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esm3-conformational-sampling
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Tonic commited on
Commit
21e6511
•
1 Parent(s): 335fce6

add examples and sliders for esm3

Browse files
Files changed (4) hide show
  1. app.py +55 -26
  2. examples/11gs.pdb +0 -0
  3. examples/1ywi.pdb +0 -0
  4. examples/5awl.pdb +475 -0
app.py CHANGED
@@ -19,6 +19,34 @@ import time
19
  from Bio.PDB import PDBParser
20
  import itertools
21
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
22
  load_dotenv()
23
 
24
  API_URL = "https://forge.evolutionaryscale.ai/api/v1"
@@ -176,11 +204,11 @@ def add_noise_to_coordinates(protein: ESMProtein, noise_level: float) -> ESMProt
176
  noisy_coordinates = coordinates + noise
177
  return ESMProtein(sequence=protein.sequence, coordinates=noisy_coordinates)
178
 
179
- def run_structure_prediction(protein: ESMProtein) -> ESMProtein:
180
  structure_prediction_config = GenerationConfig(
181
  track="structure",
182
- num_steps=10,
183
- temperature=0.7,
184
  )
185
  try:
186
  response = model.generate(protein, structure_prediction_config)
@@ -254,7 +282,7 @@ def protein_to_pdb(protein: ESMProtein):
254
  pdb_str += f"ATOM {i*37+j+1:5d} {atom:3s} {aa:3s} A{i+1:4d} {x:8.3f}{y:8.3f}{z:8.3f}\n"
255
  return pdb_str
256
 
257
- def prediction_visualization(pdb_file, num_runs: int, noise_level: float, num_frames: int, progress=gr.Progress()):
258
  protein = get_protein(pdb_file)
259
  runs = []
260
 
@@ -266,7 +294,7 @@ def prediction_visualization(pdb_file, num_runs: int, noise_level: float, num_fr
266
 
267
  for i in range(num_runs):
268
  progress((frame * num_runs + i + 1) / total_iterations, desc=f"Frame {frame+1}, Run {i+1}")
269
- structure_prediction = run_structure_prediction(noisy_protein)
270
  if structure_prediction is not None:
271
  aligned, crmsd = align_after_prediction(protein, structure_prediction)
272
  if aligned is not None:
@@ -280,13 +308,13 @@ def prediction_visualization(pdb_file, num_runs: int, noise_level: float, num_fr
280
  view_data = visualize_after_pred(protein, best_aligned[1])
281
  return view_data, f"Best cRMSD: {best_aligned[0]:.4f}"
282
 
283
- def run_prediction(pdb_file, num_runs, noise_level, num_frames, progress=gr.Progress()):
284
  try:
285
  if pdb_file is None:
286
  return "Please upload a PDB file.", "No file uploaded", "", ""
287
 
288
  progress(0, desc="Starting prediction")
289
- view, crmsd_text = prediction_visualization(pdb_file, num_runs, noise_level, num_frames, progress)
290
  steric_clash_text, norm_steric_clash_text = calculate_clashes_for_pdb(pdb_file)
291
  if view is None:
292
  return "No successful predictions were made. Try adjusting the parameters or check the PDB file.", crmsd_text, steric_clash_text, norm_steric_clash_text
@@ -320,13 +348,20 @@ def run_prediction(pdb_file, num_runs, noise_level, num_frames, progress=gr.Prog
320
  def create_demo():
321
  with gr.Blocks() as demo:
322
  gr.Markdown("# Protein Structure Prediction and Visualization with Noise and MD Frames")
323
-
 
 
 
 
 
324
  with gr.Row():
325
  with gr.Column(scale=1):
326
  pdb_file = gr.File(label="Upload PDB file")
327
  num_runs = gr.Slider(minimum=1, maximum=10, step=1, value=3, label="Number of runs per frame")
328
  noise_level = gr.Slider(minimum=0, maximum=1, step=0.1, value=0.1, label="Noise level")
329
  num_frames = gr.Slider(minimum=1, maximum=10, step=1, value=1, label="Number of MD frames")
 
 
330
  run_button = gr.Button("Run Prediction")
331
 
332
  with gr.Column(scale=2):
@@ -337,26 +372,20 @@ def create_demo():
337
 
338
  run_button.click(
339
  fn=run_prediction,
340
- inputs=[pdb_file, num_runs, noise_level, num_frames],
341
  outputs=[visualization, alignment_result, steric_clash_result, norm_steric_clash_result]
342
  )
343
-
344
-
345
- gr.Markdown("""
346
- ## How to use
347
- 1. Upload a PDB file using the file uploader.
348
- 2. Adjust the number of prediction runs per frame using the slider.
349
- 3. Set the noise level to add random perturbations to the structure.
350
- 4. Choose the number of MD frames to simulate.
351
- 5. Click the "Run Prediction" button to start the process.
352
- 6. The 3D visualization will show the original structure (grey) and the best predicted structure (green).
353
- 7. The alignment result will display the best cRMSD (lower is better).
354
- 8. Total and Normalized (per atom) steric clashes (lower is better)
355
-
356
- ## About
357
- This demo uses the ESM3 model to predict protein structures from PDB files.
358
- It runs multiple predictions with added noise and simulated MD frames, displaying the best result based on the lowest cRMSD.
359
- """)
360
 
361
  return demo
362
 
 
19
  from Bio.PDB import PDBParser
20
  import itertools
21
 
22
+ howtouse = """
23
+ ## How to use
24
+ 1. Upload a PDB file using the file uploader.
25
+ 2. Adjust the number of prediction runs per frame using the slider.
26
+ 3. Set the noise level to add random perturbations to the structure.
27
+ 4. Choose the number of MD frames to simulate.
28
+ 5. Click the "Run Prediction" button to start the process.
29
+ 6. The 3D visualization will show the original structure (grey) and the best predicted structure (green).
30
+ 7. The alignment result will display the best cRMSD (lower is better).
31
+ 8. Total and Normalized (per atom) steric clashes (lower is better)
32
+ """
33
+ about = """ ## Background
34
+
35
+ - 3D protein structures typically come from crystal structures, which are densely packed and lack flexibility.
36
+ - Different proteins require varying levels of noise to achieve overlap in conformational space.
37
+ - We've developed an adaptability model that predicts the appropriate noise level for each protein.
38
+
39
+ ## Our Approach
40
+
41
+ 1. **Adaptability Model**: Trained on Molecular Dynamics (MD) data, our model predicts flexibility at the atomic level.
42
+ 2. **Correlation**: The adaptability predictions correlate well with the RMSD (Root Mean Square Deviation) from ESM3 sampling.
43
+ 3. **Noise Application**: We apply noise to simulate protein flexibility, mimicking MD-like behavior.
44
+
45
+ ## About
46
+ This demo uses the ESM3 model to predict protein structures from PDB files.
47
+ It runs multiple predictions with added noise and simulated MD frames, displaying the best result based on the lowest cRMSD.
48
+ """
49
+
50
  load_dotenv()
51
 
52
  API_URL = "https://forge.evolutionaryscale.ai/api/v1"
 
204
  noisy_coordinates = coordinates + noise
205
  return ESMProtein(sequence=protein.sequence, coordinates=noisy_coordinates)
206
 
207
+ def run_structure_prediction(protein: ESMProtein, temperature: float, num_steps: int) -> ESMProtein:
208
  structure_prediction_config = GenerationConfig(
209
  track="structure",
210
+ num_steps=num_steps,
211
+ temperature=temperature,
212
  )
213
  try:
214
  response = model.generate(protein, structure_prediction_config)
 
282
  pdb_str += f"ATOM {i*37+j+1:5d} {atom:3s} {aa:3s} A{i+1:4d} {x:8.3f}{y:8.3f}{z:8.3f}\n"
283
  return pdb_str
284
 
285
+ def prediction_visualization(pdb_file, num_runs: int, noise_level: float, num_frames: int, temperature: float, num_steps: int, progress=gr.Progress()):
286
  protein = get_protein(pdb_file)
287
  runs = []
288
 
 
294
 
295
  for i in range(num_runs):
296
  progress((frame * num_runs + i + 1) / total_iterations, desc=f"Frame {frame+1}, Run {i+1}")
297
+ structure_prediction = run_structure_prediction(noisy_protein, temperature, num_steps)
298
  if structure_prediction is not None:
299
  aligned, crmsd = align_after_prediction(protein, structure_prediction)
300
  if aligned is not None:
 
308
  view_data = visualize_after_pred(protein, best_aligned[1])
309
  return view_data, f"Best cRMSD: {best_aligned[0]:.4f}"
310
 
311
+ def run_prediction(pdb_file, num_runs, noise_level, num_frames, temperature, num_steps, progress=gr.Progress()):
312
  try:
313
  if pdb_file is None:
314
  return "Please upload a PDB file.", "No file uploaded", "", ""
315
 
316
  progress(0, desc="Starting prediction")
317
+ view, crmsd_text = prediction_visualization(pdb_file, num_runs, noise_level, num_frames, temperature, num_steps, progress)
318
  steric_clash_text, norm_steric_clash_text = calculate_clashes_for_pdb(pdb_file)
319
  if view is None:
320
  return "No successful predictions were made. Try adjusting the parameters or check the PDB file.", crmsd_text, steric_clash_text, norm_steric_clash_text
 
348
  def create_demo():
349
  with gr.Blocks() as demo:
350
  gr.Markdown("# Protein Structure Prediction and Visualization with Noise and MD Frames")
351
+ with gr.Accordion(label='learn more about MISATO ESM3 conformational sampling', open=False)
352
+ with gr.Row():
353
+ with gr.Column():
354
+ gr.Markdown(about)
355
+ with gr.Column():
356
+ gr.Markdown(howtouse)
357
  with gr.Row():
358
  with gr.Column(scale=1):
359
  pdb_file = gr.File(label="Upload PDB file")
360
  num_runs = gr.Slider(minimum=1, maximum=10, step=1, value=3, label="Number of runs per frame")
361
  noise_level = gr.Slider(minimum=0, maximum=1, step=0.1, value=0.1, label="Noise level")
362
  num_frames = gr.Slider(minimum=1, maximum=10, step=1, value=1, label="Number of MD frames")
363
+ temperature = gr.Slider(minimum=0.1, maximum=1.0, step=0.05, value=0.7, label="Temperature")
364
+ num_steps = gr.Slider(minimum=1, maximum=10, step=1, value=10, label="Number of steps")
365
  run_button = gr.Button("Run Prediction")
366
 
367
  with gr.Column(scale=2):
 
372
 
373
  run_button.click(
374
  fn=run_prediction,
375
+ inputs=[pdb_file, num_runs, noise_level, num_frames, temperature, num_steps],
376
  outputs=[visualization, alignment_result, steric_clash_result, norm_steric_clash_result]
377
  )
378
+ gr.Examples(
379
+ examples=[
380
+ ["examples/1ywi.pdb"],
381
+ ["examples/5awl.pdb"],
382
+ ["examples/11gs.pdb"],
383
+ ],
384
+ inputs=[pdb_file],
385
+ outputs=[visualization, alignment_result, steric_clash_result, norm_steric_clash_result],
386
+ fn=run_prediction,
387
+ cache_examples=False,
388
+ )
 
 
 
 
 
 
389
 
390
  return demo
391
 
examples/11gs.pdb ADDED
The diff for this file is too large to render. See raw diff
 
examples/1ywi.pdb ADDED
The diff for this file is too large to render. See raw diff
 
examples/5awl.pdb ADDED
@@ -0,0 +1,475 @@
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
1
+ HEADER DE NOVO PROTEIN 05-JUL-15 5AWL
2
+ TITLE CRYSTAL STRUCTURE OF A MUTANT OF CHIGNOLIN, CLN025
3
+ COMPND MOL_ID: 1;
4
+ COMPND 2 MOLECULE: A MUTANT OF CHIGNOLIN, CLN025;
5
+ COMPND 3 CHAIN: A;
6
+ COMPND 4 ENGINEERED: YES;
7
+ COMPND 5 MUTATION: YES
8
+ SOURCE MOL_ID: 1;
9
+ SOURCE 2 SYNTHETIC: YES;
10
+ SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
11
+ SOURCE 4 ORGANISM_TAXID: 32630
12
+ KEYWDS DE NOVO PROTEIN, BETA-HAIRPIN, MINI-PROTEIN, MINIATURE PROTEIN
13
+ EXPDTA X-RAY DIFFRACTION
14
+ AUTHOR T.AKIBA,M.ISHIMURA,T.ODAHARA,K.HARATA,S.HONDA
15
+ REVDAT 3 20-MAR-24 5AWL 1 SOURCE REMARK
16
+ REVDAT 2 26-AUG-15 5AWL 1 REMARK
17
+ REVDAT 1 12-AUG-15 5AWL 0
18
+ JRNL AUTH S.HONDA,T.AKIBA,Y.S.KATO,Y.SAWADA,M.SEKIJIMA,M.ISHIMURA,
19
+ JRNL AUTH 2 A.OOISHI,H.WATANABE,T.ODAHARA,K.HARATA
20
+ JRNL TITL CRYSTAL STRUCTURE OF A TEN-AMINO ACID PROTEIN
21
+ JRNL REF J.AM.CHEM.SOC. V. 130 15327 2008
22
+ JRNL REFN ESSN 1520-5126
23
+ JRNL PMID 18950166
24
+ JRNL DOI 10.1021/JA8030533
25
+ REMARK 1
26
+ REMARK 1 REFERENCE 1
27
+ REMARK 1 AUTH S.HONDA,K.YAMASAKI,Y.SAWADA,H.MORII
28
+ REMARK 1 TITL 10 RESIDUE FOLDED PEPTIDE DESIGNED BY SEGMENT STATISTICS.
29
+ REMARK 1 REF STRUCTURE V. 12 1507 2004
30
+ REMARK 1 REFN ISSN 0969-2126
31
+ REMARK 1 PMID 15296744
32
+ REMARK 1 DOI 10.1016/J.STR.2004.05.022
33
+ REMARK 2
34
+ REMARK 2 RESOLUTION. 1.11 ANGSTROMS.
35
+ REMARK 3
36
+ REMARK 3 REFINEMENT.
37
+ REMARK 3 PROGRAM : CNS
38
+ REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
39
+ REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
40
+ REMARK 3 : READ,RICE,SIMONSON,WARREN
41
+ REMARK 3
42
+ REMARK 3 DATA USED IN REFINEMENT.
43
+ REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.11
44
+ REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.80
45
+ REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
46
+ REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
47
+ REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
48
+ REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
49
+ REMARK 3
50
+ REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
51
+ REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
52
+ REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.088
53
+ REMARK 3 FREE R VALUE (NO CUTOFF) : 0.119
54
+ REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.200
55
+ REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 287
56
+ REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 3087
57
+ REMARK 3
58
+ REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
59
+ REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.080
60
+ REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.081
61
+ REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.113
62
+ REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 10.400
63
+ REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 253
64
+ REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 2682
65
+ REMARK 3
66
+ REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
67
+ REMARK 3 PROTEIN ATOMS : 93
68
+ REMARK 3 NUCLEIC ACID ATOMS : 0
69
+ REMARK 3 HETEROGEN ATOMS : 0
70
+ REMARK 3 SOLVENT ATOMS : 12
71
+ REMARK 3
72
+ REMARK 3 MODEL REFINEMENT.
73
+ REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 103.50
74
+ REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 73.00
75
+ REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
76
+ REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 940
77
+ REMARK 3 NUMBER OF RESTRAINTS : 1193
78
+ REMARK 3
79
+ REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
80
+ REMARK 3 BOND LENGTHS (A) : 0.016
81
+ REMARK 3 ANGLE DISTANCES (A) : 0.026
82
+ REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
83
+ REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.022
84
+ REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.079
85
+ REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.100
86
+ REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.193
87
+ REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006
88
+ REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.035
89
+ REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.110
90
+ REMARK 3
91
+ REMARK 3 BULK SOLVENT MODELING.
92
+ REMARK 3 METHOD USED: NULL
93
+ REMARK 3
94
+ REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
95
+ REMARK 3 SPECIAL CASE: NULL
96
+ REMARK 3
97
+ REMARK 3 OTHER REFINEMENT REMARKS: NULL
98
+ REMARK 4
99
+ REMARK 4 5AWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
100
+ REMARK 100
101
+ REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-15.
102
+ REMARK 100 THE DEPOSITION ID IS D_1300000091.
103
+ REMARK 200
104
+ REMARK 200 EXPERIMENTAL DETAILS
105
+ REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
106
+ REMARK 200 DATE OF DATA COLLECTION : 09-DEC-05
107
+ REMARK 200 TEMPERATURE (KELVIN) : 290
108
+ REMARK 200 PH : 5.0
109
+ REMARK 200 NUMBER OF CRYSTALS USED : 1
110
+ REMARK 200
111
+ REMARK 200 SYNCHROTRON (Y/N) : N
112
+ REMARK 200 RADIATION SOURCE : ROTATING ANODE
113
+ REMARK 200 BEAMLINE : NULL
114
+ REMARK 200 X-RAY GENERATOR MODEL : MACSCIENCE
115
+ REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
116
+ REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
117
+ REMARK 200 MONOCHROMATOR : NULL
118
+ REMARK 200 OPTICS : OSMIC CONFOCAL MAX-FLUX
119
+ REMARK 200
120
+ REMARK 200 DETECTOR TYPE : CCD
121
+ REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
122
+ REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SMART6000
123
+ REMARK 200 DATA SCALING SOFTWARE : SAINTPLUS
124
+ REMARK 200
125
+ REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 3094
126
+ REMARK 200 RESOLUTION RANGE HIGH (A) : 1.110
127
+ REMARK 200 RESOLUTION RANGE LOW (A) : 16.800
128
+ REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
129
+ REMARK 200
130
+ REMARK 200 OVERALL.
131
+ REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
132
+ REMARK 200 DATA REDUNDANCY : 6.500
133
+ REMARK 200 R MERGE (I) : 0.05700
134
+ REMARK 200 R SYM (I) : NULL
135
+ REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000
136
+ REMARK 200
137
+ REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
138
+ REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.11
139
+ REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
140
+ REMARK 200 COMPLETENESS FOR SHELL (%) : 88.9
141
+ REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
142
+ REMARK 200 R MERGE FOR SHELL (I) : 0.20300
143
+ REMARK 200 R SYM FOR SHELL (I) : NULL
144
+ REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
145
+ REMARK 200
146
+ REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
147
+ REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING
148
+ REMARK 200 SOFTWARE USED: SNB 2.2
149
+ REMARK 200 STARTING MODEL: NULL
150
+ REMARK 200
151
+ REMARK 200 REMARK: NULL
152
+ REMARK 280
153
+ REMARK 280 CRYSTAL
154
+ REMARK 280 SOLVENT CONTENT, VS (%): 14.10
155
+ REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.40
156
+ REMARK 280
157
+ REMARK 280 CRYSTALLIZATION CONDITIONS: USING 2 UL DROP OF PROTEIN AT 5 MG/ML
158
+ REMARK 280 IN A SOLUTION OF 35.7 MM SODIUM CITRATE-CITRIC ACID BUFFER (PH
159
+ REMARK 280 5.0) CONTAINING 14.5% SATURATED AMMONIUM SULFATE AGAINST A
160
+ REMARK 280 CRYSTALLIZATION WELL SOLUTION OF 71.4 MM SODIUM CITRATE-CITRIC
161
+ REMARK 280 ACID BUFFER (PH 5.0) CONTAINING 29% SATURATED AMMONIUM SULFATE.,
162
+ REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K
163
+ REMARK 290
164
+ REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
165
+ REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
166
+ REMARK 290
167
+ REMARK 290 SYMOP SYMMETRY
168
+ REMARK 290 NNNMMM OPERATOR
169
+ REMARK 290 1555 X,Y,Z
170
+ REMARK 290 2555 -X,-Y,Z
171
+ REMARK 290 3555 -X+1/2,Y+1/2,-Z
172
+ REMARK 290 4555 X+1/2,-Y+1/2,-Z
173
+ REMARK 290
174
+ REMARK 290 WHERE NNN -> OPERATOR NUMBER
175
+ REMARK 290 MMM -> TRANSLATION VECTOR
176
+ REMARK 290
177
+ REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
178
+ REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
179
+ REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
180
+ REMARK 290 RELATED MOLECULES.
181
+ REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
182
+ REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
183
+ REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
184
+ REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
185
+ REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
186
+ REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
187
+ REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 9.62300
188
+ REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.79850
189
+ REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
190
+ REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 9.62300
191
+ REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 16.79850
192
+ REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
193
+ REMARK 290
194
+ REMARK 290 REMARK: NULL
195
+ REMARK 300
196
+ REMARK 300 BIOMOLECULE: 1
197
+ REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
198
+ REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
199
+ REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
200
+ REMARK 300 BURIED SURFACE AREA.
201
+ REMARK 350
202
+ REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
203
+ REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
204
+ REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
205
+ REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
206
+ REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
207
+ REMARK 350
208
+ REMARK 350 BIOMOLECULE: 1
209
+ REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
210
+ REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
211
+ REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
212
+ REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
213
+ REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
214
+ REMARK 375
215
+ REMARK 375 SPECIAL POSITION
216
+ REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
217
+ REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
218
+ REMARK 375 POSITIONS.
219
+ REMARK 375
220
+ REMARK 375 ATOM RES CSSEQI
221
+ REMARK 375 HOH A 105 LIES ON A SPECIAL POSITION.
222
+ REMARK 375 HOH A 112 LIES ON A SPECIAL POSITION.
223
+ REMARK 500
224
+ REMARK 500 GEOMETRY AND STEREOCHEMISTRY
225
+ REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
226
+ REMARK 500
227
+ REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
228
+ REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
229
+ REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
230
+ REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
231
+ REMARK 500
232
+ REMARK 500 STANDARD TABLE:
233
+ REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
234
+ REMARK 500
235
+ REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
236
+ REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
237
+ REMARK 500
238
+ REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
239
+ REMARK 500 TYR A 1 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
240
+ REMARK 500
241
+ REMARK 500 REMARK: NULL
242
+ REMARK 900
243
+ REMARK 900 RELATED ENTRIES
244
+ REMARK 900 RELATED ID: 1UAO RELATED DB: PDB
245
+ REMARK 900 NMR STRUCTURE OF DESIGNED PROTEIN, CHIGNOLIN, CONSISTING OF ONLY
246
+ REMARK 900 TEN AMINO ACIDS
247
+ REMARK 900 RELATED ID: 2RVD RELATED DB: PDB
248
+ REMARK 900 NMR STRUCTURE OF A MUTANT OF CHIGNOLIN, CLN025
249
+ REMARK 999
250
+ REMARK 999 SEQUENCE
251
+ REMARK 999 THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT
252
+ REMARK 999 KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE TIME OF DEPOSITION.
253
+ DBREF 5AWL A 1 10 PDB 5AWL 5AWL 1 10
254
+ SEQRES 1 A 10 TYR TYR ASP PRO GLU THR GLY THR TRP TYR
255
+ FORMUL 2 HOH *12(H2 O)
256
+ CRYST1 19.246 33.597 11.551 90.00 90.00 90.00 P 21 21 2 4
257
+ ORIGX1 1.000000 0.000000 0.000000 0.00000
258
+ ORIGX2 0.000000 1.000000 0.000000 0.00000
259
+ ORIGX3 0.000000 0.000000 1.000000 0.00000
260
+ SCALE1 0.051959 0.000000 0.000000 0.00000
261
+ SCALE2 0.000000 0.029765 0.000000 0.00000
262
+ SCALE3 0.000000 0.000000 0.086573 0.00000
263
+ ATOM 1 N TYR A 1 25.824 21.671 10.238 1.00 8.64 N
264
+ ANISOU 1 N TYR A 1 1043 1239 1000 -391 -82 -168 N
265
+ ATOM 2 CA TYR A 1 24.935 20.652 10.774 1.00 7.05 C
266
+ ANISOU 2 CA TYR A 1 874 959 848 -150 -142 73 C
267
+ ATOM 3 C TYR A 1 23.729 20.558 9.852 1.00 5.69 C
268
+ ANISOU 3 C TYR A 1 651 640 871 69 -92 15 C
269
+ ATOM 4 O TYR A 1 23.390 21.602 9.289 1.00 6.82 O
270
+ ANISOU 4 O TYR A 1 1096 550 944 -80 -219 69 O
271
+ ATOM 5 CB TYR A 1 24.425 21.029 12.167 1.00 10.53 C
272
+ ANISOU 5 CB TYR A 1 1050 2114 836 -206 -52 -78 C
273
+ ATOM 6 CG TYR A 1 25.525 21.526 13.070 1.00 12.94 C
274
+ ANISOU 6 CG TYR A 1 1132 2825 962 -258 -69 -301 C
275
+ ATOM 7 CD1 TYR A 1 25.829 22.870 13.275 1.00 15.47 C
276
+ ANISOU 7 CD1 TYR A 1 1558 2870 1451 -244 -188 -875 C
277
+ ATOM 8 CD2 TYR A 1 26.291 20.564 13.736 1.00 15.46 C
278
+ ANISOU 8 CD2 TYR A 1 1280 3172 1420 -249 -474 -90 C
279
+ ATOM 9 CE1 TYR A 1 26.870 23.242 14.135 1.00 18.04 C
280
+ ANISOU 9 CE1 TYR A 1 1225 3434 2196 -320 -335 -812 C
281
+ ATOM 10 CE2 TYR A 1 27.325 20.871 14.577 1.00 17.34 C
282
+ ANISOU 10 CE2 TYR A 1 1416 3544 1629 60 -564 -866 C
283
+ ATOM 11 CZ TYR A 1 27.577 22.231 14.752 1.00 16.51 C
284
+ ANISOU 11 CZ TYR A 1 1332 3627 1315 -31 -172 -1216 C
285
+ ATOM 12 OH TYR A 1 28.648 22.620 15.582 1.00 23.32 O
286
+ ANISOU 12 OH TYR A 1 2211 3383 3267 -126 -1462 -950 O
287
+ ATOM 13 N TYR A 2 23.068 19.430 9.704 1.00 5.68 N
288
+ ANISOU 13 N TYR A 2 543 564 1051 30 -34 171 N
289
+ ATOM 14 CA TYR A 2 21.801 19.381 9.017 1.00 4.77 C
290
+ ANISOU 14 CA TYR A 2 551 418 842 72 51 88 C
291
+ ATOM 15 C TYR A 2 20.667 19.519 10.021 1.00 4.55 C
292
+ ANISOU 15 C TYR A 2 506 487 737 -17 2 36 C
293
+ ATOM 16 O TYR A 2 20.667 18.957 11.087 1.00 6.56 O
294
+ ANISOU 16 O TYR A 2 744 926 824 171 80 280 O
295
+ ATOM 17 CB TYR A 2 21.648 18.114 8.208 1.00 5.98 C
296
+ ANISOU 17 CB TYR A 2 688 538 1048 -45 188 -11 C
297
+ ATOM 18 CG TYR A 2 22.553 17.960 7.031 1.00 5.31 C
298
+ ANISOU 18 CG TYR A 2 689 498 832 -106 76 -33 C
299
+ ATOM 19 CD1 TYR A 2 23.698 17.188 7.095 1.00 6.77 C
300
+ ANISOU 19 CD1 TYR A 2 947 627 999 133 199 -12 C
301
+ ATOM 20 CD2 TYR A 2 22.271 18.556 5.816 1.00 6.83 C
302
+ ANISOU 20 CD2 TYR A 2 1024 687 884 -37 -41 -54 C
303
+ ATOM 21 CE1 TYR A 2 24.520 17.039 5.991 1.00 8.06 C
304
+ ANISOU 21 CE1 TYR A 2 840 883 1339 98 232 -60 C
305
+ ATOM 22 CE2 TYR A 2 23.080 18.377 4.709 1.00 8.18 C
306
+ ANISOU 22 CE2 TYR A 2 1563 844 701 -50 42 97 C
307
+ ATOM 23 CZ TYR A 2 24.229 17.647 4.778 1.00 8.72 C
308
+ ANISOU 23 CZ TYR A 2 1372 881 1061 -191 467 -87 C
309
+ ATOM 24 OH TYR A 2 24.977 17.478 3.665 1.00 13.52 O
310
+ ANISOU 24 OH TYR A 2 1632 2220 1284 -243 586 -421 O
311
+ ATOM 25 N ASP A 3 19.665 20.306 9.626 1.00 5.27 N
312
+ ANISOU 25 N ASP A 3 586 666 749 107 11 2 N
313
+ ATOM 26 CA ASP A 3 18.477 20.539 10.432 1.00 5.27 C
314
+ ANISOU 26 CA ASP A 3 729 665 608 158 98 -64 C
315
+ ATOM 27 C ASP A 3 17.534 19.329 10.398 1.00 4.73 C
316
+ ANISOU 27 C ASP A 3 517 722 561 228 19 -18 C
317
+ ATOM 28 O ASP A 3 17.294 18.804 9.311 1.00 5.80 O
318
+ ANISOU 28 O ASP A 3 894 748 563 23 9 -51 O
319
+ ATOM 29 CB ASP A 3 17.779 21.778 9.904 1.00 6.15 C
320
+ ANISOU 29 CB ASP A 3 792 596 950 201 73 -131 C
321
+ ATOM 30 CG ASP A 3 16.612 22.194 10.723 1.00 6.26 C
322
+ ANISOU 30 CG ASP A 3 807 686 886 145 46 -73 C
323
+ ATOM 31 OD1 ASP A 3 15.530 21.611 10.650 1.00 7.43 O
324
+ ANISOU 31 OD1 ASP A 3 855 729 1239 -35 230 -262 O
325
+ ATOM 32 OD2 ASP A 3 16.854 23.197 11.512 1.00 8.48 O
326
+ ANISOU 32 OD2 ASP A 3 998 933 1290 179 -54 -517 O
327
+ ATOM 33 N PRO A 4 17.026 18.889 11.526 1.00 5.29 N
328
+ ANISOU 33 N PRO A 4 749 688 573 57 42 -32 N
329
+ ATOM 34 CA PRO A 4 16.223 17.660 11.537 1.00 5.94 C
330
+ ANISOU 34 CA PRO A 4 910 578 767 82 75 -31 C
331
+ ATOM 35 C PRO A 4 14.852 17.788 10.907 1.00 6.30 C
332
+ ANISOU 35 C PRO A 4 692 672 1031 -38 172 57 C
333
+ ATOM 36 O PRO A 4 14.260 16.756 10.578 1.00 8.02 O
334
+ ANISOU 36 O PRO A 4 874 679 1495 -137 172 -66 O
335
+ ATOM 37 CB PRO A 4 16.101 17.319 13.047 1.00 9.97 C
336
+ ANISOU 37 CB PRO A 4 1896 1139 755 -475 111 214 C
337
+ ATOM 38 CG PRO A 4 16.246 18.639 13.686 1.00 12.06 C
338
+ ANISOU 38 CG PRO A 4 2379 1471 731 -718 399 -34 C
339
+ ATOM 39 CD PRO A 4 17.243 19.407 12.889 1.00 7.32 C
340
+ ANISOU 39 CD PRO A 4 1185 1090 506 -247 67 -115 C
341
+ ATOM 40 N GLU A 5 14.331 19.012 10.801 1.00 6.60 N
342
+ ANISOU 40 N GLU A 5 829 693 986 99 19 -110 N
343
+ ATOM 41 CA GLU A 5 13.040 19.289 10.212 1.00 7.65 C
344
+ ANISOU 41 CA GLU A 5 663 949 1296 212 156 10 C
345
+ ATOM 42 C GLU A 5 13.132 19.592 8.736 1.00 7.27 C
346
+ ANISOU 42 C GLU A 5 585 926 1251 112 -61 -89 C
347
+ ATOM 43 O GLU A 5 12.258 19.150 7.953 1.00 10.19 O
348
+ ANISOU 43 O GLU A 5 897 1427 1547 -45 -265 -230 O
349
+ ATOM 44 CB GLU A 5 12.286 20.421 10.964 1.00 9.50 C
350
+ ANISOU 44 CB GLU A 5 1030 1024 1555 287 -43 -347 C
351
+ ATOM 45 CG GLU A 5 11.645 19.982 12.241 1.00 18.27 C
352
+ ANISOU 45 CG GLU A 5 1652 3412 1879 -101 762 -781 C
353
+ ATOM 46 CD GLU A 5 10.495 19.012 12.167 1.00 19.12 C
354
+ ANISOU 46 CD GLU A 5 1637 3889 1737 -473 650 -139 C
355
+ ATOM 47 OE1 GLU A 5 10.278 18.221 13.127 1.00 30.90 O
356
+ ANISOU 47 OE1 GLU A 5 4613 4730 2399 -1474 290 555 O
357
+ ATOM 48 OE2 GLU A 5 9.752 19.067 11.167 1.00 28.34 O
358
+ ANISOU 48 OE2 GLU A 5 2949 5569 2251 -1216 -282 29 O
359
+ ATOM 49 N THR A 6 14.137 20.351 8.314 1.00 7.56 N
360
+ ANISOU 49 N THR A 6 763 1147 962 18 -132 29 N
361
+ ATOM 50 CA THR A 6 14.200 20.806 6.941 1.00 8.29 C
362
+ ANISOU 50 CA THR A 6 1051 1116 983 74 -166 74 C
363
+ ATOM 51 C THR A 6 15.255 20.072 6.135 1.00 6.59 C
364
+ ANISOU 51 C THR A 6 827 908 771 -50 -269 107 C
365
+ ATOM 52 O THR A 6 15.240 20.133 4.900 1.00 8.09 O
366
+ ANISOU 52 O THR A 6 1125 1125 824 25 -303 34 O
367
+ ATOM 53 CB THR A 6 14.511 22.290 6.824 1.00 10.65 C
368
+ ANISOU 53 CB THR A 6 2052 977 1016 402 -142 73 C
369
+ ATOM 54 OG1 THR A 6 15.802 22.534 7.368 1.00 11.20 O
370
+ ANISOU 54 OG1 THR A 6 2386 840 1028 -267 -159 -94 O
371
+ ATOM 55 CG2 THR A 6 13.536 23.152 7.626 1.00 16.54 C
372
+ ANISOU 55 CG2 THR A 6 3334 1515 1437 1353 436 353 C
373
+ ATOM 56 N GLY A 7 16.216 19.385 6.751 1.00 6.30 N
374
+ ANISOU 56 N GLY A 7 907 665 824 -112 -74 172 N
375
+ ATOM 57 CA GLY A 7 17.256 18.676 6.039 1.00 5.88 C
376
+ ANISOU 57 CA GLY A 7 780 581 874 -199 -150 78 C
377
+ ATOM 58 C GLY A 7 18.259 19.556 5.361 1.00 6.51 C
378
+ ANISOU 58 C GLY A 7 1048 480 946 -173 30 111 C
379
+ ATOM 59 O GLY A 7 19.015 19.091 4.506 1.00 9.78 O
380
+ ANISOU 59 O GLY A 7 1166 809 1743 -78 497 29 O
381
+ ATOM 60 N THR A 8 18.362 20.804 5.695 1.00 5.98 N
382
+ ANISOU 60 N THR A 8 869 662 740 -288 -70 64 N
383
+ ATOM 61 CA THR A 8 19.242 21.760 5.125 1.00 5.66 C
384
+ ANISOU 61 CA THR A 8 740 585 827 -270 -164 23 C
385
+ ATOM 62 C THR A 8 20.419 22.026 6.074 1.00 5.15 C
386
+ ANISOU 62 C THR A 8 842 528 588 -262 -107 61 C
387
+ ATOM 63 O THR A 8 20.317 21.872 7.313 1.00 6.36 O
388
+ ANISOU 63 O THR A 8 818 962 635 -73 -91 169 O
389
+ ATOM 64 CB THR A 8 18.553 23.073 4.762 1.00 9.09 C
390
+ ANISOU 64 CB THR A 8 1397 762 1294 -179 -578 207 C
391
+ ATOM 65 OG1 THR A 8 17.905 23.602 5.922 1.00 10.05 O
392
+ ANISOU 65 OG1 THR A 8 1164 832 1823 216 -488 29 O
393
+ ATOM 66 CG2 THR A 8 17.498 22.871 3.686 1.00 11.85 C
394
+ ANISOU 66 CG2 THR A 8 1277 1603 1622 -427 -774 589 C
395
+ ATOM 67 N TRP A 9 21.517 22.418 5.517 1.00 5.75 N
396
+ ANISOU 67 N TRP A 9 823 805 556 -342 -145 82 N
397
+ ATOM 68 CA TRP A 9 22.762 22.680 6.241 1.00 4.78 C
398
+ ANISOU 68 CA TRP A 9 723 538 556 -74 0 6 C
399
+ ATOM 69 C TRP A 9 22.687 24.060 6.869 1.00 4.96 C
400
+ ANISOU 69 C TRP A 9 741 511 633 -196 -14 91 C
401
+ ATOM 70 O TRP A 9 22.321 25.031 6.185 1.00 7.83 O
402
+ ANISOU 70 O TRP A 9 1496 595 884 -23 -365 87 O
403
+ ATOM 71 CB TRP A 9 23.924 22.604 5.307 1.00 6.90 C
404
+ ANISOU 71 CB TRP A 9 781 955 884 -94 110 -69 C
405
+ ATOM 72 CG TRP A 9 25.267 22.745 5.969 1.00 6.58 C
406
+ ANISOU 72 CG TRP A 9 696 878 927 -120 153 -7 C
407
+ ATOM 73 CD1 TRP A 9 26.024 23.847 6.060 1.00 9.48 C
408
+ ANISOU 73 CD1 TRP A 9 873 1071 1659 -309 29 207 C
409
+ ATOM 74 CD2 TRP A 9 25.975 21.701 6.641 1.00 6.96 C
410
+ ANISOU 74 CD2 TRP A 9 714 994 939 -138 82 19 C
411
+ ATOM 75 NE1 TRP A 9 27.180 23.571 6.750 1.00 10.18 N
412
+ ANISOU 75 NE1 TRP A 9 736 1373 1759 -438 54 121 N
413
+ ATOM 76 CE2 TRP A 9 27.178 22.245 7.100 1.00 7.80 C
414
+ ANISOU 76 CE2 TRP A 9 657 1347 958 -292 75 32 C
415
+ ATOM 77 CE3 TRP A 9 25.747 20.347 6.894 1.00 8.84 C
416
+ ANISOU 77 CE3 TRP A 9 1082 818 1458 -23 -255 -197 C
417
+ ATOM 78 CZ2 TRP A 9 28.125 21.492 7.781 1.00 10.37 C
418
+ ANISOU 78 CZ2 TRP A 9 741 1704 1497 -42 -51 -16 C
419
+ ATOM 79 CZ3 TRP A 9 26.676 19.593 7.572 1.00 10.97 C
420
+ ANISOU 79 CZ3 TRP A 9 1153 961 2054 226 -206 -128 C
421
+ ATOM 80 CH2 TRP A 9 27.865 20.176 8.026 1.00 10.75 C
422
+ ANISOU 80 CH2 TRP A 9 1020 1424 1639 362 -201 -352 C
423
+ ATOM 81 N TYR A 10 23.053 24.188 8.139 1.00 5.32 N
424
+ ANISOU 81 N TYR A 10 835 603 582 -111 -48 41 N
425
+ ATOM 82 CA TYR A 10 23.135 25.467 8.794 1.00 5.77 C
426
+ ANISOU 82 CA TYR A 10 999 524 669 -145 -87 15 C
427
+ ATOM 83 C TYR A 10 24.386 25.590 9.646 1.00 6.26 C
428
+ ANISOU 83 C TYR A 10 921 621 836 -235 59 -128 C
429
+ ATOM 84 O TYR A 10 24.585 26.750 10.070 1.00 7.80 O
430
+ ANISOU 84 O TYR A 10 1092 746 1127 -334 -65 -227 O
431
+ ATOM 85 CB TYR A 10 21.862 25.753 9.636 1.00 6.56 C
432
+ ANISOU 85 CB TYR A 10 931 682 881 50 -102 -115 C
433
+ ATOM 86 CG TYR A 10 21.754 24.860 10.821 1.00 5.72 C
434
+ ANISOU 86 CG TYR A 10 671 779 724 -17 43 -163 C
435
+ ATOM 87 CD1 TYR A 10 22.199 25.208 12.100 1.00 8.96 C
436
+ ANISOU 87 CD1 TYR A 10 1759 892 754 -331 26 -249 C
437
+ ATOM 88 CD2 TYR A 10 21.203 23.586 10.716 1.00 6.13 C
438
+ ANISOU 88 CD2 TYR A 10 731 986 613 -201 -156 -59 C
439
+ ATOM 89 CE1 TYR A 10 22.104 24.385 13.182 1.00 9.28 C
440
+ ANISOU 89 CE1 TYR A 10 1838 1128 561 -437 -39 -241 C
441
+ ATOM 90 CE2 TYR A 10 21.118 22.747 11.804 1.00 6.42 C
442
+ ANISOU 90 CE2 TYR A 10 663 1137 641 -363 28 -79 C
443
+ ATOM 91 CZ TYR A 10 21.563 23.125 13.050 1.00 6.27 C
444
+ ANISOU 91 CZ TYR A 10 873 1043 467 -108 140 -106 C
445
+ ATOM 92 OH TYR A 10 21.499 22.315 14.128 1.00 8.82 O
446
+ ANISOU 92 OH TYR A 10 1457 1357 535 -467 60 -104 O
447
+ ATOM 93 OXT TYR A 10 25.084 24.587 9.884 1.00 6.99 O
448
+ ANISOU 93 OXT TYR A 10 773 860 1023 -125 -204 -150 O
449
+ TER 94 TYR A 10
450
+ HETATM 95 O HOH A 101 7.813 17.749 10.939 1.00 33.46 O
451
+ ANISOU 95 O HOH A 101 2429 2631 7653 759 -165 -320 O
452
+ HETATM 96 O HOH A 102 30.527 20.889 16.186 1.00 34.87 O
453
+ ANISOU 96 O HOH A 102 2466 6021 4761 931 -1857 -2131 O
454
+ HETATM 97 O HOH A 103 20.817 19.783 13.738 1.00 10.24 O
455
+ ANISOU 97 O HOH A 103 1786 1261 842 -553 -100 134 O
456
+ HETATM 98 O HOH A 104 19.706 25.504 6.460 1.00 25.64 O
457
+ ANISOU 98 O HOH A 104 2301 2218 5224 1073 -1856 -1239 O
458
+ HETATM 99 O HOH A 105 19.246 16.798 3.137 0.50 21.96 O
459
+ ANISOU 99 O HOH A 105 3268 3354 1720 1549 0 0 O
460
+ HETATM 100 O HOH A 106 13.782 21.392 2.921 1.00 14.09 O
461
+ ANISOU 100 O HOH A 106 1634 1443 2276 -166 -738 296 O
462
+ HETATM 101 O HOH A 107 27.076 15.685 3.844 1.00 33.07 O
463
+ ANISOU 101 O HOH A 107 3453 5461 3650 1924 763 -338 O
464
+ HETATM 102 O HOH A 108 28.383 22.298 11.296 1.00 18.18 O
465
+ ANISOU 102 O HOH A 108 1022 3711 2175 44 -118 -162 O
466
+ HETATM 103 O HOH A 109 29.871 24.582 7.637 1.00 68.49 O
467
+ ANISOU 103 O HOH A 109 9275 7095 9654 1983 -458 1020 O
468
+ HETATM 104 O HOH A 110 18.361 25.585 12.710 1.00 17.73 O
469
+ ANISOU 104 O HOH A 110 1576 1757 3404 -298 791 -169 O
470
+ HETATM 105 O HOH A 111 8.897 16.529 8.446 0.50 24.45 O
471
+ ANISOU 105 O HOH A 111 3279 768 5243 -397 -974 601 O
472
+ HETATM 106 O HOH A 112 9.623 16.798 5.908 0.50 64.33 O
473
+ ANISOU 106 O HOH A 112 8243 8592 7607 788 0 0 O
474
+ MASTER 228 0 0 0 0 0 0 6 105 1 0 1
475
+ END