HEADER TRANSFERASE 13-JUN-07 2JQX
TITLE SOLUTION STRUCTURE OF MALATE SYNTHASE G FROM JOINT REFINEMENT AGAINST
TITLE 2 NMR AND SAXS DATA
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: VECTOR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-28B
KEYWDS APO-MALATE SYNTHASE G, 82 KDA ENZYME, SAXS, SMALL-ANGLE X-RAY
KEYWDS 2 SCATTERING, RDC, RESIDUAL DIPOLAR COUPLING, RESIDUAL CHEMICAL SHIFT
KEYWDS 3 ANISOTROPY, ALIGNMENT, DEUTERATION, TRANSFERASE
EXPDTA SOLUTION NMR
AUTHOR A.GRISHAEV,V.TUGARINOV,L.E.KAY,J.TREWHELLA,A.BAX
REVDAT 5 20-DEC-23 2JQX 1 REMARK
REVDAT 4 20-OCT-21 2JQX 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2JQX 1 VERSN
REVDAT 2 22-JAN-08 2JQX 1 JRNL
REVDAT 1 10-JUL-07 2JQX 0
JRNL AUTH A.GRISHAEV,V.TUGARINOV,L.E.KAY,J.TREWHELLA,A.BAX
JRNL TITL REFINED SOLUTION STRUCTURE OF THE 82-KDA ENZYME MALATE
JRNL TITL 2 SYNTHASE G FROM JOINT NMR AND SYNCHROTRON SAXS RESTRAINTS
JRNL REF J.BIOMOL.NMR V. 40 95 2008
JRNL REFN ISSN 0925-2738
JRNL PMID 18008171
JRNL DOI 10.1007/S10858-007-9211-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.TUGARINOV,W.CHOY,V.Y.OREKHOV,L.E.KAY
REMARK 1 TITL SOLUTION NMR-DERIVED GLOBAL FOLD OF A MONOMERIC 82-KDA
REMARK 1 TITL 2 ENZYME
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 102 622 2005
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.GRISHAEV,J.WU,J.TREWHELLA,A.BAX
REMARK 1 TITL REFINEMENT OF MULTIDOMAIN PROTEIN STRUCTURES BY COMBINATION
REMARK 1 TITL 2 OF SOLUTION SMALL-ANGLE X-RAY SCATTERING AND NMR DATA
REMARK 1 REF J.AM.CHEM.SOC. V. 127 16621 2005
REMARK 1 REFN ISSN 0002-7863
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000100177.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : 170
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.17 MM [U-100% 15N], ILE CD1
REMARK 210 -[13CH3] MALATE SYNTHASE G, 20
REMARK 210 MM SODIUM PHOSPHATE, 5 MM DTT,
REMARK 210 150 MM SODIUM CHLORIDE, 100% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D TROSY-BASED NOESY; 4D TROSY
REMARK 210 -BASED NOESY; 3D TROSY-HNCO
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 : OTOKO, PRIMUS
REMARK 210 METHOD USED : SIMULATED ANNEALING/CARTESIAN
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 5
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : CLOSEST TO THE AVERAGE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: EXPERIMENTAL SMALL-ANGLE X-RAY SCATTERING DATA WERE
REMARK 210 ACQUIRED AT THE BEAM LINE 4-2, SSRL, USING INCIDENT RADIATION AT
REMARK 210 THE 8 KEV AND 1.25 M SAMPLE-TO-DETECTOR DISTANCE. ONE-
REMARK 210 DIMENSIONAL GAS POSITION-SENSITIVE DETECTOR WAS USED FOR DATA
REMARK 210 COLLECTION. EXPERIMENTAL NMR DATA USED FOR STRUCTURE REFINEMENT
REMARK 210 ARE THE SAME AS IN THE PDB DEPOSITION 1Y8B (CITATION 1). SAXS
REMARK 210 INTENSITIES OVER THE RANGE Q = 0.028 TO 0.780 A-1 WERE FITTED BY
REMARK 210 A SUPPLEMENTARY MODULE AS DESCRIBED IN CITATION 2.
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 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 O ASP A 106 H THR A 110 1.57
REMARK 500 H LEU A 138 O VAL A 259 1.58
REMARK 500 O MET A 422 H PHE A 448 1.58
REMARK 500 O ILE A 388 H GLY A 423 1.59
REMARK 500 H MET A 422 O VAL A 446 1.59
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 2 -71.18 -56.74
REMARK 500 SER A 8 -89.94 56.44
REMARK 500 LEU A 30 99.91 -44.05
REMARK 500 PRO A 72 154.07 -43.47
REMARK 500 GLN A 94 117.76 -160.33
REMARK 500 GLU A 96 80.63 64.77
REMARK 500 ILE A 105 -161.19 -65.53
REMARK 500 SER A 111 57.93 -176.01
REMARK 500 ALA A 153 176.66 61.19
REMARK 500 VAL A 155 -91.88 42.88
REMARK 500 LEU A 178 98.00 -177.17
REMARK 500 PRO A 179 -161.44 -68.70
REMARK 500 LEU A 180 -161.67 -103.81
REMARK 500 ASN A 182 -34.34 -169.25
REMARK 500 VAL A 189 -33.05 -140.98
REMARK 500 GLN A 197 -161.92 -167.28
REMARK 500 ARG A 211 -56.32 -28.19
REMARK 500 PHE A 216 105.04 -58.07
REMARK 500 PRO A 226 101.48 -50.74
REMARK 500 ASP A 243 101.10 -169.64
REMARK 500 ASP A 258 138.41 -172.38
REMARK 500 ASP A 270 -46.37 161.76
REMARK 500 CYS A 271 138.54 64.69
REMARK 500 GLU A 272 170.36 63.04
REMARK 500 ALA A 276 172.30 -59.41
REMARK 500 VAL A 278 101.53 -160.53
REMARK 500 ASP A 279 -176.73 -50.76
REMARK 500 THR A 297 54.38 -171.26
REMARK 500 LEU A 298 -169.10 -55.65
REMARK 500 ASN A 305 97.04 -53.31
REMARK 500 ARG A 307 79.55 65.54
REMARK 500 ASP A 315 -171.92 45.53
REMARK 500 ALA A 321 -179.03 -61.39
REMARK 500 HIS A 330 170.93 -46.35
REMARK 500 THR A 345 158.43 -49.38
REMARK 500 PRO A 347 91.22 -48.38
REMARK 500 ASN A 355 -108.61 35.01
REMARK 500 PRO A 358 -70.48 -82.27
REMARK 500 GLU A 359 157.88 75.27
REMARK 500 LYS A 379 -72.87 -155.71
REMARK 500 ASN A 380 97.96 -160.87
REMARK 500 SER A 381 176.30 -55.08
REMARK 500 SER A 385 -168.65 -164.50
REMARK 500 PRO A 391 36.73 -93.29
REMARK 500 MET A 393 56.97 -91.61
REMARK 500 LEU A 413 37.32 -96.74
REMARK 500 ALA A 416 149.44 -170.78
REMARK 500 THR A 419 33.20 37.64
REMARK 500 ASP A 426 156.14 59.59
REMARK 500 GLU A 427 -53.15 -149.61
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y8B RELATED DB: PDB
REMARK 900 NMR-REFINED STRUCTURE OF APO MALATE SYNTHASE G
REMARK 900 RELATED ID: 1D8C RELATED DB: PDB
REMARK 900 MALATE SYNTHASE G COMPLEXED WITH MAGNESIUM AND GLYOXYLATE
REMARK 950
REMARK 950 THIS ENTRY 2JQX REFLECTS A JOINT MODELING OF THE STRUCTURAL
REMARK 950 DATA IN RCSB031242.MR PDB ENTRY 1Y8B AND ADDITIONAL SAX DATA.
REMARK 950 INFORMATION IN REMARK 210 SERIES IS BASED ON SAX AND THE
REMARK 950 EXPERIMENT DESCRIBED IN PDB ENTRY 1Y8B. ORIGINAL DATA
REMARK 950 DETERMINED BY AUTHOR: V.TUGARINOV, W.-Y.CHOY, V.Y.OREKHOV,
REMARK 950 L.E.KAY
DBREF 2JQX A 1 723 UNP P37330 MASZ_ECOLI 1 723
SEQADV 2JQX ALA A 2 UNP P37330 SER 2 ENGINEERED MUTATION
SEQRES 1 A 723 MET ALA GLN THR ILE THR GLN SER ARG LEU ARG ILE ASP
SEQRES 2 A 723 ALA ASN PHE LYS ARG PHE VAL ASP GLU GLU VAL LEU PRO
SEQRES 3 A 723 GLY THR GLY LEU ASP ALA ALA ALA PHE TRP ARG ASN PHE
SEQRES 4 A 723 ASP GLU ILE VAL HIS ASP LEU ALA PRO GLU ASN ARG GLN
SEQRES 5 A 723 LEU LEU ALA GLU ARG ASP ARG ILE GLN ALA ALA LEU ASP
SEQRES 6 A 723 GLU TRP HIS ARG SER ASN PRO GLY PRO VAL LYS ASP LYS
SEQRES 7 A 723 ALA ALA TYR LYS SER PHE LEU ARG GLU LEU GLY TYR LEU
SEQRES 8 A 723 VAL PRO GLN PRO GLU ARG VAL THR VAL GLU THR THR GLY
SEQRES 9 A 723 ILE ASP SER GLU ILE THR SER GLN ALA GLY PRO GLN LEU
SEQRES 10 A 723 VAL VAL PRO ALA MET ASN ALA ARG TYR ALA LEU ASN ALA
SEQRES 11 A 723 ALA ASN ALA ARG TRP GLY SER LEU TYR ASP ALA LEU TYR
SEQRES 12 A 723 GLY SER ASP ILE ILE PRO GLN GLU GLY ALA MET VAL SER
SEQRES 13 A 723 GLY TYR ASP PRO GLN ARG GLY GLU GLN VAL ILE ALA TRP
SEQRES 14 A 723 VAL ARG ARG PHE LEU ASP GLU SER LEU PRO LEU GLU ASN
SEQRES 15 A 723 GLY SER TYR GLN ASP VAL VAL ALA PHE LYS VAL VAL ASP
SEQRES 16 A 723 LYS GLN LEU ARG ILE GLN LEU LYS ASN GLY LYS GLU THR
SEQRES 17 A 723 THR LEU ARG THR PRO ALA GLN PHE VAL GLY TYR ARG GLY
SEQRES 18 A 723 ASP ALA ALA ALA PRO THR CYS ILE LEU LEU LYS ASN ASN
SEQRES 19 A 723 GLY LEU HIS ILE GLU LEU GLN ILE ASP ALA ASN GLY ARG
SEQRES 20 A 723 ILE GLY LYS ASP ASP PRO ALA HIS ILE ASN ASP VAL ILE
SEQRES 21 A 723 VAL GLU ALA ALA ILE SER THR ILE LEU ASP CYS GLU ASP
SEQRES 22 A 723 SER VAL ALA ALA VAL ASP ALA GLU ASP LYS ILE LEU LEU
SEQRES 23 A 723 TYR ARG ASN LEU LEU GLY LEU MET GLN GLY THR LEU GLN
SEQRES 24 A 723 GLU LYS MET GLU LYS ASN GLY ARG GLN ILE VAL ARG LYS
SEQRES 25 A 723 LEU ASN ASP ASP ARG HIS TYR THR ALA ALA ASP GLY SER
SEQRES 26 A 723 GLU ILE SER LEU HIS GLY ARG SER LEU LEU PHE ILE ARG
SEQRES 27 A 723 ASN VAL GLY HIS LEU MET THR ILE PRO VAL ILE TRP ASP
SEQRES 28 A 723 SER GLU GLY ASN GLU ILE PRO GLU GLY ILE LEU ASP GLY
SEQRES 29 A 723 VAL MET THR GLY ALA ILE ALA LEU TYR ASP LEU LYS VAL
SEQRES 30 A 723 GLN LYS ASN SER ARG THR GLY SER VAL TYR ILE VAL LYS
SEQRES 31 A 723 PRO LYS MET HIS GLY PRO GLN GLU VAL ALA PHE ALA ASN
SEQRES 32 A 723 LYS LEU PHE THR ARG ILE GLU THR MET LEU GLY MET ALA
SEQRES 33 A 723 PRO ASN THR LEU LYS MET GLY ILE MET ASP GLU GLU ARG
SEQRES 34 A 723 ARG THR SER LEU ASN LEU ARG SER CYS ILE ALA GLN ALA
SEQRES 35 A 723 ARG ASN ARG VAL ALA PHE ILE ASN THR GLY PHE LEU ASP
SEQRES 36 A 723 ARG THR GLY ASP GLU MET HIS SER VAL MET GLU ALA GLY
SEQRES 37 A 723 PRO MET LEU ARG LYS ASN GLN MET LYS SER THR PRO TRP
SEQRES 38 A 723 ILE LYS ALA TYR GLU ARG ASN ASN VAL LEU SER GLY LEU
SEQRES 39 A 723 PHE CYS GLY LEU ARG GLY LYS ALA GLN ILE GLY LYS GLY
SEQRES 40 A 723 MET TRP ALA MET PRO ASP LEU MET ALA ASP MET TYR SER
SEQRES 41 A 723 GLN LYS GLY ASP GLN LEU ARG ALA GLY ALA ASN THR ALA
SEQRES 42 A 723 TRP VAL PRO SER PRO THR ALA ALA THR LEU HIS ALA LEU
SEQRES 43 A 723 HIS TYR HIS GLN THR ASN VAL GLN SER VAL GLN ALA ASN
SEQRES 44 A 723 ILE ALA GLN THR GLU PHE ASN ALA GLU PHE GLU PRO LEU
SEQRES 45 A 723 LEU ASP ASP LEU LEU THR ILE PRO VAL ALA GLU ASN ALA
SEQRES 46 A 723 ASN TRP SER ALA GLN GLU ILE GLN GLN GLU LEU ASP ASN
SEQRES 47 A 723 ASN VAL GLN GLY ILE LEU GLY TYR VAL VAL ARG TRP VAL
SEQRES 48 A 723 GLU GLN GLY ILE GLY CYS SER LYS VAL PRO ASP ILE HIS
SEQRES 49 A 723 ASN VAL ALA LEU MET GLU ASP ARG ALA THR LEU ARG ILE
SEQRES 50 A 723 SER SER GLN HIS ILE ALA ASN TRP LEU ARG HIS GLY ILE
SEQRES 51 A 723 LEU THR LYS GLU GLN VAL GLN ALA SER LEU GLU ASN MET
SEQRES 52 A 723 ALA LYS VAL VAL ASP GLN GLN ASN ALA GLY ASP PRO ALA
SEQRES 53 A 723 TYR ARG PRO MET ALA GLY ASN PHE ALA ASN SER CYS ALA
SEQRES 54 A 723 PHE LYS ALA ALA SER ASP LEU ILE PHE LEU GLY VAL LYS
SEQRES 55 A 723 GLN PRO ASN GLY TYR THR GLU PRO LEU LEU HIS ALA TRP
SEQRES 56 A 723 ARG LEU ARG GLU LYS GLU SER HIS
HELIX 1 1 ALA A 14 GLU A 22 1 9
HELIX 2 2 GLU A 23 GLY A 29 1 7
HELIX 3 3 ASP A 31 ASN A 71 1 41
HELIX 4 4 ASP A 77 GLY A 89 1 13
HELIX 5 5 ASP A 106 GLN A 112 1 7
HELIX 6 6 ALA A 124 ALA A 133 1 10
HELIX 7 7 LEU A 138 SER A 145 1 8
HELIX 8 8 ASP A 159 LEU A 178 1 20
HELIX 9 9 SER A 184 GLN A 186 5 3
HELIX 10 10 THR A 212 ALA A 214 5 3
HELIX 11 11 GLY A 246 ASP A 251 1 6
HELIX 12 12 ASP A 279 GLN A 295 1 17
HELIX 13 13 LEU A 362 GLN A 378 1 17
HELIX 14 14 GLY A 395 LEU A 413 1 19
HELIX 15 15 GLU A 428 ASN A 434 1 7
HELIX 16 16 ASN A 434 GLN A 441 1 8
HELIX 17 17 GLY A 452 SER A 463 1 12
HELIX 18 18 ARG A 472 MET A 476 5 5
HELIX 19 19 PRO A 480 PHE A 495 1 16
HELIX 20 20 LEU A 514 ALA A 528 1 15
HELIX 21 21 SER A 537 THR A 551 1 15
HELIX 22 22 ASN A 552 THR A 563 1 12
HELIX 23 23 GLU A 564 THR A 578 1 15
HELIX 24 24 SER A 588 VAL A 611 1 24
HELIX 25 25 ASP A 631 HIS A 648 1 18
HELIX 26 26 THR A 652 ASP A 674 1 23
HELIX 27 27 ASN A 683 ASN A 686 5 4
HELIX 28 28 SER A 687 GLN A 703 1 17
HELIX 29 29 THR A 708 HIS A 723 1 16
SHEET 1 A 2 THR A 4 GLN A 7 0
SHEET 2 A 2 LEU A 10 ASP A 13 -1 O LEU A 10 N GLN A 7
SHEET 1 B 8 ALA A 447 ILE A 449 0
SHEET 2 B 8 LEU A 420 ILE A 424 1 N MET A 422 O PHE A 448
SHEET 3 B 8 VAL A 386 VAL A 389 1 N VAL A 386 O LYS A 421
SHEET 4 B 8 LEU A 334 ARG A 338 1 N ILE A 337 O VAL A 389
SHEET 5 B 8 SER A 266 LEU A 269 1 N THR A 267 O PHE A 336
SHEET 6 B 8 GLN A 116 VAL A 119 1 N VAL A 119 O ILE A 268
SHEET 7 B 8 THR A 532 VAL A 535 1 O ALA A 533 N GLN A 116
SHEET 8 B 8 GLY A 505 LYS A 506 1 N LYS A 506 O THR A 532
SHEET 1 C 7 GLY A 136 SER A 137 0
SHEET 2 C 7 ILE A 256 VAL A 261 -1 O VAL A 261 N GLY A 136
SHEET 3 C 7 LEU A 236 ILE A 242 -1 N GLU A 239 O ILE A 260
SHEET 4 C 7 ALA A 225 ASN A 233 -1 N ASN A 233 O LEU A 236
SHEET 5 C 7 PHE A 216 ASP A 222 -1 N GLY A 218 O LEU A 230
SHEET 6 C 7 ARG A 317 ALA A 321 -1 O THR A 320 N TYR A 219
SHEET 7 C 7 GLU A 326 LEU A 329 -1 O ILE A 327 N TYR A 319
SHEET 1 D 3 VAL A 188 ALA A 190 0
SHEET 2 D 3 ILE A 200 LEU A 202 -1 O GLN A 201 N ALA A 190
SHEET 3 D 3 GLU A 207 THR A 208 -1 O THR A 208 N ILE A 200
SHEET 1 E 2 VAL A 620 PRO A 621 0
SHEET 2 E 2 ALA A 627 LEU A 628 -1 O LEU A 628 N VAL A 620
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
(ATOM LINES ARE NOT SHOWN.)
END
