HEADER HYDROLASE/HYDROLASE INHIBITOR 18-SEP-14 4RDD
TITLE CO-CRYSTAL STRUCTURE OF SHP2 IN COMPLEX WITH A CEFSULODIN DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SHP2 CATALYTIC DOMAIN;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1D, PTP-1D, PROTEIN-TYROSINE
COMPND 6 PHOSPHATASE 2C, PTP-2C, SH-PTP2, SHP-2, SHP2, SH-PTP3;
COMPND 7 EC: 3.1.3.48;
COMPND 8 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: PTPN11, PTP2C, SHPTP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A+
KEYWDS HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.Y.ZHANG,Z.H.YU,R.HE,R.Y.ZHANG
REVDAT 2 16-DEC-15 4RDD 1 JRNL
REVDAT 1 01-JUL-15 4RDD 0
JRNL AUTH R.HE,Z.H.YU,R.Y.ZHANG,L.WU,A.M.GUNAWAN,B.S.LANE,J.S.SHIM,
JRNL AUTH 2 L.F.ZENG,Y.HE,L.CHEN,C.D.WELLS,J.O.LIU,Z.Y.ZHANG
JRNL TITL EXPLORING THE EXISTING DRUG SPACE FOR NOVEL PTYR MIMETIC AND
JRNL TITL 2 SHP2 INHIBITORS.
JRNL REF ACS MED CHEM LETT V. 6 782 2015
JRNL REFN ISSN 1948-5875
JRNL PMID 26191366
JRNL DOI 10.1021/ACSMEDCHEMLETT.5B00118
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 35592
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1781
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 32.8577 - 3.7630 0.97 2659 141 0.1575 0.1627
REMARK 3 2 3.7630 - 2.9875 0.99 2654 140 0.1544 0.1839
REMARK 3 3 2.9875 - 2.6100 0.99 2669 140 0.1764 0.2073
REMARK 3 4 2.6100 - 2.3715 1.00 2670 140 0.1728 0.2145
REMARK 3 5 2.3715 - 2.2015 1.00 2656 139 0.1649 0.1893
REMARK 3 6 2.2015 - 2.0717 1.00 2677 141 0.1666 0.1942
REMARK 3 7 2.0717 - 1.9680 0.99 2663 141 0.1745 0.1935
REMARK 3 8 1.9680 - 1.8823 0.99 2661 140 0.1840 0.2208
REMARK 3 9 1.8823 - 1.8099 0.99 2635 139 0.2019 0.2720
REMARK 3 10 1.8099 - 1.7474 0.99 2662 138 0.2240 0.2658
REMARK 3 11 1.7474 - 1.6928 0.96 2575 137 0.2331 0.2923
REMARK 3 12 1.6928 - 1.6444 0.94 2507 131 0.2677 0.2757
REMARK 3 13 1.6444 - 1.6011 0.81 2123 114 0.2940 0.3372
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2227
REMARK 3 ANGLE : 1.098 3012
REMARK 3 CHIRALITY : 0.046 321
REMARK 3 PLANARITY : 0.006 394
REMARK 3 DIHEDRAL : 14.185 844
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4RDD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-14.
REMARK 100 THE RCSB ID CODE IS RCSB087205.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.0650
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.66600
REMARK 200 R SYM FOR SHELL (I) : 0.66600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.504
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 33 MM CITRIC ACID, 67 MM
REMARK 280 BIS-TRIS PROPANE, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 37.63700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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. (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 LEU A 529
REMARK 465 GLU A 530
REMARK 465 HIS A 531
REMARK 465 HIS A 532
REMARK 465 HIS A 533
REMARK 465 HIS A 534
REMARK 465 HIS A 535
REMARK 465 HIS A 536
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 GLU A 313 CG CD OE1 OE2
REMARK 470 GLU A 315 CB CG CD OE1 OE2
REMARK 470 THR A 316 CB OG1 CG2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 ASN A 319 CB CG OD1 ND2
REMARK 470 ASN A 320 CG OD1 ND2
REMARK 470 SER A 321 CB OG
REMARK 470 LYS A 322 CG 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 HOH A 1041 O HOH A 1052 2.12
REMARK 500 NH1 ARG A 278 O GLY A 332 2.13
REMARK 500 O HOH A 1019 O HOH A 1032 2.13
REMARK 500 O HOH A 971 O HOH A 977 2.14
REMARK 500 O HOH A 953 O HOH A 1061 2.16
REMARK 500 O HOH A 718 O HOH A 905 2.17
REMARK 500 O HOH A 955 O HOH A 1059 2.18
REMARK 500 O HOH A 754 O HOH A 953 2.18
REMARK 500 O HOH A 928 O HOH A 977 2.18
REMARK 500 OE1 GLU A 348 O HOH A 844 2.18
REMARK 500 O HOH A 720 O HOH A 907 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 LYS A 322 -137.32 -156.31
REMARK 500 CYS A 459 -123.16 -128.86
REMARK 500 ILE A 463 -42.75 -132.91
REMARK 500 VAL A 505 102.88 67.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 936 DISTANCE = 5.94 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 3LU A 600
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3LU A 600
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 Isoform 2 (identifier: Q06124-2). The sequence of this isoform
REMARK 999 differs from the canonical sequence as follows: residues 408-411
REMARK 999 are missing.
DBREF 4RDD A 262 528 UNP Q06124 PTN11_HUMAN 262 532
SEQADV 4RDD A UNP Q06124 GLN 408 SEE REMARK 999
SEQADV 4RDD A UNP Q06124 ALA 409 SEE REMARK 999
SEQADV 4RDD A UNP Q06124 LEU 410 SEE REMARK 999
SEQADV 4RDD A UNP Q06124 LEU 411 SEE REMARK 999
SEQADV 4RDD LEU A 529 UNP Q06124 EXPRESSION TAG
SEQADV 4RDD GLU A 530 UNP Q06124 EXPRESSION TAG
SEQADV 4RDD HIS A 531 UNP Q06124 EXPRESSION TAG
SEQADV 4RDD HIS A 532 UNP Q06124 EXPRESSION TAG
SEQADV 4RDD HIS A 533 UNP Q06124 EXPRESSION TAG
SEQADV 4RDD HIS A 534 UNP Q06124 EXPRESSION TAG
SEQADV 4RDD HIS A 535 UNP Q06124 EXPRESSION TAG
SEQADV 4RDD HIS A 536 UNP Q06124 EXPRESSION TAG
SEQRES 1 A 275 LEU TYR SER ARG LYS GLU GLY GLN ARG GLN GLU ASN LYS
SEQRES 2 A 275 ASN LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE ASP HIS
SEQRES 3 A 275 THR ARG VAL VAL LEU HIS ASP GLY ASP PRO ASN GLU PRO
SEQRES 4 A 275 VAL SER ASP TYR ILE ASN ALA ASN ILE ILE MET PRO GLU
SEQRES 5 A 275 PHE GLU THR LYS CYS ASN ASN SER LYS PRO LYS LYS SER
SEQRES 6 A 275 TYR ILE ALA THR GLN GLY CYS LEU GLN ASN THR VAL ASN
SEQRES 7 A 275 ASP PHE TRP ARG MET VAL PHE GLN GLU ASN SER ARG VAL
SEQRES 8 A 275 ILE VAL MET THR THR LYS GLU VAL GLU ARG GLY LYS SER
SEQRES 9 A 275 LYS CYS VAL LYS TYR TRP PRO ASP GLU TYR ALA LEU LYS
SEQRES 10 A 275 GLU TYR GLY VAL MET ARG VAL ARG ASN VAL LYS GLU SER
SEQRES 11 A 275 ALA ALA HIS ASP TYR THR LEU ARG GLU LEU LYS LEU SER
SEQRES 12 A 275 LYS VAL GLY GLN GLY ASN THR GLU ARG THR VAL TRP GLN
SEQRES 13 A 275 TYR HIS PHE ARG THR TRP PRO ASP HIS GLY VAL PRO SER
SEQRES 14 A 275 ASP PRO GLY GLY VAL LEU ASP PHE LEU GLU GLU VAL HIS
SEQRES 15 A 275 HIS LYS GLN GLU SER ILE MET ASP ALA GLY PRO VAL VAL
SEQRES 16 A 275 VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY THR PHE
SEQRES 17 A 275 ILE VAL ILE ASP ILE LEU ILE ASP ILE ILE ARG GLU LYS
SEQRES 18 A 275 GLY VAL ASP CYS ASP ILE ASP VAL PRO LYS THR ILE GLN
SEQRES 19 A 275 MET VAL ARG SER GLN ARG SER GLY MET VAL GLN THR GLU
SEQRES 20 A 275 ALA GLN TYR ARG PHE ILE TYR MET ALA VAL GLN HIS TYR
SEQRES 21 A 275 ILE GLU THR LEU GLN ARG ARG LEU GLU HIS HIS HIS HIS
SEQRES 22 A 275 HIS HIS
HET 3LU A 600 28
HETNAM 3LU 1-({(2R)-4-CARBOXY-2-[(R)-CARBOXY{[(2R)-2-PHENYL-2-
HETNAM 2 3LU SULFOACETYL]AMINO}METHYL]-3,6-DIHYDRO-2H-1,3-THIAZIN-
HETNAM 3 3LU 5-YL}METHYL)PYRIDINIUM
HETSYN 3LU CEFSULODIN, BOUND FORM
FORMUL 2 3LU C21 H22 N3 O8 S2 1+
FORMUL 3 HOH *368(H2 O)
HELIX 1 1 ARG A 265 ARG A 270 1 6
HELIX 2 2 GLN A 271 ASN A 277 5 7
HELIX 3 3 LEU A 334 ASN A 336 5 3
HELIX 4 4 THR A 337 ASN A 349 1 13
HELIX 5 5 PRO A 432 ILE A 449 1 18
HELIX 6 6 ILE A 463 GLY A 483 1 21
HELIX 7 7 ASP A 489 SER A 499 1 11
HELIX 8 8 THR A 507 ARG A 527 1 21
SHEET 1 A 9 ARG A 289 VAL A 291 0
SHEET 2 A 9 TYR A 304 ILE A 310 -1 O ALA A 307 N VAL A 290
SHEET 3 A 9 TYR A 327 THR A 330 -1 O TYR A 327 N ILE A 310
SHEET 4 A 9 VAL A 455 HIS A 458 1 O VAL A 457 N ILE A 328
SHEET 5 A 9 VAL A 352 MET A 355 1 N VAL A 354 O VAL A 456
SHEET 6 A 9 ARG A 413 PHE A 420 1 O TYR A 418 N ILE A 353
SHEET 7 A 9 TYR A 396 LYS A 405 -1 N THR A 397 O HIS A 419
SHEET 8 A 9 MET A 383 ALA A 392 -1 N ARG A 384 O SER A 404
SHEET 9 A 9 LEU A 377 TYR A 380 -1 N TYR A 380 O MET A 383
SHEET 1 B 2 VAL A 360 GLU A 361 0
SHEET 2 B 2 LYS A 364 SER A 365 -1 O LYS A 364 N GLU A 361
LINK SG CYS A 318 C16 3LU A 600 1555 1455 1.82
CISPEP 1 SER A 321 LYS A 322 0 4.28
SITE 1 AC1 20 TYR A 279 ILE A 282 CYS A 318 CYS A 459
SITE 2 AC1 20 SER A 460 ALA A 461 ILE A 463 GLY A 464
SITE 3 AC1 20 ARG A 465 GLN A 506 THR A 507 GLN A 510
SITE 4 AC1 20 HOH A 711 HOH A 716 HOH A 726 HOH A 770
SITE 5 AC1 20 HOH A 776 HOH A 786 HOH A 801 HOH A1016
CRYST1 39.638 75.274 48.046 90.00 99.11 90.00 P 1 21 1 2
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 0.025228 0.000000 0.004045 0.00000
SCALE2 0.000000 0.013285 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021079 0.00000
(ATOM LINES ARE NOT SHOWN.)
END