Should you encounter any unexpected behaviour,
please let us know.

* *

CA strain for 221128151102134046

--- normal mode 7 ---

This graph displays the distance variation between successive pairs of CA atoms in the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Large distance variations can be an indicator for residue pairs that support the important strain in that particular normal mode movement. Note that residue pairs between chain breaks or at flexible ends of the protein may also exhibit large CA-CA distance variations. If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations between CA atoms in the same block will be very low.

This feature is still experimental and will be further developped in the future.

CA i CA i+1 vari
MET 1 MET 1 -0.0005

MET 1 GLU 2 -0.0004

GLU 2 GLU 2 -0.0000

GLU 2 LEU 3 -0.0427

LEU 3 LEU 3 -0.0001

LEU 3 ARG 4 0.0000

ARG 4 ARG 4 0.0007

ARG 4 HIS 5 -0.0060

HIS 5 HIS 5 -0.0006

HIS 5 THR 6 -0.0002

THR 6 THR 6 0.0000

THR 6 PRO 7 0.0434

PRO 7 PRO 7 0.0004

PRO 7 ALA 8 -0.0003

ALA 8 ALA 8 -0.0001

ALA 8 ARG 9 -0.0312

ARG 9 ARG 9 0.0001

ARG 9 ASP 10 0.0000

ASP 10 ASP 10 -0.0003

ASP 10 LEU 11 0.0156

LEU 11 LEU 11 -0.0001

LEU 11 ASP 12 0.0002

ASP 12 ASP 12 0.0001

ASP 12 LYS 13 0.0508

LYS 13 LYS 13 -0.0001

LYS 13 PHE 14 0.0004

PHE 14 PHE 14 0.0005

PHE 14 ILE 15 0.0249

ILE 15 ILE 15 -0.0007

ILE 15 GLU 16 0.0002

GLU 16 GLU 16 0.0003

GLU 16 ASP 17 0.0370

ASP 17 ASP 17 -0.0002

ASP 17 HIS 18 -0.0006

HIS 18 HIS 18 -0.0001

HIS 18 LEU 19 -0.0259

LEU 19 LEU 19 0.0002

LEU 19 LEU 20 -0.0002

LEU 20 LEU 20 0.0002

LEU 20 PRO 21 0.0772

PRO 21 PRO 21 0.0004

PRO 21 ASN 22 0.0005

ASN 22 ASN 22 0.0001

ASN 22 THR 23 0.0940

THR 23 THR 23 -0.0002

THR 23 CYS 24 0.0002

CYS 24 CYS 24 -0.0003

CYS 24 PHE 25 0.0070

PHE 25 PHE 25 -0.0005

PHE 25 ARG 26 -0.0001

ARG 26 ARG 26 0.0002

ARG 26 THR 27 0.0837

THR 27 THR 27 -0.0004

THR 27 GLN 28 -0.0003

GLN 28 GLN 28 -0.0004

GLN 28 VAL 29 0.0197

VAL 29 VAL 29 -0.0002

VAL 29 LYS 30 0.0002

LYS 30 LYS 30 -0.0004

LYS 30 GLU 31 -0.0833

GLU 31 GLU 31 0.0007

GLU 31 ALA 32 0.0003

ALA 32 ALA 32 -0.0000

ALA 32 ILE 33 0.0161

ILE 33 ILE 33 -0.0005

ILE 33 ASP 34 -0.0003

ASP 34 ASP 34 -0.0003

ASP 34 ILE 35 -0.1187

ILE 35 ILE 35 -0.0005

ILE 35 VAL 36 0.0006

VAL 36 VAL 36 -0.0001

VAL 36 CYS 37 -0.0242

CYS 37 CYS 37 -0.0003

CYS 37 ARG 38 0.0004

ARG 38 ARG 38 0.0004

ARG 38 PHE 39 -0.1120

PHE 39 PHE 39 0.0001

PHE 39 LEU 40 0.0002

LEU 40 LEU 40 0.0000

LEU 40 LYS 41 -0.0398

LYS 41 LYS 41 0.0001

LYS 41 GLU 42 -0.0003

GLU 42 GLU 42 -0.0000

GLU 42 ARG 43 -0.1837

ARG 43 ARG 43 0.0003

ARG 43 CYS 44 0.0003

CYS 44 CYS 44 0.0000

CYS 44 PHE 45 0.0069

PHE 45 PHE 45 -0.0005

PHE 45 GLN 46 0.0001

GLN 46 GLN 46 -0.0005

GLN 46 GLY 47 -0.0500

GLY 47 GLY 47 -0.0009

GLY 47 THR 48 0.0006

THR 48 THR 48 0.0001

THR 48 ALA 49 0.0198

ALA 49 ALA 49 -0.0003

ALA 49 ASP 50 0.0003

ASP 50 ASP 50 0.0002

ASP 50 PRO 51 -0.0111

PRO 51 PRO 51 -0.0002

PRO 51 VAL 52 -0.0001

VAL 52 VAL 52 0.0002

VAL 52 ARG 53 -0.0119

ARG 53 ARG 53 0.0002

ARG 53 VAL 54 -0.0001

VAL 54 VAL 54 0.0000

VAL 54 SER 55 -0.0669

SER 55 SER 55 -0.0005

SER 55 LYS 56 -0.0001

LYS 56 LYS 56 -0.0000

LYS 56 VAL 57 0.0098

VAL 57 VAL 57 -0.0005

VAL 57 VAL 58 0.0003

VAL 58 VAL 58 -0.0002

VAL 58 LYS 59 -0.0016

LYS 59 LYS 59 0.0001

LYS 59 GLY 60 -0.0001

GLY 60 GLY 60 -0.0001

GLY 60 GLY 61 0.1101

GLY 61 GLY 61 -0.0001

GLY 61 SER 62 0.0003

SER 62 SER 62 -0.0000

SER 62 SER 63 0.0927

SER 63 SER 63 0.0003

SER 63 GLY 64 0.0002

GLY 64 GLY 64 0.0006

GLY 64 LYS 65 -0.0124

LYS 65 LYS 65 -0.0000

LYS 65 GLY 66 -0.0001

GLY 66 GLY 66 -0.0001

GLY 66 THR 67 0.0846

THR 67 THR 67 0.0001

THR 67 THR 68 -0.0001

THR 68 THR 68 -0.0001

THR 68 LEU 69 -0.0492

LEU 69 LEU 69 -0.0000

LEU 69 ARG 70 -0.0001

ARG 70 ARG 70 0.0002

ARG 70 GLY 71 -0.0219

GLY 71 GLY 71 0.0008

GLY 71 ARG 72 -0.0004

ARG 72 ARG 72 0.0005

ARG 72 SER 73 0.0744

SER 73 SER 73 -0.0004

SER 73 ASP 74 -0.0001

ASP 74 ASP 74 -0.0000

ASP 74 ALA 75 0.0658

ALA 75 ALA 75 -0.0004

ALA 75 ASP 76 0.0003

ASP 76 ASP 76 -0.0005

ASP 76 LEU 77 0.0087

LEU 77 LEU 77 0.0006

LEU 77 VAL 78 0.0001

VAL 78 VAL 78 -0.0004

VAL 78 VAL 79 0.0419

VAL 79 VAL 79 -0.0003

VAL 79 PHE 80 -0.0003

PHE 80 PHE 80 -0.0001

PHE 80 LEU 81 0.0085

LEU 81 LEU 81 0.0000

LEU 81 THR 82 0.0001

THR 82 THR 82 -0.0002

THR 82 LYS 83 0.0419

LYS 83 LYS 83 -0.0006

LYS 83 LEU 84 -0.0001

LEU 84 LEU 84 -0.0003

LEU 84 THR 85 0.0038

THR 85 THR 85 -0.0002

THR 85 SER 86 0.0001

SER 86 SER 86 -0.0006

SER 86 PHE 87 0.0193

PHE 87 PHE 87 -0.0005

PHE 87 GLU 88 0.0002

GLU 88 GLU 88 -0.0005

GLU 88 ASP 89 0.0640

ASP 89 ASP 89 0.0001

ASP 89 GLN 90 -0.0002

GLN 90 GLN 90 -0.0005

GLN 90 LEU 91 0.0249

LEU 91 LEU 91 0.0003

LEU 91 ARG 92 0.0003

ARG 92 ARG 92 -0.0006

ARG 92 ARG 93 0.0224

ARG 93 ARG 93 -0.0006

ARG 93 ARG 94 0.0005

ARG 94 ARG 94 0.0000

ARG 94 GLY 95 -0.0384

GLY 95 GLY 95 -0.0001

GLY 95 GLU 96 -0.0004

GLU 96 GLU 96 -0.0004

GLU 96 PHE 97 -0.0247

PHE 97 PHE 97 0.0002

PHE 97 ILE 98 0.0002

ILE 98 ILE 98 -0.0003

ILE 98 GLN 99 0.0278

GLN 99 GLN 99 0.0003

GLN 99 GLU 100 -0.0001

GLU 100 GLU 100 -0.0005

GLU 100 ILE 101 0.0127

ILE 101 ILE 101 -0.0004

ILE 101 ARG 102 0.0006

ARG 102 ARG 102 0.0006

ARG 102 ARG 103 -0.0329

ARG 103 ARG 103 0.0000

ARG 103 GLN 104 0.0003

GLN 104 GLN 104 -0.0001

GLN 104 LEU 105 0.0373

LEU 105 LEU 105 -0.0000

LEU 105 GLU 106 -0.0001

GLU 106 GLU 106 0.0000

GLU 106 ALA 107 -0.0237

ALA 107 ALA 107 -0.0004

ALA 107 CYS 108 -0.0002

CYS 108 CYS 108 0.0000

CYS 108 GLN 109 -0.0150

GLN 109 GLN 109 -0.0001

GLN 109 ARG 110 -0.0002

ARG 110 ARG 110 0.0000

ARG 110 GLU 111 0.0111

GLU 111 GLU 111 -0.0001

GLU 111 GLN 112 0.0002

GLN 112 GLN 112 -0.0001

GLN 112 LYS 113 -0.0383

LYS 113 LYS 113 -0.0001

LYS 113 PHE 114 0.0004

PHE 114 PHE 114 -0.0000

PHE 114 LYS 115 0.0189

LYS 115 LYS 115 -0.0001

LYS 115 VAL 116 -0.0000

VAL 116 VAL 116 -0.0001

VAL 116 THR 117 -0.0229

THR 117 THR 117 -0.0002

THR 117 PHE 118 -0.0001

PHE 118 PHE 118 -0.0005

PHE 118 GLU 119 -0.0622

GLU 119 GLU 119 -0.0005

GLU 119 VAL 120 0.0004

VAL 120 VAL 120 -0.0001

VAL 120 GLN 121 -0.0583

GLN 121 GLN 121 -0.0002

GLN 121 SER 122 -0.0004

SER 122 SER 122 -0.0005

SER 122 PRO 123 0.0265

PRO 123 PRO 123 -0.0000

PRO 123 ARG 124 -0.0001

ARG 124 ARG 124 -0.0004

ARG 124 ARG 125 0.0294

ARG 125 ARG 125 0.0000

ARG 125 GLU 126 0.0001

GLU 126 GLU 126 -0.0003

GLU 126 ASN 127 -0.1105

ASN 127 ASN 127 0.0002

ASN 127 PRO 128 -0.0003

PRO 128 PRO 128 -0.0003

PRO 128 ARG 129 -0.0367

ARG 129 ARG 129 0.0002

ARG 129 ALA 130 0.0001

ALA 130 ALA 130 -0.0008

ALA 130 LEU 131 0.0508

LEU 131 LEU 131 0.0002

LEU 131 SER 132 -0.0003

SER 132 SER 132 -0.0000

SER 132 PHE 133 -0.0568

PHE 133 PHE 133 -0.0002

PHE 133 VAL 134 0.0001

VAL 134 VAL 134 -0.0003

VAL 134 LEU 135 -0.0560

LEU 135 LEU 135 -0.0001

LEU 135 SER 136 -0.0004

SER 136 SER 136 0.0001

SER 136 SER 137 -0.0070

SER 137 SER 137 -0.0001

SER 137 PRO 138 0.0002

PRO 138 PRO 138 -0.0002

PRO 138 GLN 139 -0.0245

GLN 139 GLN 139 0.0001

GLN 139 LEU 140 -0.0000

LEU 140 LEU 140 0.0004

LEU 140 GLN 141 0.0490

GLN 141 GLN 141 -0.0002

GLN 141 GLN 142 -0.0003

GLN 142 GLN 142 0.0005

GLN 142 GLU 143 -0.1170

GLU 143 GLU 143 -0.0001

GLU 143 VAL 144 -0.0003

VAL 144 VAL 144 -0.0003

VAL 144 GLU 145 -0.0025

GLU 145 GLU 145 -0.0001

GLU 145 PHE 146 -0.0002

PHE 146 PHE 146 0.0009

PHE 146 ASP 147 -0.0407

ASP 147 ASP 147 -0.0005

ASP 147 VAL 148 0.0000

VAL 148 VAL 148 0.0001

VAL 148 LEU 149 0.0041

LEU 149 LEU 149 0.0006

LEU 149 PRO 150 -0.0003

PRO 150 PRO 150 -0.0003

PRO 150 ALA 151 -0.0395

ALA 151 ALA 151 0.0000

ALA 151 PHE 152 -0.0003

PHE 152 PHE 152 0.0006

PHE 152 ASP 153 0.0429

ASP 153 ASP 153 -0.0002

ASP 153 ALA 154 -0.0001

ALA 154 ALA 154 0.0002

ALA 154 LEU 155 0.0564

LEU 155 LEU 155 -0.0003

LEU 155 GLY 156 -0.0001

GLY 156 GLY 156 -0.0000

GLY 156 GLN 157 0.0666

GLN 157 GLN 157 -0.0003

GLN 157 TRP 158 0.0001

TRP 158 TRP 158 0.0000

TRP 158 THR 159 -0.0651

THR 159 THR 159 -0.0003

THR 159 PRO 160 -0.0004

PRO 160 PRO 160 -0.0009

PRO 160 GLY 161 0.0014

GLY 161 GLY 161 0.0002

GLY 161 TYR 162 0.0000

TYR 162 TYR 162 -0.0004

TYR 162 LYS 163 -0.0192

LYS 163 LYS 163 0.0004

LYS 163 PRO 164 0.0002

PRO 164 PRO 164 -0.0005

PRO 164 ASN 165 0.0195

ASN 165 ASN 165 -0.0005

ASN 165 PRO 166 -0.0003

PRO 166 PRO 166 0.0003

PRO 166 GLU 167 -0.0071

GLU 167 GLU 167 0.0004

GLU 167 ILE 168 0.0003

ILE 168 ILE 168 0.0001

ILE 168 TYR 169 -0.0514

TYR 169 TYR 169 0.0004

TYR 169 VAL 170 -0.0006

VAL 170 VAL 170 -0.0002

VAL 170 GLN 171 -0.0939

GLN 171 GLN 171 -0.0004

GLN 171 LEU 172 0.0004

LEU 172 LEU 172 0.0005

LEU 172 ILE 173 0.0198

ILE 173 ILE 173 -0.0001

ILE 173 LYS 174 -0.0002

LYS 174 LYS 174 -0.0003

LYS 174 GLU 175 0.0081

GLU 175 GLU 175 0.0002

GLU 175 CYS 176 -0.0005

CYS 176 CYS 176 -0.0003

CYS 176 LYS 177 0.0091

LYS 177 LYS 177 0.0005

LYS 177 SER 178 -0.0001

SER 178 SER 178 0.0002

SER 178 ARG 179 -0.0042

ARG 179 ARG 179 -0.0000

ARG 179 GLY 180 0.0005

GLY 180 GLY 180 0.0006

GLY 180 LYS 181 -0.0372

LYS 181 LYS 181 0.0002

LYS 181 GLU 182 -0.0005

GLU 182 GLU 182 0.0000

GLU 182 GLY 183 -0.0965

GLY 183 GLY 183 0.0001

GLY 183 GLU 184 -0.0001

GLU 184 GLU 184 -0.0002

GLU 184 PHE 185 -0.0533

PHE 185 PHE 185 -0.0001

PHE 185 SER 186 0.0001

SER 186 SER 186 -0.0000

SER 186 THR 187 0.1448

THR 187 THR 187 -0.0004

THR 187 CYS 188 0.0001

CYS 188 CYS 188 0.0001

CYS 188 PHE 189 0.0015

PHE 189 PHE 189 0.0003

PHE 189 THR 190 0.0003

THR 190 THR 190 0.0004

THR 190 GLU 191 0.0284

GLU 191 GLU 191 0.0005

GLU 191 LEU 192 -0.0004

LEU 192 LEU 192 -0.0000

LEU 192 GLN 193 -0.0457

GLN 193 GLN 193 0.0003

GLN 193 ARG 194 -0.0002

ARG 194 ARG 194 -0.0381

ARG 194 ARG 194 0.0001

ARG 194 ASP 195 0.0397

ASP 195 ASP 195 -0.0004

ASP 195 PHE 196 0.0000

PHE 196 PHE 196 -0.0002

PHE 196 LEU 197 0.0741

LEU 197 LEU 197 0.0000

LEU 197 ARG 198 0.0004

ARG 198 ARG 198 -0.0001

ARG 198 ASN 199 -0.0597

ASN 199 ASN 199 0.0003

ASN 199 ARG 200 -0.0002

ARG 200 ARG 200 0.0003

ARG 200 PRO 201 -0.0485

PRO 201 PRO 201 -0.0002

PRO 201 THR 202 0.0002

THR 202 THR 202 -0.0001

THR 202 LYS 203 -0.0747

LYS 203 LYS 203 0.0006

LYS 203 LEU 204 0.0002

LEU 204 LEU 204 -0.0001

LEU 204 LYS 205 -0.0066

LYS 205 LYS 205 0.0001

LYS 205 SER 206 -0.0004

SER 206 SER 206 -0.0004

SER 206 LEU 207 0.0578

LEU 207 LEU 207 0.0005

LEU 207 ILE 208 0.0001

ILE 208 ILE 208 0.0003

ILE 208 ARG 209 -0.0186

ARG 209 ARG 209 0.0004

ARG 209 LEU 210 -0.0003

LEU 210 LEU 210 0.0002

LEU 210 VAL 211 -0.0237

VAL 211 VAL 211 -0.0000

VAL 211 LYS 212 -0.0003

LYS 212 LYS 212 -0.0001

LYS 212 HIS 213 -0.0734

HIS 213 HIS 213 0.0002

HIS 213 TRP 214 0.0003

TRP 214 TRP 214 -0.0001

TRP 214 TYR 215 -0.0682

TYR 215 TYR 215 -0.0002

TYR 215 GLN 216 -0.0002

GLN 216 GLN 216 -0.0005

GLN 216 THR 217 0.0218

THR 217 THR 217 -0.0006

THR 217 CYS 218 0.0003

CYS 218 CYS 218 0.0002

CYS 218 LYS 219 0.0012

LYS 219 LYS 219 0.0004

LYS 219 LYS 220 0.0006

LYS 220 LYS 220 -0.0005

LYS 220 THR 221 0.0020

THR 221 THR 221 -0.0002

THR 221 HIS 222 0.0001

HIS 222 HIS 222 -0.0005

HIS 222 GLY 223 0.0023

GLY 223 GLY 223 0.0003

GLY 223 ASN 224 -0.0004

ASN 224 ASN 224 -0.0002

ASN 224 LYS 225 -0.0135

LYS 225 LYS 225 -0.0003

LYS 225 LEU 226 -0.0004

LEU 226 LEU 226 -0.0003

LEU 226 PRO 227 0.0258

PRO 227 PRO 227 0.0001

PRO 227 PRO 228 -0.0003

PRO 228 PRO 228 0.0004

PRO 228 GLN 229 0.0243

GLN 229 GLN 229 -0.0000

GLN 229 TYR 230 0.0000

TYR 230 TYR 230 -0.0002

TYR 230 ALA 231 0.0851

ALA 231 ALA 231 0.0003

ALA 231 LEU 232 0.0000

LEU 232 LEU 232 -0.0005

LEU 232 GLU 233 0.0563

GLU 233 GLU 233 -0.0002

GLU 233 LEU 234 0.0000

LEU 234 LEU 234 -0.0002

LEU 234 LEU 235 -0.0290

LEU 235 LEU 235 0.0002

LEU 235 THR 236 0.0002

THR 236 THR 236 -0.0001

THR 236 VAL 237 -0.0651

VAL 237 VAL 237 0.0002

VAL 237 TYR 238 0.0000

TYR 238 TYR 238 0.0002

TYR 238 ALA 239 -0.0129

ALA 239 ALA 239 0.0009

ALA 239 TRP 240 -0.0004

TRP 240 TRP 240 -0.0008

TRP 240 GLU 241 0.0655

GLU 241 GLU 241 0.0002

GLU 241 GLN 242 0.0001

GLN 242 GLN 242 -0.0001

GLN 242 GLY 243 0.0037

GLY 243 GLY 243 0.0000

GLY 243 SER 244 -0.0001

SER 244 SER 244 -0.0002

SER 244 ARG 245 -0.0521

ARG 245 ARG 245 -0.0003

ARG 245 LYS 246 -0.0002

LYS 246 LYS 246 0.0005

LYS 246 THR 247 -0.0177

THR 247 THR 247 -0.0000

THR 247 ASP 248 0.0005

ASP 248 ASP 248 -0.0005

ASP 248 PHE 249 -0.1504

PHE 249 PHE 249 0.0002

PHE 249 SER 250 0.0002

SER 250 SER 250 -0.0004

SER 250 THR 251 0.0300

THR 251 THR 251 -0.0002

THR 251 ALA 252 -0.0002

ALA 252 ALA 252 0.0004

ALA 252 GLN 253 0.0286

GLN 253 GLN 253 -0.0003

GLN 253 GLY 254 -0.0002

GLY 254 GLY 254 0.0001

GLY 254 PHE 255 -0.0226

PHE 255 PHE 255 -0.0001

PHE 255 GLN 256 0.0005

GLN 256 GLN 256 0.0000

GLN 256 THR 257 -0.0093

THR 257 THR 257 0.0005

THR 257 VAL 258 -0.0005

VAL 258 VAL 258 -0.0004

VAL 258 LEU 259 -0.0064

LEU 259 LEU 259 0.0004

LEU 259 GLU 260 0.0000

GLU 260 GLU 260 -0.0001

GLU 260 LEU 261 -0.0097

LEU 261 LEU 261 0.0001

LEU 261 VAL 262 0.0001

VAL 262 VAL 262 -0.0004

VAL 262 LEU 263 0.0218

LEU 263 LEU 263 -0.0004

LEU 263 LYS 264 0.0002

LYS 264 LYS 264 -0.0001

LYS 264 HIS 265 0.0142

HIS 265 HIS 265 -0.0003

HIS 265 GLN 266 0.0006

GLN 266 GLN 266 -0.0003

GLN 266 LYS 267 -0.0345

LYS 267 LYS 267 -0.0004

LYS 267 LEU 268 -0.0003

LEU 268 LEU 268 0.0002

LEU 268 CYS 269 -0.0718

CYS 269 CYS 269 -0.0002

CYS 269 ILE 270 -0.0003

ILE 270 ILE 270 0.0004

ILE 270 PHE 271 -0.0684

PHE 271 PHE 271 0.0002

PHE 271 TRP 272 0.0002

TRP 272 TRP 272 0.0002

TRP 272 GLU 273 -0.0629

GLU 273 GLU 273 -0.0003

GLU 273 ALA 274 0.0001

ALA 274 ALA 274 0.0001

ALA 274 TYR 275 -0.0037

TYR 275 TYR 275 0.0003

TYR 275 TYR 276 -0.0003

TYR 276 TYR 276 -0.0001

TYR 276 ASP 277 0.0457

ASP 277 ASP 277 0.0002

ASP 277 PHE 278 -0.0002

PHE 278 PHE 278 0.0004

PHE 278 THR 279 -0.0730

THR 279 THR 279 -0.0002

THR 279 ASN 280 0.0006

ASN 280 ASN 280 -0.0003

ASN 280 PRO 281 0.0040

PRO 281 PRO 281 0.0005

PRO 281 VAL 282 -0.0003

VAL 282 VAL 282 0.0004

VAL 282 VAL 283 0.0191

VAL 283 VAL 283 0.0001

VAL 283 GLY 284 0.0000

GLY 284 GLY 284 -0.0001

GLY 284 ARG 285 0.0377

ARG 285 ARG 285 0.0003

ARG 285 CYS 286 0.0000

CYS 286 CYS 286 -0.0001

CYS 286 MET 287 0.0340

MET 287 MET 287 -0.0005

MET 287 LEU 288 0.0003

LEU 288 LEU 288 -0.0002

LEU 288 GLN 289 0.0267

GLN 289 GLN 289 -0.0003

GLN 289 GLN 290 0.0003

GLN 290 GLN 290 -0.0004

GLN 290 LEU 291 0.1065

LEU 291 LEU 291 -0.0002

LEU 291 LYS 292 0.0003

LYS 292 LYS 292 0.0005

LYS 292 LYS 293 -0.0356

LYS 293 LYS 293 -0.0003

LYS 293 PRO 294 -0.0001

PRO 294 PRO 294 0.0003

PRO 294 ARG 295 0.0723

ARG 295 ARG 295 -0.0002

ARG 295 PRO 296 -0.0001

PRO 296 PRO 296 -0.0005

PRO 296 VAL 297 -0.0435

VAL 297 VAL 297 -0.0000

VAL 297 ILE 298 -0.0004

ILE 298 ILE 298 0.0006

ILE 298 LEU 299 -0.0225

LEU 299 LEU 299 0.0007

LEU 299 ASP 300 -0.0002

ASP 300 ASP 300 -0.0001

ASP 300 PRO 301 0.0162

PRO 301 PRO 301 0.0004

PRO 301 ALA 302 0.0002

ALA 302 ALA 302 0.0000

ALA 302 ASP 303 -0.0044

ASP 303 ASP 303 0.0002

ASP 303 PRO 304 0.0003

PRO 304 PRO 304 -0.0002

PRO 304 THR 305 0.0083

THR 305 THR 305 -0.0002

THR 305 GLY 306 0.0000

GLY 306 GLY 306 -0.0002

GLY 306 ASN 307 0.0619

ASN 307 ASN 307 -0.0002

ASN 307 VAL 308 0.0002

VAL 308 VAL 308 -0.0006

VAL 308 GLY 309 0.0941

GLY 309 GLY 309 0.0004

GLY 309 GLY 310 -0.0004

GLY 310 GLY 310 -0.0002

GLY 310 GLY 311 -0.0737

GLY 311 GLY 311 0.0003

GLY 311 ASP 312 -0.0005

ASP 312 ASP 312 0.0001

ASP 312 THR 313 -0.0112

THR 313 THR 313 0.0001

THR 313 HIS 314 -0.0000

HIS 314 HIS 314 0.0002

HIS 314 SER 315 0.0312

SER 315 SER 315 0.0002

SER 315 TRP 316 0.0001

TRP 316 TRP 316 0.0004

TRP 316 GLN 317 -0.0019

GLN 317 GLN 317 -0.0000

GLN 317 ARG 318 0.0003

ARG 318 ARG 318 -0.0000

ARG 318 LEU 319 -0.0026

LEU 319 LEU 319 -0.0002

LEU 319 ALA 320 -0.0003

ALA 320 ALA 320 -0.0001

ALA 320 GLN 321 -0.0076

GLN 321 GLN 321 0.0003

GLN 321 GLU 322 -0.0003

GLU 322 GLU 322 0.0003

GLU 322 ALA 323 -0.0261

ALA 323 ALA 323 -0.0001

ALA 323 ARG 324 -0.0000

ARG 324 ARG 324 0.0004

ARG 324 VAL 325 0.0269

VAL 325 VAL 325 0.0000

VAL 325 TRP 326 0.0002

TRP 326 TRP 326 -0.0003

TRP 326 LEU 327 0.0476

LEU 327 LEU 327 -0.0003

LEU 327 GLY 328 0.0001

GLY 328 GLY 328 -0.0001

GLY 328 TYR 329 0.0081

TYR 329 TYR 329 -0.0001

TYR 329 PRO 330 -0.0003

PRO 330 PRO 330 -0.0001

PRO 330 CYS 331 0.0349

CYS 331 CYS 331 0.0001

CYS 331 CYS 332 -0.0002

CYS 332 CYS 332 0.0004

CYS 332 LYS 333 -0.0212

LYS 333 LYS 333 -0.0003

LYS 333 ASN 334 -0.0002

ASN 334 ASN 334 0.0002

ASN 334 LEU 335 0.0460

LEU 335 LEU 335 -0.0001

LEU 335 ASP 336 0.0002

ASP 336 ASP 336 0.0001

ASP 336 GLY 337 0.0645

GLY 337 GLY 337 0.0001

GLY 337 SER 338 -0.0007

SER 338 SER 338 -0.0003

SER 338 LEU 339 0.0144

LEU 339 LEU 339 -0.0003

LEU 339 VAL 340 0.0003

VAL 340 VAL 340 0.0002

VAL 340 GLY 341 0.0379

GLY 341 GLY 341 -0.0001

GLY 341 ALA 342 0.0002

ALA 342 ALA 342 0.0002

ALA 342 TRP 343 -0.0316

TRP 343 TRP 343 0.0000

TRP 343 THR 344 0.0002

THR 344 THR 344 0.0001

THR 344 MET 345 0.0429

MET 345 MET 345 -0.0004

MET 345 LEU 346 -0.0001

LEU 346 LEU 346 -0.0001

LEU 346 GLN 347 0.0056

GLN 347 GLN 347 -0.0004

GLN 347 LYS 348 0.0003

LYS 348 LYS 348 -0.0006

LYS 348 ILE 349 -0.0795

ILE 349 ILE 349 -0.0002

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.

Should you encounter any unexpected behaviour, please let us know.

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CA strain for 221128151102134046

--- normal mode 7 ---

Should you encounter any unexpected behaviour,
please let us know.

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