| content |
HEADER HYDROLASE/INHIBITOR 11-MAY-10 2XE4
TITLE STRUCTURE OF OLIGOPEPTIDASE B FROM LEISHMANIA MAJOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLIGOPEPTIDASE B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FAMILY S9A-LIKE PROTEIN, SERINE PEPTIDASE;
COMPND 5 EC: 3.4.21.83;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ANTIPAIN;
COMPND 10 CHAIN: B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MAJOR;
SOURCE 3 ORGANISM_TAXID: 5664;
SOURCE 4 STRAIN: FRIEDLIN;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)(PLYS);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28A;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBP218;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ACTINOBACTERIA;
SOURCE 12 ORGANISM_TAXID: 1760
KEYWDS HYDROLASE-INHIBITOR COMPLEX, HYDROLASE, PROTEASE INHIBITOR
KEYWDS 2 TRYPANOSOMES, CLAN SC
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MCLUSKEY,N.G.PATERSON,N.D.BLAND,J.C.MOTTRAM,N.W.ISAACS
REVDAT 1 06-OCT-10 2XE4 0
JRNL AUTH K.MCLUSKEY,N.G.PATERSON,N.D.BLAND,J.C.MOTTRAM,N.W.ISAACS
JRNL TITL THE CRYSTAL STRUCTURE OF LEISHMANIA MAJOR OLIGOPEPTIDASE B
JRNL TITL 2 GIVES INSIGHT INTO THE ENZYMATIC PROPERTIES OF A
JRNL TITL 3 TRYPANOSOMATID VIRULENCE FACTOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.650
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 117.851
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.007
REMARK 3 NUMBER OF REFLECTIONS : 167169
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) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.1403
REMARK 3 FREE R VALUE : 0.1780
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.08
REMARK 3 FREE R VALUE TEST SET COUNT : 8321
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.693
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11787
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.914
REMARK 3 BIN R VALUE (WORKING SET) : 0.293
REMARK 3 BIN FREE R VALUE SET COUNT : 605
REMARK 3 BIN FREE R VALUE : 0.342
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6168
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 326
REMARK 3 SOLVENT ATOMS : 721
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.338
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.673
REMARK 3 B22 (A**2) : -1.710
REMARK 3 B33 (A**2) : -0.963
REMARK 3 B12 (A**2) : 0.000
REMARK 3 B13 (A**2) : 0.000
REMARK 3 B23 (A**2) : 0.000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.064
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.558
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6627 ; 0.035 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8977 ; 2.353 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 819 ; 6.661 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 305 ;33.738 ;23.738
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1084 ;12.490 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;15.532 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 975 ; 0.209 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5027 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3318 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4107 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 704 ; 0.161 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.065 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 91 ; 0.227 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.215 ; 0.200
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): 3852 ; 2.833 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6311 ; 4.118 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2775 ; 6.794 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2648 ; 9.512 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 6627 ; 3.903 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.400
REMARK 3 ION PROBE RADIUS : 0.800
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. RESIDUES 1-9 AND 731 ARE DISORDERED.
REMARK 4
REMARK 4 2XE4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-10.
REMARK 100 THE PDBE ID CODE IS EBI-43877.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N ; Y
REMARK 200 RADIATION SOURCE : ROTATING ANODE ; ESRF
REMARK 200 BEAMLINE : NULL ; BM14
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX 007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M ; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541 ; 1.005
REMARK 200 MONOCHROMATOR : GRAPHITE ; NULL
REMARK 200 OPTICS : MIRRORS ; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE ; CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH ; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DTREK
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 167772
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.65
REMARK 200 RESOLUTION RANGE LOW (A) : 32.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.3
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.0
REMARK 200 R MERGE FOR SHELL (I) : 0.46
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSHARP, SHELXC, SHELXD
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS DIALYZED INTO 50 MM
REMARK 280 TRIS, PH 8.0 AND INCUBATED WITH 10 MM ANTIPAIN FOR 30
REMARK 280 MINS. THIS WAS MIXED IN A 1:1 RATIO WITH 25% 1,2
REMARK 280 PROPANEDIOL, 10% GLYCEROL, 5 % PEG300 AND 0.1 M PHOSPHATE
REMARK 280 CITRATE, PH 4.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 47.73900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.38800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 104.45950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 47.73900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.38800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 104.45950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.73900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.38800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 104.45950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 47.73900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 71.38800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 104.45950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PHE 25 TO LEU
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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 ASP A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 VAL A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 ARG A 731
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 O2 PGR A 1784 O HOH A 2712 2.09
REMARK 500 O HOH A 2219 O HOH A 2654 2.10
REMARK 500 O HOH A 2110 O HOH A 2643 2.13
REMARK 500 O HOH A 2123 O HOH A 2128 2.19
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),1X,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 TYR A 71 CG TYR A 71 CD1 0.082
REMARK 500 TYR A 110 CE1 TYR A 110 CZ 0.106
REMARK 500 GLU A 205 CD GLU A 205 OE2 -0.072
REMARK 500 TYR A 217 CG TYR A 217 CD1 0.089
REMARK 500 ARG A 332 CZ ARG A 332 NH2 0.086
REMARK 500 TRP A 338 CG TRP A 338 CD1 0.099
REMARK 500 SER A 346 CB SER A 346 OG -0.083
REMARK 500 PHE A 350 CG PHE A 350 CD1 0.094
REMARK 500 GLU A 352 CB GLU A 352 CG -0.169
REMARK 500 GLU A 352 CG GLU A 352 CD 0.156
REMARK 500 ALA A 368 CA ALA A 368 CB 0.139
REMARK 500 TYR A 494 CZ TYR A 494 CE2 0.092
REMARK 500 TYR A 499 CE1 TYR A 499 CZ 0.081
REMARK 500 TYR A 514 CG TYR A 514 CD1 0.079
REMARK 500 TYR A 514 CZ TYR A 514 CE2 0.108
REMARK 500 TRP A 536 CZ3 TRP A 536 CH2 0.106
REMARK 500 TYR A 537 CG TYR A 537 CD1 0.089
REMARK 500 TYR A 537 CZ TYR A 537 CE2 0.087
REMARK 500 GLU A 538 CB GLU A 538 CG -0.156
REMARK 500 PHE A 553 CE1 PHE A 553 CZ 0.121
REMARK 500 GLU A 624 CG GLU A 624 CD 0.102
REMARK 500 GLU A 624 CD GLU A 624 OE1 0.071
REMARK 500 GLU A 624 CD GLU A 624 OE2 0.073
REMARK 500 TRP A 625 CG TRP A 625 CD1 0.089
REMARK 500 TRP A 625 CZ3 TRP A 625 CH2 0.106
REMARK 500 TYR A 633 CZ TYR A 633 CE2 0.088
REMARK 500 TYR A 667 CG TYR A 667 CD1 0.092
REMARK 500 TYR A 667 CZ TYR A 667 CE2 0.085
REMARK 500 TRP A 673 CE3 TRP A 673 CZ3 0.106
REMARK 500 PHE A 698 CZ PHE A 698 CE2 0.142
REMARK 500 PHE A 706 CE1 PHE A 706 CZ 0.117
REMARK 500 TRP A 707 CE3 TRP A 707 CZ3 0.104
REMARK 500 ARG B 2 CD ARG B 2 NE 0.135
REMARK 500 ARG B 2 NE ARG B 2 CZ 0.116
REMARK 500 ARG B 2 CZ ARG B 2 NH1 0.188
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 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 129 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 211 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 281 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 283 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 295 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 295 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 344 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 344 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 462 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 527 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 576 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 590 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ILE A 712 CG1 - CB - CG2 ANGL. DEV. = -15.5 DEGREES
REMARK 500 ARG A 726 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 726 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 2 CD - NE - CZ ANGL. DEV. = 27.3 DEGREES
REMARK 500 ARG B 2 NE - CZ - NH1 ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG B 2 NE - CZ - NH2 ANGL. DEV. = -17.0 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 ASN A 36 61.45 -152.15
REMARK 500 VAL A 294 -70.39 -81.65
REMARK 500 HIS A 325 153.19 88.92
REMARK 500 VAL A 406 74.08 -104.24
REMARK 500 TYR A 496 -81.43 -131.34
REMARK 500 TYR A 537 -61.39 -97.11
REMARK 500 ALA A 541 84.63 -163.91
REMARK 500 TYR A 543 -123.68 43.68
REMARK 500 SER A 577 -116.99 61.97
REMARK 500 VAL A 601 57.47 32.62
REMARK 500 ASP A 605 59.11 -94.31
REMARK 500 LEU A 617 -19.76 82.90
REMARK 500 GLU A 624 -69.84 -108.48
REMARK 500 SER A 699 -157.10 57.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 CHLORINE ION (CL): NA
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 NA A1795 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 94 O
REMARK 620 2 ILE A 91 O 77.9
REMARK 620 3 HOH A2132 O 86.8 107.8
REMARK 620 4 HOH A2138 O 85.8 155.6 89.0
REMARK 620 5 HOH A2131 O 170.3 99.9 102.8 93.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1797 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 174 OD1
REMARK 620 2 ASN A 178 OD1 91.9
REMARK 620 3 VAL A 180 O 90.9 90.9
REMARK 620 4 SER A 176 OG 73.5 68.7 153.3
REMARK 620 5 HOH A2226 O 150.3 113.6 74.5 128.7
REMARK 620 6 HOH A2216 O 92.5 169.6 98.4 103.6 65.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1732
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1733
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1734
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1735
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1736
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1737
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1738
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1739
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1740
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1741
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1742
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A1743
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1744
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1745
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1746
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1747
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1748
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1749
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1750
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1751
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1752
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1753
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1754
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1755
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1756
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1757
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1758
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1759
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1760
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1761
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1762
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1763
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1764
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1765
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1766
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1767
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1768
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1769
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1770
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1771
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1772
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1773
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1774
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1775
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1776
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1777
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1778
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1779
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1780
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1781
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1782
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1783
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1784
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1785
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1786
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1787
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1788
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1789
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A1790
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1791
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1793
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1794
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1795
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1796
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1797
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1798
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1799
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF
REMARK 800 RESIDUES 1 TO 4
DBREF 2XE4 A 1 731 UNP Q4QHU7 Q4QHU7_LEIMA 1 731
DBREF 2XE4 B 1 4 NORINE NOR00664 NOR00664 1 4
SEQADV 2XE4 MET A -19 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 GLY A -18 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 SER A -17 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 SER A -16 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 HIS A -15 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 HIS A -14 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 HIS A -13 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 HIS A -12 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 HIS A -11 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 HIS A -10 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 SER A -9 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 SER A -8 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 GLY A -7 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 LEU A -6 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 VAL A -5 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 PRO A -4 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 ARG A -3 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 GLY A -2 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 SER A -1 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 HIS A 0 UNP Q4QHU7 EXPRESSION TAG
SEQADV 2XE4 LEU A 25 UNP Q4QHU7 PHE 25 ENGINEERED MUTATION
SEQRES 1 A 751 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 751 LEU VAL PRO ARG GLY SER HIS MET SER SER ASP SER SER
SEQRES 3 A 751 VAL ALA ALA SER ALA GLN PRO PRO ILE ALA ALA LYS LYS
SEQRES 4 A 751 PRO HIS ARG VAL THR LEU GLY TYR VAL GLU GLY GLU ASP
SEQRES 5 A 751 ARG GLY PRO ASN PRO MET ASN PRO PRO ARG TYR ARG GLU
SEQRES 6 A 751 ASP PRO TYR PHE TRP MET ARG ASP ASP ASP ARG LYS ASP
SEQRES 7 A 751 PRO ALA VAL ILE GLU HIS LEU ASN LYS GLU LYS VAL TYR
SEQRES 8 A 751 PHE GLN ALA ARG SER ALA ASP ILE ALA GLN LEU ARG ASP
SEQRES 9 A 751 ASP ILE TYR ALA GLU HIS ILE SER HIS ILE ASN GLU ASP
SEQRES 10 A 751 ASP MET SER ALA PRO TYR VAL TYR GLY LYS TYR ARG TYR
SEQRES 11 A 751 TYR THR ARG GLU VAL LYS GLY LYS PRO TYR LYS ILE TYR
SEQRES 12 A 751 CYS ARG VAL PHE THR ASP LYS GLU PRO GLY ASP VAL ALA
SEQRES 13 A 751 ALA GLU GLU VAL ILE ILE ASP VAL ASN GLN VAL ALA GLU
SEQRES 14 A 751 GLY LYS ALA PHE CYS ASP VAL MET GLU VAL LYS PRO ALA
SEQRES 15 A 751 PRO PRO GLU HIS ASP LEU VAL ALA PHE SER VAL ASP MET
SEQRES 16 A 751 SER GLY ASN GLU VAL TYR THR ILE GLU PHE LYS ARG ILE
SEQRES 17 A 751 SER ASP PRO SER GLN THR ILE ALA ASP LYS VAL SER GLY
SEQRES 18 A 751 THR ASN GLY GLU ILE VAL TRP GLY PRO ASP HIS THR SER
SEQRES 19 A 751 LEU PHE TYR VAL THR LYS ASP GLU THR LEU ARG GLU ASN
SEQRES 20 A 751 LYS VAL TRP ARG HIS VAL MET GLY LYS LEU GLN SER GLU
SEQRES 21 A 751 ASP VAL CYS LEU TYR GLU GLU HIS ASN PRO LEU PHE SER
SEQRES 22 A 751 ALA PHE MET TYR LYS ALA ALA ASP THR ASN THR LEU CYS
SEQRES 23 A 751 ILE GLY SER GLN SER PRO GLU THR ALA GLU VAL HIS LEU
SEQRES 24 A 751 LEU ASP LEU ARG LYS GLY ASN ALA HIS ASN THR LEU GLU
SEQRES 25 A 751 ILE VAL ARG PRO ARG GLU LYS GLY VAL ARG TYR ASP VAL
SEQRES 26 A 751 GLN MET HIS GLY THR SER HIS LEU VAL ILE LEU THR ASN
SEQRES 27 A 751 GLU GLY GLY ALA VAL ASN HIS LYS LEU LEU ILE ALA PRO
SEQRES 28 A 751 ARG GLY GLN PRO SER ASP TRP SER HIS VAL LEU VAL ASP
SEQRES 29 A 751 HIS SER GLU ASP VAL PHE MET GLU SER ILE ALA VAL ARG
SEQRES 30 A 751 SER ASN TYR LEU VAL VAL ALA GLY ARG ARG ALA GLY LEU
SEQRES 31 A 751 THR ARG ILE TRP THR MET MET ALA ASP SER GLN ASP GLY
SEQRES 32 A 751 VAL PHE LYS ALA GLY THR GLY LEU ARG GLU VAL VAL MET
SEQRES 33 A 751 GLU GLU PRO ILE PHE THR VAL HIS LEU VAL GLU SER GLN
SEQRES 34 A 751 MET LEU GLU TYR GLU GLU PRO THR PHE ARG MET GLU TYR
SEQRES 35 A 751 SER SER LEU ALA THR PRO ASN THR TRP PHE ASP VAL SER
SEQRES 36 A 751 PRO GLN ASP HIS SER ARG THR ALA VAL LYS VAL ARG GLU
SEQRES 37 A 751 VAL GLY GLY GLY PHE ASP ALA ALA ASN TYR LYS VAL GLU
SEQRES 38 A 751 ARG ARG PHE ALA THR ALA PRO ASP GLN THR LYS ILE PRO
SEQRES 39 A 751 LEU SER VAL VAL TYR HIS LYS ASP LEU ASP MET SER GLN
SEQRES 40 A 751 PRO GLN PRO CYS MET LEU TYR GLY TYR GLY SER TYR GLY
SEQRES 41 A 751 LEU SER MET ASP PRO GLN PHE SER ILE GLN HIS LEU PRO
SEQRES 42 A 751 TYR CYS ASP ARG GLY MET ILE PHE ALA ILE ALA HIS ILE
SEQRES 43 A 751 ARG GLY GLY SER GLU LEU GLY ARG ALA TRP TYR GLU ILE
SEQRES 44 A 751 GLY ALA LYS TYR LEU THR LYS ARG ASN THR PHE SER ASP
SEQRES 45 A 751 PHE ILE ALA ALA ALA GLU PHE LEU VAL ASN ALA LYS LEU
SEQRES 46 A 751 THR THR PRO SER GLN LEU ALA CYS GLU GLY ARG SER ALA
SEQRES 47 A 751 GLY GLY LEU LEU MET GLY ALA VAL LEU ASN MET ARG PRO
SEQRES 48 A 751 ASP LEU PHE LYS VAL ALA LEU ALA GLY VAL PRO PHE VAL
SEQRES 49 A 751 ASP VAL MET THR THR MET CYS ASP PRO SER ILE PRO LEU
SEQRES 50 A 751 THR THR GLY GLU TRP GLU GLU TRP GLY ASN PRO ASN GLU
SEQRES 51 A 751 TYR LYS TYR TYR ASP TYR MET LEU SER TYR SER PRO MET
SEQRES 52 A 751 ASP ASN VAL ARG ALA GLN GLU TYR PRO ASN ILE MET VAL
SEQRES 53 A 751 GLN CYS GLY LEU HIS ASP PRO ARG VAL ALA TYR TRP GLU
SEQRES 54 A 751 PRO ALA LYS TRP VAL SER LYS LEU ARG GLU CYS LYS THR
SEQRES 55 A 751 ASP ASN ASN GLU ILE LEU LEU ASN ILE ASP MET GLU SER
SEQRES 56 A 751 GLY HIS PHE SER ALA LYS ASP ARG TYR LYS PHE TRP LYS
SEQRES 57 A 751 GLU SER ALA ILE GLN GLN ALA PHE VAL CYS LYS HIS LEU
SEQRES 58 A 751 LYS SER THR VAL ARG LEU LEU VAL ARG ARG
SEQRES 1 B 4 FC0 ARG VAL RGL
HET FC0 B 1 14
HET RGL B 4 11
HET GOL A1732 6
HET GOL A1733 6
HET GOL A1734 6
HET GOL A1735 6
HET GOL A1736 6
HET GOL A1737 6
HET GOL A1738 6
HET GOL A1739 6
HET GOL A1740 6
HET GOL A1741 6
HET PGR A1742 5
HET PGO A1743 5
HET PGR A1744 5
HET PGR A1745 5
HET PGR A1746 5
HET PGR A1747 5
HET PGR A1748 5
HET PGR A1749 5
HET PGR A1750 5
HET PGR A1751 5
HET PGR A1752 5
HET PGR A1753 5
HET PGR A1754 5
HET PGR A1755 5
HET PGR A1756 5
HET PGR A1757 5
HET PGR A1758 5
HET PGR A1759 5
HET PGR A1760 5
HET PGR A1761 5
HET PGR A1762 5
HET PGR A1763 5
HET PGR A1764 5
HET PGR A1765 5
HET PGR A1766 5
HET PGR A1767 5
HET PGR A1768 5
HET PGR A1769 5
HET PGR A1770 5
HET PGR A1771 5
HET PGR A1772 5
HET PGR A1773 5
HET PGR A1774 5
HET PGR A1775 5
HET PGR A1776 5
HET PGR A1777 5
HET PGR A1778 5
HET PGR A1779 5
HET PGR A1780 5
HET PGR A1781 5
HET PGR A1782 5
HET PGR A1783 5
HET PGR A1784 5
HET PGR A1785 5
HET PGR A1786 5
HET PGR A1787 5
HET PGR A1788 5
HET PGR A1789 5
HET PGR A1790 5
HET PO4 A1791 5
HET PO4 A1792 5
HET PO4 A1793 5
HET CL A1794 1
HET NA A1795 1
HET CL A1796 1
HET NA A1797 1
HET CL A1798 1
HET CL A1799 1
HETNAM RGL ARGINAL
HETNAM FC0 N-CARBOXY-L-PHENYLALANINE
HETNAM PO4 PHOSPHATE ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM PGR R-1,2-PROPANEDIOL
HETNAM PGO S-1,2-PROPANEDIOL
HETNAM GOL GLYCEROL
FORMUL 2 FC0 C10 H11 N O4
FORMUL 3 RGL C6 H14 N4 O
FORMUL 4 PO4 3(O4 P 3-)
FORMUL 5 NA 2(NA 1+)
FORMUL 6 CL 4(CL 1-)
FORMUL 7 PGR 48(C3 H8 O2)
FORMUL 8 PGO C3 H8 O2
FORMUL 9 GOL 10(C3 H8 O3)
FORMUL 10 HOH *721(H2 O)
HELIX 1 1 TYR A 48 ARG A 52 5 5
HELIX 2 2 ASP A 58 ALA A 77 1 20
HELIX 3 3 ILE A 79 HIS A 93 1 15
HELIX 4 4 VAL A 144 ALA A 148 1 5
HELIX 5 5 LEU A 237 ASP A 241 5 5
HELIX 6 6 GLU A 407 MET A 410 5 4
HELIX 7 7 ASP A 454 ALA A 456 5 3
HELIX 8 8 SER A 508 GLN A 510 5 3
HELIX 9 9 HIS A 511 ASP A 516 1 6
HELIX 10 10 ARG A 534 ILE A 539 1 6
HELIX 11 11 LYS A 542 LYS A 546 5 5
HELIX 12 12 ARG A 547 ALA A 563 1 17
HELIX 13 13 THR A 567 SER A 569 5 3
HELIX 14 14 SER A 577 ARG A 590 1 14
HELIX 15 15 PRO A 591 PHE A 594 5 4
HELIX 16 16 ASP A 605 CYS A 611 1 7
HELIX 17 17 LEU A 617 TRP A 622 1 6
HELIX 18 18 GLU A 630 SER A 641 1 12
HELIX 19 19 PRO A 642 VAL A 646 5 5
HELIX 20 20 TYR A 667 LYS A 681 1 15
HELIX 21 21 ASP A 702 LEU A 721 1 20
HELIX 22 22 ARG A 726 ARG A 730 5 5
SHEET 1 AA 2 ARG A 22 LEU A 25 0
SHEET 2 AA 2 ARG A 42 GLU A 45 -1 O ARG A 42 N LEU A 25
SHEET 1 AB 2 ASP A 98 MET A 99 0
SHEET 2 AB 2 TYR A 108 GLU A 114 -1 O GLU A 114 N ASP A 98
SHEET 1 AC 2 TYR A 103 TYR A 105 0
SHEET 2 AC 2 TYR A 108 GLU A 114 -1 O TYR A 108 N TYR A 105
SHEET 1 AD 4 GLU A 139 ASP A 143 0
SHEET 2 AD 4 ILE A 122 PHE A 127 -1 O TYR A 123 N ILE A 141
SHEET 3 AD 4 TYR A 108 GLU A 114 -1 O ARG A 109 N VAL A 126
SHEET 4 AD 4 TYR A 103 TYR A 105 -1 O TYR A 103 N TYR A 110
SHEET 1 AE 4 GLU A 139 ASP A 143 0
SHEET 2 AE 4 ILE A 122 PHE A 127 -1 O TYR A 123 N ILE A 141
SHEET 3 AE 4 TYR A 108 GLU A 114 -1 O ARG A 109 N VAL A 126
SHEET 4 AE 4 ASP A 98 MET A 99 -1 O ASP A 98 N GLU A 114
SHEET 1 AF 4 ASP A 155 PRO A 161 0
SHEET 2 AF 4 LEU A 168 ASP A 174 -1 O ALA A 170 N LYS A 160
SHEET 3 AF 4 TYR A 181 ARG A 187 -1 O THR A 182 N VAL A 173
SHEET 4 AF 4 VAL A 199 THR A 202 -1 O VAL A 199 N ILE A 183
SHEET 1 AG 4 VAL A 207 TRP A 208 0
SHEET 2 AG 4 SER A 214 LYS A 220 -1 O PHE A 216 N VAL A 207
SHEET 3 AG 4 GLU A 226 VAL A 233 -1 N ASN A 227 O THR A 219
SHEET 4 AG 4 VAL A 242 GLU A 246 -1 O VAL A 242 N ARG A 231
SHEET 1 AH 4 SER A 253 LYS A 258 0
SHEET 2 AH 4 THR A 264 GLN A 270 -1 O CYS A 266 N TYR A 257
SHEET 3 AH 4 ALA A 275 ASP A 281 -1 O GLU A 276 N SER A 269
SHEET 4 AH 4 GLU A 292 ILE A 293 -1 O GLU A 292 N LEU A 279
SHEET 1 AI 4 TYR A 303 HIS A 308 0
SHEET 2 AI 4 HIS A 312 THR A 317 -1 O HIS A 312 N HIS A 308
SHEET 3 AI 4 LYS A 326 PRO A 331 -1 O LYS A 326 N THR A 317
SHEET 4 AI 4 VAL A 341 VAL A 343 -1 N LEU A 342 O LEU A 327
SHEET 1 AJ 4 VAL A 349 VAL A 356 0
SHEET 2 AJ 4 TYR A 360 ARG A 367 -1 O VAL A 362 N ALA A 355
SHEET 3 AJ 4 LEU A 370 MET A 377 -1 O LEU A 370 N ARG A 367
SHEET 4 AJ 4 ARG A 392 GLU A 393 -1 O ARG A 392 N THR A 375
SHEET 1 AK 4 THR A 402 LEU A 405 0
SHEET 2 AK 4 PHE A 418 SER A 424 -1 O GLU A 421 N HIS A 404
SHEET 3 AK 4 THR A 427 VAL A 434 -1 O THR A 427 N SER A 424
SHEET 4 AK 4 ARG A 441 VAL A 446 -1 O THR A 442 N ASP A 433
SHEET 1 AL 8 TYR A 458 THR A 466 0
SHEET 2 AL 8 LYS A 472 HIS A 480 -1 O ILE A 473 N ALA A 465
SHEET 3 AL 8 ILE A 520 ALA A 524 -1 O PHE A 521 N VAL A 478
SHEET 4 AL 8 CYS A 491 TYR A 494 1 O MET A 492 N ALA A 522
SHEET 5 AL 8 LEU A 571 ARG A 576 1 O ALA A 572 N LEU A 493
SHEET 6 AL 8 VAL A 596 GLY A 600 1 O VAL A 596 N CYS A 573
SHEET 7 AL 8 ASN A 653 GLY A 659 1 O ASN A 653 N ALA A 597
SHEET 8 AL 8 ILE A 687 ASP A 692 1 O LEU A 688 N VAL A 656
LINK NA NA A1795 O ILE A 94 1555 1555 2.50
LINK NA NA A1795 O ILE A 91 1555 1555 2.43
LINK NA NA A1795 O HOH A2132 1555 1555 2.50
LINK NA NA A1795 O HOH A2138 1555 1555 2.55
LINK NA NA A1795 O HOH A2131 1555 1555 2.35
LINK NA NA A1797 OG SER A 176 1555 1555 3.08
LINK NA NA A1797 O VAL A 180 1555 1555 2.59
LINK NA NA A1797 OD1 ASN A 178 1555 1555 2.57
LINK NA NA A1797 OD1 ASP A 174 1555 1555 2.46
LINK NA NA A1797 O HOH A2216 1555 1555 2.65
LINK NA NA A1797 O HOH A2226 1555 1555 2.99
LINK C1 FC0 B 1 N ARG B 2 1555 1555 1.38
LINK C VAL B 3 N RGL B 4 1555 1555 1.34
LINK C RGL B 4 OG SER A 577 1555 1555 1.51
CISPEP 1 ASN A 39 PRO A 40 0 3.63
CISPEP 2 PRO A 163 PRO A 164 0 2.57
SITE 1 AC1 9 PRO A 591 ASP A 592 PHE A 594 GLU A 650
SITE 2 AC1 9 TYR A 651 PRO A 652 PGR A1766 HOH A2610
SITE 3 AC1 9 HOH A2710
SITE 1 AC2 6 HIS A 340 VAL A 341 PHE A 385 LYS A 386
SITE 2 AC2 6 ALA A 387 PGR A1759
SITE 1 AC3 8 GLY A 452 HIS A 480 ASP A 516 ARG A 726
SITE 2 AC3 8 LEU A 727 LEU A 728 HOH A2479 HOH A2682
SITE 1 AC4 5 LYS A 595 ASN A 653 ASN A 685 HIS A 720
SITE 2 AC4 5 PGR A1767
SITE 1 AC5 2 PHE A 698 HOH A2720
SITE 1 AC6 3 GLN A 437 HIS A 439 HOH A2683
SITE 1 AC7 8 SER A 311 VAL A 446 ARG A 447 GLU A 448
SITE 2 AC7 8 VAL A 449 HOH A2362 HOH A2684 HOH A2685
SITE 1 AC8 3 THR A 466 ALA A 555 GLU A 558
SITE 1 AC9 8 ARG A 547 SER A 551 MET A 589 ASP A 635
SITE 2 AC9 8 TYR A 636 HOH A2546 HOH A2590 HOH A2591
SITE 1 BC1 8 LYS A 299 TYR A 543 TRP A 622 ASN A 627
SITE 2 BC1 8 TYR A 633 HOH A2587 HOH A2686 HOH A2687
SITE 1 BC2 7 GLU A 574 GLY A 575 GLY A 600 GLN A 713
SITE 2 BC2 7 PGO A1743 HOH A2688 HOH A2706
SITE 1 BC3 7 GLN A 510 TYR A 514 GLU A 574 LEU A 598
SITE 2 BC3 7 SER A 710 PGR A1742 PGR A1777
SITE 1 BC4 6 HIS A 308 GLY A 309 SER A 311 HIS A 312
SITE 2 BC4 6 ASP A 454 HOH A2441
SITE 1 BC5 6 ALA A 700 LYS A 701 ARG A 703 PHE A 706
SITE 2 BC5 6 HOH A2162 HOH A2656
SITE 1 BC6 8 TRP A 50 ARG A 52 ASP A 53 PGR A1775
SITE 2 BC6 8 PGR A1780 HOH A2091 HOH A2691 HOH A2700
SITE 1 BC7 5 ARG A 527 ALA A 535 GLY A 540 HOH A2491
SITE 2 BC7 5 HOH A2692
SITE 1 BC8 6 ASP A 155 MET A 157 PHE A 698 LYS A 701
SITE 2 BC8 6 HOH A2195 HOH A2693
SITE 1 BC9 6 GLY A 369 ARG A 462 PRO A 474 SER A 476
SITE 2 BC9 6 HIS A 525 HOH A2716
SITE 1 CC1 5 ALA A 88 GLU A 89 SER A 92 GLY A 451
SITE 2 CC1 5 HOH A2674
SITE 1 CC2 4 TYR A 103 TYR A 110 VAL A 159 LEU A 411
SITE 1 CC3 4 ILE A 142 ASP A 143 LYS A 186 HOH A2694
SITE 1 CC4 5 ALA A 259 LEU A 411 HOH A2152 HOH A2204
SITE 2 CC4 5 HOH A2437
SITE 1 CC5 3 THR A 262 ASN A 263 LEU A 282
SITE 1 CC6 6 GLY A 300 VAL A 301 ASN A 318 GLY A 320
SITE 2 CC6 6 GLY A 321 HOH A2357
SITE 1 CC7 5 ARG A 302 ASP A 304 LEU A 316 HIS A 325
SITE 2 CC7 5 HOH A2385
SITE 1 CC8 7 ASP A 261 ASP A 454 ASN A 457 LYS A 481
SITE 2 CC8 7 HOH A2311 HOH A2442 HOH A2695
SITE 1 CC9 5 ASP A 281 ARG A 283 ARG A 332 THR A 427
SITE 2 CC9 5 HOH A2696
SITE 1 DC1 6 HIS A 312 ILE A 329 HIS A 340 GLU A 448
SITE 2 DC1 6 GOL A1733 HOH A2697
SITE 1 DC2 3 ALA A 378 SER A 380 THR A 389
SITE 1 DC3 5 TYR A 105 THR A 262 LEU A 411 GLU A 412
SITE 2 DC3 5 TYR A 413
SITE 1 DC4 4 ASP A 433 SER A 440 ARG A 441 THR A 442
SITE 1 DC5 3 THR A 290 SER A 440 ARG A 441
SITE 1 DC6 7 MET A 503 ASP A 504 GLN A 506 ILE A 523
SITE 2 DC6 7 PGR A1779 HOH A2516 HOH A2699
SITE 1 DC7 5 ARG A 447 SER A 508 ILE A 509 PGR A1779
SITE 2 DC7 5 HOH A2193
SITE 1 DC8 6 PRO A 568 SER A 569 PHE A 594 LYS A 595
SITE 2 DC8 6 GOL A1732 HOH A2567
SITE 1 DC9 7 ARG A 75 ASN A 653 ASN A 684 ASN A 685
SITE 2 DC9 7 GLU A 686 HIS A 720 GOL A1735
SITE 1 EC1 2 VAL A 104 GLU A 415
SITE 1 EC2 3 ASP A 304 GLN A 306 HOH A2393
SITE 1 EC3 6 TYR A 103 SER A 408 GLN A 409 HOH A2146
SITE 2 EC3 6 HOH A2159 HOH A2433
SITE 1 EC4 7 ALA A 17 LYS A 19 TRP A 50 HOH A2700
SITE 2 EC4 7 HOH A2701 HOH A2702 HOH A2703
SITE 1 EC5 5 ARG A 56 ILE A 62 MET A 693 HOH A2088
SITE 2 EC5 5 HOH A2650
SITE 1 EC6 2 ARG A 295 GLU A 319
SITE 1 EC7 4 ARG A 463 PHE A 464 PHE A 559 HOH A2704
SITE 1 EC8 4 ARG A 52 ASP A 54 PGR A1746 PGR A1780
SITE 1 EC9 6 GLY A 333 GLN A 334 LYS A 445 VAL A 446
SITE 2 EC9 6 GLU A 448 HOH A2705
SITE 1 FC1 8 GLN A 657 SER A 699 GLU A 709 SER A 710
SITE 2 FC1 8 GLN A 713 PGO A1743 HOH A2614 HOH A2706
SITE 1 FC2 6 ASP A 32 GLY A 34 PRO A 35 ASN A 249
SITE 2 FC2 6 TRP A 622 HOH A2707
SITE 1 FC3 5 GLN A 506 SER A 508 PGR A1764 PGR A1765
SITE 2 FC3 5 PO4 A1793
SITE 1 FC4 4 ASP A 53 ASP A 55 PGR A1746 PGR A1775
SITE 1 FC5 4 LYS A 284 GLU A 397 PHE A 432 ARG A 441
SITE 1 FC6 5 GLU A 650 ASP A 683 ASN A 684 ASN A 685
SITE 2 FC6 5 HOH A2710
SITE 1 FC7 5 ASP A 54 ARG A 56 GLU A 222 PRO A 616
SITE 2 FC7 5 TRP A 668
SITE 1 FC8 6 LEU A 638 ASN A 645 VAL A 646 ARG A 647
SITE 2 FC8 6 HOH A2711 HOH A2712
SITE 1 FC9 3 ASN A 66 LYS A 69 GLN A 73
SITE 1 GC1 3 LEU A 342 ASP A 344 ALA A 387
SITE 1 GC2 4 ASP A 281 LYS A 284 HIS A 288 GLU A 292
SITE 1 GC3 4 ARG A 283 LYS A 459 VAL A 460 HOH A2713
SITE 1 GC4 3 GLU A 246 HOH A2714 HOH A2715
SITE 1 GC5 4 ALA A 368 LEU A 532 HOH A2716 HOH A2717
SITE 1 GC6 10 TYR A 496 ARG A 576 SER A 577 HIS A 697
SITE 2 GC6 10 PHE A 698 PO4 A1793 HOH A2719 HOH A2720
SITE 3 GC6 10 VAL B 3 RGL B 4
SITE 1 GC7 5 GLY A 201 LYS A 220 ASP A 221 LEU A 224
SITE 2 GC7 5 HOH A2250
SITE 1 GC8 7 TYR A 494 TYR A 496 LEU A 501 MET A 503
SITE 2 GC8 7 ARG A 576 PGR A1779 PO4 A1791
SITE 1 GC9 3 TRP A 208 HOH A2204 HOH A2309
SITE 1 HC1 5 ILE A 91 ILE A 94 HOH A2131 HOH A2132
SITE 2 HC1 5 HOH A2138
SITE 1 HC2 3 LYS A 121 HOH A2173 HOH A2194
SITE 1 HC3 6 ASP A 174 SER A 176 ASN A 178 VAL A 180
SITE 2 HC3 6 HOH A2216 HOH A2226
SITE 1 HC4 3 HIS A 308 HIS A 312 PHE A 385
SITE 1 HC5 4 GLU A 63 ASN A 66 HOH A2093 HOH A2094
SITE 1 HC6 25 GLU A 226 SER A 253 TYR A 496 TYR A 499
SITE 2 HC6 25 LEU A 501 SER A 577 ALA A 578 PHE A 603
SITE 3 HC6 25 MET A 610 LEU A 617 GLU A 621 ARG A 664
SITE 4 HC6 25 VAL A 665 HIS A 697 PO4 A1791 HOH A2266
SITE 5 HC6 25 HOH A2267 HOH A2302 HOH A2303 HOH A2580
SITE 6 HC6 25 HOH A2622 HOH A2678 HOH A2679 HOH A2680
SITE 7 HC6 25 HOH A2681
CRYST1 95.478 142.776 208.919 90.00 90.00 90.00 I 2 2 2 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 0.010474 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004787 0.00000
TER 6126 ARG A 730
TER 6170 RGL B 4
MASTER 731 0 70 22 46 0 119 6 7215 2 363 59
END |