HEADER METAL BINDING PROTEIN 08-FEB-16 5I28
TITLE AZURIN T30R1, CRYSTAL FORM II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AZURIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 /
SOURCE 3 PAO1 / 1C / PRS 101 / LMG 12228);
SOURCE 4 ORGANISM_TAXID: 287;
SOURCE 5 GENE: AZU, PA4922;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BLUE COPPER PROTEIN, SPIN LABEL, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.HAGELUEKEN
REVDAT 3 10-JAN-24 5I28 1 LINK
REVDAT 2 20-APR-16 5I28 1 JRNL
REVDAT 1 13-APR-16 5I28 0
JRNL AUTH D.ABDULLIN,G.HAGELUEKEN,O.SCHIEMANN
JRNL TITL DETERMINATION OF NITROXIDE SPIN LABEL CONFORMATIONS VIA
JRNL TITL 2 PELDOR AND X-RAY CRYSTALLOGRAPHY.
JRNL REF PHYS CHEM CHEM PHYS V. 18 10428 2016
JRNL REFN ESSN 1463-9084
JRNL PMID 27029516
JRNL DOI 10.1039/C6CP01307D
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.180
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 166082
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.180
REMARK 3 FREE R VALUE TEST SET COUNT : 3836
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 18.2214 - 5.7889 0.95 11504 130 0.1492 0.2201
REMARK 3 2 5.7889 - 4.6195 0.99 11890 136 0.1324 0.2000
REMARK 3 3 4.6195 - 4.0428 0.99 11852 136 0.1235 0.1823
REMARK 3 4 4.0428 - 3.6765 0.98 11825 150 0.1451 0.1840
REMARK 3 5 3.6765 - 3.4148 0.99 11937 165 0.1619 0.2356
REMARK 3 6 3.4148 - 3.2146 0.99 11838 137 0.1795 0.2074
REMARK 3 7 3.2146 - 3.0544 0.99 11967 160 0.2055 0.2892
REMARK 3 8 3.0544 - 2.9220 0.99 11853 139 0.2308 0.2760
REMARK 3 9 2.9220 - 2.8100 0.99 11919 132 0.2445 0.3241
REMARK 3 10 2.8100 - 2.7133 0.99 12005 129 0.2584 0.3260
REMARK 3 11 2.7133 - 2.6287 0.99 11813 157 0.2652 0.3229
REMARK 3 12 2.6287 - 2.5538 0.99 11913 157 0.2657 0.3508
REMARK 3 13 2.5538 - 2.4867 0.99 11987 122 0.2887 0.3184
REMARK 3 14 2.4867 - 2.4262 0.99 11992 161 0.3231 0.3996
REMARK 3 15 2.4262 - 2.3712 0.99 11892 122 0.3225 0.4357
REMARK 3 16 2.3712 - 2.3208 0.99 11920 140 0.3189 0.4195
REMARK 3 17 2.3208 - 2.2745 0.99 11830 135 0.3223 0.3515
REMARK 3 18 2.2745 - 2.2316 0.99 11957 152 0.3436 0.4142
REMARK 3 19 2.2316 - 2.1918 0.99 11874 146 0.3385 0.3866
REMARK 3 20 2.1918 - 2.1548 0.99 11982 115 0.3357 0.4084
REMARK 3 21 2.1548 - 2.1200 0.99 11796 188 0.3430 0.3881
REMARK 3 22 2.1200 - 2.0875 0.99 11874 117 0.3393 0.3015
REMARK 3 23 2.0875 - 2.0568 0.99 11878 131 0.3517 0.3750
REMARK 3 24 2.0568 - 2.0279 0.99 11875 167 0.3619 0.3838
REMARK 3 25 2.0279 - 2.0005 0.99 11770 133 0.3761 0.4102
REMARK 3 26 2.0005 - 1.9746 0.99 11848 135 0.3964 0.3555
REMARK 3 27 1.9746 - 1.9499 0.93 11340 144 0.4159 0.4559
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.920
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 16511
REMARK 3 ANGLE : 1.194 22378
REMARK 3 CHIRALITY : 0.045 2469
REMARK 3 PLANARITY : 0.005 2897
REMARK 3 DIHEDRAL : 15.245 6235
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 5I28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218132.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8943
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 166299
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 18.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.16300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.60900
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: PHASER
REMARK 200 STARTING MODEL: 1E67
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -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 121.23900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.78000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 121.23900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.78000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
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: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
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: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
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: 13
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M
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: 14
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N
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: 15
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O
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: 16
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH E 308 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E 332 LIES ON A SPECIAL POSITION.
REMARK 375 HOH J 336 LIES ON A SPECIAL POSITION.
REMARK 375 HOH K 307 LIES ON A SPECIAL POSITION.
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 OE1 GLU B 106 O HOH B 301 1.88
REMARK 500 O HOH K 305 O HOH K 337 2.06
REMARK 500 OH TYR B 108 O HOH B 301 2.09
REMARK 500 OD1 ASP C 93 O HOH C 301 2.09
REMARK 500 OD1 ASP B 93 O HOH B 302 2.11
REMARK 500 O LEU D 73 O HOH D 301 2.11
REMARK 500 O HOH C 359 O HOH C 377 2.12
REMARK 500 O LEU E 102 O HOH E 301 2.12
REMARK 500 O ALA E 19 O HOH E 302 2.12
REMARK 500 O LEU J 102 O HOH J 301 2.13
REMARK 500 O HOH N 335 O HOH N 336 2.14
REMARK 500 OD1 ASP J 62 O HOH J 302 2.15
REMARK 500 O HOH C 314 O HOH C 371 2.16
REMARK 500 O HOH N 306 O HOH N 335 2.16
REMARK 500 NZ LYS I 92 OD2 ASP L 98 2.17
REMARK 500 NE2 GLN K 57 O HOH K 301 2.17
REMARK 500 O LEU K 102 O HOH K 302 2.17
REMARK 500 O LEU B 102 O HOH B 303 2.18
REMARK 500 O HOH B 303 O HOH B 344 2.18
REMARK 500 O ARG E 79 O HOH E 303 2.18
REMARK 500 OD1 ASN I 32 NE2 GLN L 28 2.18
REMARK 500 O HOH D 327 O HOH E 301 2.19
REMARK 500 O LEU P 102 O HOH P 301 2.19
REMARK 500 O GLY N 37 OG SER N 89 2.19
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 G 336 O HOH P 301 2756 2.15
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 PRO A 36 -165.85 -67.05
REMARK 500 GLN C 12 34.31 -96.68
REMARK 500 PRO D 36 48.60 -79.28
REMARK 500 ALA D 65 8.77 -66.74
REMARK 500 ASN E 10 -155.54 -118.15
REMARK 500 ASN F 10 -167.93 -109.91
REMARK 500 ALA F 19 118.36 -161.97
REMARK 500 ASN G 10 -165.05 -113.56
REMARK 500 LYS G 24 -39.29 -37.55
REMARK 500 PRO G 36 -166.73 -67.53
REMARK 500 ASN H 10 -166.72 -110.31
REMARK 500 MET H 44 41.20 -145.71
REMARK 500 ASN I 10 -167.05 -107.85
REMARK 500 MET I 44 43.41 -147.36
REMARK 500 MET I 121 78.39 -100.48
REMARK 500 ASN J 10 -168.22 -121.94
REMARK 500 PRO J 36 -165.49 -66.37
REMARK 500 ASN K 10 -160.92 -120.40
REMARK 500 LYS L 24 -38.36 -38.24
REMARK 500 ASP L 77 107.75 -59.07
REMARK 500 CYS M 3 22.32 -146.04
REMARK 500 HIS M 35 78.22 -119.32
REMARK 500 ASN N 10 -167.68 -101.04
REMARK 500 ALA N 65 23.10 -69.57
REMARK 500 SER N 89 131.84 -39.53
REMARK 500 GLU O 2 4.74 -66.15
REMARK 500 CYS O 3 21.16 -144.89
REMARK 500 HIS O 35 78.71 -116.99
REMARK 500 LYS O 92 132.80 -172.91
REMARK 500 ASN P 10 -165.90 -112.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASN E 32 0.07 SIDE CHAIN
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 K 342 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH K 343 DISTANCE = 6.62 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 CU A 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 45 O
REMARK 620 2 HIS A 46 ND1 87.0
REMARK 620 3 CYS A 112 SG 99.4 132.9
REMARK 620 4 HIS A 117 ND1 96.7 105.6 119.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 45 O
REMARK 620 2 HIS B 46 ND1 84.7
REMARK 620 3 CYS B 112 SG 97.0 129.7
REMARK 620 4 HIS B 117 ND1 96.9 111.2 118.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU C 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 45 O
REMARK 620 2 HIS C 46 ND1 88.5
REMARK 620 3 CYS C 112 SG 95.1 133.8
REMARK 620 4 HIS C 117 ND1 91.5 116.6 109.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU D 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY D 45 O
REMARK 620 2 HIS D 46 ND1 79.9
REMARK 620 3 CYS D 112 SG 93.0 133.2
REMARK 620 4 HIS D 117 ND1 91.7 116.1 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU E 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 45 O
REMARK 620 2 HIS E 46 ND1 84.5
REMARK 620 3 CYS E 112 SG 95.8 130.2
REMARK 620 4 HIS E 117 ND1 97.2 110.4 118.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU F 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY F 45 O
REMARK 620 2 HIS F 46 ND1 78.7
REMARK 620 3 CYS F 112 SG 97.8 126.6
REMARK 620 4 HIS F 117 ND1 92.1 114.4 119.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU G 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY G 45 O
REMARK 620 2 HIS G 46 ND1 77.6
REMARK 620 3 CYS G 112 SG 99.5 133.0
REMARK 620 4 HIS G 117 ND1 92.7 115.9 111.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU H 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY H 45 O
REMARK 620 2 HIS H 46 ND1 83.3
REMARK 620 3 CYS H 112 SG 97.3 131.9
REMARK 620 4 HIS H 117 ND1 94.8 112.4 115.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU I 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY I 45 O
REMARK 620 2 HIS I 46 ND1 88.9
REMARK 620 3 CYS I 112 SG 99.8 130.2
REMARK 620 4 HIS I 117 ND1 96.2 115.1 112.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU J 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY J 45 O
REMARK 620 2 HIS J 46 ND1 80.7
REMARK 620 3 CYS J 112 SG 100.7 136.8
REMARK 620 4 HIS J 117 ND1 91.8 114.6 108.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU K 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY K 45 O
REMARK 620 2 HIS K 46 ND1 85.5
REMARK 620 3 CYS K 112 SG 99.8 132.6
REMARK 620 4 HIS K 117 ND1 98.7 108.7 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU L 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY L 45 O
REMARK 620 2 HIS L 46 ND1 79.0
REMARK 620 3 CYS L 112 SG 97.5 128.5
REMARK 620 4 HIS L 117 ND1 94.3 115.7 115.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU M 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY M 45 O
REMARK 620 2 HIS M 46 ND1 80.5
REMARK 620 3 CYS M 112 SG 97.9 135.3
REMARK 620 4 HIS M 117 ND1 90.2 108.2 116.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU N 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY N 45 O
REMARK 620 2 HIS N 46 ND1 80.2
REMARK 620 3 CYS N 112 SG 97.2 128.5
REMARK 620 4 HIS N 117 ND1 96.7 116.6 114.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU O 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY O 45 O
REMARK 620 2 HIS O 46 ND1 83.5
REMARK 620 3 CYS O 112 SG 98.3 132.4
REMARK 620 4 HIS O 117 ND1 92.0 108.4 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU P 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY P 45 O
REMARK 620 2 HIS P 46 ND1 80.8
REMARK 620 3 CYS P 112 SG 98.7 133.3
REMARK 620 4 HIS P 117 ND1 93.5 107.6 119.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU H 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU K 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU L 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU M 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU O 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU P 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE B 29 and R1A B
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A B 30 and VAL B
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE C 29 and R1A C
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A C 30 and VAL C
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE D 29 and R1A D
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A D 30 and VAL D
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE E 29 and R1A E
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A E 30 and VAL E
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE F 29 and R1A F
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A F 30 and VAL F
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE G 29 and R1A G
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A G 30 and VAL G
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE H 29 and R1A H
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A H 30 and VAL H
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE I 29 and R1A I
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A I 30 and VAL I
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE J 29 and R1A J
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A J 30 and VAL J
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE K 29 and R1A K
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A K 30 and VAL K
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE L 29 and R1A L
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A L 30 and VAL L
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE M 29 and R1A M
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A M 30 and VAL M
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE N 29 and R1A N
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A N 30 and VAL N
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE O 29 and R1A O
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A O 30 and VAL O
REMARK 800 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHE P 29 and R1A P
REMARK 800 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide R1A P 30 and VAL P
REMARK 800 31
DBREF 5I28 A 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 B 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 C 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 D 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 E 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 F 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 G 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 H 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 I 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 J 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 K 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 L 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 M 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 N 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 O 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 5I28 P 1 128 UNP P00282 AZUR_PSEAE 21 148
SEQADV 5I28 R1A A 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A B 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A C 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A D 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A E 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A F 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A G 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A H 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A I 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A J 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A K 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A L 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A M 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A N 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A O 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQADV 5I28 R1A P 30 UNP P00282 THR 50 ENGINEERED MUTATION
SEQRES 1 A 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 A 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 A 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 A 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 A 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 A 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 A 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 A 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 A 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 A 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 B 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 B 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 B 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 B 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 B 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 B 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 B 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 B 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 B 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 B 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 C 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 C 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 C 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 C 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 C 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 C 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 C 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 C 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 C 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 C 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 D 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 D 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 D 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 D 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 D 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 D 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 D 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 D 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 D 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 D 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 E 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 E 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 E 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 E 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 E 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 E 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 E 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 E 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 E 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 E 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 F 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 F 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 F 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 F 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 F 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 F 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 F 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 F 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 F 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 F 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 G 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 G 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 G 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 G 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 G 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 G 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 G 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 G 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 G 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 G 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 H 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 H 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 H 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 H 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 H 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 H 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 H 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 H 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 H 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 H 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 I 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 I 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 I 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 I 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 I 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 I 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 I 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 I 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 I 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 I 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 J 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 J 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 J 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 J 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 J 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 J 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 J 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 J 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 J 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 J 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 K 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 K 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 K 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 K 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 K 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 K 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 K 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 K 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 K 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 K 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 L 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 L 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 L 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 L 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 L 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 L 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 L 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 L 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 L 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 L 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 M 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 M 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 M 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 M 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 M 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 M 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 M 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 M 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 M 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 M 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 N 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 N 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 N 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 N 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 N 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 N 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 N 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 N 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 N 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 N 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 O 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 O 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 O 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 O 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 O 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 O 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 O 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 O 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 O 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 O 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
SEQRES 1 P 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 P 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 P 128 LYS GLN PHE R1A VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 P 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 P 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 P 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 P 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 P 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 P 128 GLY GLU GLN TYR MET PHE PHE CYS THR PHE PRO GLY HIS
SEQRES 10 P 128 SER ALA LEU MET LYS GLY THR LEU THR LEU LYS
HET R1A A 30 18
HET R1A B 30 18
HET R1A C 30 18
HET R1A D 30 18
HET R1A E 30 18
HET R1A F 30 18
HET R1A G 30 18
HET R1A H 30 18
HET R1A I 30 18
HET R1A J 30 18
HET R1A K 30 18
HET R1A L 30 18
HET R1A M 30 18
HET R1A N 30 18
HET R1A O 30 18
HET R1A P 30 18
HET CU A 201 1
HET GOL A 202 6
HET CU B 201 1
HET CU C 201 1
HET CU D 201 1
HET CU E 201 1
HET CU F 201 1
HET CU G 201 1
HET CU H 201 1
HET CU I 201 1
HET CU J 201 1
HET CU K 201 1
HET CU L 201 1
HET CU M 201 1
HET CU N 201 1
HET CU O 201 1
HET CU P 201 1
HETNAM R1A 3-{[(2,2,5,5-TETRAMETHYL-1-OXO-2,5-DIHYDRO-1H-
HETNAM 2 R1A PYRROLIUM-3-YL)METHYL]DISULFANYL}-D-ALANINE
HETNAM CU COPPER (II) ION
HETNAM GOL GLYCEROL
HETSYN R1A S-(THIOMETHYL-3-[2,2,5,5-TETRAMETHYL PYRROLINE-1-OXYL])
HETSYN 2 R1A CYSTEINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 R1A 16(C12 H21 N2 O3 S2 1+)
FORMUL 17 CU 16(CU 2+)
FORMUL 18 GOL C3 H8 O3
FORMUL 34 HOH *848(H2 O)
HELIX 1 AA1 PRO A 40 GLY A 45 1 6
HELIX 2 AA2 ALA A 53 SER A 66 1 14
HELIX 3 AA3 GLY A 67 ASP A 71 5 5
HELIX 4 AA4 SER A 100 LEU A 102 5 3
HELIX 5 AA5 GLY A 116 LEU A 120 5 5
HELIX 6 AA6 PRO B 40 GLY B 45 1 6
HELIX 7 AA7 ASP B 55 GLY B 67 1 13
HELIX 8 AA8 LEU B 68 ASP B 71 5 4
HELIX 9 AA9 SER B 100 LEU B 102 5 3
HELIX 10 AB1 GLY B 116 LEU B 120 5 5
HELIX 11 AB2 PRO C 40 GLY C 45 1 6
HELIX 12 AB3 ALA C 53 GLY C 67 1 15
HELIX 13 AB4 LEU C 68 ASP C 71 5 4
HELIX 14 AB5 SER C 100 LEU C 102 5 3
HELIX 15 AB6 GLY C 116 LEU C 120 5 5
HELIX 16 AB7 ALA D 53 ALA D 65 1 13
HELIX 17 AB8 SER D 66 ASP D 71 5 6
HELIX 18 AB9 SER D 100 LEU D 102 5 3
HELIX 19 AC1 GLY D 116 LEU D 120 5 5
HELIX 20 AC2 PRO E 40 GLY E 45 1 6
HELIX 21 AC3 ASP E 55 GLY E 67 1 13
HELIX 22 AC4 LEU E 68 ASP E 71 5 4
HELIX 23 AC5 SER E 100 LEU E 102 5 3
HELIX 24 AC6 GLY E 116 LEU E 120 5 5
HELIX 25 AC7 PRO F 40 GLY F 45 1 6
HELIX 26 AC8 ASP F 55 GLY F 67 1 13
HELIX 27 AC9 LEU F 68 ASP F 71 5 4
HELIX 28 AD1 SER F 100 LEU F 102 5 3
HELIX 29 AD2 GLY F 116 LEU F 120 5 5
HELIX 30 AD3 PRO G 40 GLY G 45 1 6
HELIX 31 AD4 ALA G 53 SER G 66 1 14
HELIX 32 AD5 GLY G 67 ASP G 71 5 5
HELIX 33 AD6 SER G 100 LEU G 102 5 3
HELIX 34 AD7 GLY G 116 LEU G 120 5 5
HELIX 35 AD8 PRO H 40 GLY H 45 1 6
HELIX 36 AD9 ALA H 53 SER H 66 1 14
HELIX 37 AE1 GLY H 67 ASP H 71 5 5
HELIX 38 AE2 SER H 100 LEU H 102 5 3
HELIX 39 AE3 GLY H 116 LEU H 120 5 5
HELIX 40 AE4 PRO I 40 GLY I 45 1 6
HELIX 41 AE5 ASP I 55 GLY I 67 1 13
HELIX 42 AE6 LEU I 68 ASP I 71 5 4
HELIX 43 AE7 SER I 100 LEU I 102 5 3
HELIX 44 AE8 GLY I 116 LEU I 120 5 5
HELIX 45 AE9 ASP J 55 SER J 66 1 12
HELIX 46 AF1 GLY J 67 ASP J 71 5 5
HELIX 47 AF2 SER J 100 LEU J 102 5 3
HELIX 48 AF3 GLY J 116 LEU J 120 5 5
HELIX 49 AF4 PRO K 40 GLY K 45 1 6
HELIX 50 AF5 ALA K 53 GLY K 67 1 15
HELIX 51 AF6 LEU K 68 ASP K 71 5 4
HELIX 52 AF7 SER K 100 LEU K 102 5 3
HELIX 53 AF8 GLY K 116 LEU K 120 5 5
HELIX 54 AF9 PRO L 40 GLY L 45 1 6
HELIX 55 AG1 ASP L 55 GLY L 67 1 13
HELIX 56 AG2 LEU L 68 ASP L 71 5 4
HELIX 57 AG3 SER L 100 LEU L 102 5 3
HELIX 58 AG4 GLY L 116 LEU L 120 5 5
HELIX 59 AG5 PRO M 40 GLY M 45 1 6
HELIX 60 AG6 ASP M 55 GLY M 67 1 13
HELIX 61 AG7 LEU M 68 ASP M 71 5 4
HELIX 62 AG8 GLY M 116 LEU M 120 5 5
HELIX 63 AG9 PRO N 40 GLY N 45 1 6
HELIX 64 AH1 ALA N 53 ALA N 65 1 13
HELIX 65 AH2 SER N 66 ASP N 71 5 6
HELIX 66 AH3 SER N 100 LEU N 102 5 3
HELIX 67 AH4 GLY N 116 LEU N 120 5 5
HELIX 68 AH5 PRO O 40 GLY O 45 1 6
HELIX 69 AH6 ASP O 55 GLY O 67 1 13
HELIX 70 AH7 LEU O 68 ASP O 71 5 4
HELIX 71 AH8 GLY O 116 LEU O 120 5 5
HELIX 72 AH9 PRO P 40 GLY P 45 1 6
HELIX 73 AI1 ASP P 55 GLY P 67 1 13
HELIX 74 AI2 LEU P 68 ASP P 71 5 4
HELIX 75 AI3 SER P 100 LEU P 102 5 3
HELIX 76 AI4 GLY P 116 LEU P 120 5 5
SHEET 1 AA1 3 SER A 4 GLN A 8 0
SHEET 2 AA1 3 GLN A 28 SER A 34 1 O ASN A 32 N ILE A 7
SHEET 3 AA1 3 LYS A 92 ASP A 98 -1 O ASP A 93 N LEU A 33
SHEET 1 AA2 5 ALA A 19 ASP A 23 0
SHEET 2 AA2 5 LYS A 122 LYS A 128 1 O THR A 126 N VAL A 22
SHEET 3 AA2 5 TYR A 108 PHE A 111 -1 N TYR A 108 O LEU A 125
SHEET 4 AA2 5 VAL A 49 THR A 52 -1 N VAL A 49 O PHE A 111
SHEET 5 AA2 5 ALA A 82 HIS A 83 -1 O ALA A 82 N LEU A 50
SHEET 1 AA3 3 SER B 4 GLN B 8 0
SHEET 2 AA3 3 GLN B 28 SER B 34 1 O ASN B 32 N ILE B 7
SHEET 3 AA3 3 LYS B 92 ASP B 98 -1 O ASP B 93 N LEU B 33
SHEET 1 AA4 5 ALA B 19 ASP B 23 0
SHEET 2 AA4 5 LYS B 122 LYS B 128 1 O THR B 126 N VAL B 22
SHEET 3 AA4 5 TYR B 108 PHE B 111 -1 N TYR B 108 O LEU B 125
SHEET 4 AA4 5 VAL B 49 THR B 52 -1 N SER B 51 O MET B 109
SHEET 5 AA4 5 ALA B 82 HIS B 83 -1 O ALA B 82 N LEU B 50
SHEET 1 AA5 3 SER C 4 GLN C 8 0
SHEET 2 AA5 3 GLN C 28 SER C 34 1 O ASN C 32 N ILE C 7
SHEET 3 AA5 3 LYS C 92 ASP C 98 -1 O ASP C 93 N LEU C 33
SHEET 1 AA6 5 ALA C 19 ASP C 23 0
SHEET 2 AA6 5 LYS C 122 LYS C 128 1 O THR C 126 N VAL C 22
SHEET 3 AA6 5 TYR C 108 PHE C 111 -1 N TYR C 108 O LEU C 125
SHEET 4 AA6 5 VAL C 49 THR C 52 -1 N VAL C 49 O PHE C 111
SHEET 5 AA6 5 ALA C 82 HIS C 83 -1 O ALA C 82 N LEU C 50
SHEET 1 AA7 3 SER D 4 GLN D 8 0
SHEET 2 AA7 3 GLN D 28 SER D 34 1 O ASN D 32 N ILE D 7
SHEET 3 AA7 3 LYS D 92 ASP D 98 -1 O ASP D 93 N LEU D 33
SHEET 1 AA8 5 ALA D 19 ASP D 23 0
SHEET 2 AA8 5 LYS D 122 LYS D 128 1 O THR D 126 N VAL D 22
SHEET 3 AA8 5 TYR D 108 PHE D 111 -1 N TYR D 108 O LEU D 125
SHEET 4 AA8 5 VAL D 49 THR D 52 -1 N SER D 51 O MET D 109
SHEET 5 AA8 5 ALA D 82 HIS D 83 -1 O ALA D 82 N LEU D 50
SHEET 1 AA9 3 SER E 4 GLN E 8 0
SHEET 2 AA9 3 GLN E 28 SER E 34 1 O ASN E 32 N ILE E 7
SHEET 3 AA9 3 LYS E 92 ASP E 98 -1 O PHE E 97 N PHE E 29
SHEET 1 AB1 5 ALA E 19 ASP E 23 0
SHEET 2 AB1 5 LYS E 122 LYS E 128 1 O THR E 124 N ILE E 20
SHEET 3 AB1 5 TYR E 108 PHE E 111 -1 N TYR E 108 O LEU E 125
SHEET 4 AB1 5 VAL E 49 THR E 52 -1 N VAL E 49 O PHE E 111
SHEET 5 AB1 5 ALA E 82 HIS E 83 -1 O ALA E 82 N LEU E 50
SHEET 1 AB2 3 SER F 4 GLN F 8 0
SHEET 2 AB2 3 GLN F 28 SER F 34 1 O ASN F 32 N ILE F 7
SHEET 3 AB2 3 LYS F 92 ASP F 98 -1 O ASP F 93 N LEU F 33
SHEET 1 AB3 5 ALA F 19 ASP F 23 0
SHEET 2 AB3 5 LYS F 122 LYS F 128 1 O THR F 126 N VAL F 22
SHEET 3 AB3 5 TYR F 108 PHE F 111 -1 N PHE F 110 O GLY F 123
SHEET 4 AB3 5 VAL F 49 THR F 52 -1 N SER F 51 O MET F 109
SHEET 5 AB3 5 ALA F 82 HIS F 83 -1 O ALA F 82 N LEU F 50
SHEET 1 AB4 3 SER G 4 GLN G 8 0
SHEET 2 AB4 3 GLN G 28 SER G 34 1 O ASN G 32 N ILE G 7
SHEET 3 AB4 3 LYS G 92 ASP G 98 -1 O ASP G 93 N LEU G 33
SHEET 1 AB5 5 ALA G 19 ASP G 23 0
SHEET 2 AB5 5 LYS G 122 LYS G 128 1 O THR G 126 N VAL G 22
SHEET 3 AB5 5 TYR G 108 PHE G 111 -1 N PHE G 110 O GLY G 123
SHEET 4 AB5 5 VAL G 49 THR G 52 -1 N VAL G 49 O PHE G 111
SHEET 5 AB5 5 ALA G 82 HIS G 83 -1 O ALA G 82 N LEU G 50
SHEET 1 AB6 3 SER H 4 GLN H 8 0
SHEET 2 AB6 3 GLN H 28 SER H 34 1 O ASN H 32 N VAL H 5
SHEET 3 AB6 3 LYS H 92 ASP H 98 -1 O ASP H 93 N LEU H 33
SHEET 1 AB7 5 ALA H 19 VAL H 22 0
SHEET 2 AB7 5 LYS H 122 LEU H 127 1 O THR H 126 N VAL H 22
SHEET 3 AB7 5 TYR H 108 PHE H 111 -1 N PHE H 110 O GLY H 123
SHEET 4 AB7 5 VAL H 49 THR H 52 -1 N SER H 51 O MET H 109
SHEET 5 AB7 5 ALA H 82 HIS H 83 -1 O ALA H 82 N LEU H 50
SHEET 1 AB8 3 SER I 4 GLN I 8 0
SHEET 2 AB8 3 GLN I 28 SER I 34 1 O ASN I 32 N ILE I 7
SHEET 3 AB8 3 LYS I 92 ASP I 98 -1 O ASP I 93 N LEU I 33
SHEET 1 AB9 5 ALA I 19 ASP I 23 0
SHEET 2 AB9 5 LYS I 122 LYS I 128 1 O THR I 126 N VAL I 22
SHEET 3 AB9 5 TYR I 108 PHE I 111 -1 N PHE I 110 O GLY I 123
SHEET 4 AB9 5 VAL I 49 THR I 52 -1 N SER I 51 O MET I 109
SHEET 5 AB9 5 ALA I 82 HIS I 83 -1 O ALA I 82 N LEU I 50
SHEET 1 AC1 3 SER J 4 GLN J 8 0
SHEET 2 AC1 3 GLN J 28 SER J 34 1 O ASN J 32 N ILE J 7
SHEET 3 AC1 3 LYS J 92 ASP J 98 -1 O ASP J 93 N LEU J 33
SHEET 1 AC2 5 ALA J 19 VAL J 22 0
SHEET 2 AC2 5 LYS J 122 LEU J 127 1 O THR J 126 N VAL J 22
SHEET 3 AC2 5 TYR J 108 PHE J 111 -1 N PHE J 110 O GLY J 123
SHEET 4 AC2 5 VAL J 49 THR J 52 -1 N VAL J 49 O PHE J 111
SHEET 5 AC2 5 ALA J 82 HIS J 83 -1 O ALA J 82 N LEU J 50
SHEET 1 AC3 3 SER K 4 GLN K 8 0
SHEET 2 AC3 3 GLN K 28 SER K 34 1 O ASN K 32 N ILE K 7
SHEET 3 AC3 3 LYS K 92 ASP K 98 -1 O VAL K 95 N VAL K 31
SHEET 1 AC4 5 ALA K 19 ASP K 23 0
SHEET 2 AC4 5 LYS K 122 LYS K 128 1 O THR K 124 N ILE K 20
SHEET 3 AC4 5 TYR K 108 PHE K 111 -1 N TYR K 108 O LEU K 125
SHEET 4 AC4 5 VAL K 49 THR K 52 -1 N VAL K 49 O PHE K 111
SHEET 5 AC4 5 ALA K 82 HIS K 83 -1 O ALA K 82 N LEU K 50
SHEET 1 AC5 3 SER L 4 GLN L 8 0
SHEET 2 AC5 3 GLN L 28 SER L 34 1 O ASN L 32 N ILE L 7
SHEET 3 AC5 3 LYS L 92 ASP L 98 -1 O ASP L 93 N LEU L 33
SHEET 1 AC6 5 ALA L 19 ASP L 23 0
SHEET 2 AC6 5 LYS L 122 LYS L 128 1 O THR L 126 N VAL L 22
SHEET 3 AC6 5 TYR L 108 PHE L 111 -1 N PHE L 110 O GLY L 123
SHEET 4 AC6 5 VAL L 49 THR L 52 -1 N SER L 51 O MET L 109
SHEET 5 AC6 5 ALA L 82 HIS L 83 -1 O ALA L 82 N LEU L 50
SHEET 1 AC7 3 SER M 4 GLN M 8 0
SHEET 2 AC7 3 GLN M 28 SER M 34 1 O ASN M 32 N VAL M 5
SHEET 3 AC7 3 LYS M 92 ASP M 98 -1 O VAL M 95 N VAL M 31
SHEET 1 AC8 5 ALA M 19 THR M 21 0
SHEET 2 AC8 5 LYS M 122 THR M 126 1 O THR M 126 N ILE M 20
SHEET 3 AC8 5 TYR M 108 PHE M 111 -1 N TYR M 108 O LEU M 125
SHEET 4 AC8 5 VAL M 49 THR M 52 -1 N VAL M 49 O PHE M 111
SHEET 5 AC8 5 ALA M 82 HIS M 83 -1 O ALA M 82 N LEU M 50
SHEET 1 AC9 3 SER N 4 GLN N 8 0
SHEET 2 AC9 3 GLN N 28 SER N 34 1 O ASN N 32 N ILE N 7
SHEET 3 AC9 3 LYS N 92 ASP N 98 -1 O ASP N 93 N LEU N 33
SHEET 1 AD1 5 ALA N 19 ASP N 23 0
SHEET 2 AD1 5 LYS N 122 LYS N 128 1 O THR N 126 N VAL N 22
SHEET 3 AD1 5 TYR N 108 PHE N 111 -1 N TYR N 108 O LEU N 125
SHEET 4 AD1 5 VAL N 49 THR N 52 -1 N SER N 51 O MET N 109
SHEET 5 AD1 5 ALA N 82 HIS N 83 -1 O ALA N 82 N LEU N 50
SHEET 1 AD2 3 SER O 4 GLN O 8 0
SHEET 2 AD2 3 GLN O 28 SER O 34 1 O ASN O 32 N ILE O 7
SHEET 3 AD2 3 LYS O 92 ASP O 98 -1 O VAL O 95 N VAL O 31
SHEET 1 AD3 5 ALA O 19 THR O 21 0
SHEET 2 AD3 5 LYS O 122 THR O 126 1 O THR O 126 N ILE O 20
SHEET 3 AD3 5 TYR O 108 PHE O 111 -1 N TYR O 108 O LEU O 125
SHEET 4 AD3 5 VAL O 49 THR O 52 -1 N VAL O 49 O PHE O 111
SHEET 5 AD3 5 ALA O 82 HIS O 83 -1 O ALA O 82 N LEU O 50
SHEET 1 AD4 3 SER P 4 GLN P 8 0
SHEET 2 AD4 3 GLN P 28 SER P 34 1 O ASN P 32 N ILE P 7
SHEET 3 AD4 3 LYS P 92 ASP P 98 -1 O ASP P 93 N LEU P 33
SHEET 1 AD5 5 ALA P 19 ASP P 23 0
SHEET 2 AD5 5 LYS P 122 LYS P 128 1 O THR P 124 N ILE P 20
SHEET 3 AD5 5 TYR P 108 PHE P 111 -1 N TYR P 108 O LEU P 125
SHEET 4 AD5 5 VAL P 49 THR P 52 -1 N SER P 51 O MET P 109
SHEET 5 AD5 5 ALA P 82 HIS P 83 -1 O ALA P 82 N LEU P 50
SSBOND 1 CYS A 3 CYS A 26 1555 1555 2.03
SSBOND 2 CYS B 3 CYS B 26 1555 1555 2.04
SSBOND 3 CYS C 3 CYS C 26 1555 1555 2.04
SSBOND 4 CYS D 3 CYS D 26 1555 1555 2.04
SSBOND 5 CYS E 3 CYS E 26 1555 1555 2.02
SSBOND 6 CYS F 3 CYS F 26 1555 1555 2.02
SSBOND 7 CYS G 3 CYS G 26 1555 1555 2.03
SSBOND 8 CYS H 3 CYS H 26 1555 1555 2.03
SSBOND 9 CYS I 3 CYS I 26 1555 1555 2.02
SSBOND 10 CYS J 3 CYS J 26 1555 1555 2.03
SSBOND 11 CYS K 3 CYS K 26 1555 1555 2.03
SSBOND 12 CYS L 3 CYS L 26 1555 1555 2.02
SSBOND 13 CYS M 3 CYS M 26 1555 1555 2.03
SSBOND 14 CYS N 3 CYS N 26 1555 1555 2.03
SSBOND 15 CYS O 3 CYS O 26 1555 1555 2.03
SSBOND 16 CYS P 3 CYS P 26 1555 1555 2.03
LINK C PHE A 29 N R1A A 30 1555 1555 1.33
LINK C R1A A 30 N VAL A 31 1555 1555 1.33
LINK C PHE B 29 N R1A B 30 1555 1555 1.33
LINK C R1A B 30 N VAL B 31 1555 1555 1.33
LINK C PHE C 29 N R1A C 30 1555 1555 1.33
LINK C R1A C 30 N VAL C 31 1555 1555 1.33
LINK C PHE D 29 N R1A D 30 1555 1555 1.33
LINK C R1A D 30 N VAL D 31 1555 1555 1.32
LINK C PHE E 29 N R1A E 30 1555 1555 1.33
LINK C R1A E 30 N VAL E 31 1555 1555 1.33
LINK C PHE F 29 N R1A F 30 1555 1555 1.34
LINK C R1A F 30 N VAL F 31 1555 1555 1.33
LINK C PHE G 29 N R1A G 30 1555 1555 1.33
LINK C R1A G 30 N VAL G 31 1555 1555 1.32
LINK C PHE H 29 N R1A H 30 1555 1555 1.33
LINK C R1A H 30 N VAL H 31 1555 1555 1.32
LINK C PHE I 29 N R1A I 30 1555 1555 1.32
LINK C R1A I 30 N VAL I 31 1555 1555 1.33
LINK C PHE J 29 N R1A J 30 1555 1555 1.33
LINK C R1A J 30 N VAL J 31 1555 1555 1.33
LINK C PHE K 29 N R1A K 30 1555 1555 1.33
LINK C R1A K 30 N VAL K 31 1555 1555 1.33
LINK C PHE L 29 N R1A L 30 1555 1555 1.34
LINK C R1A L 30 N VAL L 31 1555 1555 1.32
LINK C PHE M 29 N R1A M 30 1555 1555 1.33
LINK C R1A M 30 N VAL M 31 1555 1555 1.33
LINK C PHE N 29 N R1A N 30 1555 1555 1.33
LINK C R1A N 30 N VAL N 31 1555 1555 1.33
LINK C PHE O 29 N R1A O 30 1555 1555 1.33
LINK C R1A O 30 N VAL O 31 1555 1555 1.33
LINK C PHE P 29 N R1A P 30 1555 1555 1.34
LINK C R1A P 30 N VAL P 31 1555 1555 1.33
LINK O GLY A 45 CU CU A 201 1555 1555 2.13
LINK ND1 HIS A 46 CU CU A 201 1555 1555 2.03
LINK SG CYS A 112 CU CU A 201 1555 1555 2.19
LINK ND1 HIS A 117 CU CU A 201 1555 1555 2.07
LINK O GLY B 45 CU CU B 201 1555 1555 2.29
LINK ND1 HIS B 46 CU CU B 201 1555 1555 2.01
LINK SG CYS B 112 CU CU B 201 1555 1555 2.29
LINK ND1 HIS B 117 CU CU B 201 1555 1555 2.01
LINK O GLY C 45 CU CU C 201 1555 1555 2.25
LINK ND1 HIS C 46 CU CU C 201 1555 1555 2.06
LINK SG CYS C 112 CU CU C 201 1555 1555 2.31
LINK ND1 HIS C 117 CU CU C 201 1555 1555 1.98
LINK O GLY D 45 CU CU D 201 1555 1555 2.24
LINK ND1 HIS D 46 CU CU D 201 1555 1555 1.95
LINK SG CYS D 112 CU CU D 201 1555 1555 2.31
LINK ND1 HIS D 117 CU CU D 201 1555 1555 1.84
LINK O GLY E 45 CU CU E 201 1555 1555 2.32
LINK ND1 HIS E 46 CU CU E 201 1555 1555 2.03
LINK SG CYS E 112 CU CU E 201 1555 1555 2.19
LINK ND1 HIS E 117 CU CU E 201 1555 1555 1.90
LINK O GLY F 45 CU CU F 201 1555 1555 2.14
LINK ND1 HIS F 46 CU CU F 201 1555 1555 2.03
LINK SG CYS F 112 CU CU F 201 1555 1555 2.32
LINK ND1 HIS F 117 CU CU F 201 1555 1555 2.04
LINK O GLY G 45 CU CU G 201 1555 1555 2.16
LINK ND1 HIS G 46 CU CU G 201 1555 1555 1.93
LINK SG CYS G 112 CU CU G 201 1555 1555 2.35
LINK ND1 HIS G 117 CU CU G 201 1555 1555 1.95
LINK O GLY H 45 CU CU H 201 1555 1555 2.44
LINK ND1 HIS H 46 CU CU H 201 1555 1555 2.21
LINK SG CYS H 112 CU CU H 201 1555 1555 2.32
LINK ND1 HIS H 117 CU CU H 201 1555 1555 1.95
LINK O GLY I 45 CU CU I 201 1555 1555 2.33
LINK ND1 HIS I 46 CU CU I 201 1555 1555 2.14
LINK SG CYS I 112 CU CU I 201 1555 1555 2.31
LINK ND1 HIS I 117 CU CU I 201 1555 1555 1.95
LINK O GLY J 45 CU CU J 201 1555 1555 2.15
LINK ND1 HIS J 46 CU CU J 201 1555 1555 2.08
LINK SG CYS J 112 CU CU J 201 1555 1555 2.33
LINK ND1 HIS J 117 CU CU J 201 1555 1555 1.90
LINK O GLY K 45 CU CU K 201 1555 1555 2.29
LINK ND1 HIS K 46 CU CU K 201 1555 1555 2.03
LINK SG CYS K 112 CU CU K 201 1555 1555 2.27
LINK ND1 HIS K 117 CU CU K 201 1555 1555 1.91
LINK O GLY L 45 CU CU L 201 1555 1555 2.11
LINK ND1 HIS L 46 CU CU L 201 1555 1555 2.02
LINK SG CYS L 112 CU CU L 201 1555 1555 2.31
LINK ND1 HIS L 117 CU CU L 201 1555 1555 1.94
LINK O GLY M 45 CU CU M 201 1555 1555 2.28
LINK ND1 HIS M 46 CU CU M 201 1555 1555 2.01
LINK SG CYS M 112 CU CU M 201 1555 1555 2.31
LINK ND1 HIS M 117 CU CU M 201 1555 1555 2.07
LINK O GLY N 45 CU CU N 201 1555 1555 2.28
LINK ND1 HIS N 46 CU CU N 201 1555 1555 1.97
LINK SG CYS N 112 CU CU N 201 1555 1555 2.29
LINK ND1 HIS N 117 CU CU N 201 1555 1555 1.85
LINK O GLY O 45 CU CU O 201 1555 1555 2.16
LINK ND1 HIS O 46 CU CU O 201 1555 1555 2.10
LINK SG CYS O 112 CU CU O 201 1555 1555 2.24
LINK ND1 HIS O 117 CU CU O 201 1555 1555 2.12
LINK O GLY P 45 CU CU P 201 1555 1555 2.23
LINK ND1 HIS P 46 CU CU P 201 1555 1555 2.04
LINK SG CYS P 112 CU CU P 201 1555 1555 2.29
LINK ND1 HIS P 117 CU CU P 201 1555 1555 2.03
SITE 1 AC1 5 GLY A 45 HIS A 46 CYS A 112 HIS A 117
SITE 2 AC1 5 MET A 121
SITE 1 AC2 1 ASP A 69
SITE 1 AC3 5 GLY B 45 HIS B 46 CYS B 112 HIS B 117
SITE 2 AC3 5 MET B 121
SITE 1 AC4 5 GLY C 45 HIS C 46 CYS C 112 HIS C 117
SITE 2 AC4 5 MET C 121
SITE 1 AC5 5 GLY D 45 HIS D 46 CYS D 112 HIS D 117
SITE 2 AC5 5 MET D 121
SITE 1 AC6 6 GLY E 45 HIS E 46 CYS E 112 PHE E 114
SITE 2 AC6 6 HIS E 117 MET E 121
SITE 1 AC7 5 GLY F 45 HIS F 46 CYS F 112 HIS F 117
SITE 2 AC7 5 MET F 121
SITE 1 AC8 5 GLY G 45 HIS G 46 CYS G 112 HIS G 117
SITE 2 AC8 5 MET G 121
SITE 1 AC9 5 GLY H 45 HIS H 46 CYS H 112 HIS H 117
SITE 2 AC9 5 MET H 121
SITE 1 AD1 5 GLY I 45 HIS I 46 CYS I 112 HIS I 117
SITE 2 AD1 5 MET I 121
SITE 1 AD2 5 GLY J 45 HIS J 46 CYS J 112 HIS J 117
SITE 2 AD2 5 MET J 121
SITE 1 AD3 6 GLY K 45 HIS K 46 CYS K 112 PHE K 114
SITE 2 AD3 6 HIS K 117 MET K 121
SITE 1 AD4 5 GLY L 45 HIS L 46 CYS L 112 HIS L 117
SITE 2 AD4 5 MET L 121
SITE 1 AD5 5 GLY M 45 HIS M 46 CYS M 112 HIS M 117
SITE 2 AD5 5 MET M 121
SITE 1 AD6 5 GLY N 45 HIS N 46 CYS N 112 HIS N 117
SITE 2 AD6 5 MET N 121
SITE 1 AD7 5 GLY O 45 HIS O 46 CYS O 112 HIS O 117
SITE 2 AD7 5 MET O 121
SITE 1 AD8 5 GLY P 45 HIS P 46 CYS P 112 HIS P 117
SITE 2 AD8 5 MET P 121
SITE 1 AD9 14 CYS B 3 SER B 4 VAL B 5 ASP B 6
SITE 2 AD9 14 VAL B 22 GLN B 28 VAL B 31 ASN B 32
SITE 3 AD9 14 VAL B 95 THR B 96 PHE B 97 GLN P 28
SITE 4 AD9 14 R1A P 30 THR P 96
SITE 1 AE1 13 CYS B 3 SER B 4 VAL B 5 ASP B 6
SITE 2 AE1 13 PHE B 29 ASN B 32 TRP B 48 SER B 94
SITE 3 AE1 13 VAL B 95 THR B 96 GLN P 28 R1A P 30
SITE 4 AE1 13 THR P 96
SITE 1 AE2 12 CYS A 3 GLN A 28 CYS C 3 SER C 4
SITE 2 AE2 12 VAL C 5 ASP C 6 GLN C 28 VAL C 31
SITE 3 AE2 12 ASN C 32 VAL C 95 THR C 96 PHE C 97
SITE 1 AE3 13 CYS A 3 GLN A 28 CYS C 3 SER C 4
SITE 2 AE3 13 VAL C 5 ASP C 6 ILE C 7 PHE C 29
SITE 3 AE3 13 ASN C 32 TRP C 48 SER C 94 VAL C 95
SITE 4 AE3 13 THR C 96
SITE 1 AE4 14 CYS D 3 SER D 4 VAL D 5 VAL D 22
SITE 2 AE4 14 GLN D 28 VAL D 31 ASN D 32 SER D 94
SITE 3 AE4 14 VAL D 95 THR D 96 PHE D 97 CYS M 3
SITE 4 AE4 14 GLN M 28 PHE M 29
SITE 1 AE5 13 CYS D 3 SER D 4 VAL D 5 ILE D 7
SITE 2 AE5 13 PHE D 29 ASN D 32 TRP D 48 SER D 94
SITE 3 AE5 13 VAL D 95 THR D 96 CYS M 3 GLN M 28
SITE 4 AE5 13 PHE M 29
SITE 1 AE6 11 CYS E 3 SER E 4 VAL E 5 ASP E 6
SITE 2 AE6 11 GLN E 28 VAL E 31 ASN E 32 SER E 94
SITE 3 AE6 11 VAL E 95 THR E 96 PHE E 97
SITE 1 AE7 12 CYS E 3 SER E 4 VAL E 5 ASP E 6
SITE 2 AE7 12 ILE E 7 GLN E 28 PHE E 29 ASN E 32
SITE 3 AE7 12 TRP E 48 SER E 94 VAL E 95 THR E 96
SITE 1 AE8 14 CYS F 3 SER F 4 VAL F 5 ASP F 6
SITE 2 AE8 14 GLN F 28 VAL F 31 ASN F 32 SER F 94
SITE 3 AE8 14 VAL F 95 THR F 96 PHE F 97 GLN H 28
SITE 4 AE8 14 PHE H 97 ASP H 98
SITE 1 AE9 14 CYS F 3 SER F 4 VAL F 5 ASP F 6
SITE 2 AE9 14 ILE F 7 PHE F 29 ASN F 32 TRP F 48
SITE 3 AE9 14 SER F 94 VAL F 95 THR F 96 GLN H 28
SITE 4 AE9 14 PHE H 97 ASP H 98
SITE 1 AF1 9 CYS G 3 SER G 4 VAL G 5 VAL G 22
SITE 2 AF1 9 GLN G 28 VAL G 31 VAL G 95 THR G 96
SITE 3 AF1 9 PHE G 97
SITE 1 AF2 11 CYS G 3 SER G 4 VAL G 5 ILE G 7
SITE 2 AF2 11 GLN G 28 PHE G 29 ASN G 32 TRP G 48
SITE 3 AF2 11 SER G 94 VAL G 95 THR G 96
SITE 1 AF3 13 CYS F 3 GLN F 28 THR F 96 CYS H 3
SITE 2 AF3 13 SER H 4 VAL H 5 ILE H 20 GLN H 28
SITE 3 AF3 13 VAL H 31 ASN H 32 VAL H 95 THR H 96
SITE 4 AF3 13 PHE H 97
SITE 1 AF4 15 CYS F 3 GLN F 28 THR F 96 CYS H 3
SITE 2 AF4 15 SER H 4 VAL H 5 ILE H 7 GLN H 28
SITE 3 AF4 15 PHE H 29 ASN H 32 LEU H 33 TRP H 48
SITE 4 AF4 15 SER H 94 VAL H 95 THR H 96
SITE 1 AF5 14 CYS I 3 SER I 4 VAL I 5 ILE I 20
SITE 2 AF5 14 GLN I 28 VAL I 31 VAL I 95 THR I 96
SITE 3 AF5 14 PHE I 97 VAL I 99 CYS L 3 SER L 4
SITE 4 AF5 14 GLN L 28 THR L 96
SITE 1 AF6 16 CYS I 3 SER I 4 VAL I 5 ILE I 7
SITE 2 AF6 16 GLN I 28 PHE I 29 ASN I 32 LEU I 33
SITE 3 AF6 16 TRP I 48 SER I 94 VAL I 95 THR I 96
SITE 4 AF6 16 CYS L 3 SER L 4 GLN L 28 THR L 96
SITE 1 AF7 9 CYS J 3 SER J 4 VAL J 5 GLN J 28
SITE 2 AF7 9 VAL J 31 ASN J 32 VAL J 95 THR J 96
SITE 3 AF7 9 PHE J 97
SITE 1 AF8 11 CYS J 3 SER J 4 VAL J 5 ILE J 7
SITE 2 AF8 11 GLN J 28 PHE J 29 ASN J 32 TRP J 48
SITE 3 AF8 11 SER J 94 VAL J 95 THR J 96
SITE 1 AF9 11 CYS K 3 SER K 4 VAL K 5 ASP K 6
SITE 2 AF9 11 GLN K 28 VAL K 31 ASN K 32 SER K 94
SITE 3 AF9 11 VAL K 95 THR K 96 PHE K 97
SITE 1 AG1 11 CYS K 3 SER K 4 VAL K 5 ASP K 6
SITE 2 AG1 11 GLN K 28 PHE K 29 ASN K 32 TRP K 48
SITE 3 AG1 11 SER K 94 VAL K 95 THR K 96
SITE 1 AG2 14 GLN I 28 PHE I 97 HOH I 331 CYS L 3
SITE 2 AG2 14 SER L 4 VAL L 5 VAL L 22 GLN L 28
SITE 3 AG2 14 VAL L 31 ASN L 32 SER L 94 VAL L 95
SITE 4 AG2 14 THR L 96 PHE L 97
SITE 1 AG3 12 GLN I 28 PHE I 97 HOH I 331 CYS L 3
SITE 2 AG3 12 SER L 4 VAL L 5 PHE L 29 ASN L 32
SITE 3 AG3 12 TRP L 48 SER L 94 VAL L 95 THR L 96
SITE 1 AG4 16 GLN D 28 R1A D 30 THR D 96 PHE D 97
SITE 2 AG4 16 ASP D 98 CYS M 3 SER M 4 VAL M 5
SITE 3 AG4 16 ASP M 6 GLN M 28 VAL M 31 ASN M 32
SITE 4 AG4 16 SER M 94 VAL M 95 THR M 96 PHE M 97
SITE 1 AG5 14 GLN D 28 THR D 96 PHE D 97 ASP D 98
SITE 2 AG5 14 CYS M 3 SER M 4 VAL M 5 ASP M 6
SITE 3 AG5 14 ILE M 7 PHE M 29 ASN M 32 SER M 94
SITE 4 AG5 14 VAL M 95 THR M 96
SITE 1 AG6 14 CYS N 3 SER N 4 VAL N 5 GLN N 28
SITE 2 AG6 14 VAL N 31 ASN N 32 SER N 94 VAL N 95
SITE 3 AG6 14 THR N 96 PHE N 97 CYS O 3 GLN O 28
SITE 4 AG6 14 R1A O 30 THR O 96
SITE 1 AG7 15 CYS N 3 SER N 4 VAL N 5 ILE N 7
SITE 2 AG7 15 GLN N 28 PHE N 29 ASN N 32 TRP N 48
SITE 3 AG7 15 SER N 94 VAL N 95 THR N 96 CYS O 3
SITE 4 AG7 15 GLN O 28 R1A O 30 THR O 96
SITE 1 AG8 15 GLN N 28 R1A N 30 THR N 96 PHE N 97
SITE 2 AG8 15 ASP N 98 CYS O 3 SER O 4 VAL O 5
SITE 3 AG8 15 ASP O 6 GLN O 28 VAL O 31 ASN O 32
SITE 4 AG8 15 VAL O 95 THR O 96 PHE O 97
SITE 1 AG9 16 GLN N 28 R1A N 30 THR N 96 PHE N 97
SITE 2 AG9 16 ASP N 98 CYS O 3 SER O 4 VAL O 5
SITE 3 AG9 16 ASP O 6 ILE O 7 PHE O 29 ASN O 32
SITE 4 AG9 16 TRP O 48 SER O 94 VAL O 95 THR O 96
SITE 1 AH1 11 GLN B 28 R1A B 30 CYS P 3 SER P 4
SITE 2 AH1 11 VAL P 5 GLN P 28 VAL P 31 ASN P 32
SITE 3 AH1 11 VAL P 95 THR P 96 PHE P 97
SITE 1 AH2 12 GLN B 28 R1A B 30 CYS P 3 SER P 4
SITE 2 AH2 12 VAL P 5 ILE P 7 PHE P 29 ASN P 32
SITE 3 AH2 12 TRP P 48 SER P 94 VAL P 95 THR P 96
CRYST1 242.478 105.560 100.051 90.00 114.42 90.00 C 1 2 1 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 0.004124 0.000000 0.001872 0.00000
SCALE2 0.000000 0.009473 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010977 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
