HEADER ISOMERASE 13-MAR-11 3R25
TITLE CRYSTAL STRUCTURE OF ENOLASE SUPERFAMILY MEMBER FROM VIBRIONALES
TITLE 2 BACTERIUM COMPLEXED WITH MG AND GLYCEROL IN THE ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANDELATE RACEMASE / MUCONATE LACTONIZING ENZYME;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIONALES BACTERIUM SWAT-3;
SOURCE 3 ORGANISM_TAXID: 391574;
SOURCE 4 GENE: VSWAT3_13707;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENOLASE FOLD, DEHYDRATASE, MG, ACID SUGAR, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,D.WICHELECKI,J.A.GERLT,S.C.ALMO
REVDAT 2 21-FEB-24 3R25 1 REMARK SEQADV LINK
REVDAT 1 14-MAR-12 3R25 0
JRNL AUTH A.A.FEDOROV,E.V.FEDOROV,D.WICHELECKI,J.A.GERLT,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF ENOLASE SUPERFAMILY MEMBER FROM
JRNL TITL 2 VIBRIONALES BACTERIUM COMPLEXED WITH MG AND GLYCEROL IN THE
JRNL TITL 3 ACTIVE SITE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.2
REMARK 3 NUMBER OF REFLECTIONS : 419783
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.520
REMARK 3 FREE R VALUE TEST SET COUNT : 2200
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 21.3176 - 3.8585 0.97 34589 167 0.0999 0.1232
REMARK 3 2 3.8585 - 3.0655 0.99 34501 164 0.1198 0.1407
REMARK 3 3 3.0655 - 2.6789 0.98 34154 164 0.1569 0.1709
REMARK 3 4 2.6789 - 2.4343 0.97 33690 161 0.1670 0.2216
REMARK 3 5 2.4343 - 2.2600 0.96 33246 160 0.1724 0.1960
REMARK 3 6 2.2600 - 2.1269 0.94 32652 156 0.1792 0.2332
REMARK 3 7 2.1269 - 2.0205 0.93 32163 154 0.1947 0.2264
REMARK 3 8 2.0205 - 1.9326 0.89 30881 147 0.2185 0.2262
REMARK 3 9 1.9326 - 1.8582 0.84 29118 140 0.2408 0.2564
REMARK 3 10 1.8582 - 1.7942 0.80 27565 132 0.2673 0.2844
REMARK 3 11 1.7942 - 1.7381 0.77 26512 127 0.2994 0.3066
REMARK 3 12 1.7381 - 1.6884 0.72 25000 120 0.3360 0.3725
REMARK 3 13 1.6884 - 1.6440 0.68 23599 112 0.3798 0.3984
REMARK 3 14 1.6440 - 1.6039 0.58 19848 96 0.4403 0.4338
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 37.85
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.030
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.75730
REMARK 3 B22 (A**2) : -2.52580
REMARK 3 B33 (A**2) : -0.23150
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 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.2620
REMARK 3 OPERATOR: -H,-L,-K
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 26107
REMARK 3 ANGLE : 0.980 35520
REMARK 3 CHIRALITY : 0.068 3824
REMARK 3 PLANARITY : 0.004 4664
REMARK 3 DIHEDRAL : 12.895 9553
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3R25 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 477578
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.603
REMARK 200 RESOLUTION RANGE LOW (A) : 39.036
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: BALBES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M MAGNESIUM FORMATE, 0.1 M BIS
REMARK 280 -TRIS, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
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 83.99300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 105.75800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 105.83600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 83.99300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 105.75800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 105.83600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 83.99300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 105.75800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 105.83600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 83.99300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 105.75800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 105.83600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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 TOTAL BURIED SURFACE AREA: 5640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, E, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, F, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 52120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 85710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -193.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 SER A 2
REMARK 465 GLY A 157
REMARK 465 PHE A 158
REMARK 465 TYR A 159
REMARK 465 GLY A 160
REMARK 465 GLY A 161
REMARK 465 VAL A 162
REMARK 465 PRO A 163
REMARK 465 THR A 164
REMARK 465 ASP A 165
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLY C 157
REMARK 465 PHE C 158
REMARK 465 TYR C 159
REMARK 465 GLY C 160
REMARK 465 GLY C 161
REMARK 465 VAL C 162
REMARK 465 PRO C 163
REMARK 465 THR C 164
REMARK 465 ASP C 165
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 MET E 1
REMARK 465 GLY E 160
REMARK 465 GLY E 161
REMARK 465 VAL E 162
REMARK 465 PRO E 163
REMARK 465 THR E 164
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 GLY G 160
REMARK 465 GLY G 161
REMARK 465 VAL G 162
REMARK 465 PRO G 163
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 VAL H 162
REMARK 465 PRO H 163
REMARK 465 THR H 164
REMARK 465 ASP H 165
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 O HOH B 1802 O HOH B 1803 1.99
REMARK 500 O HOH F 406 O HOH F 407 2.03
REMARK 500 O HOH G 1804 O HOH G 1805 2.07
REMARK 500 O HOH C 406 O HOH C 407 2.09
REMARK 500 O HOH E 408 O HOH E 410 2.10
REMARK 500 O HOH H 407 O HOH H 408 2.13
REMARK 500 O HOH D 407 O HOH D 408 2.14
REMARK 500 OD2 ASP G 19 OD1 ASN G 341 2.16
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 ASP A 19 -116.57 -139.84
REMARK 500 TYR A 81 -72.55 65.53
REMARK 500 ASN A 84 -175.58 64.76
REMARK 500 ASP B 19 -118.27 -136.94
REMARK 500 TYR B 81 -75.59 67.63
REMARK 500 ASN B 84 74.32 63.08
REMARK 500 ASN B 262 16.23 -146.48
REMARK 500 MET B 314 146.19 -170.30
REMARK 500 ASP C 19 -114.80 -136.48
REMARK 500 GLU C 32 42.19 -89.20
REMARK 500 TYR C 81 -75.02 68.34
REMARK 500 ASN C 84 83.53 59.77
REMARK 500 ASN C 262 27.94 -144.99
REMARK 500 CYS C 281 154.07 -47.77
REMARK 500 MET C 314 140.00 -170.60
REMARK 500 ASP D 19 -115.54 -138.60
REMARK 500 TYR D 81 -74.74 65.80
REMARK 500 ASN D 84 -174.06 59.85
REMARK 500 ASP E 19 -121.42 -141.01
REMARK 500 TYR E 81 -78.37 65.84
REMARK 500 ASN E 84 177.12 64.60
REMARK 500 PHE E 158 -174.62 -56.12
REMARK 500 ASN E 262 16.35 -145.12
REMARK 500 PHE E 379 68.27 -118.81
REMARK 500 ASP F 19 -113.48 -136.59
REMARK 500 TYR F 81 -74.99 64.64
REMARK 500 ASN F 84 -179.98 59.80
REMARK 500 ASN F 262 13.23 -144.77
REMARK 500 MET F 314 144.06 -172.42
REMARK 500 ASP G 19 -120.30 -141.16
REMARK 500 ASP G 19 -116.03 -148.95
REMARK 500 TYR G 81 -74.41 68.60
REMARK 500 ASP G 165 65.39 33.37
REMARK 500 ASN G 262 17.88 -140.47
REMARK 500 ASP H 19 -110.31 -153.43
REMARK 500 TYR H 81 -76.59 69.77
REMARK 500 ASN H 84 -170.63 68.36
REMARK 500 MET H 314 140.09 -171.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 207 OD2
REMARK 620 2 GLU A 233 OE2 96.4
REMARK 620 3 GLU A 259 OE1 159.8 75.4
REMARK 620 4 HOH A 405 O 93.8 167.8 92.8
REMARK 620 5 HOH A 406 O 78.8 88.1 82.4 87.2
REMARK 620 6 HOH A 408 O 96.4 91.0 102.1 94.6 175.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 207 OD2
REMARK 620 2 GLU B 233 OE2 91.6
REMARK 620 3 GLU B 259 OE1 160.4 77.4
REMARK 620 4 HOH B 407 O 93.5 174.9 97.7
REMARK 620 5 HOH B 408 O 81.9 87.7 81.5 92.8
REMARK 620 6 HOH B1802 O 91.6 94.3 105.1 85.8 173.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1473 O
REMARK 620 2 HOH B1542 O 86.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 207 OD2
REMARK 620 2 GLU C 233 OE2 93.6
REMARK 620 3 GLU C 259 OE1 171.9 78.8
REMARK 620 4 HOH C 404 O 96.4 167.9 91.5
REMARK 620 5 HOH C 405 O 86.0 90.2 91.0 97.2
REMARK 620 6 HOH C 407 O 87.9 92.1 95.3 81.6 173.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 207 OD2
REMARK 620 2 GLU D 233 OE2 96.8
REMARK 620 3 GLU D 259 OE1 170.3 78.2
REMARK 620 4 HOH D 405 O 98.9 164.2 86.6
REMARK 620 5 HOH D 406 O 89.6 96.1 82.8 86.3
REMARK 620 6 HOH D 408 O 87.0 93.6 101.5 85.1 170.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 756 O
REMARK 620 2 HOH D1632 O 72.1
REMARK 620 3 HOH D1874 O 69.8 88.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 207 OD2
REMARK 620 2 GLU E 233 OE2 93.1
REMARK 620 3 GLU E 259 OE1 173.0 81.2
REMARK 620 4 HOH E 405 O 94.6 169.5 91.5
REMARK 620 5 HOH E 407 O 87.2 96.1 89.3 91.3
REMARK 620 6 HOH E 410 O 86.0 88.4 97.9 85.2 172.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 207 OD2
REMARK 620 2 GLU F 233 OE2 94.1
REMARK 620 3 GLU F 259 OE1 168.0 77.7
REMARK 620 4 HOH F 404 O 93.8 171.7 94.8
REMARK 620 5 HOH F 405 O 83.8 86.3 86.9 96.8
REMARK 620 6 HOH F 407 O 89.0 91.0 99.8 86.8 172.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 207 OD2
REMARK 620 2 GLU G 233 OE2 95.0
REMARK 620 3 GLU G 259 OE1 158.3 75.4
REMARK 620 4 HOH G 404 O 100.2 164.8 90.2
REMARK 620 5 HOH G 405 O 82.5 87.7 77.8 93.9
REMARK 620 6 HOH G1804 O 98.6 94.9 101.6 83.2 177.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 207 OD2
REMARK 620 2 GLU H 233 OE2 98.7
REMARK 620 3 GLU H 259 OE1 169.9 79.1
REMARK 620 4 HOH H 405 O 93.8 167.4 88.3
REMARK 620 5 HOH H 406 O 86.8 89.5 83.3 89.4
REMARK 620 6 HOH H 408 O 89.0 97.4 101.1 84.5 172.4
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 MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 403
DBREF 3R25 A 1 401 UNP A5KUH4 A5KUH4_9GAMM 1 399
DBREF 3R25 B 1 401 UNP A5KUH4 A5KUH4_9GAMM 1 399
DBREF 3R25 C 1 401 UNP A5KUH4 A5KUH4_9GAMM 1 399
DBREF 3R25 D 1 401 UNP A5KUH4 A5KUH4_9GAMM 1 399
DBREF 3R25 E 1 401 UNP A5KUH4 A5KUH4_9GAMM 1 399
DBREF 3R25 F 1 401 UNP A5KUH4 A5KUH4_9GAMM 1 399
DBREF 3R25 G 1 401 UNP A5KUH4 A5KUH4_9GAMM 1 399
DBREF 3R25 H 1 401 UNP A5KUH4 A5KUH4_9GAMM 1 399
SEQADV 3R25 SER A 2 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 LEU A 3 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 SER B 2 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 LEU B 3 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 SER C 2 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 LEU C 3 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 SER D 2 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 LEU D 3 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 SER E 2 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 LEU E 3 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 SER F 2 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 LEU F 3 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 SER G 2 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 LEU G 3 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 SER H 2 UNP A5KUH4 EXPRESSION TAG
SEQADV 3R25 LEU H 3 UNP A5KUH4 EXPRESSION TAG
SEQRES 1 A 401 MET SER LEU LYS GLU THR ILE ILE SER ASP ILE HIS CYS
SEQRES 2 A 401 ILE ILE THR LYS PRO ASP ARG HIS ASN LEU ILE THR VAL
SEQRES 3 A 401 VAL VAL GLU THR ASN GLU GLY VAL THR GLY PHE GLY CYS
SEQRES 4 A 401 ALA THR PHE GLN GLN ARG PRO LEU ALA VAL LYS THR MET
SEQRES 5 A 401 VAL ASP GLU TYR LEU LYS PRO ILE LEU ILE GLY LYS ASN
SEQRES 6 A 401 ALA ASN ASN ILE GLU ASP LEU TRP GLN MET MET MET VAL
SEQRES 7 A 401 ASN ALA TYR TRP ARG ASN GLY PRO VAL ILE ASN ASN ALA
SEQRES 8 A 401 ILE SER GLY VAL ASP MET ALA LEU TRP ASP ILE LYS ALA
SEQRES 9 A 401 LYS LEU ALA GLY MET PRO LEU HIS GLN LEU PHE GLY GLY
SEQRES 10 A 401 LYS SER ARG ASP ALA ILE PRO VAL TYR THR HIS ALA THR
SEQRES 11 A 401 SER ASP THR MET GLU GLY ILE TYR ASP LEU VAL GLU GLY
SEQRES 12 A 401 PHE LEU GLU LYS GLY TYR LYS HIS ILE ARG CYS GLN LEU
SEQRES 13 A 401 GLY PHE TYR GLY GLY VAL PRO THR ASP LEU HIS THR THR
SEQRES 14 A 401 GLN ASN PRO THR GLU GLY SER TYR TYR ASP GLN ASP GLN
SEQRES 15 A 401 TYR MET ASP ASN THR LEU THR MET PHE LYS SER LEU ARG
SEQRES 16 A 401 GLU LYS TYR GLY ASN GLN PHE HIS ILE LEU HIS ASP VAL
SEQRES 17 A 401 HIS GLU ARG LEU PHE PRO ASN GLN ALA ILE GLN PHE ALA
SEQRES 18 A 401 LYS GLU VAL GLU GLN TYR LYS PRO TYR PHE ILE GLU ASP
SEQRES 19 A 401 ILE LEU PRO PRO ASN GLN THR GLU TRP LEU ASP ASN ILE
SEQRES 20 A 401 ARG SER GLN SER SER VAL SER LEU GLY LEU GLY GLU LEU
SEQRES 21 A 401 PHE ASN ASN PRO GLU GLU TRP LYS SER LEU ILE ALA ASN
SEQRES 22 A 401 ARG ARG ILE ASP PHE ILE ARG CYS HIS VAL SER GLN ILE
SEQRES 23 A 401 GLY GLY ILE THR PRO ALA LEU LYS LEU GLY HIS LEU CYS
SEQRES 24 A 401 GLN ASN PHE GLY VAL ARG ILE ALA TRP HIS CYS PRO PRO
SEQRES 25 A 401 ASP MET THR PRO ILE GLY ALA ALA VAL ASN THR HIS LEU
SEQRES 26 A 401 ASN VAL HIS LEU HIS ASN ALA ALA ILE GLN GLU HIS VAL
SEQRES 27 A 401 GLU TYR ASN GLY ASN THR HIS LYS VAL PHE PRO ASN ALA
SEQRES 28 A 401 ALA GLU PRO ILE ASN GLY TYR LEU TYR ALA SER GLU ILE
SEQRES 29 A 401 ALA GLY ILE GLY VAL GLU ILE ASP ARG GLU ALA ALA ALA
SEQRES 30 A 401 GLU PHE PRO VAL MET TYR ARG PRO HIS GLU TRP THR GLN
SEQRES 31 A 401 SER ARG LEU PRO ASP GLY ALA ILE HIS THR PRO
SEQRES 1 B 401 MET SER LEU LYS GLU THR ILE ILE SER ASP ILE HIS CYS
SEQRES 2 B 401 ILE ILE THR LYS PRO ASP ARG HIS ASN LEU ILE THR VAL
SEQRES 3 B 401 VAL VAL GLU THR ASN GLU GLY VAL THR GLY PHE GLY CYS
SEQRES 4 B 401 ALA THR PHE GLN GLN ARG PRO LEU ALA VAL LYS THR MET
SEQRES 5 B 401 VAL ASP GLU TYR LEU LYS PRO ILE LEU ILE GLY LYS ASN
SEQRES 6 B 401 ALA ASN ASN ILE GLU ASP LEU TRP GLN MET MET MET VAL
SEQRES 7 B 401 ASN ALA TYR TRP ARG ASN GLY PRO VAL ILE ASN ASN ALA
SEQRES 8 B 401 ILE SER GLY VAL ASP MET ALA LEU TRP ASP ILE LYS ALA
SEQRES 9 B 401 LYS LEU ALA GLY MET PRO LEU HIS GLN LEU PHE GLY GLY
SEQRES 10 B 401 LYS SER ARG ASP ALA ILE PRO VAL TYR THR HIS ALA THR
SEQRES 11 B 401 SER ASP THR MET GLU GLY ILE TYR ASP LEU VAL GLU GLY
SEQRES 12 B 401 PHE LEU GLU LYS GLY TYR LYS HIS ILE ARG CYS GLN LEU
SEQRES 13 B 401 GLY PHE TYR GLY GLY VAL PRO THR ASP LEU HIS THR THR
SEQRES 14 B 401 GLN ASN PRO THR GLU GLY SER TYR TYR ASP GLN ASP GLN
SEQRES 15 B 401 TYR MET ASP ASN THR LEU THR MET PHE LYS SER LEU ARG
SEQRES 16 B 401 GLU LYS TYR GLY ASN GLN PHE HIS ILE LEU HIS ASP VAL
SEQRES 17 B 401 HIS GLU ARG LEU PHE PRO ASN GLN ALA ILE GLN PHE ALA
SEQRES 18 B 401 LYS GLU VAL GLU GLN TYR LYS PRO TYR PHE ILE GLU ASP
SEQRES 19 B 401 ILE LEU PRO PRO ASN GLN THR GLU TRP LEU ASP ASN ILE
SEQRES 20 B 401 ARG SER GLN SER SER VAL SER LEU GLY LEU GLY GLU LEU
SEQRES 21 B 401 PHE ASN ASN PRO GLU GLU TRP LYS SER LEU ILE ALA ASN
SEQRES 22 B 401 ARG ARG ILE ASP PHE ILE ARG CYS HIS VAL SER GLN ILE
SEQRES 23 B 401 GLY GLY ILE THR PRO ALA LEU LYS LEU GLY HIS LEU CYS
SEQRES 24 B 401 GLN ASN PHE GLY VAL ARG ILE ALA TRP HIS CYS PRO PRO
SEQRES 25 B 401 ASP MET THR PRO ILE GLY ALA ALA VAL ASN THR HIS LEU
SEQRES 26 B 401 ASN VAL HIS LEU HIS ASN ALA ALA ILE GLN GLU HIS VAL
SEQRES 27 B 401 GLU TYR ASN GLY ASN THR HIS LYS VAL PHE PRO ASN ALA
SEQRES 28 B 401 ALA GLU PRO ILE ASN GLY TYR LEU TYR ALA SER GLU ILE
SEQRES 29 B 401 ALA GLY ILE GLY VAL GLU ILE ASP ARG GLU ALA ALA ALA
SEQRES 30 B 401 GLU PHE PRO VAL MET TYR ARG PRO HIS GLU TRP THR GLN
SEQRES 31 B 401 SER ARG LEU PRO ASP GLY ALA ILE HIS THR PRO
SEQRES 1 C 401 MET SER LEU LYS GLU THR ILE ILE SER ASP ILE HIS CYS
SEQRES 2 C 401 ILE ILE THR LYS PRO ASP ARG HIS ASN LEU ILE THR VAL
SEQRES 3 C 401 VAL VAL GLU THR ASN GLU GLY VAL THR GLY PHE GLY CYS
SEQRES 4 C 401 ALA THR PHE GLN GLN ARG PRO LEU ALA VAL LYS THR MET
SEQRES 5 C 401 VAL ASP GLU TYR LEU LYS PRO ILE LEU ILE GLY LYS ASN
SEQRES 6 C 401 ALA ASN ASN ILE GLU ASP LEU TRP GLN MET MET MET VAL
SEQRES 7 C 401 ASN ALA TYR TRP ARG ASN GLY PRO VAL ILE ASN ASN ALA
SEQRES 8 C 401 ILE SER GLY VAL ASP MET ALA LEU TRP ASP ILE LYS ALA
SEQRES 9 C 401 LYS LEU ALA GLY MET PRO LEU HIS GLN LEU PHE GLY GLY
SEQRES 10 C 401 LYS SER ARG ASP ALA ILE PRO VAL TYR THR HIS ALA THR
SEQRES 11 C 401 SER ASP THR MET GLU GLY ILE TYR ASP LEU VAL GLU GLY
SEQRES 12 C 401 PHE LEU GLU LYS GLY TYR LYS HIS ILE ARG CYS GLN LEU
SEQRES 13 C 401 GLY PHE TYR GLY GLY VAL PRO THR ASP LEU HIS THR THR
SEQRES 14 C 401 GLN ASN PRO THR GLU GLY SER TYR TYR ASP GLN ASP GLN
SEQRES 15 C 401 TYR MET ASP ASN THR LEU THR MET PHE LYS SER LEU ARG
SEQRES 16 C 401 GLU LYS TYR GLY ASN GLN PHE HIS ILE LEU HIS ASP VAL
SEQRES 17 C 401 HIS GLU ARG LEU PHE PRO ASN GLN ALA ILE GLN PHE ALA
SEQRES 18 C 401 LYS GLU VAL GLU GLN TYR LYS PRO TYR PHE ILE GLU ASP
SEQRES 19 C 401 ILE LEU PRO PRO ASN GLN THR GLU TRP LEU ASP ASN ILE
SEQRES 20 C 401 ARG SER GLN SER SER VAL SER LEU GLY LEU GLY GLU LEU
SEQRES 21 C 401 PHE ASN ASN PRO GLU GLU TRP LYS SER LEU ILE ALA ASN
SEQRES 22 C 401 ARG ARG ILE ASP PHE ILE ARG CYS HIS VAL SER GLN ILE
SEQRES 23 C 401 GLY GLY ILE THR PRO ALA LEU LYS LEU GLY HIS LEU CYS
SEQRES 24 C 401 GLN ASN PHE GLY VAL ARG ILE ALA TRP HIS CYS PRO PRO
SEQRES 25 C 401 ASP MET THR PRO ILE GLY ALA ALA VAL ASN THR HIS LEU
SEQRES 26 C 401 ASN VAL HIS LEU HIS ASN ALA ALA ILE GLN GLU HIS VAL
SEQRES 27 C 401 GLU TYR ASN GLY ASN THR HIS LYS VAL PHE PRO ASN ALA
SEQRES 28 C 401 ALA GLU PRO ILE ASN GLY TYR LEU TYR ALA SER GLU ILE
SEQRES 29 C 401 ALA GLY ILE GLY VAL GLU ILE ASP ARG GLU ALA ALA ALA
SEQRES 30 C 401 GLU PHE PRO VAL MET TYR ARG PRO HIS GLU TRP THR GLN
SEQRES 31 C 401 SER ARG LEU PRO ASP GLY ALA ILE HIS THR PRO
SEQRES 1 D 401 MET SER LEU LYS GLU THR ILE ILE SER ASP ILE HIS CYS
SEQRES 2 D 401 ILE ILE THR LYS PRO ASP ARG HIS ASN LEU ILE THR VAL
SEQRES 3 D 401 VAL VAL GLU THR ASN GLU GLY VAL THR GLY PHE GLY CYS
SEQRES 4 D 401 ALA THR PHE GLN GLN ARG PRO LEU ALA VAL LYS THR MET
SEQRES 5 D 401 VAL ASP GLU TYR LEU LYS PRO ILE LEU ILE GLY LYS ASN
SEQRES 6 D 401 ALA ASN ASN ILE GLU ASP LEU TRP GLN MET MET MET VAL
SEQRES 7 D 401 ASN ALA TYR TRP ARG ASN GLY PRO VAL ILE ASN ASN ALA
SEQRES 8 D 401 ILE SER GLY VAL ASP MET ALA LEU TRP ASP ILE LYS ALA
SEQRES 9 D 401 LYS LEU ALA GLY MET PRO LEU HIS GLN LEU PHE GLY GLY
SEQRES 10 D 401 LYS SER ARG ASP ALA ILE PRO VAL TYR THR HIS ALA THR
SEQRES 11 D 401 SER ASP THR MET GLU GLY ILE TYR ASP LEU VAL GLU GLY
SEQRES 12 D 401 PHE LEU GLU LYS GLY TYR LYS HIS ILE ARG CYS GLN LEU
SEQRES 13 D 401 GLY PHE TYR GLY GLY VAL PRO THR ASP LEU HIS THR THR
SEQRES 14 D 401 GLN ASN PRO THR GLU GLY SER TYR TYR ASP GLN ASP GLN
SEQRES 15 D 401 TYR MET ASP ASN THR LEU THR MET PHE LYS SER LEU ARG
SEQRES 16 D 401 GLU LYS TYR GLY ASN GLN PHE HIS ILE LEU HIS ASP VAL
SEQRES 17 D 401 HIS GLU ARG LEU PHE PRO ASN GLN ALA ILE GLN PHE ALA
SEQRES 18 D 401 LYS GLU VAL GLU GLN TYR LYS PRO TYR PHE ILE GLU ASP
SEQRES 19 D 401 ILE LEU PRO PRO ASN GLN THR GLU TRP LEU ASP ASN ILE
SEQRES 20 D 401 ARG SER GLN SER SER VAL SER LEU GLY LEU GLY GLU LEU
SEQRES 21 D 401 PHE ASN ASN PRO GLU GLU TRP LYS SER LEU ILE ALA ASN
SEQRES 22 D 401 ARG ARG ILE ASP PHE ILE ARG CYS HIS VAL SER GLN ILE
SEQRES 23 D 401 GLY GLY ILE THR PRO ALA LEU LYS LEU GLY HIS LEU CYS
SEQRES 24 D 401 GLN ASN PHE GLY VAL ARG ILE ALA TRP HIS CYS PRO PRO
SEQRES 25 D 401 ASP MET THR PRO ILE GLY ALA ALA VAL ASN THR HIS LEU
SEQRES 26 D 401 ASN VAL HIS LEU HIS ASN ALA ALA ILE GLN GLU HIS VAL
SEQRES 27 D 401 GLU TYR ASN GLY ASN THR HIS LYS VAL PHE PRO ASN ALA
SEQRES 28 D 401 ALA GLU PRO ILE ASN GLY TYR LEU TYR ALA SER GLU ILE
SEQRES 29 D 401 ALA GLY ILE GLY VAL GLU ILE ASP ARG GLU ALA ALA ALA
SEQRES 30 D 401 GLU PHE PRO VAL MET TYR ARG PRO HIS GLU TRP THR GLN
SEQRES 31 D 401 SER ARG LEU PRO ASP GLY ALA ILE HIS THR PRO
SEQRES 1 E 401 MET SER LEU LYS GLU THR ILE ILE SER ASP ILE HIS CYS
SEQRES 2 E 401 ILE ILE THR LYS PRO ASP ARG HIS ASN LEU ILE THR VAL
SEQRES 3 E 401 VAL VAL GLU THR ASN GLU GLY VAL THR GLY PHE GLY CYS
SEQRES 4 E 401 ALA THR PHE GLN GLN ARG PRO LEU ALA VAL LYS THR MET
SEQRES 5 E 401 VAL ASP GLU TYR LEU LYS PRO ILE LEU ILE GLY LYS ASN
SEQRES 6 E 401 ALA ASN ASN ILE GLU ASP LEU TRP GLN MET MET MET VAL
SEQRES 7 E 401 ASN ALA TYR TRP ARG ASN GLY PRO VAL ILE ASN ASN ALA
SEQRES 8 E 401 ILE SER GLY VAL ASP MET ALA LEU TRP ASP ILE LYS ALA
SEQRES 9 E 401 LYS LEU ALA GLY MET PRO LEU HIS GLN LEU PHE GLY GLY
SEQRES 10 E 401 LYS SER ARG ASP ALA ILE PRO VAL TYR THR HIS ALA THR
SEQRES 11 E 401 SER ASP THR MET GLU GLY ILE TYR ASP LEU VAL GLU GLY
SEQRES 12 E 401 PHE LEU GLU LYS GLY TYR LYS HIS ILE ARG CYS GLN LEU
SEQRES 13 E 401 GLY PHE TYR GLY GLY VAL PRO THR ASP LEU HIS THR THR
SEQRES 14 E 401 GLN ASN PRO THR GLU GLY SER TYR TYR ASP GLN ASP GLN
SEQRES 15 E 401 TYR MET ASP ASN THR LEU THR MET PHE LYS SER LEU ARG
SEQRES 16 E 401 GLU LYS TYR GLY ASN GLN PHE HIS ILE LEU HIS ASP VAL
SEQRES 17 E 401 HIS GLU ARG LEU PHE PRO ASN GLN ALA ILE GLN PHE ALA
SEQRES 18 E 401 LYS GLU VAL GLU GLN TYR LYS PRO TYR PHE ILE GLU ASP
SEQRES 19 E 401 ILE LEU PRO PRO ASN GLN THR GLU TRP LEU ASP ASN ILE
SEQRES 20 E 401 ARG SER GLN SER SER VAL SER LEU GLY LEU GLY GLU LEU
SEQRES 21 E 401 PHE ASN ASN PRO GLU GLU TRP LYS SER LEU ILE ALA ASN
SEQRES 22 E 401 ARG ARG ILE ASP PHE ILE ARG CYS HIS VAL SER GLN ILE
SEQRES 23 E 401 GLY GLY ILE THR PRO ALA LEU LYS LEU GLY HIS LEU CYS
SEQRES 24 E 401 GLN ASN PHE GLY VAL ARG ILE ALA TRP HIS CYS PRO PRO
SEQRES 25 E 401 ASP MET THR PRO ILE GLY ALA ALA VAL ASN THR HIS LEU
SEQRES 26 E 401 ASN VAL HIS LEU HIS ASN ALA ALA ILE GLN GLU HIS VAL
SEQRES 27 E 401 GLU TYR ASN GLY ASN THR HIS LYS VAL PHE PRO ASN ALA
SEQRES 28 E 401 ALA GLU PRO ILE ASN GLY TYR LEU TYR ALA SER GLU ILE
SEQRES 29 E 401 ALA GLY ILE GLY VAL GLU ILE ASP ARG GLU ALA ALA ALA
SEQRES 30 E 401 GLU PHE PRO VAL MET TYR ARG PRO HIS GLU TRP THR GLN
SEQRES 31 E 401 SER ARG LEU PRO ASP GLY ALA ILE HIS THR PRO
SEQRES 1 F 401 MET SER LEU LYS GLU THR ILE ILE SER ASP ILE HIS CYS
SEQRES 2 F 401 ILE ILE THR LYS PRO ASP ARG HIS ASN LEU ILE THR VAL
SEQRES 3 F 401 VAL VAL GLU THR ASN GLU GLY VAL THR GLY PHE GLY CYS
SEQRES 4 F 401 ALA THR PHE GLN GLN ARG PRO LEU ALA VAL LYS THR MET
SEQRES 5 F 401 VAL ASP GLU TYR LEU LYS PRO ILE LEU ILE GLY LYS ASN
SEQRES 6 F 401 ALA ASN ASN ILE GLU ASP LEU TRP GLN MET MET MET VAL
SEQRES 7 F 401 ASN ALA TYR TRP ARG ASN GLY PRO VAL ILE ASN ASN ALA
SEQRES 8 F 401 ILE SER GLY VAL ASP MET ALA LEU TRP ASP ILE LYS ALA
SEQRES 9 F 401 LYS LEU ALA GLY MET PRO LEU HIS GLN LEU PHE GLY GLY
SEQRES 10 F 401 LYS SER ARG ASP ALA ILE PRO VAL TYR THR HIS ALA THR
SEQRES 11 F 401 SER ASP THR MET GLU GLY ILE TYR ASP LEU VAL GLU GLY
SEQRES 12 F 401 PHE LEU GLU LYS GLY TYR LYS HIS ILE ARG CYS GLN LEU
SEQRES 13 F 401 GLY PHE TYR GLY GLY VAL PRO THR ASP LEU HIS THR THR
SEQRES 14 F 401 GLN ASN PRO THR GLU GLY SER TYR TYR ASP GLN ASP GLN
SEQRES 15 F 401 TYR MET ASP ASN THR LEU THR MET PHE LYS SER LEU ARG
SEQRES 16 F 401 GLU LYS TYR GLY ASN GLN PHE HIS ILE LEU HIS ASP VAL
SEQRES 17 F 401 HIS GLU ARG LEU PHE PRO ASN GLN ALA ILE GLN PHE ALA
SEQRES 18 F 401 LYS GLU VAL GLU GLN TYR LYS PRO TYR PHE ILE GLU ASP
SEQRES 19 F 401 ILE LEU PRO PRO ASN GLN THR GLU TRP LEU ASP ASN ILE
SEQRES 20 F 401 ARG SER GLN SER SER VAL SER LEU GLY LEU GLY GLU LEU
SEQRES 21 F 401 PHE ASN ASN PRO GLU GLU TRP LYS SER LEU ILE ALA ASN
SEQRES 22 F 401 ARG ARG ILE ASP PHE ILE ARG CYS HIS VAL SER GLN ILE
SEQRES 23 F 401 GLY GLY ILE THR PRO ALA LEU LYS LEU GLY HIS LEU CYS
SEQRES 24 F 401 GLN ASN PHE GLY VAL ARG ILE ALA TRP HIS CYS PRO PRO
SEQRES 25 F 401 ASP MET THR PRO ILE GLY ALA ALA VAL ASN THR HIS LEU
SEQRES 26 F 401 ASN VAL HIS LEU HIS ASN ALA ALA ILE GLN GLU HIS VAL
SEQRES 27 F 401 GLU TYR ASN GLY ASN THR HIS LYS VAL PHE PRO ASN ALA
SEQRES 28 F 401 ALA GLU PRO ILE ASN GLY TYR LEU TYR ALA SER GLU ILE
SEQRES 29 F 401 ALA GLY ILE GLY VAL GLU ILE ASP ARG GLU ALA ALA ALA
SEQRES 30 F 401 GLU PHE PRO VAL MET TYR ARG PRO HIS GLU TRP THR GLN
SEQRES 31 F 401 SER ARG LEU PRO ASP GLY ALA ILE HIS THR PRO
SEQRES 1 G 401 MET SER LEU LYS GLU THR ILE ILE SER ASP ILE HIS CYS
SEQRES 2 G 401 ILE ILE THR LYS PRO ASP ARG HIS ASN LEU ILE THR VAL
SEQRES 3 G 401 VAL VAL GLU THR ASN GLU GLY VAL THR GLY PHE GLY CYS
SEQRES 4 G 401 ALA THR PHE GLN GLN ARG PRO LEU ALA VAL LYS THR MET
SEQRES 5 G 401 VAL ASP GLU TYR LEU LYS PRO ILE LEU ILE GLY LYS ASN
SEQRES 6 G 401 ALA ASN ASN ILE GLU ASP LEU TRP GLN MET MET MET VAL
SEQRES 7 G 401 ASN ALA TYR TRP ARG ASN GLY PRO VAL ILE ASN ASN ALA
SEQRES 8 G 401 ILE SER GLY VAL ASP MET ALA LEU TRP ASP ILE LYS ALA
SEQRES 9 G 401 LYS LEU ALA GLY MET PRO LEU HIS GLN LEU PHE GLY GLY
SEQRES 10 G 401 LYS SER ARG ASP ALA ILE PRO VAL TYR THR HIS ALA THR
SEQRES 11 G 401 SER ASP THR MET GLU GLY ILE TYR ASP LEU VAL GLU GLY
SEQRES 12 G 401 PHE LEU GLU LYS GLY TYR LYS HIS ILE ARG CYS GLN LEU
SEQRES 13 G 401 GLY PHE TYR GLY GLY VAL PRO THR ASP LEU HIS THR THR
SEQRES 14 G 401 GLN ASN PRO THR GLU GLY SER TYR TYR ASP GLN ASP GLN
SEQRES 15 G 401 TYR MET ASP ASN THR LEU THR MET PHE LYS SER LEU ARG
SEQRES 16 G 401 GLU LYS TYR GLY ASN GLN PHE HIS ILE LEU HIS ASP VAL
SEQRES 17 G 401 HIS GLU ARG LEU PHE PRO ASN GLN ALA ILE GLN PHE ALA
SEQRES 18 G 401 LYS GLU VAL GLU GLN TYR LYS PRO TYR PHE ILE GLU ASP
SEQRES 19 G 401 ILE LEU PRO PRO ASN GLN THR GLU TRP LEU ASP ASN ILE
SEQRES 20 G 401 ARG SER GLN SER SER VAL SER LEU GLY LEU GLY GLU LEU
SEQRES 21 G 401 PHE ASN ASN PRO GLU GLU TRP LYS SER LEU ILE ALA ASN
SEQRES 22 G 401 ARG ARG ILE ASP PHE ILE ARG CYS HIS VAL SER GLN ILE
SEQRES 23 G 401 GLY GLY ILE THR PRO ALA LEU LYS LEU GLY HIS LEU CYS
SEQRES 24 G 401 GLN ASN PHE GLY VAL ARG ILE ALA TRP HIS CYS PRO PRO
SEQRES 25 G 401 ASP MET THR PRO ILE GLY ALA ALA VAL ASN THR HIS LEU
SEQRES 26 G 401 ASN VAL HIS LEU HIS ASN ALA ALA ILE GLN GLU HIS VAL
SEQRES 27 G 401 GLU TYR ASN GLY ASN THR HIS LYS VAL PHE PRO ASN ALA
SEQRES 28 G 401 ALA GLU PRO ILE ASN GLY TYR LEU TYR ALA SER GLU ILE
SEQRES 29 G 401 ALA GLY ILE GLY VAL GLU ILE ASP ARG GLU ALA ALA ALA
SEQRES 30 G 401 GLU PHE PRO VAL MET TYR ARG PRO HIS GLU TRP THR GLN
SEQRES 31 G 401 SER ARG LEU PRO ASP GLY ALA ILE HIS THR PRO
SEQRES 1 H 401 MET SER LEU LYS GLU THR ILE ILE SER ASP ILE HIS CYS
SEQRES 2 H 401 ILE ILE THR LYS PRO ASP ARG HIS ASN LEU ILE THR VAL
SEQRES 3 H 401 VAL VAL GLU THR ASN GLU GLY VAL THR GLY PHE GLY CYS
SEQRES 4 H 401 ALA THR PHE GLN GLN ARG PRO LEU ALA VAL LYS THR MET
SEQRES 5 H 401 VAL ASP GLU TYR LEU LYS PRO ILE LEU ILE GLY LYS ASN
SEQRES 6 H 401 ALA ASN ASN ILE GLU ASP LEU TRP GLN MET MET MET VAL
SEQRES 7 H 401 ASN ALA TYR TRP ARG ASN GLY PRO VAL ILE ASN ASN ALA
SEQRES 8 H 401 ILE SER GLY VAL ASP MET ALA LEU TRP ASP ILE LYS ALA
SEQRES 9 H 401 LYS LEU ALA GLY MET PRO LEU HIS GLN LEU PHE GLY GLY
SEQRES 10 H 401 LYS SER ARG ASP ALA ILE PRO VAL TYR THR HIS ALA THR
SEQRES 11 H 401 SER ASP THR MET GLU GLY ILE TYR ASP LEU VAL GLU GLY
SEQRES 12 H 401 PHE LEU GLU LYS GLY TYR LYS HIS ILE ARG CYS GLN LEU
SEQRES 13 H 401 GLY PHE TYR GLY GLY VAL PRO THR ASP LEU HIS THR THR
SEQRES 14 H 401 GLN ASN PRO THR GLU GLY SER TYR TYR ASP GLN ASP GLN
SEQRES 15 H 401 TYR MET ASP ASN THR LEU THR MET PHE LYS SER LEU ARG
SEQRES 16 H 401 GLU LYS TYR GLY ASN GLN PHE HIS ILE LEU HIS ASP VAL
SEQRES 17 H 401 HIS GLU ARG LEU PHE PRO ASN GLN ALA ILE GLN PHE ALA
SEQRES 18 H 401 LYS GLU VAL GLU GLN TYR LYS PRO TYR PHE ILE GLU ASP
SEQRES 19 H 401 ILE LEU PRO PRO ASN GLN THR GLU TRP LEU ASP ASN ILE
SEQRES 20 H 401 ARG SER GLN SER SER VAL SER LEU GLY LEU GLY GLU LEU
SEQRES 21 H 401 PHE ASN ASN PRO GLU GLU TRP LYS SER LEU ILE ALA ASN
SEQRES 22 H 401 ARG ARG ILE ASP PHE ILE ARG CYS HIS VAL SER GLN ILE
SEQRES 23 H 401 GLY GLY ILE THR PRO ALA LEU LYS LEU GLY HIS LEU CYS
SEQRES 24 H 401 GLN ASN PHE GLY VAL ARG ILE ALA TRP HIS CYS PRO PRO
SEQRES 25 H 401 ASP MET THR PRO ILE GLY ALA ALA VAL ASN THR HIS LEU
SEQRES 26 H 401 ASN VAL HIS LEU HIS ASN ALA ALA ILE GLN GLU HIS VAL
SEQRES 27 H 401 GLU TYR ASN GLY ASN THR HIS LYS VAL PHE PRO ASN ALA
SEQRES 28 H 401 ALA GLU PRO ILE ASN GLY TYR LEU TYR ALA SER GLU ILE
SEQRES 29 H 401 ALA GLY ILE GLY VAL GLU ILE ASP ARG GLU ALA ALA ALA
SEQRES 30 H 401 GLU PHE PRO VAL MET TYR ARG PRO HIS GLU TRP THR GLN
SEQRES 31 H 401 SER ARG LEU PRO ASP GLY ALA ILE HIS THR PRO
HET MG A 402 1
HET GOL A 403 6
HET MG B 402 1
HET MG B 403 1
HET GOL B 404 6
HET MG C 402 1
HET GOL C 403 6
HET MG D 402 1
HET MG D 403 1
HET GOL D 404 6
HET MG E 402 1
HET GOL E 403 6
HET MG F 402 1
HET GOL F 403 6
HET MG G 402 1
HET GOL G 403 6
HET MG H 402 1
HET GOL H 403 6
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 MG 10(MG 2+)
FORMUL 10 GOL 8(C3 H8 O3)
FORMUL 27 HOH *1827(H2 O)
HELIX 1 1 ARG A 45 TYR A 56 1 12
HELIX 2 2 TYR A 56 ILE A 62 1 7
HELIX 3 3 ASN A 68 ASN A 79 1 12
HELIX 4 4 GLY A 85 GLY A 108 1 24
HELIX 5 5 PRO A 110 GLY A 116 1 7
HELIX 6 6 THR A 133 GLY A 148 1 16
HELIX 7 7 ASP A 179 GLY A 199 1 21
HELIX 8 8 PHE A 213 GLU A 225 1 13
HELIX 9 9 GLN A 226 LYS A 228 5 3
HELIX 10 10 PRO A 237 GLU A 242 5 6
HELIX 11 11 TRP A 243 SER A 249 1 7
HELIX 12 12 ASN A 263 GLU A 266 5 4
HELIX 13 13 TRP A 267 ASN A 273 1 7
HELIX 14 14 HIS A 282 ILE A 286 5 5
HELIX 15 15 GLY A 288 PHE A 302 1 15
HELIX 16 16 THR A 315 LEU A 329 1 15
HELIX 17 17 ASN A 341 PHE A 348 1 8
HELIX 18 18 ASP A 372 ALA A 377 1 6
HELIX 19 19 HIS A 386 THR A 389 5 4
HELIX 20 20 ARG B 45 TYR B 56 1 12
HELIX 21 21 TYR B 56 ILE B 62 1 7
HELIX 22 22 ASN B 68 ASN B 79 1 12
HELIX 23 23 GLY B 85 GLY B 108 1 24
HELIX 24 24 PRO B 110 GLY B 116 1 7
HELIX 25 25 THR B 133 LYS B 147 1 15
HELIX 26 26 PHE B 158 VAL B 162 5 5
HELIX 27 27 ASP B 179 GLY B 199 1 21
HELIX 28 28 PHE B 213 GLU B 225 1 13
HELIX 29 29 GLN B 226 LYS B 228 5 3
HELIX 30 30 PRO B 237 GLU B 242 5 6
HELIX 31 31 TRP B 243 SER B 251 1 9
HELIX 32 32 PRO B 264 ASN B 273 1 10
HELIX 33 33 HIS B 282 ILE B 286 5 5
HELIX 34 34 GLY B 288 GLY B 303 1 16
HELIX 35 35 THR B 315 LEU B 329 1 15
HELIX 36 36 ASN B 341 PHE B 348 1 8
HELIX 37 37 ASP B 372 ALA B 377 1 6
HELIX 38 38 HIS B 386 THR B 389 5 4
HELIX 39 39 ARG C 45 TYR C 56 1 12
HELIX 40 40 TYR C 56 ILE C 62 1 7
HELIX 41 41 ASN C 68 ASN C 79 1 12
HELIX 42 42 GLY C 85 GLY C 108 1 24
HELIX 43 43 PRO C 110 GLY C 116 1 7
HELIX 44 44 THR C 133 LYS C 147 1 15
HELIX 45 45 ASP C 179 GLY C 199 1 21
HELIX 46 46 PHE C 213 GLN C 226 1 14
HELIX 47 47 PRO C 237 GLU C 242 5 6
HELIX 48 48 TRP C 243 SER C 249 1 7
HELIX 49 49 ASN C 263 GLU C 266 5 4
HELIX 50 50 TRP C 267 ASN C 273 1 7
HELIX 51 51 HIS C 282 ILE C 286 5 5
HELIX 52 52 GLY C 288 GLY C 303 1 16
HELIX 53 53 THR C 315 LEU C 329 1 15
HELIX 54 54 ASN C 341 PHE C 348 1 8
HELIX 55 55 ASP C 372 GLU C 378 1 7
HELIX 56 56 HIS C 386 THR C 389 5 4
HELIX 57 57 ARG D 45 TYR D 56 1 12
HELIX 58 58 TYR D 56 ILE D 62 1 7
HELIX 59 59 ASN D 68 VAL D 78 1 11
HELIX 60 60 GLY D 85 GLY D 108 1 24
HELIX 61 61 PRO D 110 PHE D 115 1 6
HELIX 62 62 THR D 133 LYS D 147 1 15
HELIX 63 63 PHE D 158 VAL D 162 5 5
HELIX 64 64 ASP D 179 GLY D 199 1 21
HELIX 65 65 PHE D 213 GLU D 225 1 13
HELIX 66 66 GLN D 226 LYS D 228 5 3
HELIX 67 67 PRO D 237 GLU D 242 5 6
HELIX 68 68 TRP D 243 SER D 249 1 7
HELIX 69 69 ASN D 263 GLU D 266 5 4
HELIX 70 70 TRP D 267 ASN D 273 1 7
HELIX 71 71 HIS D 282 GLY D 287 5 6
HELIX 72 72 GLY D 288 GLY D 303 1 16
HELIX 73 73 THR D 315 LEU D 329 1 15
HELIX 74 74 ASN D 341 PHE D 348 1 8
HELIX 75 75 ASP D 372 GLU D 378 1 7
HELIX 76 76 HIS D 386 THR D 389 5 4
HELIX 77 77 ARG E 45 TYR E 56 1 12
HELIX 78 78 TYR E 56 ILE E 62 1 7
HELIX 79 79 ASN E 68 VAL E 78 1 11
HELIX 80 80 GLY E 85 GLY E 108 1 24
HELIX 81 81 PRO E 110 GLY E 116 1 7
HELIX 82 82 THR E 133 LYS E 147 1 15
HELIX 83 83 ASP E 179 GLY E 199 1 21
HELIX 84 84 PHE E 213 GLU E 225 1 13
HELIX 85 85 GLN E 226 LYS E 228 5 3
HELIX 86 86 PRO E 237 GLU E 242 5 6
HELIX 87 87 TRP E 243 SER E 249 1 7
HELIX 88 88 PRO E 264 ASN E 273 1 10
HELIX 89 89 HIS E 282 GLY E 287 5 6
HELIX 90 90 GLY E 288 GLY E 303 1 16
HELIX 91 91 THR E 315 LEU E 329 1 15
HELIX 92 92 ASN E 341 PHE E 348 1 8
HELIX 93 93 ASP E 372 ALA E 377 1 6
HELIX 94 94 HIS E 386 THR E 389 5 4
HELIX 95 95 ARG F 45 TYR F 56 1 12
HELIX 96 96 TYR F 56 ILE F 62 1 7
HELIX 97 97 ASN F 68 VAL F 78 1 11
HELIX 98 98 GLY F 85 GLY F 108 1 24
HELIX 99 99 PRO F 110 GLY F 116 1 7
HELIX 100 100 THR F 133 LYS F 147 1 15
HELIX 101 101 PHE F 158 VAL F 162 5 5
HELIX 102 102 ASP F 179 GLY F 199 1 21
HELIX 103 103 PHE F 213 GLN F 226 1 14
HELIX 104 104 PRO F 237 GLU F 242 5 6
HELIX 105 105 TRP F 243 SER F 251 1 9
HELIX 106 106 ASN F 263 GLU F 266 5 4
HELIX 107 107 TRP F 267 ASN F 273 1 7
HELIX 108 108 HIS F 282 GLY F 287 5 6
HELIX 109 109 GLY F 288 GLY F 303 1 16
HELIX 110 110 THR F 315 LEU F 329 1 15
HELIX 111 111 ASN F 341 PHE F 348 1 8
HELIX 112 112 ASP F 372 GLU F 378 1 7
HELIX 113 113 HIS F 386 THR F 389 5 4
HELIX 114 114 ARG G 45 TYR G 56 1 12
HELIX 115 115 TYR G 56 ILE G 62 1 7
HELIX 116 116 ASN G 68 ASN G 79 1 12
HELIX 117 117 GLY G 85 GLY G 108 1 24
HELIX 118 118 PRO G 110 GLY G 116 1 7
HELIX 119 119 THR G 133 LYS G 147 1 15
HELIX 120 120 ASP G 179 GLY G 199 1 21
HELIX 121 121 PHE G 213 GLN G 226 1 14
HELIX 122 122 GLN G 240 GLU G 242 5 3
HELIX 123 123 TRP G 243 SER G 249 1 7
HELIX 124 124 ASN G 263 GLU G 266 5 4
HELIX 125 125 TRP G 267 ASN G 273 1 7
HELIX 126 126 HIS G 282 GLY G 287 5 6
HELIX 127 127 GLY G 288 GLY G 303 1 16
HELIX 128 128 THR G 315 LEU G 329 1 15
HELIX 129 129 ASN G 341 PHE G 348 1 8
HELIX 130 130 ASP G 372 ALA G 377 1 6
HELIX 131 131 HIS G 386 THR G 389 5 4
HELIX 132 132 ARG H 45 TYR H 56 1 12
HELIX 133 133 TYR H 56 ILE H 62 1 7
HELIX 134 134 ASN H 68 ASN H 79 1 12
HELIX 135 135 GLY H 85 GLY H 108 1 24
HELIX 136 136 PRO H 110 PHE H 115 1 6
HELIX 137 137 THR H 133 LYS H 147 1 15
HELIX 138 138 ASP H 179 GLY H 199 1 21
HELIX 139 139 PHE H 213 GLN H 226 1 14
HELIX 140 140 GLN H 240 GLU H 242 5 3
HELIX 141 141 TRP H 243 SER H 249 1 7
HELIX 142 142 ASN H 263 GLU H 266 5 4
HELIX 143 143 TRP H 267 ASN H 273 1 7
HELIX 144 144 HIS H 282 GLY H 287 5 6
HELIX 145 145 GLY H 288 PHE H 302 1 15
HELIX 146 146 THR H 315 LEU H 329 1 15
HELIX 147 147 ASN H 341 PHE H 348 1 8
HELIX 148 148 ASP H 372 ALA H 377 1 6
HELIX 149 149 HIS H 386 THR H 389 5 4
SHEET 1 A 3 ILE A 8 THR A 16 0
SHEET 2 A 3 LEU A 23 THR A 30 -1 O THR A 25 N ILE A 14
SHEET 3 A 3 GLY A 36 CYS A 39 -1 O GLY A 38 N VAL A 26
SHEET 1 B 8 ARG A 305 ILE A 306 0
SHEET 2 B 8 PHE A 278 ILE A 279 1 N ILE A 279 O ARG A 305
SHEET 3 B 8 LEU A 255 LEU A 257 1 N LEU A 257 O PHE A 278
SHEET 4 B 8 PHE A 231 GLU A 233 1 N ILE A 232 O GLY A 256
SHEET 5 B 8 HIS A 203 ASP A 207 1 N HIS A 206 O GLU A 233
SHEET 6 B 8 HIS A 151 GLN A 155 1 N CYS A 154 O LEU A 205
SHEET 7 B 8 ILE A 123 THR A 130 1 N ALA A 129 O ARG A 153
SHEET 8 B 8 GLN A 335 GLU A 336 1 O GLN A 335 N PRO A 124
SHEET 1 C 8 ARG A 305 ILE A 306 0
SHEET 2 C 8 PHE A 278 ILE A 279 1 N ILE A 279 O ARG A 305
SHEET 3 C 8 LEU A 255 LEU A 257 1 N LEU A 257 O PHE A 278
SHEET 4 C 8 PHE A 231 GLU A 233 1 N ILE A 232 O GLY A 256
SHEET 5 C 8 HIS A 203 ASP A 207 1 N HIS A 206 O GLU A 233
SHEET 6 C 8 HIS A 151 GLN A 155 1 N CYS A 154 O LEU A 205
SHEET 7 C 8 ILE A 123 THR A 130 1 N ALA A 129 O ARG A 153
SHEET 8 C 8 TYR A 358 LEU A 359 -1 O LEU A 359 N ILE A 123
SHEET 1 D 2 SER A 176 TYR A 177 0
SHEET 2 D 2 SER A 391 ARG A 392 1 O ARG A 392 N SER A 176
SHEET 1 E 3 ILE B 8 THR B 16 0
SHEET 2 E 3 LEU B 23 THR B 30 -1 O LEU B 23 N THR B 16
SHEET 3 E 3 GLY B 36 CYS B 39 -1 O GLY B 36 N VAL B 28
SHEET 1 F 8 ARG B 305 ILE B 306 0
SHEET 2 F 8 PHE B 278 ILE B 279 1 N ILE B 279 O ARG B 305
SHEET 3 F 8 LEU B 255 LEU B 257 1 N LEU B 257 O PHE B 278
SHEET 4 F 8 PHE B 231 GLU B 233 1 N ILE B 232 O GLY B 256
SHEET 5 F 8 HIS B 203 ASP B 207 1 N HIS B 206 O GLU B 233
SHEET 6 F 8 HIS B 151 LEU B 156 1 N CYS B 154 O LEU B 205
SHEET 7 F 8 ILE B 123 SER B 131 1 N THR B 127 O ARG B 153
SHEET 8 F 8 GLN B 335 GLU B 336 1 O GLN B 335 N PRO B 124
SHEET 1 G 8 ARG B 305 ILE B 306 0
SHEET 2 G 8 PHE B 278 ILE B 279 1 N ILE B 279 O ARG B 305
SHEET 3 G 8 LEU B 255 LEU B 257 1 N LEU B 257 O PHE B 278
SHEET 4 G 8 PHE B 231 GLU B 233 1 N ILE B 232 O GLY B 256
SHEET 5 G 8 HIS B 203 ASP B 207 1 N HIS B 206 O GLU B 233
SHEET 6 G 8 HIS B 151 LEU B 156 1 N CYS B 154 O LEU B 205
SHEET 7 G 8 ILE B 123 SER B 131 1 N THR B 127 O ARG B 153
SHEET 8 G 8 TYR B 358 LEU B 359 -1 O LEU B 359 N ILE B 123
SHEET 1 H 2 SER B 176 TYR B 177 0
SHEET 2 H 2 SER B 391 ARG B 392 1 O ARG B 392 N SER B 176
SHEET 1 I 3 ILE C 8 THR C 16 0
SHEET 2 I 3 LEU C 23 THR C 30 -1 O THR C 25 N ILE C 14
SHEET 3 I 3 GLY C 36 CYS C 39 -1 O GLY C 36 N VAL C 28
SHEET 1 J 8 ARG C 305 ILE C 306 0
SHEET 2 J 8 PHE C 278 ILE C 279 1 N ILE C 279 O ARG C 305
SHEET 3 J 8 LEU C 255 LEU C 257 1 N LEU C 257 O PHE C 278
SHEET 4 J 8 PHE C 231 GLU C 233 1 N ILE C 232 O GLY C 256
SHEET 5 J 8 HIS C 203 ASP C 207 1 N HIS C 206 O GLU C 233
SHEET 6 J 8 HIS C 151 GLN C 155 1 N ILE C 152 O HIS C 203
SHEET 7 J 8 ILE C 123 THR C 130 1 N THR C 127 O ARG C 153
SHEET 8 J 8 GLN C 335 GLU C 336 1 O GLN C 335 N PRO C 124
SHEET 1 K 8 ARG C 305 ILE C 306 0
SHEET 2 K 8 PHE C 278 ILE C 279 1 N ILE C 279 O ARG C 305
SHEET 3 K 8 LEU C 255 LEU C 257 1 N LEU C 257 O PHE C 278
SHEET 4 K 8 PHE C 231 GLU C 233 1 N ILE C 232 O GLY C 256
SHEET 5 K 8 HIS C 203 ASP C 207 1 N HIS C 206 O GLU C 233
SHEET 6 K 8 HIS C 151 GLN C 155 1 N ILE C 152 O HIS C 203
SHEET 7 K 8 ILE C 123 THR C 130 1 N THR C 127 O ARG C 153
SHEET 8 K 8 TYR C 358 LEU C 359 -1 O LEU C 359 N ILE C 123
SHEET 1 L 2 SER C 176 TYR C 177 0
SHEET 2 L 2 SER C 391 ARG C 392 1 O ARG C 392 N SER C 176
SHEET 1 M 3 ILE D 8 THR D 16 0
SHEET 2 M 3 LEU D 23 THR D 30 -1 O GLU D 29 N SER D 9
SHEET 3 M 3 GLY D 36 CYS D 39 -1 O GLY D 36 N VAL D 28
SHEET 1 N 8 ARG D 305 ILE D 306 0
SHEET 2 N 8 PHE D 278 ILE D 279 1 N ILE D 279 O ARG D 305
SHEET 3 N 8 LEU D 255 LEU D 257 1 N LEU D 257 O PHE D 278
SHEET 4 N 8 PHE D 231 GLU D 233 1 N ILE D 232 O GLY D 256
SHEET 5 N 8 HIS D 203 ASP D 207 1 N HIS D 206 O GLU D 233
SHEET 6 N 8 HIS D 151 LEU D 156 1 N CYS D 154 O LEU D 205
SHEET 7 N 8 ILE D 123 SER D 131 1 N THR D 127 O ARG D 153
SHEET 8 N 8 GLN D 335 GLU D 336 1 O GLN D 335 N PRO D 124
SHEET 1 O 8 ARG D 305 ILE D 306 0
SHEET 2 O 8 PHE D 278 ILE D 279 1 N ILE D 279 O ARG D 305
SHEET 3 O 8 LEU D 255 LEU D 257 1 N LEU D 257 O PHE D 278
SHEET 4 O 8 PHE D 231 GLU D 233 1 N ILE D 232 O GLY D 256
SHEET 5 O 8 HIS D 203 ASP D 207 1 N HIS D 206 O GLU D 233
SHEET 6 O 8 HIS D 151 LEU D 156 1 N CYS D 154 O LEU D 205
SHEET 7 O 8 ILE D 123 SER D 131 1 N THR D 127 O ARG D 153
SHEET 8 O 8 TYR D 358 LEU D 359 -1 O LEU D 359 N ILE D 123
SHEET 1 P 2 SER D 176 TYR D 177 0
SHEET 2 P 2 SER D 391 ARG D 392 1 O ARG D 392 N SER D 176
SHEET 1 Q 3 ILE E 8 THR E 16 0
SHEET 2 Q 3 LEU E 23 THR E 30 -1 O LEU E 23 N THR E 16
SHEET 3 Q 3 GLY E 36 CYS E 39 -1 O GLY E 38 N VAL E 26
SHEET 1 R 8 ARG E 305 ILE E 306 0
SHEET 2 R 8 PHE E 278 ILE E 279 1 N ILE E 279 O ARG E 305
SHEET 3 R 8 LEU E 255 LEU E 257 1 O LEU E 255 N PHE E 278
SHEET 4 R 8 PHE E 231 GLU E 233 1 N ILE E 232 O GLY E 256
SHEET 5 R 8 HIS E 203 ASP E 207 1 N HIS E 206 O GLU E 233
SHEET 6 R 8 HIS E 151 LEU E 156 1 N CYS E 154 O LEU E 205
SHEET 7 R 8 ILE E 123 SER E 131 1 N THR E 127 O ARG E 153
SHEET 8 R 8 GLN E 335 GLU E 336 1 O GLN E 335 N PRO E 124
SHEET 1 S 8 ARG E 305 ILE E 306 0
SHEET 2 S 8 PHE E 278 ILE E 279 1 N ILE E 279 O ARG E 305
SHEET 3 S 8 LEU E 255 LEU E 257 1 O LEU E 255 N PHE E 278
SHEET 4 S 8 PHE E 231 GLU E 233 1 N ILE E 232 O GLY E 256
SHEET 5 S 8 HIS E 203 ASP E 207 1 N HIS E 206 O GLU E 233
SHEET 6 S 8 HIS E 151 LEU E 156 1 N CYS E 154 O LEU E 205
SHEET 7 S 8 ILE E 123 SER E 131 1 N THR E 127 O ARG E 153
SHEET 8 S 8 TYR E 358 LEU E 359 -1 O LEU E 359 N ILE E 123
SHEET 1 T 2 SER E 176 TYR E 177 0
SHEET 2 T 2 SER E 391 ARG E 392 1 O ARG E 392 N SER E 176
SHEET 1 U 3 ILE F 8 THR F 16 0
SHEET 2 U 3 LEU F 23 THR F 30 -1 O LEU F 23 N THR F 16
SHEET 3 U 3 THR F 35 CYS F 39 -1 O GLY F 36 N VAL F 28
SHEET 1 V 8 ARG F 305 ILE F 306 0
SHEET 2 V 8 PHE F 278 ILE F 279 1 N ILE F 279 O ARG F 305
SHEET 3 V 8 LEU F 255 LEU F 257 1 O LEU F 255 N PHE F 278
SHEET 4 V 8 PHE F 231 GLU F 233 1 N ILE F 232 O GLY F 256
SHEET 5 V 8 HIS F 203 ASP F 207 1 N HIS F 206 O GLU F 233
SHEET 6 V 8 HIS F 151 LEU F 156 1 N ILE F 152 O HIS F 203
SHEET 7 V 8 ILE F 123 SER F 131 1 N THR F 127 O ARG F 153
SHEET 8 V 8 GLN F 335 GLU F 336 1 O GLN F 335 N PRO F 124
SHEET 1 W 8 ARG F 305 ILE F 306 0
SHEET 2 W 8 PHE F 278 ILE F 279 1 N ILE F 279 O ARG F 305
SHEET 3 W 8 LEU F 255 LEU F 257 1 O LEU F 255 N PHE F 278
SHEET 4 W 8 PHE F 231 GLU F 233 1 N ILE F 232 O GLY F 256
SHEET 5 W 8 HIS F 203 ASP F 207 1 N HIS F 206 O GLU F 233
SHEET 6 W 8 HIS F 151 LEU F 156 1 N ILE F 152 O HIS F 203
SHEET 7 W 8 ILE F 123 SER F 131 1 N THR F 127 O ARG F 153
SHEET 8 W 8 TYR F 358 LEU F 359 -1 O LEU F 359 N ILE F 123
SHEET 1 X 2 SER F 176 TYR F 177 0
SHEET 2 X 2 SER F 391 ARG F 392 1 O ARG F 392 N SER F 176
SHEET 1 Y 3 ILE G 8 THR G 16 0
SHEET 2 Y 3 LEU G 23 THR G 30 -1 O GLU G 29 N ASP G 10
SHEET 3 Y 3 GLY G 36 CYS G 39 -1 O GLY G 36 N VAL G 28
SHEET 1 Z 8 ARG G 305 ILE G 306 0
SHEET 2 Z 8 PHE G 278 ILE G 279 1 N ILE G 279 O ARG G 305
SHEET 3 Z 8 LEU G 255 LEU G 257 1 O LEU G 255 N PHE G 278
SHEET 4 Z 8 PHE G 231 GLU G 233 1 N ILE G 232 O GLY G 256
SHEET 5 Z 8 HIS G 203 ASP G 207 1 N HIS G 206 O GLU G 233
SHEET 6 Z 8 HIS G 151 LEU G 156 1 N ILE G 152 O HIS G 203
SHEET 7 Z 8 ILE G 123 SER G 131 1 N ALA G 129 O ARG G 153
SHEET 8 Z 8 GLN G 335 GLU G 336 1 O GLN G 335 N PRO G 124
SHEET 1 AA 8 ARG G 305 ILE G 306 0
SHEET 2 AA 8 PHE G 278 ILE G 279 1 N ILE G 279 O ARG G 305
SHEET 3 AA 8 LEU G 255 LEU G 257 1 O LEU G 255 N PHE G 278
SHEET 4 AA 8 PHE G 231 GLU G 233 1 N ILE G 232 O GLY G 256
SHEET 5 AA 8 HIS G 203 ASP G 207 1 N HIS G 206 O GLU G 233
SHEET 6 AA 8 HIS G 151 LEU G 156 1 N ILE G 152 O HIS G 203
SHEET 7 AA 8 ILE G 123 SER G 131 1 N ALA G 129 O ARG G 153
SHEET 8 AA 8 TYR G 358 LEU G 359 -1 O LEU G 359 N ILE G 123
SHEET 1 AB 2 SER G 176 TYR G 177 0
SHEET 2 AB 2 SER G 391 ARG G 392 1 O ARG G 392 N SER G 176
SHEET 1 AC 3 ILE H 8 THR H 16 0
SHEET 2 AC 3 LEU H 23 THR H 30 -1 O GLU H 29 N SER H 9
SHEET 3 AC 3 THR H 35 CYS H 39 -1 O GLY H 36 N VAL H 28
SHEET 1 AD 8 ARG H 305 ILE H 306 0
SHEET 2 AD 8 PHE H 278 ILE H 279 1 N ILE H 279 O ARG H 305
SHEET 3 AD 8 LEU H 255 LEU H 257 1 O LEU H 255 N PHE H 278
SHEET 4 AD 8 PHE H 231 GLU H 233 1 N ILE H 232 O GLY H 256
SHEET 5 AD 8 HIS H 203 ASP H 207 1 N HIS H 206 O GLU H 233
SHEET 6 AD 8 HIS H 151 LEU H 156 1 N ILE H 152 O HIS H 203
SHEET 7 AD 8 ILE H 123 SER H 131 1 N THR H 127 O ARG H 153
SHEET 8 AD 8 GLN H 335 GLU H 336 1 O GLN H 335 N PRO H 124
SHEET 1 AE 8 ARG H 305 ILE H 306 0
SHEET 2 AE 8 PHE H 278 ILE H 279 1 N ILE H 279 O ARG H 305
SHEET 3 AE 8 LEU H 255 LEU H 257 1 O LEU H 255 N PHE H 278
SHEET 4 AE 8 PHE H 231 GLU H 233 1 N ILE H 232 O GLY H 256
SHEET 5 AE 8 HIS H 203 ASP H 207 1 N HIS H 206 O GLU H 233
SHEET 6 AE 8 HIS H 151 LEU H 156 1 N ILE H 152 O HIS H 203
SHEET 7 AE 8 ILE H 123 SER H 131 1 N THR H 127 O ARG H 153
SHEET 8 AE 8 TYR H 358 LEU H 359 -1 O LEU H 359 N ILE H 123
SHEET 1 AF 2 SER H 176 TYR H 177 0
SHEET 2 AF 2 SER H 391 ARG H 392 1 O ARG H 392 N SER H 176
LINK OD2 ASP A 207 MG MG A 402 1555 1555 2.21
LINK OE2 GLU A 233 MG MG A 402 1555 1555 2.22
LINK OE1 GLU A 259 MG MG A 402 1555 1555 2.25
LINK MG MG A 402 O HOH A 405 1555 1555 2.21
LINK MG MG A 402 O HOH A 406 1555 1555 2.40
LINK MG MG A 402 O HOH A 408 1555 1555 2.25
LINK OD2 ASP B 207 MG MG B 402 1555 1555 2.19
LINK OE2 GLU B 233 MG MG B 402 1555 1555 2.19
LINK OE1 GLU B 259 MG MG B 402 1555 1555 2.20
LINK MG MG B 402 O HOH B 407 1555 1555 2.10
LINK MG MG B 402 O HOH B 408 1555 1555 2.32
LINK MG MG B 402 O HOH B1802 1555 1555 2.30
LINK MG MG B 403 O HOH B1473 1555 1555 2.44
LINK MG MG B 403 O HOH B1542 1555 1555 2.54
LINK OD2 ASP C 207 MG MG C 402 1555 1555 2.20
LINK OE2 GLU C 233 MG MG C 402 1555 1555 2.20
LINK OE1 GLU C 259 MG MG C 402 1555 1555 2.23
LINK MG MG C 402 O HOH C 404 1555 1555 2.20
LINK MG MG C 402 O HOH C 405 1555 1555 2.24
LINK MG MG C 402 O HOH C 407 1555 1555 2.36
LINK OD2 ASP D 207 MG MG D 402 1555 1555 2.14
LINK OE2 GLU D 233 MG MG D 402 1555 1555 2.16
LINK OE1 GLU D 259 MG MG D 402 1555 1555 2.18
LINK MG MG D 402 O HOH D 405 1555 1555 2.21
LINK MG MG D 402 O HOH D 406 1555 1555 2.26
LINK MG MG D 402 O HOH D 408 1555 1555 2.28
LINK MG MG D 403 O HOH D 756 1555 1555 2.70
LINK MG MG D 403 O HOH D1632 1555 1555 2.69
LINK MG MG D 403 O HOH D1874 1555 1555 2.61
LINK OD2 ASP E 207 MG MG E 402 1555 1555 2.16
LINK OE2 GLU E 233 MG MG E 402 1555 1555 2.28
LINK OE1 GLU E 259 MG MG E 402 1555 1555 2.20
LINK MG MG E 402 O HOH E 405 1555 1555 2.10
LINK MG MG E 402 O HOH E 407 1555 1555 2.22
LINK MG MG E 402 O HOH E 410 1555 1555 2.34
LINK OD2 ASP F 207 MG MG F 402 1555 1555 2.15
LINK OE2 GLU F 233 MG MG F 402 1555 1555 2.25
LINK OE1 GLU F 259 MG MG F 402 1555 1555 2.16
LINK MG MG F 402 O HOH F 404 1555 1555 2.14
LINK MG MG F 402 O HOH F 405 1555 1555 2.24
LINK MG MG F 402 O HOH F 407 1555 1555 2.28
LINK OD2 ASP G 207 MG MG G 402 1555 1555 2.15
LINK OE2 GLU G 233 MG MG G 402 1555 1555 2.23
LINK OE1 GLU G 259 MG MG G 402 1555 1555 2.21
LINK MG MG G 402 O HOH G 404 1555 1555 2.28
LINK MG MG G 402 O HOH G 405 1555 1555 2.25
LINK MG MG G 402 O HOH G1804 1555 1555 2.41
LINK OD2 ASP H 207 MG MG H 402 1555 1555 2.18
LINK OE2 GLU H 233 MG MG H 402 1555 1555 2.20
LINK OE1 GLU H 259 MG MG H 402 1555 1555 2.27
LINK MG MG H 402 O HOH H 405 1555 1555 2.32
LINK MG MG H 402 O HOH H 406 1555 1555 2.31
LINK MG MG H 402 O HOH H 408 1555 1555 2.33
SITE 1 AC1 6 ASP A 207 GLU A 233 GLU A 259 HOH A 405
SITE 2 AC1 6 HOH A 406 HOH A 408
SITE 1 AC2 6 ASP B 207 GLU B 233 GLU B 259 HOH B 407
SITE 2 AC2 6 HOH B 408 HOH B1802
SITE 1 AC3 6 ASP C 207 GLU C 233 GLU C 259 HOH C 404
SITE 2 AC3 6 HOH C 405 HOH C 407
SITE 1 AC4 6 ASP D 207 GLU D 233 GLU D 259 HOH D 405
SITE 2 AC4 6 HOH D 406 HOH D 408
SITE 1 AC5 6 ASP E 207 GLU E 233 GLU E 259 HOH E 405
SITE 2 AC5 6 HOH E 407 HOH E 410
SITE 1 AC6 6 ASP F 207 GLU F 233 GLU F 259 HOH F 404
SITE 2 AC6 6 HOH F 405 HOH F 407
SITE 1 AC7 6 ASP G 207 GLU G 233 GLU G 259 HOH G 404
SITE 2 AC7 6 HOH G 405 HOH G1804
SITE 1 AC8 6 ASP H 207 GLU H 233 GLU H 259 HOH H 405
SITE 2 AC8 6 HOH H 406 HOH H 408
SITE 1 AC9 4 LYS B 346 HOH B1473 HOH B1542 HOH E 638
SITE 1 BC1 6 LYS D 346 HOH D 756 HOH D1632 HOH D1874
SITE 2 BC1 6 HOH G1429 HOH G1854
SITE 1 BC2 9 GLN A 43 GLN A 44 HIS A 209 HIS A 309
SITE 2 BC2 9 PRO A 311 ASP A 313 HOH A 404 TYR B 81
SITE 3 BC2 9 TRP B 82
SITE 1 BC3 9 TYR A 81 TRP A 82 GLN B 43 GLN B 44
SITE 2 BC3 9 HIS B 209 GLU B 259 HIS B 309 PRO B 311
SITE 3 BC3 9 ASP B 313
SITE 1 BC4 9 GLN C 43 GLN C 44 HIS C 209 GLU C 259
SITE 2 BC4 9 HIS C 309 PRO C 311 ASP C 313 TYR D 81
SITE 3 BC4 9 TRP D 82
SITE 1 BC5 10 TYR C 81 TRP C 82 GLN D 43 GLN D 44
SITE 2 BC5 10 HIS D 209 GLU D 259 HIS D 309 PRO D 311
SITE 3 BC5 10 ASP D 313 HOH D1178
SITE 1 BC6 8 GLN E 43 GLN E 44 HIS E 209 HIS E 309
SITE 2 BC6 8 PRO E 311 ASP E 313 TYR F 81 TRP F 82
SITE 1 BC7 8 TYR E 81 TRP E 82 GLN F 43 GLN F 44
SITE 2 BC7 8 HIS F 209 HIS F 309 PRO F 311 ASP F 313
SITE 1 BC8 8 GLN G 43 GLN G 44 HIS G 209 HIS G 309
SITE 2 BC8 8 PRO G 311 ASP G 313 TYR H 81 TRP H 82
SITE 1 BC9 9 TYR G 81 TRP G 82 GLN H 43 GLN H 44
SITE 2 BC9 9 HIS H 209 HIS H 309 PRO H 311 ASP H 313
SITE 3 BC9 9 HOH H 405
CRYST1 167.986 211.516 211.672 90.00 90.00 90.00 I 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 0.005953 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004724 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
