Header list of 1y8b.pdb file
Complete list - t 20 2 Bytes
HEADER TRANSFERASE 10-DEC-04 1Y8B
TITLE SOLUTION NMR-DERIVED GLOBAL FOLD OF MALATE SYNTHASE G FROM E.COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALATE SYNTHASE G;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MSG;
COMPND 5 EC: 2.3.3.9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: GLCB, GLC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-28B
KEYWDS NMR GLOBAL FOLD, APO-MALATE SYNTHASE G, 82 KDA ENZYME, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR V.TUGARINOV,W.-Y.CHOY,V.Y.OREKHOV,L.E.KAY
REVDAT 4 20-OCT-21 1Y8B 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1Y8B 1 VERSN
REVDAT 2 01-FEB-05 1Y8B 1 JRNL
REVDAT 1 11-JAN-05 1Y8B 0
JRNL AUTH V.TUGARINOV,W.-Y.CHOY,V.Y.OREKHOV,L.E.KAY
JRNL TITL SOLUTION NMR-DERIVED GLOBAL FOLD OF A MONOMERIC 82-KDA
JRNL TITL 2 ENZYME.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 622 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15637152
JRNL DOI 10.1073/PNAS.0407792102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR-NIH 2.9.3
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Y8B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031242.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : 25 MM SODIUM PHOSPHATE; 20 MM
REMARK 210 MAGNESIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 724
REMARK 465 GLU A 725
REMARK 465 HIS A 726
REMARK 465 HIS A 727
REMARK 465 HIS A 728
REMARK 465 HIS A 729
REMARK 465 HIS A 730
REMARK 465 HIS A 731
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HD1 HIS A 713 HH21 ARG A 716 1.23
REMARK 500 HD21 ASN A 403 HE22 GLN A 441 1.33
REMARK 500 O ILE A 592 H LEU A 596 1.36
REMARK 500 O GLN A 441 H ARG A 443 1.40
REMARK 500 H MET A 422 O VAL A 446 1.41
REMARK 500 O ARG A 718 HG SER A 722 1.44
REMARK 500 O ARG A 162 H VAL A 166 1.44
REMARK 500 O ALA A 402 H PHE A 406 1.45
REMARK 500 O ASN A 559 H GLN A 562 1.46
REMARK 500 O ALA A 127 H ALA A 131 1.48
REMARK 500 HG SER A 274 OD1 ASN A 339 1.49
REMARK 500 O GLY A 152 H MET A 154 1.49
REMARK 500 O ILE A 603 H VAL A 607 1.49
REMARK 500 H LEU A 138 O VAL A 259 1.49
REMARK 500 O ALA A 484 H ASN A 488 1.50
REMARK 500 O ASN A 434 H SER A 437 1.51
REMARK 500 O ALA A 321 H GLY A 324 1.52
REMARK 500 O CYS A 688 H ALA A 692 1.52
REMARK 500 H ALA A 321 O SER A 325 1.52
REMARK 500 O VAL A 194 H LYS A 196 1.53
REMARK 500 HE ARG A 134 OD1 ASN A 314 1.53
REMARK 500 O LYS A 78 H LYS A 82 1.54
REMARK 500 O LYS A 17 H ASP A 21 1.55
REMARK 500 O GLN A 554 H ALA A 558 1.55
REMARK 500 O LEU A 526 H GLY A 529 1.56
REMARK 500 O SER A 659 H MET A 663 1.56
REMARK 500 O ALA A 516 H TYR A 519 1.56
REMARK 500 O THR A 383 H SER A 385 1.58
REMARK 500 O GLU A 66 H SER A 70 1.58
REMARK 500 O LEU A 88 H TYR A 90 1.58
REMARK 500 O ALA A 689 H ALA A 693 1.58
REMARK 500 O LEU A 454 H THR A 457 1.58
REMARK 500 O PRO A 120 H MET A 122 1.59
REMARK 500 O GLN A 61 H ASP A 65 1.59
REMARK 500 O LEU A 660 H ALA A 664 1.60
REMARK 500 O LEU A 210 H THR A 212 1.60
REMARK 500 O VAL A 217 H ALA A 322 1.60
REMARK 500 O GLN A 441 N ARG A 443 2.19
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 1 GLN A 3 -18.21 -156.38
REMARK 500 1 SER A 8 -133.27 59.74
REMARK 500 1 PRO A 74 -157.25 -75.81
REMARK 500 1 LYS A 76 -78.68 -174.83
REMARK 500 1 ASP A 77 59.58 -96.15
REMARK 500 1 PRO A 93 164.53 -45.87
REMARK 500 1 PRO A 95 -17.22 -46.87
REMARK 500 1 GLU A 96 -33.78 73.63
REMARK 500 1 ILE A 105 -160.64 -57.33
REMARK 500 1 SER A 111 4.90 -150.63
REMARK 500 1 ALA A 113 125.15 -173.85
REMARK 500 1 ALA A 121 34.26 -66.99
REMARK 500 1 MET A 122 -32.39 -145.10
REMARK 500 1 ASN A 132 5.80 -63.80
REMARK 500 1 PRO A 149 99.83 -44.71
REMARK 500 1 ALA A 153 -50.63 66.79
REMARK 500 1 VAL A 155 -90.60 -153.22
REMARK 500 1 PRO A 160 -6.88 -47.65
REMARK 500 1 ASN A 182 -54.12 -130.14
REMARK 500 1 VAL A 189 -48.79 -145.50
REMARK 500 1 ASP A 195 14.92 -53.05
REMARK 500 1 LYS A 196 -53.11 -134.04
REMARK 500 1 GLN A 197 -163.10 -179.34
REMARK 500 1 LYS A 203 -3.14 -55.33
REMARK 500 1 ARG A 211 -21.72 58.22
REMARK 500 1 THR A 212 107.43 177.66
REMARK 500 1 THR A 227 9.50 -67.09
REMARK 500 1 CYS A 228 145.87 -171.02
REMARK 500 1 ALA A 244 39.03 -76.58
REMARK 500 1 ASN A 245 19.00 -150.12
REMARK 500 1 ASP A 251 38.43 -160.59
REMARK 500 1 HIS A 255 8.27 55.47
REMARK 500 1 ASP A 270 -169.19 155.46
REMARK 500 1 CYS A 271 -142.39 -92.25
REMARK 500 1 GLU A 272 -79.21 -71.82
REMARK 500 1 SER A 274 -155.14 -167.24
REMARK 500 1 VAL A 278 98.80 -160.54
REMARK 500 1 GLN A 295 0.34 -68.96
REMARK 500 1 LEU A 298 -151.84 -71.13
REMARK 500 1 GLN A 299 147.51 -170.37
REMARK 500 1 ASN A 305 169.96 -46.70
REMARK 500 1 ARG A 307 67.84 67.90
REMARK 500 1 ASP A 315 72.62 62.72
REMARK 500 1 ASP A 316 154.43 -41.94
REMARK 500 1 SER A 325 167.75 -42.78
REMARK 500 1 MET A 344 23.68 -70.59
REMARK 500 1 THR A 345 -158.22 -103.11
REMARK 500 1 ASN A 355 -138.67 46.90
REMARK 500 1 GLU A 356 -109.93 -158.54
REMARK 500 1 PRO A 358 -87.23 -63.95
REMARK 500
REMARK 500 THIS ENTRY HAS 1023 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D8C RELATED DB: PDB
REMARK 900 MALATE SYNTHASE G COMPLEXED WITH MAGNESIUM AND GLYOXYLATE
REMARK 900 RELATED ID: 1P7T RELATED DB: PDB
REMARK 900 ABORTIVE TERNARY COMPLEX OF MALATE SYNTHASE G WITH PYRUVATE AND
REMARK 900 ACETYL-COENZYME A
DBREF 1Y8B A 2 723 UNP P37330 MASZ_ECOLI 1 722
SEQADV 1Y8B MET A 1 UNP P37330 INITIATING METHIONINE
SEQADV 1Y8B ALA A 2 UNP P37330 SER 1 ENGINEERED MUTATION
SEQADV 1Y8B LEU A 724 UNP P37330 CLONING ARTIFACT
SEQADV 1Y8B GLU A 725 UNP P37330 CLONING ARTIFACT
SEQADV 1Y8B HIS A 726 UNP P37330 EXPRESSION TAG
SEQADV 1Y8B HIS A 727 UNP P37330 EXPRESSION TAG
SEQADV 1Y8B HIS A 728 UNP P37330 EXPRESSION TAG
SEQADV 1Y8B HIS A 729 UNP P37330 EXPRESSION TAG
SEQADV 1Y8B HIS A 730 UNP P37330 EXPRESSION TAG
SEQADV 1Y8B HIS A 731 UNP P37330 EXPRESSION TAG
SEQRES 1 A 731 MET ALA GLN THR ILE THR GLN SER ARG LEU ARG ILE ASP
SEQRES 2 A 731 ALA ASN PHE LYS ARG PHE VAL ASP GLU GLU VAL LEU PRO
SEQRES 3 A 731 GLY THR GLY LEU ASP ALA ALA ALA PHE TRP ARG ASN PHE
SEQRES 4 A 731 ASP GLU ILE VAL HIS ASP LEU ALA PRO GLU ASN ARG GLN
SEQRES 5 A 731 LEU LEU ALA GLU ARG ASP ARG ILE GLN ALA ALA LEU ASP
SEQRES 6 A 731 GLU TRP HIS ARG SER ASN PRO GLY PRO VAL LYS ASP LYS
SEQRES 7 A 731 ALA ALA TYR LYS SER PHE LEU ARG GLU LEU GLY TYR LEU
SEQRES 8 A 731 VAL PRO GLN PRO GLU ARG VAL THR VAL GLU THR THR GLY
SEQRES 9 A 731 ILE ASP SER GLU ILE THR SER GLN ALA GLY PRO GLN LEU
SEQRES 10 A 731 VAL VAL PRO ALA MET ASN ALA ARG TYR ALA LEU ASN ALA
SEQRES 11 A 731 ALA ASN ALA ARG TRP GLY SER LEU TYR ASP ALA LEU TYR
SEQRES 12 A 731 GLY SER ASP ILE ILE PRO GLN GLU GLY ALA MET VAL SER
SEQRES 13 A 731 GLY TYR ASP PRO GLN ARG GLY GLU GLN VAL ILE ALA TRP
SEQRES 14 A 731 VAL ARG ARG PHE LEU ASP GLU SER LEU PRO LEU GLU ASN
SEQRES 15 A 731 GLY SER TYR GLN ASP VAL VAL ALA PHE LYS VAL VAL ASP
SEQRES 16 A 731 LYS GLN LEU ARG ILE GLN LEU LYS ASN GLY LYS GLU THR
SEQRES 17 A 731 THR LEU ARG THR PRO ALA GLN PHE VAL GLY TYR ARG GLY
SEQRES 18 A 731 ASP ALA ALA ALA PRO THR CYS ILE LEU LEU LYS ASN ASN
SEQRES 19 A 731 GLY LEU HIS ILE GLU LEU GLN ILE ASP ALA ASN GLY ARG
SEQRES 20 A 731 ILE GLY LYS ASP ASP PRO ALA HIS ILE ASN ASP VAL ILE
SEQRES 21 A 731 VAL GLU ALA ALA ILE SER THR ILE LEU ASP CYS GLU ASP
SEQRES 22 A 731 SER VAL ALA ALA VAL ASP ALA GLU ASP LYS ILE LEU LEU
SEQRES 23 A 731 TYR ARG ASN LEU LEU GLY LEU MET GLN GLY THR LEU GLN
SEQRES 24 A 731 GLU LYS MET GLU LYS ASN GLY ARG GLN ILE VAL ARG LYS
SEQRES 25 A 731 LEU ASN ASP ASP ARG HIS TYR THR ALA ALA ASP GLY SER
SEQRES 26 A 731 GLU ILE SER LEU HIS GLY ARG SER LEU LEU PHE ILE ARG
SEQRES 27 A 731 ASN VAL GLY HIS LEU MET THR ILE PRO VAL ILE TRP ASP
SEQRES 28 A 731 SER GLU GLY ASN GLU ILE PRO GLU GLY ILE LEU ASP GLY
SEQRES 29 A 731 VAL MET THR GLY ALA ILE ALA LEU TYR ASP LEU LYS VAL
SEQRES 30 A 731 GLN LYS ASN SER ARG THR GLY SER VAL TYR ILE VAL LYS
SEQRES 31 A 731 PRO LYS MET HIS GLY PRO GLN GLU VAL ALA PHE ALA ASN
SEQRES 32 A 731 LYS LEU PHE THR ARG ILE GLU THR MET LEU GLY MET ALA
SEQRES 33 A 731 PRO ASN THR LEU LYS MET GLY ILE MET ASP GLU GLU ARG
SEQRES 34 A 731 ARG THR SER LEU ASN LEU ARG SER CYS ILE ALA GLN ALA
SEQRES 35 A 731 ARG ASN ARG VAL ALA PHE ILE ASN THR GLY PHE LEU ASP
SEQRES 36 A 731 ARG THR GLY ASP GLU MET HIS SER VAL MET GLU ALA GLY
SEQRES 37 A 731 PRO MET LEU ARG LYS ASN GLN MET LYS SER THR PRO TRP
SEQRES 38 A 731 ILE LYS ALA TYR GLU ARG ASN ASN VAL LEU SER GLY LEU
SEQRES 39 A 731 PHE CYS GLY LEU ARG GLY LYS ALA GLN ILE GLY LYS GLY
SEQRES 40 A 731 MET TRP ALA MET PRO ASP LEU MET ALA ASP MET TYR SER
SEQRES 41 A 731 GLN LYS GLY ASP GLN LEU ARG ALA GLY ALA ASN THR ALA
SEQRES 42 A 731 TRP VAL PRO SER PRO THR ALA ALA THR LEU HIS ALA LEU
SEQRES 43 A 731 HIS TYR HIS GLN THR ASN VAL GLN SER VAL GLN ALA ASN
SEQRES 44 A 731 ILE ALA GLN THR GLU PHE ASN ALA GLU PHE GLU PRO LEU
SEQRES 45 A 731 LEU ASP ASP LEU LEU THR ILE PRO VAL ALA GLU ASN ALA
SEQRES 46 A 731 ASN TRP SER ALA GLN GLU ILE GLN GLN GLU LEU ASP ASN
SEQRES 47 A 731 ASN VAL GLN GLY ILE LEU GLY TYR VAL VAL ARG TRP VAL
SEQRES 48 A 731 GLU GLN GLY ILE GLY CYS SER LYS VAL PRO ASP ILE HIS
SEQRES 49 A 731 ASN VAL ALA LEU MET GLU ASP ARG ALA THR LEU ARG ILE
SEQRES 50 A 731 SER SER GLN HIS ILE ALA ASN TRP LEU ARG HIS GLY ILE
SEQRES 51 A 731 LEU THR LYS GLU GLN VAL GLN ALA SER LEU GLU ASN MET
SEQRES 52 A 731 ALA LYS VAL VAL ASP GLN GLN ASN ALA GLY ASP PRO ALA
SEQRES 53 A 731 TYR ARG PRO MET ALA GLY ASN PHE ALA ASN SER CYS ALA
SEQRES 54 A 731 PHE LYS ALA ALA SER ASP LEU ILE PHE LEU GLY VAL LYS
SEQRES 55 A 731 GLN PRO ASN GLY TYR THR GLU PRO LEU LEU HIS ALA TRP
SEQRES 56 A 731 ARG LEU ARG GLU LYS GLU SER HIS LEU GLU HIS HIS HIS
SEQRES 57 A 731 HIS HIS HIS
HELIX 1 1 ASP A 13 GLY A 29 1 17
HELIX 2 2 ASP A 31 ASN A 71 1 41
HELIX 3 3 ASP A 77 GLY A 89 1 13
HELIX 4 4 ASP A 106 SER A 111 1 6
HELIX 5 5 ASN A 123 ASN A 132 1 10
HELIX 6 6 ALA A 133 TRP A 135 5 3
HELIX 7 7 SER A 137 GLY A 144 1 8
HELIX 8 8 ASP A 159 LEU A 178 1 20
HELIX 9 9 SER A 184 VAL A 188 5 5
HELIX 10 10 THR A 212 ALA A 214 5 3
HELIX 11 11 ARG A 247 ASP A 252 5 6
HELIX 12 12 ASP A 279 MET A 294 1 16
HELIX 13 13 GLY A 360 GLN A 378 1 19
HELIX 14 14 GLY A 395 MET A 415 1 21
HELIX 15 15 ASN A 434 ALA A 440 1 7
HELIX 16 16 LEU A 454 MET A 465 1 12
HELIX 17 17 LYS A 473 SER A 478 1 6
HELIX 18 18 PRO A 480 LEU A 494 1 15
HELIX 19 19 ASP A 517 LEU A 526 1 10
HELIX 20 20 SER A 537 THR A 551 1 15
HELIX 21 21 ASN A 552 ALA A 561 1 10
HELIX 22 22 GLU A 564 LEU A 577 1 14
HELIX 23 23 SER A 588 GLN A 613 1 26
HELIX 24 24 ILE A 637 GLY A 649 1 13
HELIX 25 25 THR A 652 GLN A 669 1 18
HELIX 26 26 GLN A 669 ASP A 674 1 6
HELIX 27 27 SER A 687 LEU A 699 1 13
HELIX 28 28 THR A 708 HIS A 723 1 16
SHEET 1 A 3 SER A 266 LEU A 269 0
SHEET 2 A 3 GLN A 116 VAL A 119 1 N VAL A 119 O ILE A 268
SHEET 3 A 3 TRP A 534 VAL A 535 1 O VAL A 535 N GLN A 116
SHEET 1 B 2 ILE A 200 GLN A 201 0
SHEET 2 B 2 GLU A 207 THR A 208 -1 O THR A 208 N ILE A 200
SHEET 1 C 6 ILE A 256 VAL A 261 0
SHEET 2 C 6 LEU A 236 ILE A 242 -1 N GLU A 239 O ILE A 260
SHEET 3 C 6 ALA A 225 ASN A 233 -1 N LEU A 231 O ILE A 238
SHEET 4 C 6 PHE A 216 ASP A 222 -1 N GLY A 218 O LEU A 230
SHEET 5 C 6 HIS A 318 ALA A 321 -1 O THR A 320 N TYR A 219
SHEET 6 C 6 GLU A 326 SER A 328 -1 O ILE A 327 N TYR A 319
SHEET 1 D 2 TYR A 387 ILE A 388 0
SHEET 2 D 2 LYS A 421 MET A 422 1 O LYS A 421 N ILE A 388
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - t 20 2 Bytes