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HEADER HYDROLASE/COMPLEX 03-JAN-05 2BGR
TITLE CRYSTAL STRUCTURE OF HIV-1 TAT DERIVED NONAPEPTIDES TAT(1-9)
TITLE 2 BOUND TO THE ACTIVE SITE OF DIPEPTIDYL PEPTIDASE IV (CD26)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26, TP103,
COMPND 4 ADENOSINE DEAMINASE COMPLEXING PROTEIN-2, ADABP;
COMPND 5 CHAIN: A, B;
COMPND 6 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 29-766;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: TAT PROTEIN;
COMPND 11 SYNONYM: TRANSACTIVATING REGULATORY PROTEIN;
COMPND 12 MOLECULE: HIV-1 TAT PROTEIN DERIVED N-TERMINAL
COMPND 13 NONAPEPTIDE;
COMPND 14 CHAIN: Y, Z
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: SPODOPTERS FRUGIPERDA;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: SF9 CELLS;
SOURCE 4 EXPRESSION_SYSTEM_VECTOR: BACULAOVIRUS;
SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTC;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGAN: KIDNEY;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;
KEYWDS DIPETIDYL PEPTIDASE IV, DPPIV, CD26, ALPHA/BETA-HYDROLASE
KEYWDS 2 FOLD, BETA-PROPELLER FOLD, HIV-1 TAT PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.A.WEIHOFEN,J.LIU,W.REUTTER,W.SAENGER,H.FAN
REVDAT 1 27-JAN-05 2BGR 0
JRNL AUTH W.A.WEIHOFEN,J.LIU,W.REUTTER,W.SAENGER,H.FAN
JRNL TITL CRYSTAL STRUCTURES OF HIV-1 TAT DERIVED
JRNL TITL 2 NONAPEPTIDES TAT(1-9) AND TRP2-TAT(1-9) BOUND TO
JRNL TITL 3 THE ACTIVE SITE OF DIPEPTIDYL PEPTIDASE IV (CD26)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.0 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.1999
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) : 2.0
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.12
REMARK 3 NUMBER OF REFLECTIONS : 127470
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) : 0.16
REMARK 3 R VALUE (WORKING SET) : 0.16
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1297
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) : 2.000
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.052
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8872
REMARK 3 BIN R VALUE (WORKING SET) : 0.202
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.247
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 364
REMARK 3 SOLVENT ATOMS : 1750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.49
REMARK 3 B22 (A**2) : -0.11
REMARK 3 B33 (A**2) : 1.60
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.147
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.392
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 12735 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 10841 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 17354 ; 1.508 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25156 ; 0.858 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1458 ; 6.384 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 620 ;34.012 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2004 ;14.580 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;18.887 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1887 ; 0.150 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 13858 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2678 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 2144 ; 0.207 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 10711 ; 0.189 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 7131 ; 0.088 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED (A): 2041 ; 0.215 ; 0.500
REMARK 3 SYMMETRY VDW REFINED (A): 15 ; 0.129 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 38 ; 0.209 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED (A): 40 ; 0.233 ; 0.500
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 9432 ; 1.041 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 2960 ; 0.203 ; 1.500
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 6650 ; 2.066 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 5522 ; 3.048 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 41 A 278 6
REMARK 3 1 B 41 B 278 6
REMARK 3 2 A 296 A 764 6
REMARK 3 2 B 296 B 764 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 10908 ; 0.48 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 10908 ; 1.05 ; 10.00
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 : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 38 A 85
REMARK 3 RESIDUE RANGE : A 86 A 200
REMARK 3 RESIDUE RANGE : A 301 A 497
REMARK 3 RESIDUE RANGE : A 498 A 600
REMARK 3 RESIDUE RANGE : A 601 A 766
REMARK 3 RESIDUE RANGE : A 201 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 45.2820 54.8900 39.5050
REMARK 3 T TENSOR
REMARK 3 T11: -0.1848 T22: -0.2903
REMARK 3 T33: -0.2995 T12: -0.0037
REMARK 3 T13: 0.0129 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 1.3739 L22: 0.2899
REMARK 3 L33: 0.6331 L12: -0.0499
REMARK 3 L13: 0.0654 L23: -0.0861
REMARK 3 S TENSOR
REMARK 3 S11: 0.0264 S12: 0.0219 S13: 0.0788
REMARK 3 S21: 0.0125 S22: -0.0197 S23: -0.0581
REMARK 3 S31: -0.0534 S32: 0.0494 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 38 B 85
REMARK 3 RESIDUE RANGE : B 86 B 300
REMARK 3 RESIDUE RANGE : B 301 B 497
REMARK 3 RESIDUE RANGE : B 498 B 766
REMARK 3 RESIDUE RANGE : B 601 B 766
REMARK 3 RESIDUE RANGE : B 201 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5200 60.3050 31.9770
REMARK 3 T TENSOR
REMARK 3 T11: -0.1855 T22: -0.2485
REMARK 3 T33: -0.2452 T12: -0.0084
REMARK 3 T13: 0.0232 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.0067 L22: 0.3226
REMARK 3 L33: 0.5385 L12: -0.1119
REMARK 3 L13: 0.1444 L23: -0.2425
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: -0.0716 S13: -0.1091
REMARK 3 S21: -0.0171 S22: 0.0095 S23: 0.0652
REMARK 3 S31: 0.0689 S32: -0.1017 S33: -0.0133
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. RESIDUES 29 - 37 ARE DISORDERED AND WERE
REMARK 3 NOT MODELLED
REMARK 4
REMARK 4 2BGR COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 17-JAN-2005.
REMARK 100 THE EBI ID CODE IS EBI-22256.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-2004
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE ID14-EH2
REMARK 200 BEAMLINE : ID 14-EH2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 4)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127470
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 4.3
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.80
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4
REMARK 200 R MERGE FOR SHELL (I) : 0.37
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1N1M
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
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 59.14950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.66600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.52150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.66600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.14950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.52150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 M 1 B 38 .. 766 A 38 .. 766 0.566
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: TETRAMERIC
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, Y, Z
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 ASN A 29
REMARK 465 LYS A 30
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 ASN B 29
REMARK 465 LYS B 30
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 VAL Y 4
REMARK 465 ASP Y 5
REMARK 465 PRO Y 6
REMARK 465 ASN Y 7
REMARK 465 ILE Y 8
REMARK 465 GLU Y 9
REMARK 465 VAL Z 4
REMARK 465 ASP Z 5
REMARK 465 PRO Z 6
REMARK 465 ASN Z 7
REMARK 465 ILE Z 8
REMARK 465 GLU Z 9
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 LEU A 366 CA - CB - CG ANGL. DEV. = -9.8 DEGREES
REMARK 500 LEU A 415 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 LEU A 415 CB - CG - CD1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG A 492 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 LEU B 60 CA - CB - CG ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU B 316 CA - CB - CG ANGL. DEV. = 9.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 DISTANCE
REMARK 500 SG CYS A 472 O HOH A 2617 2.01
REMARK 500 O LEU B 276 O HOH B 2348 2.19
REMARK 500 OH TYR B 439 O HOH B 2556 2.18
REMARK 500 SG CYS B 472 O HOH B 2579 2.14
REMARK 500 O HOH A 2005 O HOH A 2007 2.19
REMARK 500 O HOH A 2042 O HOH A 2054 2.15
REMARK 500 O HOH A 2094 O HOH A 2265 2.15
REMARK 500 O HOH B 2184 O HOH B 2500 2.10
REMARK 500 O HOH B 2393 O HOH B 2395 2.16
REMARK 500 O HOH B 2526 O HOH B 2589 2.17
REMARK 500 O HOH B 2613 O HOH B 2617 2.20
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 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 SER A 630 -118.22 66.14
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A A
REMARK 525 B B
REMARK 525 Y Y
REMARK 525 Z Z
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: AFL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: AFL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J2E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV
REMARK 900 RELATED ID: 1N1M RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN
REMARK 900 COMPLEX WITH ANINHIBITOR
REMARK 900 RELATED ID: 1NU6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPP-IV)
REMARK 900 RELATED ID: 1NU8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPP-IV)IN COMPLEX WITH
REMARK 900 DIPROTIN A (ILI)
REMARK 900 RELATED ID: 1PFQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL
REMARK 900 PEPTIDASE IV /CD26
REMARK 900 RELATED ID: 1R9M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV AT 2.1ANG. RESOLUTION.
REMARK 900 RELATED ID: 1RWQ RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH 5-AMINOMETHYL-6-(2,4-DICHLORO-PHENYL
REMARK 900 )-2-(3,5-DIMETHOXY-PHENYL)-PYRIMIDIN-4-
REMARK 900 YLAMINE
REMARK 900 RELATED ID: 1TK3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL
REMARK 900 PEPTIDASE IV/CD26
REMARK 900 RELATED ID: 1TKR RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 INHIBITED
REMARK 900 WITHDIISOPROPYL FLUOROPHOSPHATE
REMARK 900 RELATED ID: 1U8E RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 MUTANT
REMARK 900 Y547F
REMARK 900 RELATED ID: 1W1I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV
REMARK 900 (DPPIV OR CD26) IN COMPLEX WITH ADENOSINE
REMARK 900 DEAMINASE
REMARK 900 RELATED ID: 2BGN RELATED DB: PDB
REMARK 900 HIV-1 TAT PROTEIN DERIVED N-TERMINAL
REMARK 900 NONAPEPTIDE TRP2-TAT(1-9) BOUND TO THE
REMARK 900 ACTIVE SITE OF DIPEPTIDYL PEPTIDASE IV (CD26)
DBREF 2BGR A 29 766 UNP P27487 DPP4_HUMAN 29 766
DBREF 2BGR B 29 766 UNP P27487 DPP4_HUMAN 29 766
DBREF 2BGR Y 1 9 UNP P12506 TAT_HV1Z2 1 9
DBREF 2BGR Z 1 9 UNP P12506 TAT_HV1Z2 1 9
SEQRES 1 A 738 ASN LYS GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS
SEQRES 2 A 738 THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG
SEQRES 3 A 738 LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU
SEQRES 4 A 738 TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN
SEQRES 5 A 738 ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER
SEQRES 6 A 738 THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER
SEQRES 7 A 738 ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN
SEQRES 8 A 738 TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR
SEQRES 9 A 738 ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU
SEQRES 10 A 738 GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP SER
SEQRES 11 A 738 PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP
SEQRES 12 A 738 ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG
SEQRES 13 A 738 ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY
SEQRES 14 A 738 ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA
SEQRES 15 A 738 TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU
SEQRES 16 A 738 ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE
SEQRES 17 A 738 GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO
SEQRES 18 A 738 LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL
SEQRES 19 A 738 ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER
SEQRES 20 A 738 LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE THR
SEQRES 21 A 738 ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS
SEQRES 22 A 738 ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN
SEQRES 23 A 738 TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE
SEQRES 24 A 738 CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU
SEQRES 25 A 738 VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY TRP
SEQRES 26 A 738 VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU
SEQRES 27 A 738 ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU
SEQRES 28 A 738 GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS
SEQRES 29 A 738 ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE
SEQRES 30 A 738 GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE
SEQRES 31 A 738 SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU
SEQRES 32 A 738 TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS
SEQRES 33 A 738 LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR
SEQRES 34 A 738 SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU
SEQRES 35 A 738 ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS
SEQRES 36 A 738 SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP
SEQRES 37 A 738 ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET
SEQRES 38 A 738 PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU THR
SEQRES 39 A 738 LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP
SEQRES 40 A 738 LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA
SEQRES 41 A 738 GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU
SEQRES 42 A 738 ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE
SEQRES 43 A 738 VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY
SEQRES 44 A 738 ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR
SEQRES 45 A 738 PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE
SEQRES 46 A 738 SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE
SEQRES 47 A 738 TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET VAL
SEQRES 48 A 738 LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA
SEQRES 49 A 738 VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL
SEQRES 50 A 738 TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP
SEQRES 51 A 738 ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER ARG
SEQRES 52 A 738 ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS
SEQRES 53 A 738 GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA
SEQRES 54 A 738 GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE
SEQRES 55 A 738 GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA
SEQRES 56 A 738 SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET SER
SEQRES 57 A 738 HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 738 ASN LYS GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS
SEQRES 2 B 738 THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG
SEQRES 3 B 738 LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU
SEQRES 4 B 738 TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN
SEQRES 5 B 738 ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER
SEQRES 6 B 738 THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER
SEQRES 7 B 738 ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN
SEQRES 8 B 738 TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR
SEQRES 9 B 738 ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU
SEQRES 10 B 738 GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP SER
SEQRES 11 B 738 PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP
SEQRES 12 B 738 ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG
SEQRES 13 B 738 ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY
SEQRES 14 B 738 ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA
SEQRES 15 B 738 TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU
SEQRES 16 B 738 ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE
SEQRES 17 B 738 GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO
SEQRES 18 B 738 LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL
SEQRES 19 B 738 ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER
SEQRES 20 B 738 LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE THR
SEQRES 21 B 738 ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS
SEQRES 22 B 738 ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN
SEQRES 23 B 738 TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE
SEQRES 24 B 738 CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU
SEQRES 25 B 738 VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY TRP
SEQRES 26 B 738 VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU
SEQRES 27 B 738 ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU
SEQRES 28 B 738 GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS
SEQRES 29 B 738 ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE
SEQRES 30 B 738 GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE
SEQRES 31 B 738 SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU
SEQRES 32 B 738 TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS
SEQRES 33 B 738 LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR
SEQRES 34 B 738 SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU
SEQRES 35 B 738 ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS
SEQRES 36 B 738 SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP
SEQRES 37 B 738 ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET
SEQRES 38 B 738 PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU THR
SEQRES 39 B 738 LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP
SEQRES 40 B 738 LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA
SEQRES 41 B 738 GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU
SEQRES 42 B 738 ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE
SEQRES 43 B 738 VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY
SEQRES 44 B 738 ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR
SEQRES 45 B 738 PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE
SEQRES 46 B 738 SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE
SEQRES 47 B 738 TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET VAL
SEQRES 48 B 738 LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA
SEQRES 49 B 738 VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL
SEQRES 50 B 738 TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP
SEQRES 51 B 738 ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER ARG
SEQRES 52 B 738 ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS
SEQRES 53 B 738 GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA
SEQRES 54 B 738 GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE
SEQRES 55 B 738 GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA
SEQRES 56 B 738 SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET SER
SEQRES 57 B 738 HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 Y 9 MET ASP PRO VAL ASP PRO ASN ILE GLU
SEQRES 1 Z 9 MET ASP PRO VAL ASP PRO ASN ILE GLU
HET NAG A1767 14
HET AFL A1768 10
HET NAG A1769 14
HET NAG A1770 14
HET NAG A1771 14
HET NAG A1772 14
HET NAG A1773 14
HET NAG A1774 14
HET BMA A1775 11
HET NAG A1776 14
HET NAG A1777 14
HET NAG A1778 14
HET NAG A1779 14
HET NAG B1767 14
HET AFL B1768 10
HET NAG B1769 14
HET NAG B1770 14
HET NAG B1771 14
HET NAG B1772 14
HET NAG B1773 14
HET BMA B1774 11
HET NAG B1775 14
HET NAG B1776 14
HET NAG B1777 14
HET NAG B1778 14
HET NAG B1779 14
HET NAG A1780 14
HETNAM BMA BETA-D-MANNOSE
HETNAM AFL ALPHA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 6 AFL 2(C6 H12 O5)
FORMUL 7 NAG 23(C8 H15 N1 O6)
FORMUL 8 HOH *1750(H2 O1)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
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 VAL A 341 GLN A 344 5 4
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 GLN A 505 1 9
HELIX 8 8 ASN A 562 THR A 570 1 9
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
HELIX 11 11 THR A 600 SER A 614 1 15
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 ARG A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 GLY A 672 1 10
HELIX 15 15 ASN A 679 SER A 686 1 8
HELIX 16 16 VAL A 688 VAL A 698 5 11
HELIX 17 17 PHE A 713 VAL A 726 1 14
HELIX 18 18 SER A 744 PHE A 763 1 20
HELIX 19 19 THR B 44 ASN B 51 1 8
HELIX 20 20 ASP B 200 VAL B 207 1 8
HELIX 21 21 ASP B 274 LEU B 276 5 3
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 VAL B 341 GLN B 344 5 4
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 ASN B 497 GLN B 505 1 9
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 MET B 616 1 17
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 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 VAL B 726 1 15
HELIX 36 36 SER B 744 PHE B 763 1 20
SHEET 1 AA 2 LYS A 41 THR A 42 0
SHEET 2 AA 2 VAL A 507 GLN A 508 1 N GLN A 508 O LYS A 41
SHEET 1 AB 4 ARG A 61 TRP A 62 0
SHEET 2 AB 4 GLU A 67 LYS A 71 -1 O LEU A 69 N ARG A 61
SHEET 3 AB 4 ILE A 76 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 AB 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AC 4 ASP A 104 ILE A 107 0
SHEET 2 AC 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AC 4 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 4 AC 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AD 4 TRP A 154 TRP A 157 0
SHEET 2 AD 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 AD 4 ASP A 171 LYS A 175 -1 O ASP A 171 N TRP A 168
SHEET 4 AD 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AE 3 ILE A 194 ASN A 196 0
SHEET 2 AE 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AE 3 LEU A 214 TRP A 216 -1 O TRP A 215 N ALA A 224
SHEET 1 AF 4 ILE A 194 ASN A 196 0
SHEET 2 AF 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AF 4 THR A 265 ASN A 272 -1 O THR A 265 N ASN A 229
SHEET 4 AF 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 AG 2 LEU A 235 PHE A 240 0
SHEET 2 AG 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AH 4 HIS A 298 THR A 307 0
SHEET 2 AH 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AH 4 TYR A 322 ASP A 331 -1 O TYR A 322 N ARG A 317
SHEET 4 AH 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 AI 4 HIS A 298 THR A 307 0
SHEET 2 AI 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AI 4 TYR A 322 ASP A 331 -1 O TYR A 322 N ARG A 317
SHEET 4 AI 4 ARG A 336 CYS A 339 -1 O ARG A 336 N ASP A 331
SHEET 1 AJ 4 HIS A 363 PHE A 364 0
SHEET 2 AJ 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AJ 4 ARG A 382 GLN A 388 -1 O HIS A 383 N ILE A 375
SHEET 4 AJ 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AK 4 VAL A 404 LEU A 410 0
SHEET 2 AK 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 AK 4 ASN A 430 GLN A 435 -1 O ASN A 430 N SER A 419
SHEET 4 AK 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AL 4 TYR A 457 PHE A 461 0
SHEET 2 AL 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 AL 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AL 4 LYS A 489 GLU A 495 -1 O LYS A 489 N SER A 484
SHEET 1 AM 8 SER A 511 LEU A 519 0
SHEET 2 AM 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 AM 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AM 8 TYR A 540 ASP A 545 1 O PRO A 541 N ILE A 574
SHEET 5 AM 8 VAL A 619 TRP A 629 1 N ASP A 620 O TYR A 540
SHEET 6 AM 8 CYS A 649 VAL A 653 1 O CYS A 649 N ILE A 626
SHEET 7 AM 8 GLU A 699 GLY A 705 1 O GLU A 699 N GLY A 650
SHEET 8 AM 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 BA 2 LYS B 41 THR B 42 0
SHEET 2 BA 2 VAL B 507 GLN B 508 1 N GLN B 508 O LYS B 41
SHEET 1 BB 4 ARG B 61 TRP B 62 0
SHEET 2 BB 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 BB 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 BB 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 BC 4 ILE B 102 ILE B 107 0
SHEET 2 BC 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 BC 4 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 4 BC 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 BD 4 TRP B 154 TRP B 157 0
SHEET 2 BD 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 BD 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 BD 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 BE 3 ILE B 194 ASN B 196 0
SHEET 2 BE 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BE 3 LEU B 214 TRP B 216 -1 O TRP B 215 N ALA B 224
SHEET 1 BF 4 ILE B 194 ASN B 196 0
SHEET 2 BF 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BF 4 THR B 265 ASN B 272 -1 O THR B 265 N ASN B 229
SHEET 4 BF 4 SER B 284 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 BG 2 LEU B 235 PHE B 240 0
SHEET 2 BG 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 BH 7 HIS B 298 THR B 307 0
SHEET 2 BH 7 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 BH 7 TYR B 322 ASP B 331 -1 O TYR B 322 N ARG B 317
SHEET 4 BH 7 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 5 BH 7 TYR B 322 ASP B 331 -1 O ASP B 329 N ASN B 338
SHEET 6 BH 7 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 7 BH 7 TYR B 322 ASP B 331 -1 O SER B 323 N GLU B 347
SHEET 1 BI 4 HIS B 363 PHE B 364 0
SHEET 2 BI 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 BI 4 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 BI 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 BJ 4 VAL B 404 LEU B 410 0
SHEET 2 BJ 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 BJ 4 ASN B 430 GLN B 435 -1 O ASN B 430 N SER B 419
SHEET 4 BJ 4 ASP B 438 CYS B 444 -1 N ASP B 438 O GLN B 435
SHEET 1 BK 4 TYR B 457 PHE B 461 0
SHEET 2 BK 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 BK 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 BK 4 LYS B 489 GLU B 495 -1 O LYS B 489 N SER B 484
SHEET 1 BL 8 SER B 511 LEU B 519 0
SHEET 2 BL 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 BL 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 BL 8 TYR B 540 VAL B 546 1 O PRO B 541 N ILE B 574
SHEET 5 BL 8 VAL B 619 TRP B 629 1 N ASP B 620 O TYR B 540
SHEET 6 BL 8 CYS B 649 VAL B 653 1 O CYS B 649 N ILE B 626
SHEET 7 BL 8 GLU B 699 GLY B 705 1 O GLU B 699 N GLY B 650
SHEET 8 BL 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
SSBOND 1 CYS A 328 CYS A 339 1555 1555
SSBOND 2 CYS A 385 CYS A 394 1555 1555
SSBOND 3 CYS A 444 CYS A 447 1555 1555
SSBOND 4 CYS A 454 CYS A 472 1555 1555
SSBOND 5 CYS A 649 CYS A 762 1555 1555
SSBOND 6 CYS B 328 CYS B 339 1555 1555
SSBOND 7 CYS B 385 CYS B 394 1555 1555
SSBOND 8 CYS B 444 CYS B 447 1555 1555
SSBOND 9 CYS B 454 CYS B 472 1555 1555
SSBOND 10 CYS B 649 CYS B 762 1555 1555
LINK ND2 ASN A 85 C1 NAG A1767 1555 1555
LINK ND2 ASN A 92 C1 NAG A1780 1555 1555
LINK ND2 ASN A 150 C1 NAG A1770 1555 1555
LINK ND2 ASN A 219 C1 NAG A1771 1555 1555
LINK ND2 ASN A 229 C1 NAG A1773 1555 1555
LINK ND2 ASN A 281 C1 NAG A1776 1555 1555
LINK ND2 ASN A 321 C1 NAG A1778 1555 1555
LINK O4 NAG A1767 C1 NAG A1769 1555 1555
LINK O6 NAG A1767 C1 AFL A1768 1555 1555
LINK O4 NAG A1771 C1 NAG A1772 1555 1555
LINK O4 NAG A1773 C1 NAG A1774 1555 1555
LINK O4 NAG A1774 C1 BMA A1775 1555 1555
LINK O4 NAG A1776 C1 NAG A1777 1555 1555
LINK O4 NAG A1778 C1 NAG A1779 1555 1555
LINK ND2 ASN B 85 C1 NAG B1767 1555 1555
LINK ND2 ASN B 92 C1 NAG B1779 1555 1555
LINK ND2 ASN B 150 C1 NAG B1769 1555 1555
LINK ND2 ASN B 219 C1 NAG B1770 1555 1555
LINK ND2 ASN B 229 C1 NAG B1772 1555 1555
LINK ND2 ASN B 281 C1 NAG B1775 1555 1555
LINK ND2 ASN B 321 C1 NAG B1777 1555 1555
LINK O6 NAG B1767 C1 AFL B1768 1555 1555
LINK O4 NAG B1770 C1 NAG B1771 1555 1555
LINK O4 NAG B1772 C1 NAG B1773 1555 1555
LINK O4 NAG B1773 C1 BMA B1774 1555 1555
LINK O4 NAG B1775 C1 NAG B1776 1555 1555
LINK O4 NAG B1777 C1 NAG B1778 1555 1555
CISPEP 1 GLY A 474 PRO A 475 0 18.13
CISPEP 2 GLY B 474 PRO B 475 0 19.24
SITE 1 AC1 5 GLU A 67 ASN A 85 SER A 86 SER A 87
SITE 2 AC1 5 HOH A2052
SITE 1 AC2 2 TYR A 83 ASN B 179
SITE 1 AC4 4 ILE A 148 ASN A 150 HOH A2172 HOH A2874
SITE 1 AC5 5 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 2 AC5 5 HOH A2876
SITE 1 AC6 3 PHE A 222 TYR A 330 GLU A 332
SITE 1 AC7 5 ASN A 229 THR A 231 GLU A 232 HOH A2360
SITE 2 AC7 5 HOH A2879
SITE 1 BC1 5 TRP A 187 ASN A 281 HOH A2880 HOH A2881
SITE 2 BC1 5 HOH A2882
SITE 1 BC2 1 HOH A2883
SITE 1 BC3 5 ASN A 321 SER A 349 THR A 350 HOH A2884
SITE 2 BC3 5 HOH A2885
SITE 1 BC4 2 ASP A 678 HOH A2886
SITE 1 BC5 7 ASN B 85 SER B 86 SER B 87 HOH B2037
SITE 2 BC5 7 HOH B2833 HOH B2834 HOH B2835
SITE 1 BC6 2 TYR B 83 HOH B2835
SITE 1 BC7 5 ARG B 147 ILE B 148 ASN B 150 HOH B2836
SITE 2 BC7 5 HOH B2837
SITE 1 BC8 7 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC8 7 HOH B2261 HOH B2838 HOH B2839
SITE 1 BC9 5 PHE B 222 ASN B 272 TYR B 330 HOH B2344
SITE 2 BC9 5 HOH B2413
SITE 1 CC1 8 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 CC1 8 HOH B2336 HOH B2840 HOH B2841 HOH B2843
SITE 1 CC2 1 HOH B2843
SITE 1 CC3 2 SER B 39 HOH B2844
SITE 1 CC4 8 HOH A2587 HOH A2594 TRP B 187 ASN B 281
SITE 2 CC4 8 HOH B2845 HOH B2846 HOH B2847 HOH B2848
SITE 1 CC5 6 THR B 188 HOH B2848 HOH B2849 HOH B2850
SITE 2 CC5 6 HOH B2851 HOH B2852
SITE 1 CC6 3 ASN B 321 SER B 349 THR B 350
SITE 1 CC7 3 ARG B 596 ASP B 678 HOH B2853
SITE 1 CC8 5 GLU B 73 ASN B 74 ASN B 75 ASN B 92
SITE 2 CC8 5 HOH B2854
SITE 1 CC9 4 GLU A 73 ASN A 74 ASN A 75 ASN A 92
CRYST1 118.299 127.043 137.332 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 0.008453 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007871 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007282 0.00000
MTRIX1 1 -0.946000 0.152000 -0.287000 35.34585 1
MTRIX2 1 0.185000 -0.473000 -0.861000 112.96806 1
MTRIX3 1 -0.266000 -0.868000 0.420000 75.64200 1
TER 5973 PRO A 766
TER 11946 PRO B 766
TER 11970 PRO Y 3
TER 11994 PRO Z 3
MASTER 509 0 27 36 101 0 37 914100 4 398 116
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