELIX 33 33 GLY B 341 CYS B 352 1 12
HELIX 34 34 THR B 374 GLY B 387 1 14
HELIX 35 35 ASP B 393 TRP B 400 1 8
HELIX 36 36 TRP B 420 GLY B 424 5 5
HELIX 37 37 HIS B 444 ARG B 448 5 5
HELIX 38 38 PRO B 455 ARG B 477 1 23
SHEET 1 A 8 GLN A 32 ARG A 39 0
SHEET 2 A 8 THR A 52 SER A 60 -1 O PHE A 53 N GLN A 38
SHEET 3 A 8 LEU A 101 ALA A 105 -1 O PHE A 104 N LEU A 58
SHEET 4 A 8 ILE A 71 THR A 75 1 N PHE A 72 O LEU A 101
SHEET 5 A 8 ALA A 156 GLY A 161 1 O ILE A 157 N ILE A 71
SHEET 6 A 8 GLY A 181 ALA A 185 1 O ALA A 185 N GLY A 160
SHEET 7 A 8 ILE A 410 GLY A 415 1 O ILE A 411 N ALA A 184
SHEET 8 A 8 VAL A 433 ILE A 438 1 O ILE A 434 N PHE A 412
SHEET 1 B 2 THR A 278 ASP A 279 0
SHEET 2 B 2 PRO A 283 LEU A 284 -1 O LEU A 284 N THR A 278
SHEET 1 C 8 GLN B 32 ARG B 39 0
SHEET 2 C 8 THR B 52 SER B 60 -1 O GLN B 55 N PHE B 36
SHEET 3 C 8 LEU B 101 ALA B 105 -1 O PHE B 104 N LEU B 58
SHEET 4 C 8 ILE B 71 THR B 75 1 N PHE B 72 O LEU B 101
SHEET 5 C 8 ALA B 156 GLY B 161 1 O ILE B 157 N PHE B 73
SHEET 6 C 8 GLY B 181 ALA B 185 1 O LEU B 183 N ALA B 158
SHEET 7 C 8 ILE B 410 GLY B 415 1 O ILE B 411 N ALA B 184
SHEET 8 C 8 VAL B 433 ILE B 438 1 O ILE B 434 N PHE B 412
SHEET 1 D 2 THR B 278 ASP B 279 0
SHEET 2 D 2 PRO B 283 LEU B 284 -1 O LEU B 284 N THR B 278
SSBOND 1 CYS A 216 CYS A 293 1555 1555 2.03
SSBOND 2 CYS A 246 CYS A 322 1555 1555 2.04
SSBOND 3 CYS A 332 CYS A 338 1555 1555 2.03
SSBOND 4 CYS A 352 CYS A 382 1555 1555 2.03
SSBOND 5 CYS B 216 CYS B 293 1555 1555 2.03
SSBOND 6 CYS B 246 CYS B 322 1555 1555 2.03
SSBOND 7 CYS B 332 CYS B 338 1555 1555 2.03
SSBOND 8 CYS B 352 CYS B 382 1555 1555 2.03
LINK C GLY A 165 N MSE A 166 1555 1555 1.33
LINK C MSE A 166 N LEU A 167 1555 1555 1.33
LINK C ARG A 172 N MSE A 173 1555 1555 1.33
LINK C MSE A 173 N LYS A 174 1555 1555 1.33
LINK C PHE A 259 N MSE A 260 1555 1555 1.33
LINK C MSE A 260 N PHE A 261 1555 1555 1.33
LINK C ALA A 270 N MSE A 271 1555 1555 1.33
LINK C MSE A 271 N MSE A 272 1555 1555 1.33
LINK C MSE A 272 N ASP A 273 1555 1555 1.33
LINK C ASP A 366 N MSE A 367 1555 1555 1.33
LINK C MSE A 367 N PHE A 368 1555 1555 1.33
LINK C GLY B 165 N MSE B 166 1555 1555 1.34
LINK C MSE B 166 N LEU B 167 1555 1555 1.33
LINK C ARG B 172 N MSE B 173 1555 1555 1.33
LINK C MSE B 173 N LYS B 174 1555 1555 1.33
LINK C PHE B 259 N MSE B 260 1555 1555 1.33
LINK C MSE B 260 N PHE B 261 1555 1555 1.33
LINK C ALA B 270 N MSE B 271 1555 1555 1.33
LINK C MSE B 271 N MSE B 272 1555 1555 1.33
LINK C MSE B 272 N ASP B 273 1555 1555 1.33
LINK C ASP B 366 N MSE B 367 1555 1555 1.33
LINK C MSE B 367 N PHE B 368 1555 1555 1.33
LINK ND2 ASN A 315 C1 NAG A 501 1555 1555 1.44
LINK ND2 ASN A 363 C1 NAG A 502 1555 1555 1.44
LINK ND2 ASN B 363 C1 NAG B 501 1555 1555 1.44
LINK OE1 GLU A 453 ZN ZN A 504 1555 1555 1.99
LINK NE2 HIS A 125 ZN ZN A 503 1555 1555 2.07
LINK ND1 HIS A 451 ZN ZN A 504 1555 1555 2.17
LINK OD2 ASP A 251 ZN ZN A 505 1555 1555 2.20
SITE 1 AC1 8 ARG A 307 ASN A 315 GLY A 318 GLU A 320
SITE 2 AC1 8 TYR A 323 HOH A 716 HOH A 764 HOH A 871
SITE 1 AC2 7 PHE A 224 ARG A 225 LYS A 228 ASN A 363
SITE 2 AC2 7 HOH A 615 HOH A 781 HOH A 829
SITE 1 AC3 4 GLN A 119 HIS A 125 ASP B 279 HOH B 810
SITE 1 AC4 4 HIS A 321 HIS A 451 GLU A 453 HOH A 851
SITE 1 AC5 1 ASP A 251
SITE 1 AC6 6 PHE B 224 ARG B 225 LYS B 228 ASN B 363
SITE 2 AC6 6 HOH B 732 HOH B 786
CRYST1 61.089 96.447 192.137 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 0.016370 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010368 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005205 0.00000
TER 3536 ARG A 477
TER 6997 ARG B 477
MASTER 455 0 18 38 20 0 9 6 7519 2 194 74
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