HEADER HYDROLASE 28-JUL-14 4U6B
TITLE ZG3597, A FAMILY 117 GLYCOSIDE HYDROLASE, PRODUCED BY THE MARINE
TITLE 2 BACTERIUM ZOBELLIA GALACTANIVORANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL LIPOPROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GLYCOSIDE HYDROLASE;
COMPND 5 EC: 3.2.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZOBELLIA GALACTANIVORANS;
SOURCE 3 ORGANISM_TAXID: 63186;
SOURCE 4 STRAIN: DSM 12802 / CIP 106680 / NCIMB 13871 / DSIJ;
SOURCE 5 GENE: ZOBELLIA_3597;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GH117, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.FICKO-BLEAN
REVDAT 3 20-DEC-23 4U6B 1 LINK
REVDAT 2 25-FEB-15 4U6B 1 JRNL
REVDAT 1 11-FEB-15 4U6B 0
JRNL AUTH E.FICKO-BLEAN,D.DUFFIEUX,E.REBUFFET,R.LAROCQUE,
JRNL AUTH 2 A.GROISILLIER,G.MICHEL,M.CZJZEK
JRNL TITL BIOCHEMICAL AND STRUCTURAL INVESTIGATION OF TWO PARALOGOUS
JRNL TITL 2 GLYCOSIDE HYDROLASES FROM ZOBELLIA GALACTANIVORANS: NOVEL
JRNL TITL 3 INSIGHTS INTO THE EVOLUTION, DIMERIZATION PLASTICITY AND
JRNL TITL 4 CATALYTIC MECHANISM OF THE GH117 FAMILY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 209 2015
JRNL REFN ESSN 1399-0047
JRNL PMID 25664732
JRNL DOI 10.1107/S1399004714025024
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 98705
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5189
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7181
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 400
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10693
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 701
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.66000
REMARK 3 B22 (A**2) : 1.24000
REMARK 3 B33 (A**2) : 0.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.196
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.786
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11179 ; 0.017 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15271 ; 1.885 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1383 ; 7.569 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 529 ;37.665 ;24.026
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1552 ;17.178 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;19.325 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1554 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8936 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5503 ; 3.801 ; 3.792
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6871 ; 5.806 ; 5.656
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5676 ; 4.539 ; 3.960
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 17563 ; 9.322 ;31.513
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: NULL
REMARK 4
REMARK 4 4U6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202273.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103865
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 3P2N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE OPTIMIZED CRYSTALLIZATION
REMARK 280 CONDITIONS FOR ZG3597 WERE: 16% GLYCEROL, 0.15 M AMMONIUM
REMARK 280 SULFATE, AND 20 % PEG 4000 IN A 1:1 RATIO WITH PROTEIN AT 5 AND
REMARK 280 2.5 MG/ML AND 14% PEG 3350 AND 75 MM SODIUM ACETATE WITH A RATIO
REMARK 280 OF 2:1 PROTEIN (AT 7.5 MG/ML) TO MOTHER LIQUOR., VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 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,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 111.76000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 112.61000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 111.76000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 112.61000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 111.76000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.61000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 111.76000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 112.61000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 93.89500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 112.61000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 93.89500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 112.61000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 93.89500
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 112.61000
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 93.89500
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 112.61000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 93.89500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 111.76000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 93.89500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 111.76000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 93.89500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 111.76000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 93.89500
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 111.76000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 MET A 1
REMARK 465 GLN A 2
REMARK 465 ILE A 3
REMARK 465 ASN A 4
REMARK 465 LEU A 5
REMARK 465 PHE A 6
REMARK 465 LEU A 7
REMARK 465 LYS A 8
REMARK 465 GLN A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 PHE A 12
REMARK 465 SER A 13
REMARK 465 LEU A 14
REMARK 465 LEU A 15
REMARK 465 MET A 16
REMARK 465 ALA A 17
REMARK 465 LEU A 18
REMARK 465 SER A 19
REMARK 465 LEU A 20
REMARK 465 ILE A 21
REMARK 465 ALA A 22
REMARK 465 CYS A 23
REMARK 465 SER A 24
REMARK 465 GLU A 25
REMARK 465 GLN A 26
REMARK 465 LYS A 27
REMARK 465 THR A 28
REMARK 465 GLU A 29
REMARK 465 THR A 30
REMARK 465 LYS A 31
REMARK 465 SER A 32
REMARK 465 THR A 33
REMARK 465 PRO A 34
REMARK 465 THR A 35
REMARK 465 GLU A 36
REMARK 465 ASP A 37
REMARK 465 SER A 38
REMARK 465 ALA A 39
REMARK 465 THR A 40
REMARK 465 THR A 41
REMARK 465 GLU A 42
REMARK 465 HIS A 43
REMARK 465 LYS A 44
REMARK 465 VAL A 45
REMARK 465 PHE A 46
REMARK 465 PRO A 47
REMARK 465 HIS A 48
REMARK 465 LYS A 49
REMARK 465 MET A 50
REMARK 465 PRO A 51
REMARK 465 SER A 52
REMARK 465 GLU A 53
REMARK 465 LYS A 54
REMARK 465 PRO A 55
REMARK 465 ASP A 56
REMARK 465 MET A 57
REMARK 465 PRO A 58
REMARK 465 LEU A 59
REMARK 465 SER A 60
REMARK 465 ALA A 61
REMARK 465 ALA A 62
REMARK 465 ALA A 63
REMARK 465 GLU A 64
REMARK 465 ARG A 65
REMARK 465 MET A 66
REMARK 465 PHE A 67
REMARK 465 SER A 68
REMARK 465 TYR A 69
REMARK 465 PRO A 70
REMARK 465 ALA A 71
REMARK 465 PRO A 72
REMARK 465 ARG A 73
REMARK 465 VAL A 74
REMARK 465 GLN A 75
REMARK 465 LYS A 269
REMARK 465 TRP A 270
REMARK 465 PRO A 271
REMARK 465 ASP A 272
REMARK 465 ILE A 273
REMARK 465 ARG A 274
REMARK 465 ASP A 275
REMARK 465 LYS A 426
REMARK 465 ASN A 427
REMARK 465 LEU A 428
REMARK 465 SER A 429
REMARK 465 PRO A 430
REMARK 465 GLU A 431
REMARK 465 GLY A 432
REMARK 465 ARG A 433
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 ILE B 3
REMARK 465 ASN B 4
REMARK 465 LEU B 5
REMARK 465 PHE B 6
REMARK 465 LEU B 7
REMARK 465 LYS B 8
REMARK 465 GLN B 9
REMARK 465 SER B 10
REMARK 465 THR B 11
REMARK 465 PHE B 12
REMARK 465 SER B 13
REMARK 465 LEU B 14
REMARK 465 LEU B 15
REMARK 465 MET B 16
REMARK 465 ALA B 17
REMARK 465 LEU B 18
REMARK 465 SER B 19
REMARK 465 LEU B 20
REMARK 465 ILE B 21
REMARK 465 ALA B 22
REMARK 465 CYS B 23
REMARK 465 SER B 24
REMARK 465 GLU B 25
REMARK 465 GLN B 26
REMARK 465 LYS B 27
REMARK 465 THR B 28
REMARK 465 GLU B 29
REMARK 465 THR B 30
REMARK 465 LYS B 31
REMARK 465 SER B 32
REMARK 465 THR B 33
REMARK 465 PRO B 34
REMARK 465 THR B 35
REMARK 465 GLU B 36
REMARK 465 ASP B 37
REMARK 465 SER B 38
REMARK 465 ALA B 39
REMARK 465 THR B 40
REMARK 465 THR B 41
REMARK 465 GLU B 42
REMARK 465 HIS B 43
REMARK 465 LYS B 44
REMARK 465 VAL B 45
REMARK 465 PHE B 46
REMARK 465 PRO B 47
REMARK 465 HIS B 48
REMARK 465 LYS B 49
REMARK 465 MET B 50
REMARK 465 PRO B 51
REMARK 465 SER B 52
REMARK 465 GLU B 53
REMARK 465 LYS B 54
REMARK 465 PRO B 55
REMARK 465 ASP B 56
REMARK 465 MET B 57
REMARK 465 PRO B 58
REMARK 465 LEU B 59
REMARK 465 SER B 60
REMARK 465 ALA B 61
REMARK 465 ALA B 62
REMARK 465 ALA B 63
REMARK 465 GLU B 64
REMARK 465 ARG B 65
REMARK 465 MET B 66
REMARK 465 PHE B 67
REMARK 465 SER B 68
REMARK 465 TYR B 69
REMARK 465 PRO B 70
REMARK 465 ALA B 71
REMARK 465 PRO B 72
REMARK 465 ARG B 73
REMARK 465 VAL B 74
REMARK 465 GLN B 75
REMARK 465 LYS B 269
REMARK 465 TRP B 270
REMARK 465 PRO B 271
REMARK 465 ASP B 272
REMARK 465 ILE B 273
REMARK 465 ARG B 274
REMARK 465 ASP B 275
REMARK 465 LYS B 426
REMARK 465 ASN B 427
REMARK 465 LEU B 428
REMARK 465 SER B 429
REMARK 465 PRO B 430
REMARK 465 GLU B 431
REMARK 465 GLY B 432
REMARK 465 ARG B 433
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 ILE C 3
REMARK 465 ASN C 4
REMARK 465 LEU C 5
REMARK 465 PHE C 6
REMARK 465 LEU C 7
REMARK 465 LYS C 8
REMARK 465 GLN C 9
REMARK 465 SER C 10
REMARK 465 THR C 11
REMARK 465 PHE C 12
REMARK 465 SER C 13
REMARK 465 LEU C 14
REMARK 465 LEU C 15
REMARK 465 MET C 16
REMARK 465 ALA C 17
REMARK 465 LEU C 18
REMARK 465 SER C 19
REMARK 465 LEU C 20
REMARK 465 ILE C 21
REMARK 465 ALA C 22
REMARK 465 CYS C 23
REMARK 465 SER C 24
REMARK 465 GLU C 25
REMARK 465 GLN C 26
REMARK 465 LYS C 27
REMARK 465 THR C 28
REMARK 465 GLU C 29
REMARK 465 THR C 30
REMARK 465 LYS C 31
REMARK 465 SER C 32
REMARK 465 THR C 33
REMARK 465 PRO C 34
REMARK 465 THR C 35
REMARK 465 GLU C 36
REMARK 465 ASP C 37
REMARK 465 SER C 38
REMARK 465 ALA C 39
REMARK 465 THR C 40
REMARK 465 THR C 41
REMARK 465 GLU C 42
REMARK 465 HIS C 43
REMARK 465 LYS C 44
REMARK 465 VAL C 45
REMARK 465 PHE C 46
REMARK 465 PRO C 47
REMARK 465 HIS C 48
REMARK 465 LYS C 49
REMARK 465 MET C 50
REMARK 465 PRO C 51
REMARK 465 SER C 52
REMARK 465 GLU C 53
REMARK 465 LYS C 54
REMARK 465 PRO C 55
REMARK 465 ASP C 56
REMARK 465 MET C 57
REMARK 465 PRO C 58
REMARK 465 LEU C 59
REMARK 465 SER C 60
REMARK 465 ALA C 61
REMARK 465 ALA C 62
REMARK 465 ALA C 63
REMARK 465 GLU C 64
REMARK 465 ARG C 65
REMARK 465 MET C 66
REMARK 465 PHE C 67
REMARK 465 SER C 68
REMARK 465 TYR C 69
REMARK 465 PRO C 70
REMARK 465 ALA C 71
REMARK 465 PRO C 72
REMARK 465 ARG C 73
REMARK 465 VAL C 74
REMARK 465 GLN C 75
REMARK 465 LYS C 269
REMARK 465 TRP C 270
REMARK 465 PRO C 271
REMARK 465 ASP C 272
REMARK 465 ILE C 273
REMARK 465 ARG C 274
REMARK 465 ASP C 275
REMARK 465 LYS C 276
REMARK 465 LYS C 426
REMARK 465 ASN C 427
REMARK 465 LEU C 428
REMARK 465 SER C 429
REMARK 465 PRO C 430
REMARK 465 GLU C 431
REMARK 465 GLY C 432
REMARK 465 ARG C 433
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 ILE D 3
REMARK 465 ASN D 4
REMARK 465 LEU D 5
REMARK 465 PHE D 6
REMARK 465 LEU D 7
REMARK 465 LYS D 8
REMARK 465 GLN D 9
REMARK 465 SER D 10
REMARK 465 THR D 11
REMARK 465 PHE D 12
REMARK 465 SER D 13
REMARK 465 LEU D 14
REMARK 465 LEU D 15
REMARK 465 MET D 16
REMARK 465 ALA D 17
REMARK 465 LEU D 18
REMARK 465 SER D 19
REMARK 465 LEU D 20
REMARK 465 ILE D 21
REMARK 465 ALA D 22
REMARK 465 CYS D 23
REMARK 465 SER D 24
REMARK 465 GLU D 25
REMARK 465 GLN D 26
REMARK 465 LYS D 27
REMARK 465 THR D 28
REMARK 465 GLU D 29
REMARK 465 THR D 30
REMARK 465 LYS D 31
REMARK 465 SER D 32
REMARK 465 THR D 33
REMARK 465 PRO D 34
REMARK 465 THR D 35
REMARK 465 GLU D 36
REMARK 465 ASP D 37
REMARK 465 SER D 38
REMARK 465 ALA D 39
REMARK 465 THR D 40
REMARK 465 THR D 41
REMARK 465 GLU D 42
REMARK 465 HIS D 43
REMARK 465 LYS D 44
REMARK 465 VAL D 45
REMARK 465 PHE D 46
REMARK 465 PRO D 47
REMARK 465 HIS D 48
REMARK 465 LYS D 49
REMARK 465 MET D 50
REMARK 465 PRO D 51
REMARK 465 SER D 52
REMARK 465 GLU D 53
REMARK 465 LYS D 54
REMARK 465 PRO D 55
REMARK 465 ASP D 56
REMARK 465 MET D 57
REMARK 465 PRO D 58
REMARK 465 LEU D 59
REMARK 465 SER D 60
REMARK 465 ALA D 61
REMARK 465 ALA D 62
REMARK 465 ALA D 63
REMARK 465 GLU D 64
REMARK 465 ARG D 65
REMARK 465 MET D 66
REMARK 465 PHE D 67
REMARK 465 SER D 68
REMARK 465 TYR D 69
REMARK 465 PRO D 70
REMARK 465 ALA D 71
REMARK 465 PRO D 72
REMARK 465 ARG D 73
REMARK 465 VAL D 74
REMARK 465 GLN D 75
REMARK 465 LYS D 269
REMARK 465 TRP D 270
REMARK 465 PRO D 271
REMARK 465 ASP D 272
REMARK 465 ILE D 273
REMARK 465 ARG D 274
REMARK 465 ASP D 275
REMARK 465 LYS D 426
REMARK 465 ASN D 427
REMARK 465 LEU D 428
REMARK 465 SER D 429
REMARK 465 PRO D 430
REMARK 465 GLU D 431
REMARK 465 GLY D 432
REMARK 465 ARG D 433
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 TRP A 131 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 131 CZ3 CH2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 LYS A 238 CG CD CE NZ
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 TYR A 277 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 323 CG CD CE NZ
REMARK 470 ARG A 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 335 CG CD CE NZ
REMARK 470 GLU A 341 CG CD OE1 OE2
REMARK 470 LYS A 385 CG CD CE NZ
REMARK 470 ARG A 425 CG CD NE CZ NH1 NH2
REMARK 470 TRP B 131 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 131 CZ3 CH2
REMARK 470 ARG B 208 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 470 LYS B 239 CG CD CE NZ
REMARK 470 LYS B 276 CG CD CE NZ
REMARK 470 TYR B 277 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 323 CG CD CE NZ
REMARK 470 ARG B 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 335 CG CD CE NZ
REMARK 470 LYS B 385 CG CD CE NZ
REMARK 470 ARG B 425 CG CD NE CZ NH1 NH2
REMARK 470 TRP C 131 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 131 CZ3 CH2
REMARK 470 ARG C 208 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 238 CG CD CE NZ
REMARK 470 TYR C 277 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 323 CG CD CE NZ
REMARK 470 GLU C 327 CG CD OE1 OE2
REMARK 470 ARG C 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 385 CG CD CE NZ
REMARK 470 ARG C 425 CG CD NE CZ NH1 NH2
REMARK 470 TRP D 131 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 131 CZ3 CH2
REMARK 470 LYS D 135 CG CD CE NZ
REMARK 470 ARG D 208 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 238 CG CD CE NZ
REMARK 470 LYS D 239 CG CD CE NZ
REMARK 470 LYS D 276 CG CD CE NZ
REMARK 470 TYR D 277 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 335 CG CD CE NZ
REMARK 470 LYS D 385 CG CD CE NZ
REMARK 470 ARG D 425 CG CD NE CZ NH1 NH2
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 NH2 ARG C 133 OE1 GLU C 136 1.18
REMARK 500 NH2 ARG D 133 OE1 GLU D 136 2.03
REMARK 500 O SER B 221 O ASP B 223 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH D 601 O HOH D 601 2555 2.02
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 TRP C 152 CE3 TRP C 152 CZ3 0.127
REMARK 500 ASP D 243 CB ASP D 243 CG -0.139
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 PRO A 175 C - N - CD ANGL. DEV. = 19.1 DEGREES
REMARK 500 GLY A 224 C - N - CA ANGL. DEV. = -15.2 DEGREES
REMARK 500 PRO A 300 C - N - CD ANGL. DEV. = 18.4 DEGREES
REMARK 500 MET A 331 CG - SD - CE ANGL. DEV. = -11.9 DEGREES
REMARK 500 PRO B 175 C - N - CD ANGL. DEV. = 19.5 DEGREES
REMARK 500 PRO B 225 C - N - CD ANGL. DEV. = 18.0 DEGREES
REMARK 500 ASP B 243 CB - CG - OD1 ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASP B 243 CB - CG - OD2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 LEU B 374 CB - CG - CD1 ANGL. DEV. = -11.2 DEGREES
REMARK 500 PRO C 175 C - N - CD ANGL. DEV. = 19.5 DEGREES
REMARK 500 PRO C 175 CA - N - CD ANGL. DEV. = -8.4 DEGREES
REMARK 500 ASP D 243 CB - CG - OD1 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP D 243 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 MET D 331 CG - SD - CE ANGL. DEV. = -16.2 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 132 -5.91 -58.52
REMARK 500 PRO A 175 40.24 -109.54
REMARK 500 THR A 184 64.33 68.52
REMARK 500 ARG A 208 -152.82 -120.79
REMARK 500 ASP A 210 -139.03 48.86
REMARK 500 TRP A 211 81.40 89.56
REMARK 500 LEU A 298 -6.40 91.03
REMARK 500 LYS A 314 -136.70 55.15
REMARK 500 ASP A 363 39.97 76.15
REMARK 500 ASN A 379 45.34 -106.28
REMARK 500 GLN A 422 79.41 -104.19
REMARK 500 ASN B 132 7.48 -59.58
REMARK 500 ARG B 133 28.56 -142.38
REMARK 500 THR B 184 62.68 64.15
REMARK 500 TRP B 211 102.48 -163.85
REMARK 500 LYS B 314 -126.75 53.04
REMARK 500 ASN B 379 45.35 -109.44
REMARK 500 THR C 184 64.14 66.16
REMARK 500 ARG C 208 40.94 -151.21
REMARK 500 LYS C 239 138.18 -35.11
REMARK 500 ASP C 243 0.12 -68.30
REMARK 500 LYS C 314 -123.94 45.26
REMARK 500 LYS C 314 -124.60 46.23
REMARK 500 ASN C 379 51.61 -111.27
REMARK 500 PRO D 175 40.92 -104.03
REMARK 500 THR D 184 63.88 65.86
REMARK 500 ARG D 208 -151.57 -118.73
REMARK 500 LYS D 314 -121.37 62.32
REMARK 500 ARG D 328 88.52 -69.75
REMARK 500 ASN D 379 47.02 -105.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 753 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH C 777 DISTANCE = 5.84 ANGSTROMS
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 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 78 OE1
REMARK 620 2 ASP A 397 OD1 160.1
REMARK 620 3 ASP A 397 OD2 133.9 49.6
REMARK 620 4 SER A 399 O 87.0 87.9 137.4
REMARK 620 5 VAL A 402 O 119.1 79.0 85.9 81.3
REMARK 620 6 HOH A 729 O 82.8 78.9 79.9 97.8 157.9
REMARK 620 7 HOH A 737 O 65.4 115.1 68.7 151.2 118.3 71.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 633 O
REMARK 620 2 HOH A 634 O 77.3
REMARK 620 3 HOH A 635 O 150.2 76.4
REMARK 620 4 HOH A 636 O 79.9 80.4 109.0
REMARK 620 5 HOH A 637 O 79.3 156.5 125.6 97.4
REMARK 620 6 HOH A 638 O 83.6 85.5 80.7 160.3 90.0
REMARK 620 7 HOH A 671 O 132.1 133.7 77.1 73.2 66.1 126.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 78 OE1
REMARK 620 2 ASP B 397 OD1 144.6
REMARK 620 3 ASP B 397 OD2 140.9 48.5
REMARK 620 4 SER B 399 O 81.9 87.0 133.6
REMARK 620 5 VAL B 402 O 128.5 81.4 81.4 79.3
REMARK 620 6 HOH B 671 O 75.0 113.8 69.3 156.7 112.9
REMARK 620 7 HOH B 675 O 75.6 74.6 79.5 103.5 155.6 73.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 634 O
REMARK 620 2 HOH B 635 O 83.4
REMARK 620 3 HOH B 636 O 89.1 74.4
REMARK 620 4 HOH B 638 O 162.6 81.6 78.4
REMARK 620 5 HOH B 639 O 128.7 127.1 134.5 68.2
REMARK 620 6 HOH B 640 O 81.7 149.3 78.7 107.3 82.6
REMARK 620 7 HOH B 641 O 91.8 80.3 154.4 94.4 60.9 126.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 78 OE1
REMARK 620 2 ASP C 397 OD1 128.9
REMARK 620 3 ASP C 397 OD2 125.3 49.0
REMARK 620 4 SER C 399 O 89.7 87.0 134.2
REMARK 620 5 VAL C 402 O 146.7 84.0 78.4 86.2
REMARK 620 6 HOH C 683 O 59.3 70.0 83.1 93.7 153.9
REMARK 620 7 HOH C 761 O 82.3 148.1 122.9 86.6 64.5 141.6
REMARK 620 8 HOH C 762 O 66.3 111.4 68.4 155.5 110.9 78.6 85.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 630 O
REMARK 620 2 HOH C 631 O 79.5
REMARK 620 3 HOH C 632 O 76.9 75.5
REMARK 620 4 HOH C 633 O 79.7 154.1 84.9
REMARK 620 5 HOH C 635 O 134.0 76.6 132.0 129.3
REMARK 620 6 HOH C 636 O 81.2 102.8 158.0 89.0 66.8
REMARK 620 7 HOH C 637 O 147.6 108.4 75.0 82.1 77.8 125.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 78 OE1
REMARK 620 2 ASP D 397 OD1 142.6
REMARK 620 3 ASP D 397 OD2 136.0 48.8
REMARK 620 4 SER D 399 O 88.1 83.8 130.8
REMARK 620 5 VAL D 402 O 135.2 79.2 79.0 80.3
REMARK 620 6 HOH D 741 O 67.7 76.7 86.8 94.9 155.8
REMARK 620 7 HOH D 752 O 68.5 118.0 73.0 155.9 112.1 81.6
REMARK 620 8 HOH D 753 O 71.2 144.2 122.2 87.1 65.1 138.7 80.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 628 O
REMARK 620 2 HOH D 630 O 80.7
REMARK 620 3 HOH D 631 O 144.8 79.5
REMARK 620 4 HOH D 632 O 107.6 161.4 84.7
REMARK 620 5 HOH D 633 O 126.2 87.0 81.3 100.5
REMARK 620 6 HOH D 634 O 76.0 87.1 74.3 79.1 155.5
REMARK 620 7 HOH D 635 O 78.4 127.1 136.3 71.4 68.4 132.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4AK5 RELATED DB: PDB
REMARK 900 RELATED ID: 3P2N RELATED DB: PDB
REMARK 900 RELATED ID: 3R4Y RELATED DB: PDB
DBREF 4U6B A 1 433 UNP F0V1E1 F0V1E1_ZOBGA 1 433
DBREF 4U6B B 1 433 UNP F0V1E1 F0V1E1_ZOBGA 1 433
DBREF 4U6B C 1 433 UNP F0V1E1 F0V1E1_ZOBGA 1 433
DBREF 4U6B D 1 433 UNP F0V1E1 F0V1E1_ZOBGA 1 433
SEQRES 1 A 433 MET GLN ILE ASN LEU PHE LEU LYS GLN SER THR PHE SER
SEQRES 2 A 433 LEU LEU MET ALA LEU SER LEU ILE ALA CYS SER GLU GLN
SEQRES 3 A 433 LYS THR GLU THR LYS SER THR PRO THR GLU ASP SER ALA
SEQRES 4 A 433 THR THR GLU HIS LYS VAL PHE PRO HIS LYS MET PRO SER
SEQRES 5 A 433 GLU LYS PRO ASP MET PRO LEU SER ALA ALA ALA GLU ARG
SEQRES 6 A 433 MET PHE SER TYR PRO ALA PRO ARG VAL GLN ASP ASN GLU
SEQRES 7 A 433 LEU PHE SER GLN PHE LYS TYR THR ARG LEU LYS GLY PHE
SEQRES 8 A 433 ASP TYR ASN ASN GLY ASP GLY THR ILE SER ARG ARG ASP
SEQRES 9 A 433 PRO SER ARG PRO ILE LEU VAL ASN GLY LYS TYR TYR ILE
SEQRES 10 A 433 TYR TYR THR LYS ARG ASP THR LYS VAL PRO PRO ILE GLY
SEQRES 11 A 433 TRP ASN ARG ALA LYS GLU ALA THR ASP GLU ILE PRO SER
SEQRES 12 A 433 THR ASP TRP ASP LEU CYS GLU ILE TRP TYR ALA THR SER
SEQRES 13 A 433 GLU ASP GLY THR THR TRP LYS GLU GLU GLY VAL ALA ILE
SEQRES 14 A 433 ALA ARG PRO GLU LYS PRO LYS PRO GLY TRP ARG SER VAL
SEQRES 15 A 433 ALA THR PRO ASP ILE LEU VAL TRP LYS GLY LYS TYR TYR
SEQRES 16 A 433 LEU TYR TYR GLN ALA PHE ASN GLU PRO SER GLY LEU ARG
SEQRES 17 A 433 GLY ASP TRP CYS PRO VAL SER VAL SER TYR ALA ASP SER
SEQRES 18 A 433 PRO ASP GLY PRO TRP THR HIS GLY GLY ASP SER VAL ILE
SEQRES 19 A 433 PRO PHE GLY LYS LYS GLY GLU TRP ASP GLN ASP ALA THR
SEQRES 20 A 433 HIS ASP PRO GLN PRO ILE VAL TYR LYS GLY LYS ILE HIS
SEQRES 21 A 433 LEU TYR TYR LYS ALA ALA TYR ASN LYS TRP PRO ASP ILE
SEQRES 22 A 433 ARG ASP LYS TYR ALA VAL GLY HIS GLY LEU ALA ILE ALA
SEQRES 23 A 433 ASP ASP PRO LEU GLY PRO PHE GLU LYS HIS PRO LEU ASN
SEQRES 24 A 433 PRO VAL MET THR SER GLY HIS GLU THR THR TYR PHE PRO
SEQRES 25 A 433 PHE LYS GLU GLY VAL ALA THR LEU ALA ILE LYS ASP GLY
SEQRES 26 A 433 ASN GLU ARG TYR THR MET GLN TYR ALA LYS ASP GLY VAL
SEQRES 27 A 433 ASN PHE GLU ILE ALA SER VAL VAL SER LEU ALA PRO THR
SEQRES 28 A 433 ALA ALA ALA PRO PHE ALA ALA ASP ALA PHE THR ASP SER
SEQRES 29 A 433 GLY ASN GLY ARG GLY VAL THR TRP GLY LEU CYS HIS PHE
SEQRES 30 A 433 THR ASN ALA SER ASN ASN PRO LYS LYS GLY TYR SER ILE
SEQRES 31 A 433 ILE ALA ARG PHE ASP CYS ASP LEU SER LEU ASP VAL ASP
SEQRES 32 A 433 ASP PRO PHE TYR LYS ASN THR GLY VAL TRP HIS ARG PRO
SEQRES 33 A 433 GLU VAL TYR PHE ALA GLN ALA PRO ARG LYS ASN LEU SER
SEQRES 34 A 433 PRO GLU GLY ARG
SEQRES 1 B 433 MET GLN ILE ASN LEU PHE LEU LYS GLN SER THR PHE SER
SEQRES 2 B 433 LEU LEU MET ALA LEU SER LEU ILE ALA CYS SER GLU GLN
SEQRES 3 B 433 LYS THR GLU THR LYS SER THR PRO THR GLU ASP SER ALA
SEQRES 4 B 433 THR THR GLU HIS LYS VAL PHE PRO HIS LYS MET PRO SER
SEQRES 5 B 433 GLU LYS PRO ASP MET PRO LEU SER ALA ALA ALA GLU ARG
SEQRES 6 B 433 MET PHE SER TYR PRO ALA PRO ARG VAL GLN ASP ASN GLU
SEQRES 7 B 433 LEU PHE SER GLN PHE LYS TYR THR ARG LEU LYS GLY PHE
SEQRES 8 B 433 ASP TYR ASN ASN GLY ASP GLY THR ILE SER ARG ARG ASP
SEQRES 9 B 433 PRO SER ARG PRO ILE LEU VAL ASN GLY LYS TYR TYR ILE
SEQRES 10 B 433 TYR TYR THR LYS ARG ASP THR LYS VAL PRO PRO ILE GLY
SEQRES 11 B 433 TRP ASN ARG ALA LYS GLU ALA THR ASP GLU ILE PRO SER
SEQRES 12 B 433 THR ASP TRP ASP LEU CYS GLU ILE TRP TYR ALA THR SER
SEQRES 13 B 433 GLU ASP GLY THR THR TRP LYS GLU GLU GLY VAL ALA ILE
SEQRES 14 B 433 ALA ARG PRO GLU LYS PRO LYS PRO GLY TRP ARG SER VAL
SEQRES 15 B 433 ALA THR PRO ASP ILE LEU VAL TRP LYS GLY LYS TYR TYR
SEQRES 16 B 433 LEU TYR TYR GLN ALA PHE ASN GLU PRO SER GLY LEU ARG
SEQRES 17 B 433 GLY ASP TRP CYS PRO VAL SER VAL SER TYR ALA ASP SER
SEQRES 18 B 433 PRO ASP GLY PRO TRP THR HIS GLY GLY ASP SER VAL ILE
SEQRES 19 B 433 PRO PHE GLY LYS LYS GLY GLU TRP ASP GLN ASP ALA THR
SEQRES 20 B 433 HIS ASP PRO GLN PRO ILE VAL TYR LYS GLY LYS ILE HIS
SEQRES 21 B 433 LEU TYR TYR LYS ALA ALA TYR ASN LYS TRP PRO ASP ILE
SEQRES 22 B 433 ARG ASP LYS TYR ALA VAL GLY HIS GLY LEU ALA ILE ALA
SEQRES 23 B 433 ASP ASP PRO LEU GLY PRO PHE GLU LYS HIS PRO LEU ASN
SEQRES 24 B 433 PRO VAL MET THR SER GLY HIS GLU THR THR TYR PHE PRO
SEQRES 25 B 433 PHE LYS GLU GLY VAL ALA THR LEU ALA ILE LYS ASP GLY
SEQRES 26 B 433 ASN GLU ARG TYR THR MET GLN TYR ALA LYS ASP GLY VAL
SEQRES 27 B 433 ASN PHE GLU ILE ALA SER VAL VAL SER LEU ALA PRO THR
SEQRES 28 B 433 ALA ALA ALA PRO PHE ALA ALA ASP ALA PHE THR ASP SER
SEQRES 29 B 433 GLY ASN GLY ARG GLY VAL THR TRP GLY LEU CYS HIS PHE
SEQRES 30 B 433 THR ASN ALA SER ASN ASN PRO LYS LYS GLY TYR SER ILE
SEQRES 31 B 433 ILE ALA ARG PHE ASP CYS ASP LEU SER LEU ASP VAL ASP
SEQRES 32 B 433 ASP PRO PHE TYR LYS ASN THR GLY VAL TRP HIS ARG PRO
SEQRES 33 B 433 GLU VAL TYR PHE ALA GLN ALA PRO ARG LYS ASN LEU SER
SEQRES 34 B 433 PRO GLU GLY ARG
SEQRES 1 C 433 MET GLN ILE ASN LEU PHE LEU LYS GLN SER THR PHE SER
SEQRES 2 C 433 LEU LEU MET ALA LEU SER LEU ILE ALA CYS SER GLU GLN
SEQRES 3 C 433 LYS THR GLU THR LYS SER THR PRO THR GLU ASP SER ALA
SEQRES 4 C 433 THR THR GLU HIS LYS VAL PHE PRO HIS LYS MET PRO SER
SEQRES 5 C 433 GLU LYS PRO ASP MET PRO LEU SER ALA ALA ALA GLU ARG
SEQRES 6 C 433 MET PHE SER TYR PRO ALA PRO ARG VAL GLN ASP ASN GLU
SEQRES 7 C 433 LEU PHE SER GLN PHE LYS TYR THR ARG LEU LYS GLY PHE
SEQRES 8 C 433 ASP TYR ASN ASN GLY ASP GLY THR ILE SER ARG ARG ASP
SEQRES 9 C 433 PRO SER ARG PRO ILE LEU VAL ASN GLY LYS TYR TYR ILE
SEQRES 10 C 433 TYR TYR THR LYS ARG ASP THR LYS VAL PRO PRO ILE GLY
SEQRES 11 C 433 TRP ASN ARG ALA LYS GLU ALA THR ASP GLU ILE PRO SER
SEQRES 12 C 433 THR ASP TRP ASP LEU CYS GLU ILE TRP TYR ALA THR SER
SEQRES 13 C 433 GLU ASP GLY THR THR TRP LYS GLU GLU GLY VAL ALA ILE
SEQRES 14 C 433 ALA ARG PRO GLU LYS PRO LYS PRO GLY TRP ARG SER VAL
SEQRES 15 C 433 ALA THR PRO ASP ILE LEU VAL TRP LYS GLY LYS TYR TYR
SEQRES 16 C 433 LEU TYR TYR GLN ALA PHE ASN GLU PRO SER GLY LEU ARG
SEQRES 17 C 433 GLY ASP TRP CYS PRO VAL SER VAL SER TYR ALA ASP SER
SEQRES 18 C 433 PRO ASP GLY PRO TRP THR HIS GLY GLY ASP SER VAL ILE
SEQRES 19 C 433 PRO PHE GLY LYS LYS GLY GLU TRP ASP GLN ASP ALA THR
SEQRES 20 C 433 HIS ASP PRO GLN PRO ILE VAL TYR LYS GLY LYS ILE HIS
SEQRES 21 C 433 LEU TYR TYR LYS ALA ALA TYR ASN LYS TRP PRO ASP ILE
SEQRES 22 C 433 ARG ASP LYS TYR ALA VAL GLY HIS GLY LEU ALA ILE ALA
SEQRES 23 C 433 ASP ASP PRO LEU GLY PRO PHE GLU LYS HIS PRO LEU ASN
SEQRES 24 C 433 PRO VAL MET THR SER GLY HIS GLU THR THR TYR PHE PRO
SEQRES 25 C 433 PHE LYS GLU GLY VAL ALA THR LEU ALA ILE LYS ASP GLY
SEQRES 26 C 433 ASN GLU ARG TYR THR MET GLN TYR ALA LYS ASP GLY VAL
SEQRES 27 C 433 ASN PHE GLU ILE ALA SER VAL VAL SER LEU ALA PRO THR
SEQRES 28 C 433 ALA ALA ALA PRO PHE ALA ALA ASP ALA PHE THR ASP SER
SEQRES 29 C 433 GLY ASN GLY ARG GLY VAL THR TRP GLY LEU CYS HIS PHE
SEQRES 30 C 433 THR ASN ALA SER ASN ASN PRO LYS LYS GLY TYR SER ILE
SEQRES 31 C 433 ILE ALA ARG PHE ASP CYS ASP LEU SER LEU ASP VAL ASP
SEQRES 32 C 433 ASP PRO PHE TYR LYS ASN THR GLY VAL TRP HIS ARG PRO
SEQRES 33 C 433 GLU VAL TYR PHE ALA GLN ALA PRO ARG LYS ASN LEU SER
SEQRES 34 C 433 PRO GLU GLY ARG
SEQRES 1 D 433 MET GLN ILE ASN LEU PHE LEU LYS GLN SER THR PHE SER
SEQRES 2 D 433 LEU LEU MET ALA LEU SER LEU ILE ALA CYS SER GLU GLN
SEQRES 3 D 433 LYS THR GLU THR LYS SER THR PRO THR GLU ASP SER ALA
SEQRES 4 D 433 THR THR GLU HIS LYS VAL PHE PRO HIS LYS MET PRO SER
SEQRES 5 D 433 GLU LYS PRO ASP MET PRO LEU SER ALA ALA ALA GLU ARG
SEQRES 6 D 433 MET PHE SER TYR PRO ALA PRO ARG VAL GLN ASP ASN GLU
SEQRES 7 D 433 LEU PHE SER GLN PHE LYS TYR THR ARG LEU LYS GLY PHE
SEQRES 8 D 433 ASP TYR ASN ASN GLY ASP GLY THR ILE SER ARG ARG ASP
SEQRES 9 D 433 PRO SER ARG PRO ILE LEU VAL ASN GLY LYS TYR TYR ILE
SEQRES 10 D 433 TYR TYR THR LYS ARG ASP THR LYS VAL PRO PRO ILE GLY
SEQRES 11 D 433 TRP ASN ARG ALA LYS GLU ALA THR ASP GLU ILE PRO SER
SEQRES 12 D 433 THR ASP TRP ASP LEU CYS GLU ILE TRP TYR ALA THR SER
SEQRES 13 D 433 GLU ASP GLY THR THR TRP LYS GLU GLU GLY VAL ALA ILE
SEQRES 14 D 433 ALA ARG PRO GLU LYS PRO LYS PRO GLY TRP ARG SER VAL
SEQRES 15 D 433 ALA THR PRO ASP ILE LEU VAL TRP LYS GLY LYS TYR TYR
SEQRES 16 D 433 LEU TYR TYR GLN ALA PHE ASN GLU PRO SER GLY LEU ARG
SEQRES 17 D 433 GLY ASP TRP CYS PRO VAL SER VAL SER TYR ALA ASP SER
SEQRES 18 D 433 PRO ASP GLY PRO TRP THR HIS GLY GLY ASP SER VAL ILE
SEQRES 19 D 433 PRO PHE GLY LYS LYS GLY GLU TRP ASP GLN ASP ALA THR
SEQRES 20 D 433 HIS ASP PRO GLN PRO ILE VAL TYR LYS GLY LYS ILE HIS
SEQRES 21 D 433 LEU TYR TYR LYS ALA ALA TYR ASN LYS TRP PRO ASP ILE
SEQRES 22 D 433 ARG ASP LYS TYR ALA VAL GLY HIS GLY LEU ALA ILE ALA
SEQRES 23 D 433 ASP ASP PRO LEU GLY PRO PHE GLU LYS HIS PRO LEU ASN
SEQRES 24 D 433 PRO VAL MET THR SER GLY HIS GLU THR THR TYR PHE PRO
SEQRES 25 D 433 PHE LYS GLU GLY VAL ALA THR LEU ALA ILE LYS ASP GLY
SEQRES 26 D 433 ASN GLU ARG TYR THR MET GLN TYR ALA LYS ASP GLY VAL
SEQRES 27 D 433 ASN PHE GLU ILE ALA SER VAL VAL SER LEU ALA PRO THR
SEQRES 28 D 433 ALA ALA ALA PRO PHE ALA ALA ASP ALA PHE THR ASP SER
SEQRES 29 D 433 GLY ASN GLY ARG GLY VAL THR TRP GLY LEU CYS HIS PHE
SEQRES 30 D 433 THR ASN ALA SER ASN ASN PRO LYS LYS GLY TYR SER ILE
SEQRES 31 D 433 ILE ALA ARG PHE ASP CYS ASP LEU SER LEU ASP VAL ASP
SEQRES 32 D 433 ASP PRO PHE TYR LYS ASN THR GLY VAL TRP HIS ARG PRO
SEQRES 33 D 433 GLU VAL TYR PHE ALA GLN ALA PRO ARG LYS ASN LEU SER
SEQRES 34 D 433 PRO GLU GLY ARG
HET CA A 501 1
HET CA A 502 1
HET PEG A 503 7
HET PEG A 504 7
HET EDO A 505 4
HET NA A 506 1
HET CA B 501 1
HET CA B 502 1
HET ACY B 503 4
HET EDO B 504 4
HET EDO B 505 4
HET EDO B 506 4
HET CA C 501 1
HET CA C 502 1
HET EDO C 503 4
HET EDO C 504 4
HET EDO C 505 4
HET CA D 501 1
HET CA D 502 1
HET EDO D 503 4
HET EDO D 504 4
HET EDO D 505 4
HETNAM CA CALCIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETNAM ACY ACETIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 CA 8(CA 2+)
FORMUL 7 PEG 2(C4 H10 O3)
FORMUL 9 EDO 10(C2 H6 O2)
FORMUL 10 NA NA 1+
FORMUL 13 ACY C2 H4 O2
FORMUL 27 HOH *701(H2 O)
HELIX 1 AA1 TYR A 93 ASP A 97 5 5
HELIX 2 AA2 GLY A 130 ALA A 137 5 8
HELIX 3 AA3 ASN A 383 GLY A 387 5 5
HELIX 4 AA4 ASP A 404 LYS A 408 5 5
HELIX 5 AA5 ARG A 415 ALA A 421 1 7
HELIX 6 AA6 TYR B 93 ASP B 97 5 5
HELIX 7 AA7 GLY B 130 ALA B 137 5 8
HELIX 8 AA8 ASN B 383 GLY B 387 5 5
HELIX 9 AA9 ASP B 404 LYS B 408 5 5
HELIX 10 AB1 ARG B 415 GLN B 422 1 8
HELIX 11 AB2 TYR C 93 ASP C 97 5 5
HELIX 12 AB3 GLY C 130 ALA C 137 5 8
HELIX 13 AB4 ASN C 383 GLY C 387 5 5
HELIX 14 AB5 ASP C 404 LYS C 408 5 5
HELIX 15 AB6 ARG C 415 ALA C 421 1 7
HELIX 16 AB7 TYR D 93 ASP D 97 5 5
HELIX 17 AB8 GLY D 130 ALA D 137 5 8
HELIX 18 AB9 ASN D 383 GLY D 387 5 5
HELIX 19 AC1 ASP D 404 LYS D 408 5 5
HELIX 20 AC2 ARG D 415 ALA D 421 1 7
SHEET 1 AA1 7 LYS A 84 ARG A 87 0
SHEET 2 AA1 7 ILE A 390 SER A 399 -1 O ASP A 395 N LYS A 84
SHEET 3 AA1 7 GLY A 367 PHE A 377 -1 N THR A 371 O CYS A 396
SHEET 4 AA1 7 GLU A 307 LYS A 314 -1 N LYS A 314 O GLY A 367
SHEET 5 AA1 7 GLY A 316 ILE A 322 -1 O ALA A 318 N PHE A 311
SHEET 6 AA1 7 TYR A 329 ALA A 334 -1 O THR A 330 N ALA A 321
SHEET 7 AA1 7 GLU A 341 VAL A 346 -1 O ALA A 343 N MET A 331
SHEET 1 AA2 4 LYS A 84 ARG A 87 0
SHEET 2 AA2 4 ILE A 390 SER A 399 -1 O ASP A 395 N LYS A 84
SHEET 3 AA2 4 GLY A 367 PHE A 377 -1 N THR A 371 O CYS A 396
SHEET 4 AA2 4 THR A 351 PRO A 355 -1 N ALA A 354 O LEU A 374
SHEET 1 AA3 3 ILE A 100 ARG A 103 0
SHEET 2 AA3 3 LYS A 114 ASP A 123 -1 O ARG A 122 N SER A 101
SHEET 3 AA3 3 ILE A 109 VAL A 111 -1 N VAL A 111 O LYS A 114
SHEET 1 AA4 4 ILE A 100 ARG A 103 0
SHEET 2 AA4 4 LYS A 114 ASP A 123 -1 O ARG A 122 N SER A 101
SHEET 3 AA4 4 GLU A 150 SER A 156 -1 O SER A 156 N TYR A 115
SHEET 4 AA4 4 LYS A 163 ILE A 169 -1 O LYS A 163 N THR A 155
SHEET 1 AA5 4 SER A 181 TRP A 190 0
SHEET 2 AA5 4 LYS A 193 PHE A 201 -1 O PHE A 201 N SER A 181
SHEET 3 AA5 4 VAL A 214 ALA A 219 -1 O ALA A 219 N TYR A 194
SHEET 4 AA5 4 THR A 227 GLY A 230 -1 O GLY A 229 N VAL A 216
SHEET 1 AA6 4 HIS A 248 TYR A 255 0
SHEET 2 AA6 4 LYS A 258 TYR A 267 -1 O HIS A 260 N ILE A 253
SHEET 3 AA6 4 ALA A 278 ALA A 286 -1 O ALA A 284 N LEU A 261
SHEET 4 AA6 4 GLU A 294 LYS A 295 -1 O GLU A 294 N ILE A 285
SHEET 1 AA7 7 LYS B 84 ARG B 87 0
SHEET 2 AA7 7 ILE B 390 SER B 399 -1 O ASP B 395 N LYS B 84
SHEET 3 AA7 7 GLY B 367 PHE B 377 -1 N THR B 371 O CYS B 396
SHEET 4 AA7 7 GLU B 307 LYS B 314 -1 N LYS B 314 O GLY B 367
SHEET 5 AA7 7 GLY B 316 ILE B 322 -1 O ALA B 318 N PHE B 311
SHEET 6 AA7 7 TYR B 329 ALA B 334 -1 O THR B 330 N ALA B 321
SHEET 7 AA7 7 GLU B 341 VAL B 346 -1 O ALA B 343 N MET B 331
SHEET 1 AA8 4 LYS B 84 ARG B 87 0
SHEET 2 AA8 4 ILE B 390 SER B 399 -1 O ASP B 395 N LYS B 84
SHEET 3 AA8 4 GLY B 367 PHE B 377 -1 N THR B 371 O CYS B 396
SHEET 4 AA8 4 ALA B 354 PRO B 355 -1 N ALA B 354 O LEU B 374
SHEET 1 AA9 3 ILE B 100 ARG B 103 0
SHEET 2 AA9 3 LYS B 114 ASP B 123 -1 O ARG B 122 N SER B 101
SHEET 3 AA9 3 ILE B 109 VAL B 111 -1 N VAL B 111 O LYS B 114
SHEET 1 AB1 4 ILE B 100 ARG B 103 0
SHEET 2 AB1 4 LYS B 114 ASP B 123 -1 O ARG B 122 N SER B 101
SHEET 3 AB1 4 CYS B 149 SER B 156 -1 O GLU B 150 N LYS B 121
SHEET 4 AB1 4 TRP B 162 ILE B 169 -1 O ALA B 168 N ILE B 151
SHEET 1 AB2 4 SER B 181 TRP B 190 0
SHEET 2 AB2 4 LYS B 193 PHE B 201 -1 O PHE B 201 N SER B 181
SHEET 3 AB2 4 VAL B 214 ALA B 219 -1 O ALA B 219 N TYR B 194
SHEET 4 AB2 4 THR B 227 GLY B 230 -1 O THR B 227 N TYR B 218
SHEET 1 AB3 4 HIS B 248 TYR B 255 0
SHEET 2 AB3 4 LYS B 258 TYR B 267 -1 O HIS B 260 N ILE B 253
SHEET 3 AB3 4 ALA B 278 ALA B 286 -1 O ALA B 284 N LEU B 261
SHEET 4 AB3 4 GLU B 294 LYS B 295 -1 O GLU B 294 N ILE B 285
SHEET 1 AB4 7 PHE C 83 ARG C 87 0
SHEET 2 AB4 7 ILE C 390 SER C 399 -1 O ASP C 395 N LYS C 84
SHEET 3 AB4 7 GLY C 367 PHE C 377 -1 N THR C 371 O CYS C 396
SHEET 4 AB4 7 GLU C 307 LYS C 314 -1 N LYS C 314 O GLY C 367
SHEET 5 AB4 7 GLY C 316 ILE C 322 -1 O ILE C 322 N GLU C 307
SHEET 6 AB4 7 TYR C 329 ALA C 334 -1 O THR C 330 N ALA C 321
SHEET 7 AB4 7 PHE C 340 VAL C 346 -1 O GLU C 341 N TYR C 333
SHEET 1 AB5 4 PHE C 83 ARG C 87 0
SHEET 2 AB5 4 ILE C 390 SER C 399 -1 O ASP C 395 N LYS C 84
SHEET 3 AB5 4 GLY C 367 PHE C 377 -1 N THR C 371 O CYS C 396
SHEET 4 AB5 4 THR C 351 PRO C 355 -1 N ALA C 354 O LEU C 374
SHEET 1 AB6 3 ILE C 100 ARG C 103 0
SHEET 2 AB6 3 LYS C 114 ASP C 123 -1 O ARG C 122 N SER C 101
SHEET 3 AB6 3 ILE C 109 VAL C 111 -1 N VAL C 111 O LYS C 114
SHEET 1 AB7 4 ILE C 100 ARG C 103 0
SHEET 2 AB7 4 LYS C 114 ASP C 123 -1 O ARG C 122 N SER C 101
SHEET 3 AB7 4 CYS C 149 SER C 156 -1 O GLU C 150 N LYS C 121
SHEET 4 AB7 4 LYS C 163 ILE C 169 -1 O ALA C 168 N ILE C 151
SHEET 1 AB8 4 SER C 181 TRP C 190 0
SHEET 2 AB8 4 LYS C 193 PHE C 201 -1 O PHE C 201 N SER C 181
SHEET 3 AB8 4 VAL C 214 ALA C 219 -1 O ALA C 219 N TYR C 194
SHEET 4 AB8 4 THR C 227 GLY C 230 -1 O GLY C 229 N VAL C 216
SHEET 1 AB9 4 HIS C 248 TYR C 255 0
SHEET 2 AB9 4 LYS C 258 TYR C 267 -1 O LYS C 258 N TYR C 255
SHEET 3 AB9 4 ALA C 278 ALA C 286 -1 O ALA C 284 N LEU C 261
SHEET 4 AB9 4 GLU C 294 LYS C 295 -1 O GLU C 294 N ILE C 285
SHEET 1 AC1 7 PHE D 83 ARG D 87 0
SHEET 2 AC1 7 ILE D 390 SER D 399 -1 O ASP D 395 N LYS D 84
SHEET 3 AC1 7 GLY D 367 PHE D 377 -1 N THR D 371 O CYS D 396
SHEET 4 AC1 7 GLU D 307 LYS D 314 -1 N LYS D 314 O GLY D 367
SHEET 5 AC1 7 GLY D 316 ILE D 322 -1 O ALA D 318 N PHE D 311
SHEET 6 AC1 7 TYR D 329 ALA D 334 -1 O GLN D 332 N THR D 319
SHEET 7 AC1 7 GLU D 341 VAL D 346 -1 O ALA D 343 N MET D 331
SHEET 1 AC2 4 PHE D 83 ARG D 87 0
SHEET 2 AC2 4 ILE D 390 SER D 399 -1 O ASP D 395 N LYS D 84
SHEET 3 AC2 4 GLY D 367 PHE D 377 -1 N THR D 371 O CYS D 396
SHEET 4 AC2 4 THR D 351 PRO D 355 -1 N ALA D 354 O LEU D 374
SHEET 1 AC3 3 ILE D 100 ARG D 103 0
SHEET 2 AC3 3 LYS D 114 ASP D 123 -1 O ARG D 122 N SER D 101
SHEET 3 AC3 3 ILE D 109 VAL D 111 -1 N VAL D 111 O LYS D 114
SHEET 1 AC4 4 ILE D 100 ARG D 103 0
SHEET 2 AC4 4 LYS D 114 ASP D 123 -1 O ARG D 122 N SER D 101
SHEET 3 AC4 4 GLU D 150 SER D 156 -1 O GLU D 150 N LYS D 121
SHEET 4 AC4 4 LYS D 163 ILE D 169 -1 O ALA D 168 N ILE D 151
SHEET 1 AC5 4 SER D 181 TRP D 190 0
SHEET 2 AC5 4 LYS D 193 PHE D 201 -1 O PHE D 201 N SER D 181
SHEET 3 AC5 4 VAL D 214 ALA D 219 -1 O SER D 215 N TYR D 198
SHEET 4 AC5 4 THR D 227 GLY D 230 -1 O THR D 227 N TYR D 218
SHEET 1 AC6 4 HIS D 248 TYR D 255 0
SHEET 2 AC6 4 LYS D 258 TYR D 267 -1 O HIS D 260 N ILE D 253
SHEET 3 AC6 4 ALA D 278 ALA D 286 -1 O GLY D 280 N ALA D 265
SHEET 4 AC6 4 GLU D 294 LYS D 295 -1 O GLU D 294 N ILE D 285
LINK OE1 GLU A 78 CA CA A 501 1555 1555 2.38
LINK O PRO A 292 NA NA A 506 1555 1555 2.84
LINK OD1 ASP A 397 CA CA A 501 1555 1555 2.54
LINK OD2 ASP A 397 CA CA A 501 1555 1555 2.68
LINK O SER A 399 CA CA A 501 1555 1555 2.18
LINK O VAL A 402 CA CA A 501 1555 1555 2.25
LINK CA CA A 501 O HOH A 729 1555 1555 2.58
LINK CA CA A 501 O HOH A 737 1555 1555 2.38
LINK CA CA A 502 O HOH A 633 1555 1555 2.47
LINK CA CA A 502 O HOH A 634 1555 1555 2.40
LINK CA CA A 502 O HOH A 635 1555 1555 2.18
LINK CA CA A 502 O HOH A 636 1555 1555 2.30
LINK CA CA A 502 O HOH A 637 1555 1555 2.25
LINK CA CA A 502 O HOH A 638 1555 1555 2.50
LINK CA CA A 502 O HOH A 671 1555 1555 2.59
LINK OE1 GLU B 78 CA CA B 501 1555 1555 2.17
LINK OD1 ASP B 397 CA CA B 501 1555 1555 2.58
LINK OD2 ASP B 397 CA CA B 501 1555 1555 2.79
LINK O SER B 399 CA CA B 501 1555 1555 2.28
LINK O VAL B 402 CA CA B 501 1555 1555 2.13
LINK CA CA B 501 O HOH B 671 1555 1555 2.50
LINK CA CA B 501 O HOH B 675 1555 1555 2.43
LINK CA CA B 502 O HOH B 634 1555 1555 2.52
LINK CA CA B 502 O HOH B 635 1555 1555 2.54
LINK CA CA B 502 O HOH B 636 1555 1555 2.27
LINK CA CA B 502 O HOH B 638 1555 1555 2.40
LINK CA CA B 502 O HOH B 639 1555 1555 2.55
LINK CA CA B 502 O HOH B 640 1555 1555 2.36
LINK CA CA B 502 O HOH B 641 1555 1555 2.49
LINK OE1 GLU C 78 CA CA C 501 1555 1555 2.32
LINK OD1 ASP C 397 CA CA C 501 1555 1555 2.53
LINK OD2 ASP C 397 CA CA C 501 1555 1555 2.69
LINK O SER C 399 CA CA C 501 1555 1555 2.23
LINK O VAL C 402 CA CA C 501 1555 1555 2.13
LINK CA CA C 501 O HOH C 683 1555 1555 2.54
LINK CA CA C 501 O HOH C 761 1555 1555 2.78
LINK CA CA C 501 O HOH C 762 1555 1555 2.56
LINK CA CA C 502 O HOH C 630 1555 1555 2.47
LINK CA CA C 502 O HOH C 631 1555 1555 2.31
LINK CA CA C 502 O HOH C 632 1555 1555 2.25
LINK CA CA C 502 O HOH C 633 1555 1555 2.45
LINK CA CA C 502 O HOH C 635 1555 1555 2.52
LINK CA CA C 502 O AHOH C 636 1555 1555 2.33
LINK CA CA C 502 O HOH C 637 1555 1555 2.48
LINK OE1 GLU D 78 CA CA D 501 1555 1555 2.41
LINK OD1 ASP D 397 CA CA D 501 1555 1555 2.61
LINK OD2 ASP D 397 CA CA D 501 1555 1555 2.72
LINK O SER D 399 CA CA D 501 1555 1555 2.37
LINK O VAL D 402 CA CA D 501 1555 1555 2.32
LINK CA CA D 501 O HOH D 741 1555 1555 2.19
LINK CA CA D 501 O HOH D 752 1555 1555 2.56
LINK CA CA D 501 O HOH D 753 1555 1555 2.75
LINK CA CA D 502 O HOH D 628 1555 1555 2.52
LINK CA CA D 502 O HOH D 630 1555 1555 2.61
LINK CA CA D 502 O HOH D 631 1555 1555 2.51
LINK CA CA D 502 O HOH D 632 1555 1555 2.36
LINK CA CA D 502 O HOH D 633 1555 1555 2.25
LINK CA CA D 502 O HOH D 634 1555 1555 2.37
LINK CA CA D 502 O HOH D 635 1555 1555 2.53
CISPEP 1 LYS A 174 PRO A 175 0 7.41
CISPEP 2 GLY A 224 PRO A 225 0 -16.71
CISPEP 3 GLY A 291 PRO A 292 0 7.59
CISPEP 4 ASN A 299 PRO A 300 0 -1.51
CISPEP 5 LYS B 174 PRO B 175 0 4.59
CISPEP 6 LEU B 207 ARG B 208 0 -16.05
CISPEP 7 GLY B 224 PRO B 225 0 -10.44
CISPEP 8 GLY B 291 PRO B 292 0 3.99
CISPEP 9 ASN B 299 PRO B 300 0 -3.18
CISPEP 10 LYS C 174 PRO C 175 0 10.38
CISPEP 11 LEU C 207 ARG C 208 0 20.79
CISPEP 12 GLY C 224 PRO C 225 0 2.92
CISPEP 13 GLY C 291 PRO C 292 0 11.63
CISPEP 14 ASN C 299 PRO C 300 0 -6.15
CISPEP 15 LYS D 174 PRO D 175 0 -0.43
CISPEP 16 LEU D 207 ARG D 208 0 5.25
CISPEP 17 GLY D 224 PRO D 225 0 -15.41
CISPEP 18 GLY D 291 PRO D 292 0 1.13
CISPEP 19 ASN D 299 PRO D 300 0 -0.94
SITE 1 AC1 6 GLU A 78 ASP A 397 SER A 399 VAL A 402
SITE 2 AC1 6 HOH A 729 HOH A 737
SITE 1 AC2 7 HOH A 633 HOH A 634 HOH A 635 HOH A 636
SITE 2 AC2 7 HOH A 637 HOH A 638 HOH A 671
SITE 1 AC3 6 ARG A 103 ASP A 104 THR A 184 GLN A 199
SITE 2 AC3 6 LYS A 264 GLU A 307
SITE 1 AC4 5 ALA A 137 ASP A 139 LYS A 174 TRP A 179
SITE 2 AC4 5 LYS C 239
SITE 1 AC5 5 ASP A 249 TYR A 263 THR A 308 TYR A 310
SITE 2 AC5 5 HOH A 671
SITE 1 AC6 5 ALA A 286 ASP A 287 ASP A 288 GLY A 291
SITE 2 AC6 5 PRO A 292
SITE 1 AC7 6 GLU B 78 ASP B 397 SER B 399 VAL B 402
SITE 2 AC7 6 HOH B 671 HOH B 675
SITE 1 AC8 7 HOH B 634 HOH B 635 HOH B 636 HOH B 638
SITE 2 AC8 7 HOH B 639 HOH B 640 HOH B 641
SITE 1 AC9 5 HIS A 414 THR B 351 PHE B 377 THR B 378
SITE 2 AC9 5 ASN B 379
SITE 1 AD1 8 ASP B 249 GLN B 251 TYR B 262 TYR B 263
SITE 2 AD1 8 THR B 308 TYR B 310 HOH B 639 HOH B 733
SITE 1 AD2 1 LYS B 264
SITE 1 AD3 3 GLY B 113 GLU B 157 HOH B 719
SITE 1 AD4 7 GLU C 78 ASP C 397 SER C 399 VAL C 402
SITE 2 AD4 7 HOH C 683 HOH C 761 HOH C 762
SITE 1 AD5 7 HOH C 630 HOH C 631 HOH C 632 HOH C 633
SITE 2 AD5 7 HOH C 635 HOH C 636 HOH C 637
SITE 1 AD6 2 ASP C 123 HOH C 752
SITE 1 AD7 3 GLY C 257 LYS C 258 ASP C 287
SITE 1 AD8 7 ASP C 249 GLN C 251 TYR C 262 HIS C 281
SITE 2 AD8 7 THR C 308 HOH C 635 HOH C 687
SITE 1 AD9 7 GLU D 78 ASP D 397 SER D 399 VAL D 402
SITE 2 AD9 7 HOH D 741 HOH D 752 HOH D 753
SITE 1 AE1 7 HOH D 628 HOH D 630 HOH D 631 HOH D 632
SITE 2 AE1 7 HOH D 633 HOH D 634 HOH D 635
SITE 1 AE2 3 GLU C 417 PHE C 420 ARG D 87
SITE 1 AE3 3 TYR D 153 GLU D 165 VAL D 167
SITE 1 AE4 2 ASP D 123 HOH D 746
CRYST1 187.790 223.520 225.220 90.00 90.00 90.00 F 2 2 2 64
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 0.005325 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004474 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004440 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
