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HEADER HYDROLASE 09-JUL-07 2QJR
TITLE DIPEPDYL PEPTIDASE IV IN COMPLEX WITH INHIBITOR PZF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 31-766;
COMPND 5 EC: 3.4.14.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DPP4, ADCP2, CD26;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS
KEYWDS PROTEIN-INHIBITOR COMPLEX, AMINOPEPTIDASE, GLYCOPROTEIN,
KEYWDS 2 HYDROLASE, MEMBRANE, PROTEASE, SECRETED, SERINE PROTEASE,
KEYWDS 3 SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SHENPING
REVDAT 2 05-AUG-08 2QJR 1 HEADER
REVDAT 1 29-JUL-08 2QJR 0
JRNL AUTH W.STEPHEN,A.MARK,A.KIM,B.ANNE,D.DENNIS,L.JAY,
JRNL AUTH 2 L.SHENPING,M.LESTER,M.KIK,O.THANH
JRNL TITL (3R,4S)-4-(2,4,5-TRIFLUOROPHENYL)-PYRROLIDIN-3-
JRNL TITL 2 YLAMINE INHIBITORS OF DIPEPTIDYL PEPTIDASE IV:
JRNL TITL 3 SYNTHESIS, IN VITRO, IN VIVO AND X-RAY
JRNL TITL 4 CRYSTALLOGRAPHIC CHARACTERIZATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.7
REMARK 3 NUMBER OF REFLECTIONS : 80198
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4234
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6018
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 319
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 12532
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.90000
REMARK 3 B22 (A**2) : 7.59000
REMARK 3 B33 (A**2) : -2.69000
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): 0.291
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.236
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.182
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.021
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12578 ; 0.026 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 10717 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17138 ; 2.147 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 24897 ; 1.027 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1454 ; 7.502 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 612 ;33.880 ;23.922
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1990 ;18.381 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;21.880 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1839 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13802 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2688 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2350 ; 0.227 ; 0.600
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 10920 ; 0.237 ; 0.600
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6084 ; 0.204 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 7141 ; 0.110 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 863 ; 0.219 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 8 ; 0.111 ; 0.500
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): 12 ; 0.175 ; 0.600
REMARK 3 SYMMETRY VDW OTHERS (A): 43 ; 0.288 ; 0.600
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.185 ; 0.500
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): 9116 ; 1.432 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2942 ; 0.292 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11762 ; 1.725 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6537 ; 2.939 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5376 ; 4.174 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 39 A 766 2
REMARK 3 1 B 39 B 766 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4300 ; 0.07 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 6912 ; 0.52 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 4300 ; 0.26 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 6912 ; 0.91 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 39 A 796
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6237 15.9839 27.6147
REMARK 3 T TENSOR
REMARK 3 T11: -0.1517 T22: 0.1830
REMARK 3 T33: -0.0621 T12: -0.0095
REMARK 3 T13: 0.0049 T23: 0.2067
REMARK 3 L TENSOR
REMARK 3 L11: 0.4342 L22: 0.4450
REMARK 3 L33: 1.3934 L12: -0.0350
REMARK 3 L13: -0.1755 L23: -0.3124
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: 0.2683 S13: 0.0957
REMARK 3 S21: -0.0303 S22: -0.0094 S23: -0.0080
REMARK 3 S31: 0.0230 S32: -0.0087 S33: -0.0321
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 39 B 796
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0559 -3.2045 78.2353
REMARK 3 T TENSOR
REMARK 3 T11: -0.0489 T22: -0.3467
REMARK 3 T33: -0.0869 T12: 0.0127
REMARK 3 T13: 0.0497 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 1.0761 L22: 0.3495
REMARK 3 L33: 1.3320 L12: 0.1057
REMARK 3 L13: -0.3520 L23: -0.2880
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: 0.2074 S13: 0.0150
REMARK 3 S21: 0.0775 S22: 0.0781 S23: 0.0338
REMARK 3 S31: 0.0751 S32: -0.0933 S33: -0.0530
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2QJR COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB043685.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85437
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.5
REMARK 200 DATA REDUNDANCY : 3.750
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : 0.09900
REMARK 200 FOR THE DATA SET : 19.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.49200
REMARK 200 R SYM FOR SHELL (I) : 0.49200
REMARK 200 FOR SHELL : 2.330
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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 (%): 55.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
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 32.73500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 211.30550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.39800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 211.30550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.73500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.39800
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
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 GLY A 31
REMARK 465 THR A 32
REMARK 465 ASP A 33
REMARK 465 ASP A 34
REMARK 465 ALA A 35
REMARK 465 THR A 36
REMARK 465 ALA A 37
REMARK 465 ASP A 38
REMARK 465 LEU A 767
REMARK 465 VAL A 768
REMARK 465 PRO A 769
REMARK 465 ARG A 770
REMARK 465 GLY A 771
REMARK 465 SER A 772
REMARK 465 HIS A 773
REMARK 465 HIS A 774
REMARK 465 HIS A 775
REMARK 465 HIS A 776
REMARK 465 HIS A 777
REMARK 465 HIS A 778
REMARK 465 GLY B 31
REMARK 465 THR B 32
REMARK 465 ASP B 33
REMARK 465 ASP B 34
REMARK 465 ALA B 35
REMARK 465 THR B 36
REMARK 465 ALA B 37
REMARK 465 ASP B 38
REMARK 465 LEU B 767
REMARK 465 VAL B 768
REMARK 465 PRO B 769
REMARK 465 ARG B 770
REMARK 465 GLY B 771
REMARK 465 SER B 772
REMARK 465 HIS B 773
REMARK 465 HIS B 774
REMARK 465 HIS B 775
REMARK 465 HIS B 776
REMARK 465 HIS B 777
REMARK 465 HIS B 778
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 ASN A 150 CG OD1 ND2
REMARK 470 ASN A 520 CG OD1 ND2
REMARK 470 ASN B 150 CG OD1 ND2
REMARK 470 ASN B 520 CG OD1 ND2
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 O SER B 39 O HOH B 1122 1.93
REMARK 500 NE ARG A 658 O HOH A 1002 1.93
REMARK 500 OD1 ASP B 65 O LYS B 463 1.95
REMARK 500 O ILE B 389 O HOH B 1045 2.06
REMARK 500 OG SER A 630 NE2 HIS A 740 2.09
REMARK 500 OE2 GLU A 206 OD2 ASP A 663 2.11
REMARK 500 O HOH B 1121 O HOH B 1122 2.11
REMARK 500 O4 NAG B 794 O5 NAG B 797 2.17
REMARK 500 ND2 ASN B 321 O NDG B 800 2.18
REMARK 500 NE ARG B 429 O HOH B 916 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 658 NE ARG A 658 CZ 0.083
REMARK 500 GLU B 82 CD GLU B 82 OE1 0.071
REMARK 500 TYR B 83 CE1 TYR B 83 CZ 0.084
REMARK 500 TYR B 203 CE1 TYR B 203 CZ 0.080
REMARK 500 GLU B 244 CD GLU B 244 OE1 0.073
REMARK 500 LYS B 250 CD LYS B 250 CE 0.169
REMARK 500 CYS B 385 CB CYS B 385 SG -0.130
REMARK 500 TYR B 417 CD1 TYR B 417 CE1 -0.094
REMARK 500 ARG B 429 NE ARG B 429 CZ 0.078
REMARK 500 LYS B 463 CE LYS B 463 NZ 0.159
REMARK 500 TYR B 480 CZ TYR B 480 CE2 -0.081
REMARK 500 ARG B 669 CD ARG B 669 NE -0.107
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 65 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 104 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 133 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 243 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 302 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 329 CB - CG - OD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 367 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 393 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 THR A 401 OG1 - CB - CG2 ANGL. DEV. = -16.2 DEGREES
REMARK 500 THR A 443 OG1 - CB - CG2 ANGL. DEV. = -14.0 DEGREES
REMARK 500 ASP A 501 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP A 515 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 535 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 560 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 579 CB - CG - OD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG A 658 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 669 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 669 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 678 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 691 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 691 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP B 47 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU B 60 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 ARG B 61 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 61 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ASP B 65 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 133 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 230 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 VAL B 271 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASP B 302 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 LEU B 316 CB - CG - CD1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 LEU B 316 CB - CG - CD2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ASN B 321 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 CYS B 385 CA - CB - SG ANGL. DEV. = -10.8 DEGREES
REMARK 500 ASP B 390 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 CYS B 394 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP B 413 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 429 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP B 438 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG B 453 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 453 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP B 501 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 515 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP B 556 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG B 669 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 669 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP B 678 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP B 725 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP B 729 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 40 -120.99 -111.81
REMARK 500 SER A 64 -175.32 -175.45
REMARK 500 GLU A 73 94.80 41.81
REMARK 500 GLN A 123 -100.44 -108.34
REMARK 500 TRP A 124 -148.17 -98.48
REMARK 500 HIS A 162 26.54 -149.95
REMARK 500 ILE A 193 -57.49 -132.98
REMARK 500 SER A 242 -158.61 64.28
REMARK 500 GLN A 320 36.75 -78.14
REMARK 500 ASP A 393 -145.09 -83.73
REMARK 500 LYS A 423 19.78 55.17
REMARK 500 ASP A 438 98.89 -160.86
REMARK 500 ASN A 450 77.15 -160.22
REMARK 500 TYR A 547 -74.62 -115.65
REMARK 500 ASN A 562 -158.74 -148.85
REMARK 500 ARG A 596 17.35 58.05
REMARK 500 ARG A 597 37.33 -148.26
REMARK 500 THR A 600 -94.60 -121.32
REMARK 500 SER A 630 -107.12 66.40
REMARK 500 ASP A 678 -100.63 -119.44
REMARK 500 ASN A 710 -70.18 -98.70
REMARK 500 ASP A 739 -152.92 -105.08
REMARK 500 ARG B 40 -141.54 -93.88
REMARK 500 SER B 64 -168.94 -172.96
REMARK 500 GLU B 73 78.37 51.62
REMARK 500 GLN B 123 -94.50 -97.24
REMARK 500 TRP B 124 -141.11 -105.43
REMARK 500 HIS B 162 28.32 -155.26
REMARK 500 ILE B 193 -62.48 -132.12
REMARK 500 ALA B 213 51.20 -140.08
REMARK 500 SER B 242 -156.72 73.16
REMARK 500 GLN B 320 42.04 -77.72
REMARK 500 ASP B 393 -149.24 -83.51
REMARK 500 THR B 401 49.69 -81.10
REMARK 500 LYS B 423 27.92 41.87
REMARK 500 ASN B 450 74.02 -164.02
REMARK 500 GLU B 464 -3.65 75.28
REMARK 500 ARG B 492 137.29 -170.05
REMARK 500 ASP B 515 -169.00 -163.45
REMARK 500 TYR B 547 -76.28 -117.94
REMARK 500 TYR B 585 12.71 81.21
REMARK 500 ARG B 596 12.22 55.70
REMARK 500 ARG B 597 41.20 -141.68
REMARK 500 THR B 600 -91.45 -115.18
REMARK 500 SER B 630 -110.43 74.80
REMARK 500 ASP B 678 -95.18 -118.84
REMARK 500 ASN B 710 -70.66 -97.41
REMARK 500 ASP B 739 -152.04 -103.91
REMARK 500 ILE B 742 57.01 39.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 RESIDUES NAG B799,NAG B800 CHANGED TO NDG;
REMARK 600 RESIDUES MAN A802, MAN A804 CHANGED TO LGU
REMARK 600 DUE TO INCORRECT STEREOCHEMISTRY AT THE LINKER ATOM.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 LGU A 802
REMARK 610 LGU A 804
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 794
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 796
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 798
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR RESIDUE A 803
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 799
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 801
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 794
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 797
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 796
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR RESIDUE B 799
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 805
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR RESIDUE B 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 801
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: PZF BINDING SITE FOR RESIDUE A 900
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: PZF BINDING SITE FOR RESIDUE B 900
DBREF 2QJR A 31 766 UNP P27487 DPP4_HUMAN 31 766
DBREF 2QJR B 31 766 UNP P27487 DPP4_HUMAN 31 766
SEQADV 2QJR LEU A 767 UNP P27487 EXPRESSION TAG
SEQADV 2QJR VAL A 768 UNP P27487 EXPRESSION TAG
SEQADV 2QJR PRO A 769 UNP P27487 EXPRESSION TAG
SEQADV 2QJR ARG A 770 UNP P27487 EXPRESSION TAG
SEQADV 2QJR GLY A 771 UNP P27487 EXPRESSION TAG
SEQADV 2QJR SER A 772 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS A 773 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS A 774 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS A 775 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS A 776 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS A 777 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS A 778 UNP P27487 EXPRESSION TAG
SEQADV 2QJR LEU B 767 UNP P27487 EXPRESSION TAG
SEQADV 2QJR VAL B 768 UNP P27487 EXPRESSION TAG
SEQADV 2QJR PRO B 769 UNP P27487 EXPRESSION TAG
SEQADV 2QJR ARG B 770 UNP P27487 EXPRESSION TAG
SEQADV 2QJR GLY B 771 UNP P27487 EXPRESSION TAG
SEQADV 2QJR SER B 772 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS B 773 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS B 774 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS B 775 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS B 776 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS B 777 UNP P27487 EXPRESSION TAG
SEQADV 2QJR HIS B 778 UNP P27487 EXPRESSION TAG
SEQRES 1 A 748 GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR
SEQRES 2 A 748 THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS
SEQRES 3 A 748 LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU
SEQRES 4 A 748 TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU
SEQRES 5 A 748 TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER THR PHE
SEQRES 6 A 748 ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER
SEQRES 7 A 748 PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL
SEQRES 8 A 748 LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE
SEQRES 9 A 748 TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG
SEQRES 10 A 748 ILE PRO ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL
SEQRES 11 A 748 GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR
SEQRES 12 A 748 VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR
SEQRES 13 A 748 TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR
SEQRES 14 A 748 ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER
SEQRES 15 A 748 ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR
SEQRES 16 A 748 ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR
SEQRES 17 A 748 SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR
SEQRES 18 A 748 VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO
SEQRES 19 A 748 THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER
SEQRES 20 A 748 SER VAL THR ASN ALA THR SER ILE GLN ILE THR ALA PRO
SEQRES 21 A 748 ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL
SEQRES 22 A 748 THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU
SEQRES 23 A 748 ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP
SEQRES 24 A 748 TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA
SEQRES 25 A 748 ARG GLN HIS ILE GLU MET SER THR THR GLY TRP VAL GLY
SEQRES 26 A 748 ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY
SEQRES 27 A 748 ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR
SEQRES 28 A 748 ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS
SEQRES 29 A 748 THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE
SEQRES 30 A 748 GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN
SEQRES 31 A 748 GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS
SEQRES 32 A 748 ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS LEU SER
SEQRES 33 A 748 CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL
SEQRES 34 A 748 SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS
SEQRES 35 A 748 SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER
SEQRES 36 A 748 VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER
SEQRES 37 A 748 ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER
SEQRES 38 A 748 LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE
SEQRES 39 A 748 TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER
SEQRES 40 A 748 LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO
SEQRES 41 A 748 CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP
SEQRES 42 A 748 ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA
SEQRES 43 A 748 SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS
SEQRES 44 A 748 ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU
SEQRES 45 A 748 VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS
SEQRES 46 A 748 MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY
SEQRES 47 A 748 TRP SER TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY
SEQRES 48 A 748 SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA
SEQRES 49 A 748 PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR
SEQRES 50 A 748 GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU
SEQRES 51 A 748 ASP HIS TYR ARG ASN SER THR VAL MET SER ARG ALA GLU
SEQRES 52 A 748 ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR
SEQRES 53 A 748 ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE
SEQRES 54 A 748 SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA
SEQRES 55 A 748 MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER
SEQRES 56 A 748 THR ALA HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE
SEQRES 57 A 748 ILE LYS GLN CYS PHE SER LEU PRO LEU VAL PRO ARG GLY
SEQRES 58 A 748 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 748 GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR
SEQRES 2 B 748 THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS
SEQRES 3 B 748 LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU
SEQRES 4 B 748 TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU
SEQRES 5 B 748 TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER THR PHE
SEQRES 6 B 748 ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER
SEQRES 7 B 748 PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL
SEQRES 8 B 748 LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE
SEQRES 9 B 748 TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG
SEQRES 10 B 748 ILE PRO ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL
SEQRES 11 B 748 GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR
SEQRES 12 B 748 VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR
SEQRES 13 B 748 TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR
SEQRES 14 B 748 ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER
SEQRES 15 B 748 ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR
SEQRES 16 B 748 ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR
SEQRES 17 B 748 SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR
SEQRES 18 B 748 VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO
SEQRES 19 B 748 THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER
SEQRES 20 B 748 SER VAL THR ASN ALA THR SER ILE GLN ILE THR ALA PRO
SEQRES 21 B 748 ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL
SEQRES 22 B 748 THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU
SEQRES 23 B 748 ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP
SEQRES 24 B 748 TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA
SEQRES 25 B 748 ARG GLN HIS ILE GLU MET SER THR THR GLY TRP VAL GLY
SEQRES 26 B 748 ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY
SEQRES 27 B 748 ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR
SEQRES 28 B 748 ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS
SEQRES 29 B 748 THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE
SEQRES 30 B 748 GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN
SEQRES 31 B 748 GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS
SEQRES 32 B 748 ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS LEU SER
SEQRES 33 B 748 CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL
SEQRES 34 B 748 SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS
SEQRES 35 B 748 SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER
SEQRES 36 B 748 VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER
SEQRES 37 B 748 ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER
SEQRES 38 B 748 LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE
SEQRES 39 B 748 TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER
SEQRES 40 B 748 LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO
SEQRES 41 B 748 CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP
SEQRES 42 B 748 ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA
SEQRES 43 B 748 SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS
SEQRES 44 B 748 ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU
SEQRES 45 B 748 VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS
SEQRES 46 B 748 MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY
SEQRES 47 B 748 TRP SER TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY
SEQRES 48 B 748 SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA
SEQRES 49 B 748 PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR
SEQRES 50 B 748 GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU
SEQRES 51 B 748 ASP HIS TYR ARG ASN SER THR VAL MET SER ARG ALA GLU
SEQRES 52 B 748 ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR
SEQRES 53 B 748 ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE
SEQRES 54 B 748 SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA
SEQRES 55 B 748 MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER
SEQRES 56 B 748 THR ALA HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE
SEQRES 57 B 748 ILE LYS GLN CYS PHE SER LEU PRO LEU VAL PRO ARG GLY
SEQRES 58 B 748 SER HIS HIS HIS HIS HIS HIS
MODRES 2QJR ASN A 85 ASN GLYCOSYLATION SITE
MODRES 2QJR ASN A 219 ASN GLYCOSYLATION SITE
MODRES 2QJR ASN A 229 ASN GLYCOSYLATION SITE
MODRES 2QJR ASN A 321 ASN GLYCOSYLATION SITE
MODRES 2QJR ASN B 85 ASN GLYCOSYLATION SITE
MODRES 2QJR ASN B 229 ASN GLYCOSYLATION SITE
MODRES 2QJR ASN B 321 ASN GLYCOSYLATION SITE
MODRES 2QJR ASN B 219 ASN GLYCOSYLATION SITE
HET NAG A 794 14
HET NAG A 797 14
HET NAG A 796 14
HET NAG A 798 14
HET LGU A 802 11
HET MAN A 803 11
HET LGU A 804 11
HET NAG A 799 14
HET NAG A 800 14
HET NAG A 801 14
HET NAG B 794 14
HET NAG B 797 14
HET NAG B 796 14
HET NDG B 799 14
HET NAG B 805 14
HET NDG B 800 14
HET NAG B 801 14
HET PZF A 900 29
HET PZF B 900 29
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM LGU ALPHA-L-GULURONATE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM PZF (3R,4S)-1-[6-(6-METHOXYPYRIDIN-3-YL)PYRIMIDIN-4-YL]-4-
HETNAM 2 PZF (2,4,5-TRIFLUOROPHENYL)PYRROLIDIN-3-AMINE
HETSYN NAG NAG
HETSYN LGU ALPHA-L-GULOPYRANURONIC ACID
FORMUL 3 NAG 12(C8 H15 N O6)
FORMUL 4 LGU 2(C6 H10 O7)
FORMUL 4 MAN C6 H12 O6
FORMUL 9 NDG 2(C8 H15 N O6)
FORMUL 11 PZF 2(C20 H18 F3 N5 O)
FORMUL 13 HOH *331(H2 O)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 SER A 93 ASP A 96 5 4
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 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 ASN A 506 1 10
HELIX 9 9 ASN A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 SER A 614 1 15
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 THR A 687 VAL A 698 5 12
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 LYS B 50 1 7
HELIX 21 21 SER B 93 ASP B 96 5 4
HELIX 22 22 ASP B 200 VAL B 207 1 8
HELIX 23 23 PRO B 290 ILE B 295 1 6
HELIX 24 24 LEU B 340 GLN B 344 5 5
HELIX 25 25 GLU B 421 MET B 425 5 5
HELIX 26 26 LYS B 463 ALA B 465 5 3
HELIX 27 27 ASN B 497 ASN B 506 1 10
HELIX 28 28 ASN B 562 THR B 570 1 9
HELIX 29 29 GLY B 587 HIS B 592 1 6
HELIX 30 30 ALA B 593 ASN B 595 5 3
HELIX 31 31 THR B 600 SER B 614 1 15
HELIX 32 32 SER B 630 GLY B 641 1 12
HELIX 33 33 ARG B 658 TYR B 662 5 5
HELIX 34 34 ASP B 663 GLY B 672 1 10
HELIX 35 35 ASN B 679 SER B 686 1 8
HELIX 36 36 VAL B 688 VAL B 698 5 11
HELIX 37 37 PHE B 713 VAL B 726 1 14
HELIX 38 38 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 LYS A 71 -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 GLU A 91 -1 O PHE A 89 N ILE A 76
SHEET 1 C 4 ASP A 104 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 TRP A 154 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 F 4 SER A 284 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 TRP A 337 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 ARG A 310 N ALA A 306
SHEET 3 I 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 I 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O 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 ILE A 418 N ILE A 405
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 ASP A 438 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 L 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 L 4 GLY A 490 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 ARG B 61 TRP B 62 0
SHEET 2 O 4 GLU B 67 LYS B 71 -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 GLU B 91 -1 O PHE B 89 N ILE B 76
SHEET 1 P 4 ASP B 104 ILE B 107 0
SHEET 2 P 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 P 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 P 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 Q 4 TRP B 154 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 Q 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O 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 VAL B 254 N ILE B 236
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 U 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 U 4 ARG B 336 ASN B 338 -1 O ARG B 336 N ASP B 331
SHEET 1 V 4 HIS B 298 THR B 307 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 V 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 V 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 W 4 HIS B 363 PHE B 364 0
SHEET 2 W 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 W 4 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
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 GLY B 490 GLU B 495 -1 O LEU B 494 N TYR B 480
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 SER B 577 N GLN B 527
SHEET 4 Z 8 TYR B 540 ASP B 545 1 N ASP B 545 O ALA B 576
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O ASP B 620 N TYR B 540
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Z 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.07
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.08
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.01
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.24
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.09
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.12
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.06
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.06
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.15
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.13
LINK ND2 ASN A 85 C1 NAG A 794 1555 1555 1.45
LINK ND2 ASN A 219 C1 NAG A 799 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG A 796 1555 1555 1.45
LINK ND2 ASN A 321 C1 NAG A 800 1555 1555 1.47
LINK ND2 ASN B 85 C1 NAG B 794 1555 1555 1.45
LINK ND2 ASN B 229 C1 NAG B 796 1555 1555 1.46
LINK O4 NAG A 794 C1 NAG A 797 1555 1555 1.45
LINK O4 NAG A 796 C1 NAG A 798 1555 1555 1.43
LINK O4 NAG A 798 C1 LGU A 802 1555 1555 1.43
LINK O3 LGU A 802 C1 MAN A 803 1555 1555 1.45
LINK O6A LGU A 802 C1 LGU A 804 1555 1555 1.44
LINK O4 NAG A 800 C1 NAG A 801 1555 1555 1.46
LINK O4 NAG B 794 C1 NAG B 797 1555 1555 1.40
LINK O4 NDG B 799 C1 NAG B 805 1555 1555 1.44
LINK O4 NDG B 800 C1 NAG B 801 1555 1555 1.44
LINK ND2 ASN B 321 C1 NDG B 800 1555 1555 1.41
LINK ND2 ASN B 219 C1 NDG B 799 1555 1555 1.43
CISPEP 1 GLY A 474 PRO A 475 0 2.16
CISPEP 2 GLY B 474 PRO B 475 0 -0.39
SITE 1 AC1 6 ASN A 85 SER A 86 SER A 87 TYR A 386
SITE 2 AC1 6 GLN A 388 THR A 395
SITE 1 AC2 5 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC2 5 LYS A 267
SITE 1 AC3 1 GLU A 232
SITE 1 AC5 2 SER B 690 GLU B 693
SITE 1 AC7 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC8 4 ILE A 319 ASN A 321 SER A 349 THR A 350
SITE 1 AC9 1 GLU A 677
SITE 1 BC1 8 ASN B 85 SER B 86 SER B 87 TYR B 386
SITE 2 BC1 8 GLN B 388 THR B 395 HOH B1042 HOH B1088
SITE 1 BC2 2 LYS B 391 HOH B1120
SITE 1 BC3 6 ASN B 229 THR B 231 GLU B 232 HOH B 973
SITE 2 BC3 6 HOH B1049 HOH B1062
SITE 1 BC4 5 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC4 5 HOH B1104
SITE 1 BC5 3 ASN B 272 TYR B 330 GLU B 332
SITE 1 BC6 4 ASN B 321 SER B 349 THR B 350 HOH B1113
SITE 1 BC7 1 ASP B 678
SITE 1 BC8 13 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 BC8 13 PHE A 357 ARG A 358 TYR A 547 SER A 630
SITE 3 BC8 13 TYR A 631 TYR A 662 TYR A 666 ASN A 710
SITE 4 BC8 13 HIS A 740
SITE 1 BC9 13 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 BC9 13 PHE B 357 ARG B 358 SER B 630 TYR B 631
SITE 3 BC9 13 TYR B 662 TYR B 666 ASN B 710 HIS B 740
SITE 4 BC9 13 HOH B 967
CRYST1 65.470 68.796 422.611 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 0.015274 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014536 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002366 0.00000
TER 5958 PRO A 766
TER 11916 PRO B 766
MASTER 566 0 19 38 102 0 27 612532 2 315 116
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