HEADER ELECTRON TRANSPORT 30-SEP-10 3P1M
TITLE CRYSTAL STRUCTURE OF HUMAN FERREDOXIN-1 (FDX1) IN COMPLEX WITH IRON-
TITLE 2 SULFUR CLUSTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADRENODOXIN, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: 2FE-2S FERREDOXIN-TYPE DOMAIN, UNP RESIDUES 61-184;
COMPND 5 SYNONYM: ADRENAL FERREDOXIN, FERREDOXIN-1, HEPATOREDOXIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADX, FDX1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF
KEYWDS STRUCTURAL GENOMICS CONSORTIUM, SGC, ELECTRON TRANSPORT, ADRENODOXIN,
KEYWDS 2 FERREDOXIN, IRON-SULFUR CLUSTER, MITOCHONDRIA
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,C.JOHANSSON,T.KROJER,W.W.YUE,C.PHILLIPS,J.E.BRAY,
AUTHOR 2 A.C.W.PIKE,J.R.C.MUNIZ,M.VOLLMAR,J.WEIGELT,C.H.ARROWSMITH,
AUTHOR 3 A.M.EDWARDS,C.BOUNTRA,K.KAVANAGH,U.OPPERMANN,STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (SGC)
REVDAT 2 01-NOV-23 3P1M 1 REMARK SEQADV LINK
REVDAT 1 03-NOV-10 3P1M 0
JRNL AUTH A.CHAIKUAD,C.JOHANSSON,T.KROJER,W.W.YUE,C.PHILLIPS,J.E.BRAY,
JRNL AUTH 2 A.C.W.PIKE,J.R.C.MUNIZ,M.VOLLMAR,J.WEIGELT,C.H.ARROWSMITH,
JRNL AUTH 3 A.M.EDWARDS,C.BOUNTRA,K.KAVANAGH,U.OPPERMANN
JRNL TITL CRYSTAL STRUCTURE OF HUMAN FERREDOXIN-1 (FDX1) IN COMPLEX
JRNL TITL 2 WITH IRON-SULFUR CLUSTER
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 48817
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1971
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.60
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3528
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 145
REMARK 3 BIN FREE R VALUE : 0.3750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7733
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 169
REMARK 3 SOLVENT ATOMS : 259
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.08000
REMARK 3 B22 (A**2) : -1.08000
REMARK 3 B33 (A**2) : 1.62000
REMARK 3 B12 (A**2) : -0.54000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.254
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.220
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.286
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7997 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5042 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10778 ; 1.486 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12363 ; 0.930 ; 3.005
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1009 ; 5.923 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 368 ;35.658 ;25.652
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1352 ;14.765 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;20.656 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1290 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8931 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1465 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5032 ; 0.421 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2108 ; 0.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8122 ; 0.786 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2965 ; 2.002 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2640 ; 2.194 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 8 ; 9.033 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 5
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : F B D E G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 F 67 F 171 1
REMARK 3 1 B 67 B 171 1
REMARK 3 1 D 67 D 171 1
REMARK 3 1 E 67 E 171 1
REMARK 3 1 G 67 G 171 1
REMARK 3 1 H 67 H 171 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 F (A): 1276 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 1276 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 1276 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 E (A): 1276 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 G (A): 1276 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 H (A): 1276 ; 0.040 ; 0.050
REMARK 3 TIGHT THERMAL 1 F (A**2): 1276 ; 0.080 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 1276 ; 0.070 ; 0.500
REMARK 3 TIGHT THERMAL 1 D (A**2): 1276 ; 0.080 ; 0.500
REMARK 3 TIGHT THERMAL 1 E (A**2): 1276 ; 0.070 ; 0.500
REMARK 3 TIGHT THERMAL 1 G (A**2): 1276 ; 0.080 ; 0.500
REMARK 3 TIGHT THERMAL 1 H (A**2): 1276 ; 0.080 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : E B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 172 E 191 5
REMARK 3 1 B 172 B 191 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 E (A): 119 ; 0.240 ; 0.500
REMARK 3 LOOSE POSITIONAL 2 E (A): 131 ; 0.870 ; 5.000
REMARK 3 MEDIUM THERMAL 2 E (A**2): 119 ; 0.280 ; 2.000
REMARK 3 LOOSE THERMAL 2 E (A**2): 131 ; 0.410 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : H D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 172 H 191 5
REMARK 3 1 D 172 D 191 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 H (A): 119 ; 0.110 ; 0.500
REMARK 3 LOOSE POSITIONAL 3 H (A): 139 ; 0.390 ; 5.000
REMARK 3 MEDIUM THERMAL 3 H (A**2): 119 ; 0.210 ; 2.000
REMARK 3 LOOSE THERMAL 3 H (A**2): 139 ; 0.340 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : G F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 G 172 G 185 5
REMARK 3 1 F 172 F 185 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 G (A): 83 ; 0.100 ; 0.500
REMARK 3 LOOSE POSITIONAL 4 G (A): 75 ; 0.450 ; 5.000
REMARK 3 MEDIUM THERMAL 4 G (A**2): 83 ; 0.600 ; 2.000
REMARK 3 LOOSE THERMAL 4 G (A**2): 75 ; 0.430 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 67 A 171 1
REMARK 3 1 C 67 C 171 1
REMARK 3 2 A 172 A 185 5
REMARK 3 2 C 172 C 185 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 1330 ; 0.110 ; 0.050
REMARK 3 MEDIUM POSITIONAL 5 A (A): 83 ; 0.060 ; 0.500
REMARK 3 LOOSE POSITIONAL 5 A (A): 80 ; 0.110 ; 5.000
REMARK 3 TIGHT THERMAL 5 A (A**2): 1330 ; 0.290 ; 0.500
REMARK 3 MEDIUM THERMAL 5 A (A**2): 83 ; 0.270 ; 2.000
REMARK 3 LOOSE THERMAL 5 A (A**2): 80 ; 0.450 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 66 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5975 16.0234 2.3919
REMARK 3 T TENSOR
REMARK 3 T11: 0.6340 T22: 0.1305
REMARK 3 T33: 0.1052 T12: -0.1510
REMARK 3 T13: -0.0522 T23: 0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 8.1660 L22: 1.0923
REMARK 3 L33: 1.0888 L12: -0.0952
REMARK 3 L13: 0.0137 L23: -0.2654
REMARK 3 S TENSOR
REMARK 3 S11: -0.1208 S12: 0.7213 S13: 0.7222
REMARK 3 S21: -0.5185 S22: 0.0989 S23: 0.0018
REMARK 3 S31: -0.4882 S32: 0.1573 S33: 0.0219
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 114 A 191
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9218 12.4119 16.8495
REMARK 3 T TENSOR
REMARK 3 T11: 0.0931 T22: 0.0164
REMARK 3 T33: 0.0284 T12: 0.0062
REMARK 3 T13: -0.0038 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 3.4968 L22: 2.6220
REMARK 3 L33: 2.9688 L12: 1.9331
REMARK 3 L13: 2.3134 L23: 1.6102
REMARK 3 S TENSOR
REMARK 3 S11: 0.0369 S12: 0.0704 S13: -0.1341
REMARK 3 S21: -0.2980 S22: -0.0294 S23: -0.1130
REMARK 3 S31: 0.0091 S32: 0.0925 S33: -0.0075
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 66 B 113
REMARK 3 ORIGIN FOR THE GROUP (A): 78.0061 15.8432 85.0910
REMARK 3 T TENSOR
REMARK 3 T11: 0.2534 T22: 0.3426
REMARK 3 T33: 0.4630 T12: 0.0633
REMARK 3 T13: -0.0282 T23: 0.1045
REMARK 3 L TENSOR
REMARK 3 L11: 3.2560 L22: 3.2210
REMARK 3 L33: 5.2976 L12: 2.5106
REMARK 3 L13: 0.5245 L23: -2.0593
REMARK 3 S TENSOR
REMARK 3 S11: 0.3322 S12: -0.1221 S13: -0.2618
REMARK 3 S21: 0.5155 S22: -0.1325 S23: -0.3363
REMARK 3 S31: -0.4017 S32: 0.1286 S33: -0.1997
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 114 B 165
REMARK 3 ORIGIN FOR THE GROUP (A): 69.8419 16.2492 75.7246
REMARK 3 T TENSOR
REMARK 3 T11: 0.0645 T22: 0.3011
REMARK 3 T33: 0.2151 T12: 0.0731
REMARK 3 T13: 0.0274 T23: 0.1732
REMARK 3 L TENSOR
REMARK 3 L11: 4.5183 L22: 3.6932
REMARK 3 L33: 5.9082 L12: 1.5021
REMARK 3 L13: -2.0511 L23: 0.3901
REMARK 3 S TENSOR
REMARK 3 S11: 0.1337 S12: -0.3036 S13: 0.3452
REMARK 3 S21: 0.1795 S22: 0.0737 S23: 0.2901
REMARK 3 S31: -0.5184 S32: -0.5079 S33: -0.2074
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 166 B 191
REMARK 3 ORIGIN FOR THE GROUP (A): 92.7661 13.0439 58.1356
REMARK 3 T TENSOR
REMARK 3 T11: 0.1994 T22: 0.3076
REMARK 3 T33: 0.3966 T12: -0.1318
REMARK 3 T13: 0.0505 T23: 0.1522
REMARK 3 L TENSOR
REMARK 3 L11: 6.7067 L22: 0.2904
REMARK 3 L33: 16.0925 L12: 0.1843
REMARK 3 L13: -9.8745 L23: -0.6219
REMARK 3 S TENSOR
REMARK 3 S11: -0.2746 S12: 0.6170 S13: -0.4736
REMARK 3 S21: 0.0145 S22: -0.1066 S23: -0.1054
REMARK 3 S31: -0.0097 S32: -0.7324 S33: 0.3813
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 65 C 113
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8149 44.3608 46.4303
REMARK 3 T TENSOR
REMARK 3 T11: 0.2688 T22: 0.3487
REMARK 3 T33: 0.1146 T12: -0.2194
REMARK 3 T13: -0.0651 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.7141 L22: 7.5672
REMARK 3 L33: 1.5503 L12: -2.3190
REMARK 3 L13: 0.2610 L23: -0.5834
REMARK 3 S TENSOR
REMARK 3 S11: 0.0736 S12: -0.6511 S13: 0.3266
REMARK 3 S21: 0.9456 S22: -0.1158 S23: -0.6379
REMARK 3 S31: -0.3985 S32: 0.3101 S33: 0.0422
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 114 C 191
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5821 46.4387 31.8074
REMARK 3 T TENSOR
REMARK 3 T11: 0.0289 T22: 0.0894
REMARK 3 T33: 0.0210 T12: -0.0342
REMARK 3 T13: -0.0145 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.0663 L22: 5.1462
REMARK 3 L33: 2.9745 L12: 0.4968
REMARK 3 L13: -0.3223 L23: -2.8474
REMARK 3 S TENSOR
REMARK 3 S11: 0.0548 S12: -0.2544 S13: 0.0052
REMARK 3 S21: 0.1023 S22: -0.0803 S23: 0.1191
REMARK 3 S31: -0.0458 S32: -0.0699 S33: 0.0255
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 65 D 113
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7695 -10.2182 68.5410
REMARK 3 T TENSOR
REMARK 3 T11: 0.2643 T22: 0.2306
REMARK 3 T33: 0.4889 T12: -0.0490
REMARK 3 T13: -0.0116 T23: 0.1916
REMARK 3 L TENSOR
REMARK 3 L11: 4.0587 L22: 3.5167
REMARK 3 L33: 7.6995 L12: -1.4223
REMARK 3 L13: 2.2001 L23: 0.0934
REMARK 3 S TENSOR
REMARK 3 S11: 0.3498 S12: -0.0983 S13: -0.7270
REMARK 3 S21: 0.1785 S22: -0.0999 S23: 0.3257
REMARK 3 S31: 0.6735 S32: -0.3675 S33: -0.2499
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 114 D 191
REMARK 3 ORIGIN FOR THE GROUP (A): 53.1118 2.9816 62.0753
REMARK 3 T TENSOR
REMARK 3 T11: 0.1064 T22: 0.1928
REMARK 3 T33: 0.1856 T12: -0.0386
REMARK 3 T13: -0.0160 T23: 0.1312
REMARK 3 L TENSOR
REMARK 3 L11: 3.9940 L22: 1.6410
REMARK 3 L33: 2.9127 L12: -1.8746
REMARK 3 L13: 2.6582 L23: -1.5776
REMARK 3 S TENSOR
REMARK 3 S11: 0.1857 S12: 0.0604 S13: -0.2690
REMARK 3 S21: -0.1359 S22: -0.0325 S23: 0.0012
REMARK 3 S31: 0.2877 S32: 0.1827 S33: -0.1533
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 65 E 113
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3796 6.2205 41.4136
REMARK 3 T TENSOR
REMARK 3 T11: 0.2303 T22: 0.3285
REMARK 3 T33: 0.5099 T12: -0.0479
REMARK 3 T13: -0.0066 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 3.1554 L22: 5.5120
REMARK 3 L33: 5.8546 L12: -3.1771
REMARK 3 L13: -0.2590 L23: -3.1524
REMARK 3 S TENSOR
REMARK 3 S11: 0.2826 S12: 0.1824 S13: 0.2186
REMARK 3 S21: -0.5969 S22: -0.1238 S23: -0.5033
REMARK 3 S31: 0.4852 S32: 0.0496 S33: -0.1588
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 114 E 165
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6629 5.8599 51.2453
REMARK 3 T TENSOR
REMARK 3 T11: 0.0823 T22: 0.3132
REMARK 3 T33: 0.2466 T12: -0.0920
REMARK 3 T13: -0.0332 T23: 0.1945
REMARK 3 L TENSOR
REMARK 3 L11: 4.1658 L22: 2.0667
REMARK 3 L33: 5.3198 L12: -0.9528
REMARK 3 L13: 2.2136 L23: 0.6645
REMARK 3 S TENSOR
REMARK 3 S11: 0.1167 S12: 0.2104 S13: -0.3729
REMARK 3 S21: -0.1022 S22: 0.1091 S23: 0.3473
REMARK 3 S31: 0.5153 S32: -0.5093 S33: -0.2258
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 166 E 191
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4163 9.1409 68.3544
REMARK 3 T TENSOR
REMARK 3 T11: 0.0701 T22: 0.3053
REMARK 3 T33: 0.3265 T12: 0.1223
REMARK 3 T13: -0.0116 T23: 0.0799
REMARK 3 L TENSOR
REMARK 3 L11: 6.4021 L22: 0.6321
REMARK 3 L33: 10.2764 L12: -0.1856
REMARK 3 L13: 7.3286 L23: -0.9517
REMARK 3 S TENSOR
REMARK 3 S11: -0.3863 S12: -0.5725 S13: 0.3721
REMARK 3 S21: 0.1209 S22: 0.0919 S23: -0.1120
REMARK 3 S31: -0.4659 S32: -0.4639 S33: 0.2944
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 64 F 113
REMARK 3 ORIGIN FOR THE GROUP (A): 65.7241 3.3331 29.8818
REMARK 3 T TENSOR
REMARK 3 T11: 0.1719 T22: 0.2908
REMARK 3 T33: 0.5190 T12: -0.0279
REMARK 3 T13: 0.0231 T23: -0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 3.7803 L22: 2.5133
REMARK 3 L33: 4.1431 L12: -1.2004
REMARK 3 L13: -0.0331 L23: -2.8700
REMARK 3 S TENSOR
REMARK 3 S11: 0.1157 S12: 0.1021 S13: -0.1295
REMARK 3 S21: 0.2251 S22: 0.2886 S23: 0.5586
REMARK 3 S31: -0.3136 S32: -0.6200 S33: -0.4044
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 114 F 184
REMARK 3 ORIGIN FOR THE GROUP (A): 77.8908 -0.9592 28.4068
REMARK 3 T TENSOR
REMARK 3 T11: 0.0533 T22: 0.1096
REMARK 3 T33: 0.0708 T12: -0.0338
REMARK 3 T13: -0.0145 T23: -0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 2.2418 L22: 5.8709
REMARK 3 L33: 1.3914 L12: 0.5134
REMARK 3 L13: -0.3252 L23: -1.0862
REMARK 3 S TENSOR
REMARK 3 S11: 0.0673 S12: -0.2073 S13: 0.3520
REMARK 3 S21: 0.1118 S22: -0.0736 S23: 0.1497
REMARK 3 S31: -0.1845 S32: -0.0679 S33: 0.0063
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 185 F 191
REMARK 3 ORIGIN FOR THE GROUP (A): 91.4430 -40.9639 33.0246
REMARK 3 T TENSOR
REMARK 3 T11: 0.9061 T22: 0.6722
REMARK 3 T33: 1.0818 T12: 0.4003
REMARK 3 T13: -0.3630 T23: -0.2553
REMARK 3 L TENSOR
REMARK 3 L11: 0.6242 L22: 26.3038
REMARK 3 L33: 48.9379 L12: 3.4240
REMARK 3 L13: -2.7407 L23: -31.6749
REMARK 3 S TENSOR
REMARK 3 S11: 0.5822 S12: 0.2867 S13: -0.4010
REMARK 3 S21: 2.3749 S22: 0.0463 S23: -1.0706
REMARK 3 S31: -0.3243 S32: 1.9583 S33: -0.6285
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 64 G 113
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6033 14.3130 18.7401
REMARK 3 T TENSOR
REMARK 3 T11: 0.3620 T22: 0.1869
REMARK 3 T33: 0.5721 T12: 0.0578
REMARK 3 T13: 0.1738 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 3.7919 L22: 3.0604
REMARK 3 L33: 5.0544 L12: -0.9484
REMARK 3 L13: 2.9381 L23: 1.9583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0746 S12: 0.2265 S13: -0.5545
REMARK 3 S21: 0.1667 S22: 0.3399 S23: -0.1577
REMARK 3 S31: 0.4328 S32: 0.5656 S33: -0.4145
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 114 G 184
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7937 22.7224 20.3388
REMARK 3 T TENSOR
REMARK 3 T11: 0.1196 T22: 0.0347
REMARK 3 T33: 0.0765 T12: 0.0141
REMARK 3 T13: 0.0192 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 5.3246 L22: 3.5382
REMARK 3 L33: 1.5306 L12: 2.2457
REMARK 3 L13: 0.6401 L23: 0.6507
REMARK 3 S TENSOR
REMARK 3 S11: 0.0267 S12: 0.1004 S13: -0.0234
REMARK 3 S21: -0.1730 S22: 0.0227 S23: -0.4247
REMARK 3 S31: -0.0711 S32: 0.1964 S33: -0.0494
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 185 G 191
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9995 14.2488 15.7235
REMARK 3 T TENSOR
REMARK 3 T11: 0.4911 T22: 0.5271
REMARK 3 T33: 0.6890 T12: 0.2752
REMARK 3 T13: 0.0705 T23: 0.1981
REMARK 3 L TENSOR
REMARK 3 L11: 18.3056 L22: 7.4959
REMARK 3 L33: 30.8387 L12: -0.1192
REMARK 3 L13: -9.7695 L23: 8.1038
REMARK 3 S TENSOR
REMARK 3 S11: -0.0449 S12: 2.2926 S13: -0.0998
REMARK 3 S21: -0.2914 S22: 0.2661 S23: 1.6383
REMARK 3 S31: -1.7297 S32: -1.8088 S33: -0.2212
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 64 H 113
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8000 32.6099 58.2607
REMARK 3 T TENSOR
REMARK 3 T11: 0.2712 T22: 0.2342
REMARK 3 T33: 0.4697 T12: 0.0502
REMARK 3 T13: 0.0021 T23: 0.1898
REMARK 3 L TENSOR
REMARK 3 L11: 4.3292 L22: 3.0873
REMARK 3 L33: 6.2796 L12: 1.2567
REMARK 3 L13: -2.3369 L23: -0.3652
REMARK 3 S TENSOR
REMARK 3 S11: 0.2921 S12: 0.1666 S13: 0.7221
REMARK 3 S21: -0.1509 S22: -0.0145 S23: 0.4469
REMARK 3 S31: -0.8394 S32: -0.3570 S33: -0.2776
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 114 H 191
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6716 18.9395 64.8148
REMARK 3 T TENSOR
REMARK 3 T11: 0.1028 T22: 0.1761
REMARK 3 T33: 0.1652 T12: 0.0319
REMARK 3 T13: -0.0019 T23: 0.1211
REMARK 3 L TENSOR
REMARK 3 L11: 4.7204 L22: 1.8706
REMARK 3 L33: 2.9602 L12: 2.1671
REMARK 3 L13: -3.1184 L23: -1.8886
REMARK 3 S TENSOR
REMARK 3 S11: 0.1894 S12: -0.0081 S13: 0.2662
REMARK 3 S21: 0.1406 S22: -0.0545 S23: -0.0101
REMARK 3 S31: -0.2572 S32: 0.1367 S33: -0.1349
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS DURING REFINEMENT
REMARK 4
REMARK 4 3P1M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000061843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH MIRROR
REMARK 200 PAIR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50786
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 50.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.72100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRY 1CJE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75M POTASSIUM CITRATE (K3CIT), PH
REMARK 280 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 156.27333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 78.13667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 300 REMARK: AUTHOR DETERMINED BIOLOGICAL UNIT: UNKNOWN.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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 60
REMARK 465 SER A 61
REMARK 465 SER A 62
REMARK 465 SER A 63
REMARK 465 GLU A 64
REMARK 465 ASP A 65
REMARK 465 MET B 60
REMARK 465 SER B 61
REMARK 465 SER B 62
REMARK 465 SER B 63
REMARK 465 GLU B 64
REMARK 465 ASP B 65
REMARK 465 MET C 60
REMARK 465 SER C 61
REMARK 465 SER C 62
REMARK 465 SER C 63
REMARK 465 GLU C 64
REMARK 465 MET D 60
REMARK 465 SER D 61
REMARK 465 SER D 62
REMARK 465 SER D 63
REMARK 465 GLU D 64
REMARK 465 MET E 60
REMARK 465 SER E 61
REMARK 465 SER E 62
REMARK 465 SER E 63
REMARK 465 GLU E 64
REMARK 465 MET F 60
REMARK 465 SER F 61
REMARK 465 SER F 62
REMARK 465 SER F 63
REMARK 465 MET G 60
REMARK 465 SER G 61
REMARK 465 SER G 62
REMARK 465 SER G 63
REMARK 465 MET H 60
REMARK 465 SER H 61
REMARK 465 SER H 62
REMARK 465 SER H 63
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 LYS B 66 CG CD CE NZ
REMARK 470 GLU B 77 CD OE1 OE2
REMARK 470 LYS B 126 CG CD CE NZ
REMARK 470 ASP C 65 CG OD1 OD2
REMARK 470 LYS C 66 CG CD CE NZ
REMARK 470 ASP D 65 CG OD1 OD2
REMARK 470 LYS D 66 CG CD CE NZ
REMARK 470 LYS D 82 CE NZ
REMARK 470 LYS D 84 CD CE NZ
REMARK 470 GLU D 95 CD OE1 OE2
REMARK 470 ASP E 65 CG OD1 OD2
REMARK 470 GLU E 77 CD OE1 OE2
REMARK 470 GLU E 95 CD OE1 OE2
REMARK 470 LYS E 126 CG CD CE NZ
REMARK 470 LYS E 158 CE NZ
REMARK 470 GLU E 186 CG CD OE1 OE2
REMARK 470 GLU F 64 CG CD OE1 OE2
REMARK 470 ASN F 97 CG OD1 ND2
REMARK 470 LYS F 158 CD CE NZ
REMARK 470 GLN F 176 CD OE1 NE2
REMARK 470 GLU G 64 CG CD OE1 OE2
REMARK 470 LYS G 158 CE NZ
REMARK 470 GLU G 186 CG CD OE1 OE2
REMARK 470 GLU H 64 CG CD OE1 OE2
REMARK 470 ASP H 65 CG OD1 OD2
REMARK 470 LYS H 66 CG CD CE NZ
REMARK 470 LYS H 82 CE NZ
REMARK 470 GLU H 95 CG CD OE1 OE2
REMARK 470 ASN H 97 CG OD1 ND2
REMARK 470 LYS H 158 CD CE NZ
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 ARG H 74 O HOH H 55 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 175 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 111 16.04 -151.41
REMARK 500 ASN A 187 76.49 -117.13
REMARK 500 LEU A 188 0.82 -67.25
REMARK 500 ALA C 111 19.09 -157.95
REMARK 500 ALA D 185 -147.37 -109.66
REMARK 500 ASN E 187 170.25 -42.75
REMARK 500 ASP H 65 56.73 -109.09
REMARK 500 ALA H 185 -143.32 -100.28
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 FES A 2 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 106 SG
REMARK 620 2 FES A 2 S1 103.2
REMARK 620 3 FES A 2 S2 108.4 93.5
REMARK 620 4 CYS A 112 SG 113.3 118.0 117.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 2 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 115 SG
REMARK 620 2 FES A 2 S1 120.1
REMARK 620 3 FES A 2 S2 115.2 95.2
REMARK 620 4 CYS A 152 SG 103.7 107.8 115.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 192 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC A 6 OHB
REMARK 620 2 SER A 177 O 128.5
REMARK 620 3 ASP A 179 OD1 103.0 108.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G 193 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 197 O
REMARK 620 2 HOH G 47 O 123.1
REMARK 620 3 SER G 177 O 83.2 84.5
REMARK 620 4 ASP G 179 OD1 84.5 49.5 110.6
REMARK 620 5 FLC G 192 OHB 103.7 128.9 123.2 126.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 3 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 106 SG
REMARK 620 2 FES B 3 S1 110.9
REMARK 620 3 FES B 3 S2 107.5 96.8
REMARK 620 4 CYS B 112 SG 111.8 115.2 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 3 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 115 SG
REMARK 620 2 FES B 3 S1 104.5
REMARK 620 3 FES B 3 S2 113.4 96.9
REMARK 620 4 CYS B 152 SG 107.3 119.4 114.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K H 192 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 177 O
REMARK 620 2 ASP B 179 OD1 105.0
REMARK 620 3 FLC H 7 OHB 154.7 96.5
REMARK 620 4 FLC H 7 OA1 103.1 133.1 51.7
REMARK 620 5 FLC H 7 OB2 119.2 133.6 46.1 51.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 193 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC B 192 OHB
REMARK 620 2 HOH B 201 O 73.0
REMARK 620 3 SER H 177 O 119.8 68.1
REMARK 620 4 ASP H 179 OD1 119.7 88.3 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 4 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 106 SG
REMARK 620 2 FES C 4 S1 111.6
REMARK 620 3 FES C 4 S2 121.1 97.3
REMARK 620 4 CYS C 112 SG 107.8 110.5 108.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 4 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 115 SG
REMARK 620 2 FES C 4 S1 118.7
REMARK 620 3 FES C 4 S2 116.1 97.4
REMARK 620 4 CYS C 152 SG 101.7 110.4 113.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 192 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC C 5 OB2
REMARK 620 2 FLC C 5 OHB 56.6
REMARK 620 3 SER C 177 O 121.3 141.4
REMARK 620 4 ASP C 179 OD1 135.7 90.3 103.0
REMARK 620 5 HOH C 203 O 52.3 108.4 86.2 137.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K F 8 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC C 8 OHB
REMARK 620 2 FLC C 8 OG2 48.7
REMARK 620 3 HOH C 222 O 103.0 116.7
REMARK 620 4 SER F 177 O 124.3 154.8 88.1
REMARK 620 5 ASP F 179 OD1 129.6 81.5 92.1 103.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D 192 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC D 2 OHB
REMARK 620 2 FLC D 2 OG1 56.8
REMARK 620 3 SER D 177 O 131.9 166.3
REMARK 620 4 SER D 177 OG 122.8 126.5 60.7
REMARK 620 5 ASP D 179 OD1 120.7 64.0 107.0 88.2
REMARK 620 6 HOH D 205 O 97.5 92.4 76.6 134.1 88.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES D 5 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 106 SG
REMARK 620 2 FES D 5 S1 97.6
REMARK 620 3 FES D 5 S2 115.6 94.4
REMARK 620 4 CYS D 112 SG 119.4 115.8 110.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES D 5 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 115 SG
REMARK 620 2 FES D 5 S1 119.1
REMARK 620 3 FES D 5 S2 106.2 93.4
REMARK 620 4 CYS D 152 SG 109.2 117.1 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E 192 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC E 4 OHB
REMARK 620 2 SER E 177 O 108.4
REMARK 620 3 ASP E 179 OD1 139.1 112.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 6 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 106 SG
REMARK 620 2 FES E 6 S1 113.7
REMARK 620 3 FES E 6 S2 106.4 96.9
REMARK 620 4 CYS E 112 SG 115.1 110.6 112.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 6 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 115 SG
REMARK 620 2 FES E 6 S1 102.5
REMARK 620 3 FES E 6 S2 117.8 95.3
REMARK 620 4 CYS E 152 SG 105.5 120.4 115.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES F 7 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 106 SG
REMARK 620 2 FES F 7 S1 107.6
REMARK 620 3 FES F 7 S2 107.5 94.5
REMARK 620 4 CYS F 112 SG 111.9 120.4 113.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES F 7 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 115 SG
REMARK 620 2 FES F 7 S1 109.0
REMARK 620 3 FES F 7 S2 119.4 95.9
REMARK 620 4 CYS F 152 SG 104.1 110.0 117.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES G 1 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 106 SG
REMARK 620 2 FES G 1 S1 109.9
REMARK 620 3 FES G 1 S2 109.6 95.0
REMARK 620 4 CYS G 112 SG 110.8 118.2 112.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES G 1 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 115 SG
REMARK 620 2 FES G 1 S1 110.1
REMARK 620 3 FES G 1 S2 119.5 96.5
REMARK 620 4 CYS G 152 SG 102.9 111.5 116.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES H 8 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 106 SG
REMARK 620 2 FES H 8 S1 102.7
REMARK 620 3 FES H 8 S2 110.3 93.7
REMARK 620 4 CYS H 112 SG 117.2 121.6 108.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES H 8 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 115 SG
REMARK 620 2 FES H 8 S1 113.9
REMARK 620 3 FES H 8 S2 113.3 93.4
REMARK 620 4 CYS H 152 SG 111.9 110.5 112.5
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 FES A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES C 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC C 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC C 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES D 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC D 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC D 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC E 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES F 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES G 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC G 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 193
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 194
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES H 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC H 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 192
DBREF 3P1M A 61 184 UNP P10109 ADX_HUMAN 61 184
DBREF 3P1M B 61 184 UNP P10109 ADX_HUMAN 61 184
DBREF 3P1M C 61 184 UNP P10109 ADX_HUMAN 61 184
DBREF 3P1M D 61 184 UNP P10109 ADX_HUMAN 61 184
DBREF 3P1M E 61 184 UNP P10109 ADX_HUMAN 61 184
DBREF 3P1M F 61 184 UNP P10109 ADX_HUMAN 61 184
DBREF 3P1M G 61 184 UNP P10109 ADX_HUMAN 61 184
DBREF 3P1M H 61 184 UNP P10109 ADX_HUMAN 61 184
SEQADV 3P1M MET A 60 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ALA A 185 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLU A 186 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ASN A 187 UNP P10109 EXPRESSION TAG
SEQADV 3P1M LEU A 188 UNP P10109 EXPRESSION TAG
SEQADV 3P1M TYR A 189 UNP P10109 EXPRESSION TAG
SEQADV 3P1M PHE A 190 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLN A 191 UNP P10109 EXPRESSION TAG
SEQADV 3P1M MET B 60 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ALA B 185 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLU B 186 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ASN B 187 UNP P10109 EXPRESSION TAG
SEQADV 3P1M LEU B 188 UNP P10109 EXPRESSION TAG
SEQADV 3P1M TYR B 189 UNP P10109 EXPRESSION TAG
SEQADV 3P1M PHE B 190 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLN B 191 UNP P10109 EXPRESSION TAG
SEQADV 3P1M MET C 60 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ALA C 185 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLU C 186 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ASN C 187 UNP P10109 EXPRESSION TAG
SEQADV 3P1M LEU C 188 UNP P10109 EXPRESSION TAG
SEQADV 3P1M TYR C 189 UNP P10109 EXPRESSION TAG
SEQADV 3P1M PHE C 190 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLN C 191 UNP P10109 EXPRESSION TAG
SEQADV 3P1M MET D 60 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ALA D 185 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLU D 186 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ASN D 187 UNP P10109 EXPRESSION TAG
SEQADV 3P1M LEU D 188 UNP P10109 EXPRESSION TAG
SEQADV 3P1M TYR D 189 UNP P10109 EXPRESSION TAG
SEQADV 3P1M PHE D 190 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLN D 191 UNP P10109 EXPRESSION TAG
SEQADV 3P1M MET E 60 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ALA E 185 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLU E 186 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ASN E 187 UNP P10109 EXPRESSION TAG
SEQADV 3P1M LEU E 188 UNP P10109 EXPRESSION TAG
SEQADV 3P1M TYR E 189 UNP P10109 EXPRESSION TAG
SEQADV 3P1M PHE E 190 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLN E 191 UNP P10109 EXPRESSION TAG
SEQADV 3P1M MET F 60 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ALA F 185 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLU F 186 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ASN F 187 UNP P10109 EXPRESSION TAG
SEQADV 3P1M LEU F 188 UNP P10109 EXPRESSION TAG
SEQADV 3P1M TYR F 189 UNP P10109 EXPRESSION TAG
SEQADV 3P1M PHE F 190 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLN F 191 UNP P10109 EXPRESSION TAG
SEQADV 3P1M MET G 60 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ALA G 185 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLU G 186 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ASN G 187 UNP P10109 EXPRESSION TAG
SEQADV 3P1M LEU G 188 UNP P10109 EXPRESSION TAG
SEQADV 3P1M TYR G 189 UNP P10109 EXPRESSION TAG
SEQADV 3P1M PHE G 190 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLN G 191 UNP P10109 EXPRESSION TAG
SEQADV 3P1M MET H 60 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ALA H 185 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLU H 186 UNP P10109 EXPRESSION TAG
SEQADV 3P1M ASN H 187 UNP P10109 EXPRESSION TAG
SEQADV 3P1M LEU H 188 UNP P10109 EXPRESSION TAG
SEQADV 3P1M TYR H 189 UNP P10109 EXPRESSION TAG
SEQADV 3P1M PHE H 190 UNP P10109 EXPRESSION TAG
SEQADV 3P1M GLN H 191 UNP P10109 EXPRESSION TAG
SEQRES 1 A 132 MET SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE
SEQRES 2 A 132 ASN ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL
SEQRES 3 A 132 GLY ASP SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU
SEQRES 4 A 132 ASP ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA
SEQRES 5 A 132 CYS SER THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR
SEQRES 6 A 132 GLU LYS LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET
SEQRES 7 A 132 LEU ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU
SEQRES 8 A 132 GLY CYS GLN ILE CYS LEU THR LYS SER MET ASP ASN MET
SEQRES 9 A 132 THR VAL ARG VAL PRO GLU THR VAL ALA ASP ALA ARG GLN
SEQRES 10 A 132 SER ILE ASP VAL GLY LYS THR SER ALA GLU ASN LEU TYR
SEQRES 11 A 132 PHE GLN
SEQRES 1 B 132 MET SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE
SEQRES 2 B 132 ASN ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL
SEQRES 3 B 132 GLY ASP SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU
SEQRES 4 B 132 ASP ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA
SEQRES 5 B 132 CYS SER THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR
SEQRES 6 B 132 GLU LYS LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET
SEQRES 7 B 132 LEU ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU
SEQRES 8 B 132 GLY CYS GLN ILE CYS LEU THR LYS SER MET ASP ASN MET
SEQRES 9 B 132 THR VAL ARG VAL PRO GLU THR VAL ALA ASP ALA ARG GLN
SEQRES 10 B 132 SER ILE ASP VAL GLY LYS THR SER ALA GLU ASN LEU TYR
SEQRES 11 B 132 PHE GLN
SEQRES 1 C 132 MET SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE
SEQRES 2 C 132 ASN ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL
SEQRES 3 C 132 GLY ASP SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU
SEQRES 4 C 132 ASP ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA
SEQRES 5 C 132 CYS SER THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR
SEQRES 6 C 132 GLU LYS LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET
SEQRES 7 C 132 LEU ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU
SEQRES 8 C 132 GLY CYS GLN ILE CYS LEU THR LYS SER MET ASP ASN MET
SEQRES 9 C 132 THR VAL ARG VAL PRO GLU THR VAL ALA ASP ALA ARG GLN
SEQRES 10 C 132 SER ILE ASP VAL GLY LYS THR SER ALA GLU ASN LEU TYR
SEQRES 11 C 132 PHE GLN
SEQRES 1 D 132 MET SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE
SEQRES 2 D 132 ASN ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL
SEQRES 3 D 132 GLY ASP SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU
SEQRES 4 D 132 ASP ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA
SEQRES 5 D 132 CYS SER THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR
SEQRES 6 D 132 GLU LYS LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET
SEQRES 7 D 132 LEU ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU
SEQRES 8 D 132 GLY CYS GLN ILE CYS LEU THR LYS SER MET ASP ASN MET
SEQRES 9 D 132 THR VAL ARG VAL PRO GLU THR VAL ALA ASP ALA ARG GLN
SEQRES 10 D 132 SER ILE ASP VAL GLY LYS THR SER ALA GLU ASN LEU TYR
SEQRES 11 D 132 PHE GLN
SEQRES 1 E 132 MET SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE
SEQRES 2 E 132 ASN ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL
SEQRES 3 E 132 GLY ASP SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU
SEQRES 4 E 132 ASP ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA
SEQRES 5 E 132 CYS SER THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR
SEQRES 6 E 132 GLU LYS LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET
SEQRES 7 E 132 LEU ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU
SEQRES 8 E 132 GLY CYS GLN ILE CYS LEU THR LYS SER MET ASP ASN MET
SEQRES 9 E 132 THR VAL ARG VAL PRO GLU THR VAL ALA ASP ALA ARG GLN
SEQRES 10 E 132 SER ILE ASP VAL GLY LYS THR SER ALA GLU ASN LEU TYR
SEQRES 11 E 132 PHE GLN
SEQRES 1 F 132 MET SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE
SEQRES 2 F 132 ASN ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL
SEQRES 3 F 132 GLY ASP SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU
SEQRES 4 F 132 ASP ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA
SEQRES 5 F 132 CYS SER THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR
SEQRES 6 F 132 GLU LYS LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET
SEQRES 7 F 132 LEU ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU
SEQRES 8 F 132 GLY CYS GLN ILE CYS LEU THR LYS SER MET ASP ASN MET
SEQRES 9 F 132 THR VAL ARG VAL PRO GLU THR VAL ALA ASP ALA ARG GLN
SEQRES 10 F 132 SER ILE ASP VAL GLY LYS THR SER ALA GLU ASN LEU TYR
SEQRES 11 F 132 PHE GLN
SEQRES 1 G 132 MET SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE
SEQRES 2 G 132 ASN ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL
SEQRES 3 G 132 GLY ASP SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU
SEQRES 4 G 132 ASP ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA
SEQRES 5 G 132 CYS SER THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR
SEQRES 6 G 132 GLU LYS LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET
SEQRES 7 G 132 LEU ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU
SEQRES 8 G 132 GLY CYS GLN ILE CYS LEU THR LYS SER MET ASP ASN MET
SEQRES 9 G 132 THR VAL ARG VAL PRO GLU THR VAL ALA ASP ALA ARG GLN
SEQRES 10 G 132 SER ILE ASP VAL GLY LYS THR SER ALA GLU ASN LEU TYR
SEQRES 11 G 132 PHE GLN
SEQRES 1 H 132 MET SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE
SEQRES 2 H 132 ASN ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS VAL
SEQRES 3 H 132 GLY ASP SER LEU LEU ASP VAL VAL VAL GLU ASN ASN LEU
SEQRES 4 H 132 ASP ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA
SEQRES 5 H 132 CYS SER THR CYS HIS LEU ILE PHE GLU ASP HIS ILE TYR
SEQRES 6 H 132 GLU LYS LEU ASP ALA ILE THR ASP GLU GLU ASN ASP MET
SEQRES 7 H 132 LEU ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU
SEQRES 8 H 132 GLY CYS GLN ILE CYS LEU THR LYS SER MET ASP ASN MET
SEQRES 9 H 132 THR VAL ARG VAL PRO GLU THR VAL ALA ASP ALA ARG GLN
SEQRES 10 H 132 SER ILE ASP VAL GLY LYS THR SER ALA GLU ASN LEU TYR
SEQRES 11 H 132 PHE GLN
HET FES A 2 4
HET FLC A 6 13
HET K A 192 1
HET FES B 3 4
HET FLC B 192 13
HET K B 193 1
HET FES C 4 4
HET FLC C 5 13
HET FLC C 8 13
HET K C 192 1
HET FES D 5 4
HET FLC D 2 13
HET FLC D 9 13
HET K D 192 1
HET FES E 6 4
HET FLC E 4 13
HET K E 192 1
HET FES F 7 4
HET K F 8 1
HET GOL F 1 6
HET FES G 1 4
HET FLC G 192 13
HET K G 193 1
HET GOL G 194 6
HET FES H 8 4
HET FLC H 7 13
HET K H 192 1
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM FLC CITRATE ANION
HETNAM K POTASSIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 FES 8(FE2 S2)
FORMUL 10 FLC 9(C6 H5 O7 3-)
FORMUL 11 K 8(K 1+)
FORMUL 28 GOL 2(C3 H8 O3)
FORMUL 36 HOH *259(H2 O)
HELIX 1 1 SER A 88 ASN A 96 1 9
HELIX 2 2 GLU A 120 LYS A 126 1 7
HELIX 3 3 THR A 131 ASP A 139 1 9
HELIX 4 4 THR A 157 ASP A 161 5 5
HELIX 5 5 THR A 170 ARG A 175 1 6
HELIX 6 6 ASN A 187 GLN A 191 5 5
HELIX 7 7 SER B 88 ASN B 96 1 9
HELIX 8 8 GLU B 120 GLU B 125 1 6
HELIX 9 9 THR B 131 ASP B 139 1 9
HELIX 10 10 THR B 157 ASP B 161 5 5
HELIX 11 11 THR B 170 ARG B 175 1 6
HELIX 12 12 SER C 88 ASN C 96 1 9
HELIX 13 13 GLU C 120 LYS C 126 1 7
HELIX 14 14 THR C 131 ASP C 139 1 9
HELIX 15 15 THR C 157 ASP C 161 5 5
HELIX 16 16 THR C 170 ARG C 175 1 6
HELIX 17 17 ASN C 187 GLN C 191 5 5
HELIX 18 18 SER D 88 ASN D 96 1 9
HELIX 19 19 GLU D 120 GLU D 125 1 6
HELIX 20 20 THR D 131 LEU D 140 1 10
HELIX 21 21 THR D 157 ASP D 161 5 5
HELIX 22 22 THR D 170 ARG D 175 1 6
HELIX 23 23 SER E 88 ASN E 96 1 9
HELIX 24 24 GLU E 120 GLU E 125 1 6
HELIX 25 25 THR E 131 ASP E 139 1 9
HELIX 26 26 THR E 157 ASP E 161 5 5
HELIX 27 27 THR E 170 ARG E 175 1 6
HELIX 28 28 SER F 88 ASN F 96 1 9
HELIX 29 29 GLU F 120 GLU F 125 1 6
HELIX 30 30 THR F 131 ASP F 139 1 9
HELIX 31 31 THR F 157 ASP F 161 5 5
HELIX 32 32 THR F 170 ARG F 175 1 6
HELIX 33 33 SER G 88 ASN G 96 1 9
HELIX 34 34 GLU G 120 GLU G 125 1 6
HELIX 35 35 THR G 131 ASP G 139 1 9
HELIX 36 36 THR G 157 ASP G 161 5 5
HELIX 37 37 THR G 170 ARG G 175 1 6
HELIX 38 38 SER H 88 ASN H 96 1 9
HELIX 39 39 GLU H 120 GLU H 125 1 6
HELIX 40 40 THR H 131 LEU H 140 1 10
HELIX 41 41 THR H 157 ASP H 161 5 5
HELIX 42 42 THR H 170 ARG H 175 1 6
SHEET 1 A 5 THR A 78 GLY A 83 0
SHEET 2 A 5 ILE A 67 ILE A 72 -1 N ILE A 67 O GLY A 83
SHEET 3 A 5 MET A 163 ARG A 166 1 O VAL A 165 N ILE A 72
SHEET 4 A 5 HIS A 116 PHE A 119 -1 N ILE A 118 O ARG A 166
SHEET 5 A 5 SER A 148 LEU A 150 -1 O ARG A 149 N LEU A 117
SHEET 1 B 3 THR B 78 GLY B 83 0
SHEET 2 B 3 ILE B 67 ILE B 72 -1 N ILE B 67 O GLY B 83
SHEET 3 B 3 MET B 163 ARG B 166 1 O MET B 163 N HIS B 70
SHEET 1 C 2 HIS B 116 ILE B 118 0
SHEET 2 C 2 SER B 148 LEU B 150 -1 O ARG B 149 N LEU B 117
SHEET 1 D 5 THR C 78 LYS C 84 0
SHEET 2 D 5 LYS C 66 ILE C 72 -1 N PHE C 71 O LEU C 79
SHEET 3 D 5 MET C 163 ARG C 166 1 O MET C 163 N HIS C 70
SHEET 4 D 5 HIS C 116 PHE C 119 -1 N ILE C 118 O ARG C 166
SHEET 5 D 5 SER C 148 LEU C 150 -1 O ARG C 149 N LEU C 117
SHEET 1 E 5 THR D 78 LYS D 84 0
SHEET 2 E 5 LYS D 66 ILE D 72 -1 N PHE D 71 O LEU D 79
SHEET 3 E 5 MET D 163 ARG D 166 1 O MET D 163 N HIS D 70
SHEET 4 E 5 HIS D 116 PHE D 119 -1 N ILE D 118 O ARG D 166
SHEET 5 E 5 SER D 148 LEU D 150 -1 O ARG D 149 N LEU D 117
SHEET 1 F 3 THR E 78 LYS E 84 0
SHEET 2 F 3 LYS E 66 ILE E 72 -1 N ILE E 67 O GLY E 83
SHEET 3 F 3 MET E 163 ARG E 166 1 O MET E 163 N HIS E 70
SHEET 1 G 2 HIS E 116 ILE E 118 0
SHEET 2 G 2 SER E 148 LEU E 150 -1 O ARG E 149 N LEU E 117
SHEET 1 H 3 THR F 78 LYS F 84 0
SHEET 2 H 3 LYS F 66 ILE F 72 -1 N ILE F 67 O GLY F 83
SHEET 3 H 3 MET F 163 ARG F 166 1 O MET F 163 N HIS F 70
SHEET 1 I 2 HIS F 116 ILE F 118 0
SHEET 2 I 2 SER F 148 LEU F 150 -1 O ARG F 149 N LEU F 117
SHEET 1 J 3 THR G 78 LYS G 84 0
SHEET 2 J 3 LYS G 66 ILE G 72 -1 N ILE G 67 O GLY G 83
SHEET 3 J 3 MET G 163 ARG G 166 1 O MET G 163 N HIS G 70
SHEET 1 K 2 HIS G 116 ILE G 118 0
SHEET 2 K 2 SER G 148 LEU G 150 -1 O ARG G 149 N LEU G 117
SHEET 1 L 5 THR H 78 LYS H 84 0
SHEET 2 L 5 LYS H 66 ILE H 72 -1 N PHE H 71 O LEU H 79
SHEET 3 L 5 MET H 163 ARG H 166 1 O MET H 163 N HIS H 70
SHEET 4 L 5 HIS H 116 PHE H 119 -1 N ILE H 118 O ARG H 166
SHEET 5 L 5 SER H 148 LEU H 150 -1 O ARG H 149 N LEU H 117
LINK FE1 FES A 2 SG CYS A 106 1555 1555 2.06
LINK FE1 FES A 2 SG CYS A 112 1555 1555 2.09
LINK FE2 FES A 2 SG CYS A 115 1555 1555 2.05
LINK FE2 FES A 2 SG CYS A 152 1555 1555 2.07
LINK OHB FLC A 6 K K A 192 1555 1555 2.29
LINK O SER A 177 K K A 192 1555 1555 2.43
LINK OD1 ASP A 179 K K A 192 1555 1555 2.94
LINK O HOH A 197 K K G 193 1555 1555 2.82
LINK FE1 FES B 3 SG CYS B 106 1555 1555 2.06
LINK FE1 FES B 3 SG CYS B 112 1555 1555 2.06
LINK FE2 FES B 3 SG CYS B 115 1555 1555 2.08
LINK FE2 FES B 3 SG CYS B 152 1555 1555 2.06
LINK O SER B 177 K K H 192 1555 1555 2.57
LINK OD1 ASP B 179 K K H 192 1555 1555 2.63
LINK OHB FLC B 192 K K B 193 1555 1555 2.63
LINK K K B 193 O HOH B 201 1555 1555 2.32
LINK K K B 193 O SER H 177 1555 1555 2.70
LINK K K B 193 OD1 ASP H 179 1555 1555 2.80
LINK FE1 FES C 4 SG CYS C 106 1555 1555 2.05
LINK FE1 FES C 4 SG CYS C 112 1555 1555 2.08
LINK FE2 FES C 4 SG CYS C 115 1555 1555 2.05
LINK FE2 FES C 4 SG CYS C 152 1555 1555 2.10
LINK OB2 FLC C 5 K K C 192 1555 1555 2.81
LINK OHB FLC C 5 K K C 192 1555 1555 2.82
LINK OHB FLC C 8 K K F 8 1555 1555 2.75
LINK OG2 FLC C 8 K K F 8 1555 1555 3.35
LINK O SER C 177 K K C 192 1555 1555 2.45
LINK OD1 ASP C 179 K K C 192 1555 1555 2.93
LINK K K C 192 O HOH C 203 1555 1555 3.36
LINK O HOH C 222 K K F 8 1555 1555 2.64
LINK OHB FLC D 2 K K D 192 1555 1555 2.75
LINK OG1 FLC D 2 K K D 192 1555 1555 3.25
LINK FE1 FES D 5 SG CYS D 106 1555 1555 2.01
LINK FE1 FES D 5 SG CYS D 112 1555 1555 2.10
LINK FE2 FES D 5 SG CYS D 115 1555 1555 2.10
LINK FE2 FES D 5 SG CYS D 152 1555 1555 2.09
LINK O SER D 177 K K D 192 1555 1555 2.56
LINK OG SER D 177 K K D 192 1555 1555 3.24
LINK OD1 ASP D 179 K K D 192 1555 1555 2.87
LINK K K D 192 O HOH D 205 1555 1555 2.71
LINK OHB FLC E 4 K K E 192 1555 1555 2.76
LINK FE1 FES E 6 SG CYS E 106 1555 1555 2.04
LINK FE1 FES E 6 SG CYS E 112 1555 1555 2.05
LINK FE2 FES E 6 SG CYS E 115 1555 1555 2.06
LINK FE2 FES E 6 SG CYS E 152 1555 1555 2.07
LINK O SER E 177 K K E 192 1555 1555 2.67
LINK OD1 ASP E 179 K K E 192 1555 1555 2.61
LINK FE1 FES F 7 SG CYS F 106 1555 1555 2.06
LINK FE1 FES F 7 SG CYS F 112 1555 1555 2.07
LINK FE2 FES F 7 SG CYS F 115 1555 1555 2.09
LINK FE2 FES F 7 SG CYS F 152 1555 1555 2.12
LINK K K F 8 O SER F 177 1555 1555 2.58
LINK K K F 8 OD1 ASP F 179 1555 1555 2.86
LINK FE1 FES G 1 SG CYS G 106 1555 1555 2.06
LINK FE1 FES G 1 SG CYS G 112 1555 1555 2.07
LINK FE2 FES G 1 SG CYS G 115 1555 1555 2.09
LINK FE2 FES G 1 SG CYS G 152 1555 1555 2.16
LINK O HOH G 47 K K G 193 1555 1555 3.14
LINK O SER G 177 K K G 193 1555 1555 2.38
LINK OD1 ASP G 179 K K G 193 1555 1555 2.98
LINK OHB FLC G 192 K K G 193 1555 1555 3.04
LINK OHB FLC H 7 K K H 192 1555 1555 3.06
LINK OA1 FLC H 7 K K H 192 1555 1555 3.38
LINK OB2 FLC H 7 K K H 192 1555 1555 3.41
LINK FE1 FES H 8 SG CYS H 106 1555 1555 2.03
LINK FE1 FES H 8 SG CYS H 112 1555 1555 2.09
LINK FE2 FES H 8 SG CYS H 115 1555 1555 2.07
LINK FE2 FES H 8 SG CYS H 152 1555 1555 2.09
SITE 1 AC1 8 GLY A 104 CYS A 106 GLY A 108 LEU A 110
SITE 2 AC1 8 ALA A 111 CYS A 112 CYS A 115 CYS A 152
SITE 1 AC2 7 VAL A 171 ARG A 175 ASP A 179 K A 192
SITE 2 AC2 7 TYR G 142 GLY G 143 LEU G 144
SITE 1 AC3 3 FLC A 6 SER A 177 ASP A 179
SITE 1 AC4 5 CYS B 106 GLY B 108 CYS B 112 CYS B 115
SITE 2 AC4 5 CYS B 152
SITE 1 AC5 9 TYR B 142 GLY B 143 LEU B 144 K B 193
SITE 2 AC5 9 HOH B 201 TYR H 142 VAL H 171 ARG H 175
SITE 3 AC5 9 ASP H 179
SITE 1 AC6 4 FLC B 192 HOH B 201 SER H 177 ASP H 179
SITE 1 AC7 7 GLY C 104 CYS C 106 GLY C 108 LEU C 110
SITE 2 AC7 7 CYS C 112 CYS C 115 CYS C 152
SITE 1 AC8 6 ARG C 175 ASP C 179 K C 192 HOH C 203
SITE 2 AC8 6 GLY F 143 LEU F 144
SITE 1 AC9 6 GLY C 143 K F 8 TYR F 142 VAL F 171
SITE 2 AC9 6 ARG F 175 ASP F 179
SITE 1 BC1 3 FLC C 5 SER C 177 ASP C 179
SITE 1 BC2 7 CYS D 106 GLY D 108 LEU D 110 ALA D 111
SITE 2 BC2 7 CYS D 112 CYS D 115 CYS D 152
SITE 1 BC3 8 VAL D 171 ARG D 175 ASP D 179 K D 192
SITE 2 BC3 8 HOH D 205 TYR E 142 GLY E 143 LEU E 144
SITE 1 BC4 3 LEU D 79 THR D 80 HOH D 200
SITE 1 BC5 4 FLC D 2 SER D 177 ASP D 179 HOH D 205
SITE 1 BC6 5 CYS E 106 GLY E 108 CYS E 112 CYS E 115
SITE 2 BC6 5 CYS E 152
SITE 1 BC7 9 ALA D 141 TYR D 142 GLY D 143 LEU D 144
SITE 2 BC7 9 VAL E 171 ALA E 174 ARG E 175 K E 192
SITE 3 BC7 9 HOH E 202
SITE 1 BC8 3 FLC E 4 SER E 177 ASP E 179
SITE 1 BC9 6 GLY F 104 CYS F 106 GLY F 108 CYS F 112
SITE 2 BC9 6 CYS F 115 CYS F 152
SITE 1 CC1 4 FLC C 8 HOH C 222 SER F 177 ASP F 179
SITE 1 CC2 6 LEU C 140 HOH C 265 HOH C 266 LEU F 140
SITE 2 CC2 6 VAL F 171 HOH F 216
SITE 1 CC3 6 GLY G 104 CYS G 106 GLY G 108 CYS G 112
SITE 2 CC3 6 CYS G 115 CYS G 152
SITE 1 CC4 6 GLY A 143 TYR G 142 VAL G 171 ARG G 175
SITE 2 CC4 6 ASP G 179 K G 193
SITE 1 CC5 4 HOH A 197 SER G 177 ASP G 179 FLC G 192
SITE 1 CC6 4 LEU A 140 LEU G 140 VAL G 171 HOH G 207
SITE 1 CC7 6 CYS H 106 GLY H 108 LEU H 110 CYS H 112
SITE 2 CC7 6 CYS H 115 CYS H 152
SITE 1 CC8 6 VAL B 171 ARG B 175 TYR H 142 GLY H 143
SITE 2 CC8 6 LEU H 144 K H 192
SITE 1 CC9 3 SER B 177 ASP B 179 FLC H 7
CRYST1 76.576 76.576 234.410 90.00 90.00 120.00 P 32 24
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 0.013059 0.007540 0.000000 0.00000
SCALE2 0.000000 0.015079 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004266 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
