HEADER PROTEIN BINDING 17-OCT-14 4WPB
TITLE VASCULAR ENDOTHELIAL GROWTH FACTOR IN COMPLEX WITH ALPHA/BETA-VEGF-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: VEGF-A,VASCULAR PERMEABILITY FACTOR,VPF;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ALPHA/BETA-VEGF-1;
COMPND 8 CHAIN: C, D;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: THIS IS A SYNTHETIC DESIGNED MOLECULE BASED INITIALLY
COMPND 11 ON THE B DOMAIN OF STAPH AUREUS PROTEIN A.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: VEGFA, VEGF;
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: PET-3D;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 14 ORGANISM_TAXID: 1280
KEYWDS ALPHA/BETA-PEPTIDE, FOLDAMER, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR D.F.KREITLER,J.W.CHECCO,S.H.GELLMAN,K.T.FOREST
REVDAT 6 27-DEC-23 4WPB 1 REMARK
REVDAT 5 25-DEC-19 4WPB 1 REMARK
REVDAT 4 11-OCT-17 4WPB 1 REMARK
REVDAT 3 20-SEP-17 4WPB 1 SOURCE JRNL REMARK
REVDAT 2 29-APR-15 4WPB 1 JRNL
REVDAT 1 15-APR-15 4WPB 0
JRNL AUTH J.W.CHECCO,D.F.KREITLER,N.C.THOMAS,D.G.BELAIR,N.J.RETTKO,
JRNL AUTH 2 W.L.MURPHY,K.T.FOREST,S.H.GELLMAN
JRNL TITL TARGETING DIVERSE PROTEIN-PROTEIN INTERACTION INTERFACES
JRNL TITL 2 WITH ALPHA / BETA-PEPTIDES DERIVED FROM THE Z-DOMAIN
JRNL TITL 3 SCAFFOLD.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 112 4552 2015
JRNL REFN ESSN 1091-6490
JRNL PMID 25825775
JRNL DOI 10.1073/PNAS.1420380112
REMARK 2
REMARK 2 RESOLUTION. 3.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9-1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 6017
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.410
REMARK 3 FREE R VALUE TEST SET COUNT : 506
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 45.0800 - 4.9353 0.99 1398 129 0.2337 0.2783
REMARK 3 2 4.9353 - 3.9180 0.99 1371 126 0.2209 0.2742
REMARK 3 3 3.9180 - 3.4230 1.00 1376 125 0.2584 0.3254
REMARK 3 4 3.4230 - 3.1101 0.99 1366 126 0.2679 0.3605
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.030
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.80
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 : 0.025 1995
REMARK 3 ANGLE : 1.475 2682
REMARK 3 CHIRALITY : 0.059 295
REMARK 3 PLANARITY : 0.011 352
REMARK 3 DIHEDRAL : 13.519 666
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8996 -13.8189 27.0333
REMARK 3 T TENSOR
REMARK 3 T11: 1.3853 T22: 0.4915
REMARK 3 T33: 0.2613 T12: 0.0240
REMARK 3 T13: 0.2759 T23: 0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 2.9752 L22: 4.7537
REMARK 3 L33: 0.6035 L12: 1.5976
REMARK 3 L13: 1.1102 L23: -2.451
REMARK 3 S TENSOR
REMARK 3 S11: 0.5021 S12: 0.2845 S13: 0.5005
REMARK 3 S21: -0.0872 S22: 0.2809 S23: -0.0986
REMARK 3 S31: -0.1495 S32: -0.0511 S33: -0.6134
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6364 5.2198 4.6995
REMARK 3 T TENSOR
REMARK 3 T11: 1.6525 T22: 0.5730
REMARK 3 T33: 0.3152 T12: -0.0738
REMARK 3 T13: 0.4013 T23: 0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 2.4063 L22: 1.0858
REMARK 3 L33: 2.4545 L12: 1.5973
REMARK 3 L13: -2.4426 L23: -1.6274
REMARK 3 S TENSOR
REMARK 3 S11: -0.2492 S12: 0.6002 S13: 0.4381
REMARK 3 S21: -0.2301 S22: 0.6145 S23: 0.6100
REMARK 3 S31: -0.9062 S32: -1.1100 S33: -0.3993
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 51 THROUGH 84 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9959 4.0776 15.4635
REMARK 3 T TENSOR
REMARK 3 T11: 1.3304 T22: 0.3466
REMARK 3 T33: 0.5169 T12: 0.0592
REMARK 3 T13: 0.4169 T23: -0.1707
REMARK 3 L TENSOR
REMARK 3 L11: 0.4072 L22: 2.9769
REMARK 3 L33: 0.0691 L12: -0.4102
REMARK 3 L13: 0.1077 L23: 0.1629
REMARK 3 S TENSOR
REMARK 3 S11: -0.1951 S12: -0.0796 S13: -0.1107
REMARK 3 S21: 0.4721 S22: 0.1490 S23: 0.4674
REMARK 3 S31: 0.2034 S32: -0.1086 S33: 0.0152
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 85 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5856 8.4599 10.9411
REMARK 3 T TENSOR
REMARK 3 T11: 0.9397 T22: 0.2655
REMARK 3 T33: 0.4488 T12: 0.0364
REMARK 3 T13: 0.2708 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 1.6430 L22: 4.2027
REMARK 3 L33: 3.2673 L12: 0.7612
REMARK 3 L13: -0.1611 L23: -2.1403
REMARK 3 S TENSOR
REMARK 3 S11: -0.2613 S12: 0.0209 S13: 0.0417
REMARK 3 S21: -0.0577 S22: -0.0287 S23: 0.1696
REMARK 3 S31: -0.0453 S32: -0.2702 S33: 0.2362
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 14 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6062 1.8500 1.8052
REMARK 3 T TENSOR
REMARK 3 T11: 1.1420 T22: 0.3034
REMARK 3 T33: 0.6122 T12: 0.0612
REMARK 3 T13: 0.3582 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 0.7868 L22: 4.1271
REMARK 3 L33: 1.9651 L12: 0.5312
REMARK 3 L13: -0.3294 L23: -1.7078
REMARK 3 S TENSOR
REMARK 3 S11: -0.1174 S12: 0.2244 S13: 0.1008
REMARK 3 S21: -0.7317 S22: 0.0933 S23: -0.5171
REMARK 3 S31: 0.3877 S32: -0.0096 S33: 0.0190
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 27 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1128 -12.4403 14.9487
REMARK 3 T TENSOR
REMARK 3 T11: 1.1300 T22: 0.5777
REMARK 3 T33: 0.4336 T12: 0.1307
REMARK 3 T13: 0.5347 T23: 0.1204
REMARK 3 L TENSOR
REMARK 3 L11: 0.8729 L22: 1.9599
REMARK 3 L33: 2.9359 L12: 0.8132
REMARK 3 L13: -0.4551 L23: -1.1157
REMARK 3 S TENSOR
REMARK 3 S11: -0.2184 S12: 0.2869 S13: -0.0835
REMARK 3 S21: -0.0814 S22: 0.0471 S23: 0.0931
REMARK 3 S31: 0.0611 S32: -0.2688 S33: 0.1397
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 39 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3448 -21.6885 21.8339
REMARK 3 T TENSOR
REMARK 3 T11: 1.1217 T22: 1.1363
REMARK 3 T33: 0.5403 T12: -0.3113
REMARK 3 T13: 0.2047 T23: 0.1242
REMARK 3 L TENSOR
REMARK 3 L11: 1.5541 L22: 9.5531
REMARK 3 L33: 3.7093 L12: 0.8640
REMARK 3 L13: 0.8769 L23: -4.9146
REMARK 3 S TENSOR
REMARK 3 S11: 0.0130 S12: -0.3717 S13: -0.1748
REMARK 3 S21: -0.3046 S22: 1.0378 S23: 1.0688
REMARK 3 S31: 0.5279 S32: -0.7583 S33: -1.0493
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 84 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4420 -15.1596 13.5631
REMARK 3 T TENSOR
REMARK 3 T11: 1.6370 T22: 0.3514
REMARK 3 T33: 0.3069 T12: 0.1538
REMARK 3 T13: 0.4293 T23: -0.1849
REMARK 3 L TENSOR
REMARK 3 L11: 0.2687 L22: 2.1311
REMARK 3 L33: 0.0520 L12: -0.2841
REMARK 3 L13: 0.0572 L23: 0.2376
REMARK 3 S TENSOR
REMARK 3 S11: -0.1087 S12: 0.1252 S13: 0.0686
REMARK 3 S21: -0.5069 S22: 0.0997 S23: 0.5455
REMARK 3 S31: -0.2241 S32: -0.4654 S33: 0.0541
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 85 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9538 -19.6339 16.0686
REMARK 3 T TENSOR
REMARK 3 T11: 1.0563 T22: 0.3421
REMARK 3 T33: 0.3413 T12: 0.0215
REMARK 3 T13: 0.1146 T23: -0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 1.4193 L22: 3.4071
REMARK 3 L33: 5.4560 L12: 0.0782
REMARK 3 L13: 0.3519 L23: -2.6420
REMARK 3 S TENSOR
REMARK 3 S11: -0.1302 S12: 0.1582 S13: 0.1450
REMARK 3 S21: -0.6117 S22: 0.1925 S23: -0.0562
REMARK 3 S31: -0.0414 S32: -0.6685 S33: -0.1332
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 8 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2180 -19.5089 37.6187
REMARK 3 T TENSOR
REMARK 3 T11: 0.9864 T22: 0.5703
REMARK 3 T33: 0.3434 T12: -0.0784
REMARK 3 T13: 0.0367 T23: 0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 4.0078 L22: 6.1665
REMARK 3 L33: 2.1804 L12: 2.6046
REMARK 3 L13: -2.5144 L23: -3.2719
REMARK 3 S TENSOR
REMARK 3 S11: 0.5410 S12: -0.6303 S13: 0.0469
REMARK 3 S21: 1.4596 S22: -0.2868 S23: -0.1548
REMARK 3 S31: -0.8551 S32: 0.1766 S33: -0.2776
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 21 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3511 -14.3490 41.4365
REMARK 3 T TENSOR
REMARK 3 T11: 1.8271 T22: 0.5337
REMARK 3 T33: 0.7112 T12: 0.1878
REMARK 3 T13: -0.0655 T23: -0.0836
REMARK 3 L TENSOR
REMARK 3 L11: 0.0212 L22: 7.1292
REMARK 3 L33: 2.7370 L12: 0.2778
REMARK 3 L13: -0.2432 L23: -3.0516
REMARK 3 S TENSOR
REMARK 3 S11: 0.2524 S12: -0.2560 S13: 0.4821
REMARK 3 S21: 2.1764 S22: -0.0220 S23: 0.6385
REMARK 3 S31: -1.2253 S32: -0.3101 S33: -0.2626
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 26 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8108 -9.1351 38.8466
REMARK 3 T TENSOR
REMARK 3 T11: 1.8491 T22: 0.6525
REMARK 3 T33: 0.2304 T12: -0.0216
REMARK 3 T13: 0.1385 T23: 0.3696
REMARK 3 L TENSOR
REMARK 3 L11: 0.0882 L22: 2.7196
REMARK 3 L33: 1.1621 L12: -0.0498
REMARK 3 L13: 0.3158 L23: 0.0617
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: -0.4112 S13: -0.0187
REMARK 3 S21: 0.7855 S22: -0.0339 S23: 0.1717
REMARK 3 S31: -0.6984 S32: -0.1125 S33: -0.0114
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 32 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9323 -8.6220 37.1402
REMARK 3 T TENSOR
REMARK 3 T11: 1.9154 T22: 0.6097
REMARK 3 T33: 1.2096 T12: -0.2145
REMARK 3 T13: -0.3314 T23: 0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 1.8126 L22: 2.3224
REMARK 3 L33: 0.5274 L12: -0.1827
REMARK 3 L13: -0.8436 L23: -0.4735
REMARK 3 S TENSOR
REMARK 3 S11: 0.5908 S12: -0.5305 S13: 0.4456
REMARK 3 S21: 1.9668 S22: -0.3443 S23: -0.4703
REMARK 3 S31: -0.8080 S32: 0.4272 S33: -0.2046
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 39 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1156 -11.4867 35.4041
REMARK 3 T TENSOR
REMARK 3 T11: 1.7876 T22: 1.0496
REMARK 3 T33: 0.6380 T12: -0.1607
REMARK 3 T13: -0.3020 T23: -0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 2.0001 L22: 2.0000
REMARK 3 L33: 2.0000 L12: 2.0000
REMARK 3 L13: 2.0000 L23: 2.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.5937 S12: -1.7361 S13: -1.4224
REMARK 3 S21: -1.5417 S22: 1.7335 S23: 5.2440
REMARK 3 S31: -0.4316 S32: 0.6305 S33: -2.3242
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 8 THROUGH 14 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1557 8.1098 -3.4724
REMARK 3 T TENSOR
REMARK 3 T11: 0.9479 T22: 0.7771
REMARK 3 T33: 0.6687 T12: -0.0415
REMARK 3 T13: 0.6199 T23: 0.3403
REMARK 3 L TENSOR
REMARK 3 L11: 0.8932 L22: 0.0499
REMARK 3 L33: 0.7221 L12: -0.2101
REMARK 3 L13: 0.8040 L23: -0.1914
REMARK 3 S TENSOR
REMARK 3 S11: -0.0107 S12: -0.0900 S13: -0.1309
REMARK 3 S21: -0.2206 S22: -0.1504 S23: -0.2964
REMARK 3 S31: 0.1699 S32: 0.3543 S33: 0.1406
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 15 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2293 3.0769 -12.2176
REMARK 3 T TENSOR
REMARK 3 T11: 1.5896 T22: 0.4361
REMARK 3 T33: 0.4880 T12: -0.0308
REMARK 3 T13: 0.6770 T23: -0.1450
REMARK 3 L TENSOR
REMARK 3 L11: 0.4584 L22: 0.5730
REMARK 3 L33: 0.2347 L12: -0.0214
REMARK 3 L13: -0.2655 L23: 0.2213
REMARK 3 S TENSOR
REMARK 3 S11: -0.2946 S12: 0.4288 S13: -0.2506
REMARK 3 S21: -0.3719 S22: -0.2126 S23: 0.0605
REMARK 3 S31: 0.5078 S32: -0.4063 S33: 0.3201
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 32 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9488 -2.6729 -4.8045
REMARK 3 T TENSOR
REMARK 3 T11: 1.6522 T22: 0.6967
REMARK 3 T33: 1.3225 T12: 0.1970
REMARK 3 T13: 0.7407 T23: 0.2717
REMARK 3 L TENSOR
REMARK 3 L11: 0.8145 L22: 4.6757
REMARK 3 L33: 1.9926 L12: 1.1791
REMARK 3 L13: -0.0653 L23: -2.1650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0740 S12: 0.2318 S13: -0.3957
REMARK 3 S21: -1.7201 S22: -0.0700 S23: -1.4183
REMARK 3 S31: 0.9645 S32: 0.2870 S33: 0.1948
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2226 1.0298 -1.5952
REMARK 3 T TENSOR
REMARK 3 T11: 0.8943 T22: 0.2491
REMARK 3 T33: 1.0158 T12: 0.1128
REMARK 3 T13: 0.2505 T23: 0.2041
REMARK 3 L TENSOR
REMARK 3 L11: 2.0003 L22: 2.0001
REMARK 3 L33: 2.0001 L12: 2.0000
REMARK 3 L13: 2.0000 L23: 2.0000
REMARK 3 S TENSOR
REMARK 3 S11: 1.8864 S12: 1.6291 S13: 7.7844
REMARK 3 S21: -7.8885 S22: -9.4701 S23: -3.4690
REMARK 3 S31: -5.2194 S32: -2.8548 S33: 7.5881
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 953
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 953
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 953
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WPB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000204209.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 11, 2013
REMARK 200 DATA SCALING SOFTWARE : XSCALE JANUARY 10, 2014
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6096
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 45.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.24300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.450
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: CRYSTALS WERE PARALLELEPIPED PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM FORMATE DIHYDRATE, 15%
REMARK 280 (W/V) PEG3350, 30% (V/V) GLYCEROL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 39.20000
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLY A 8
REMARK 465 GLN A 9
REMARK 465 ASN A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 LYS A 108
REMARK 465 ASP A 109
REMARK 465 GLY B 8
REMARK 465 GLN B 9
REMARK 465 ASN B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 GLU B 13
REMARK 465 LYS B 107
REMARK 465 LYS B 108
REMARK 465 ASP B 109
REMARK 465 VAL C 1
REMARK 465 B3D C 2
REMARK 465 ASN C 3
REMARK 465 LYS C 4
REMARK 465 3FB C 5
REMARK 465 ASN C 6
REMARK 465 LYS C 7
REMARK 465 VAL D 1
REMARK 465 B3D D 2
REMARK 465 ASN D 3
REMARK 465 LYS D 4
REMARK 465 3FB D 5
REMARK 465 ASN D 6
REMARK 465 LYS D 7
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 13 CG CD OE1 OE2
REMARK 470 GLN A 22 CG CD OE1 NE2
REMARK 470 GLU A 30 CG CD OE1 OE2
REMARK 470 GLU A 38 CG CD OE1 OE2
REMARK 470 ASP A 41 CG OD1 OD2
REMARK 470 ILE A 43 CG1 CG2 CD1
REMARK 470 GLU A 44 CG CD OE1 OE2
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 ARG A 82 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 83 CG1 CG2 CD1
REMARK 470 HIS A 86 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 87 CG CD OE1 NE2
REMARK 470 LEU A 97 CG CD1 CD2
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 LYS B 16 CG CD CE NZ
REMARK 470 ARG B 23 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 30 CG CD OE1 OE2
REMARK 470 GLN B 37 CG CD OE1 NE2
REMARK 470 ASP B 41 CG OD1 OD2
REMARK 470 GLU B 44 CG CD OE1 OE2
REMARK 470 GLU B 64 CG CD OE1 OE2
REMARK 470 GLU B 73 CG CD OE1 OE2
REMARK 470 HIS B 86 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 87 CG CD OE1 NE2
REMARK 470 LYS B 101 CG CD CE NZ
REMARK 470 GLU C 16 CG CD OE1 OE2
REMARK 470 LYS C 31 CG CD CE NZ
REMARK 470 ILE C 36 CG1 CG2 CD1
REMARK 470 ASP C 38 CG OD1 OD2
REMARK 470 ARG D 13 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 31 CG CD CE NZ
REMARK 470 ILE D 35 CG1 CG2 CD1
REMARK 470 ASP D 38 CG OD1 OD2
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 OH TYR B 39 O SER B 95 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 XPC C 34 C ILE C 35 N 0.182
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 XPC C 34 C - N - CA ANGL. DEV. = 30.9 DEGREES
REMARK 500 ILE C 35 C - N - CA ANGL. DEV. = -22.7 DEGREES
REMARK 500 XCP C 37 C - N - CA ANGL. DEV. = 19.0 DEGREES
REMARK 500 XCP D 9 C - N - CA ANGL. DEV. = 22.7 DEGREES
REMARK 500 XPC D 34 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 ILE D 35 C - N - CA ANGL. DEV. = -27.6 DEGREES
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 ASP A 41 -169.56 -75.65
REMARK 500 GLU A 42 -103.39 57.78
REMARK 500 THR A 71 -61.93 -97.05
REMARK 500 SER A 74 -168.29 -127.57
REMARK 500 HIS A 86 -12.34 67.61
REMARK 500 PRO A 106 179.84 -55.78
REMARK 500 THR B 71 -60.73 -96.92
REMARK 500 HIS B 86 -11.72 65.45
REMARK 500 ASN C 11 -72.50 -58.53
REMARK 500 ASP C 38 -75.18 -120.84
REMARK 500 ASP D 38 -71.38 -118.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU C 8 XCP C 9 143.59
REMARK 500 ASN C 11 XPC C 12 139.98
REMARK 500 ILE C 36 XCP C 37 137.85
REMARK 500 GLU D 8 XCP D 9 139.80
REMARK 500 ASN D 11 XPC D 12 138.16
REMARK 500 TRP D 33 XPC D 34 137.26
REMARK 500 ILE D 36 XCP D 37 139.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE C 32 13.07
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4WPB A 8 109 UNP P15692 VEGFA_HUMAN 214 315
DBREF 4WPB B 8 109 UNP P15692 VEGFA_HUMAN 214 315
DBREF 4WPB C 1 40 PDB 4WPB 4WPB 1 40
DBREF 4WPB D 1 40 PDB 4WPB 4WPB 1 40
SEQRES 1 A 102 GLY GLN ASN HIS HIS GLU VAL VAL LYS PHE MET ASP VAL
SEQRES 2 A 102 TYR GLN ARG SER TYR CYS HIS PRO ILE GLU THR LEU VAL
SEQRES 3 A 102 ASP ILE PHE GLN GLU TYR PRO ASP GLU ILE GLU TYR ILE
SEQRES 4 A 102 PHE LYS PRO SER CYS VAL PRO LEU MET ARG CYS GLY GLY
SEQRES 5 A 102 CYS CYS ASN ASP GLU GLY LEU GLU CYS VAL PRO THR GLU
SEQRES 6 A 102 GLU SER ASN ILE THR MET GLN ILE MET ARG ILE LYS PRO
SEQRES 7 A 102 HIS GLN GLY GLN HIS ILE GLY GLU MET SER PHE LEU GLN
SEQRES 8 A 102 HIS ASN LYS CYS GLU CYS ARG PRO LYS LYS ASP
SEQRES 1 B 102 GLY GLN ASN HIS HIS GLU VAL VAL LYS PHE MET ASP VAL
SEQRES 2 B 102 TYR GLN ARG SER TYR CYS HIS PRO ILE GLU THR LEU VAL
SEQRES 3 B 102 ASP ILE PHE GLN GLU TYR PRO ASP GLU ILE GLU TYR ILE
SEQRES 4 B 102 PHE LYS PRO SER CYS VAL PRO LEU MET ARG CYS GLY GLY
SEQRES 5 B 102 CYS CYS ASN ASP GLU GLY LEU GLU CYS VAL PRO THR GLU
SEQRES 6 B 102 GLU SER ASN ILE THR MET GLN ILE MET ARG ILE LYS PRO
SEQRES 7 B 102 HIS GLN GLY GLN HIS ILE GLY GLU MET SER PHE LEU GLN
SEQRES 8 B 102 HIS ASN LYS CYS GLU CYS ARG PRO LYS LYS ASP
SEQRES 1 C 40 VAL B3D ASN LYS 3FB ASN LYS GLU XCP CYS ASN XPC ARG
SEQRES 2 C 40 ALA ILE GLU AIB ALA LEU ASP PRO ASN LEU ASN ASP GLN
SEQRES 3 C 40 GLN PHE HIS AIB LYS ILE TRP XPC ILE ILE XCP ASP CYS
SEQRES 4 C 40 NH2
SEQRES 1 D 40 VAL B3D ASN LYS 3FB ASN LYS GLU XCP CYS ASN XPC ARG
SEQRES 2 D 40 ALA ILE GLU AIB ALA LEU ASP PRO ASN LEU ASN ASP GLN
SEQRES 3 D 40 GLN PHE HIS AIB LYS ILE TRP XPC ILE ILE XCP ASP CYS
SEQRES 4 D 40 NH2
HET XCP C 9 8
HET XPC C 12 8
HET AIB C 17 6
HET AIB C 30 6
HET XPC C 34 8
HET XCP C 37 8
HET NH2 C 40 1
HET XCP D 9 8
HET XPC D 12 8
HET AIB D 17 6
HET AIB D 30 6
HET XPC D 34 8
HET XCP D 37 8
HET NH2 D 40 1
HETNAM XCP (1S,2S)-2-AMINOCYCLOPENTANECARBOXYLIC ACID
HETNAM XPC (3S,4R)-4-AMINOPYRROLIDINE-3-CARBOXYLIC ACID
HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID
HETNAM NH2 AMINO GROUP
HETSYN XPC (3R,4S)-3-AMINOPYRROLIDINE-4-CARBOXYLIC ACID
FORMUL 3 XCP 4(C6 H11 N O2)
FORMUL 3 XPC 4(C5 H10 N2 O2)
FORMUL 3 AIB 4(C4 H9 N O2)
FORMUL 3 NH2 2(H2 N)
HELIX 1 AA1 LYS A 16 TYR A 25 1 10
HELIX 2 AA2 ILE A 35 TYR A 39 1 5
HELIX 3 AA3 LYS B 16 TYR B 25 1 10
HELIX 4 AA4 ILE B 35 TYR B 39 1 5
HELIX 5 AA5 XCP C 9 ASP C 20 1 12
HELIX 6 AA6 ASN C 24 ILE C 35 1 12
HELIX 7 AA7 XCP D 9 ASP D 20 1 12
HELIX 8 AA8 ASN D 24 CYS D 39 1 16
SHEET 1 AA1 2 HIS A 27 ASP A 34 0
SHEET 2 AA1 2 CYS A 51 GLY A 58 -1 O ARG A 56 N ILE A 29
SHEET 1 AA2 3 PHE A 47 LYS A 48 0
SHEET 2 AA2 3 GLU A 73 LYS A 84 -1 O MET A 81 N LYS A 48
SHEET 3 AA2 3 GLY A 88 HIS A 99 -1 O PHE A 96 N ILE A 76
SHEET 1 AA3 2 GLU A 67 PRO A 70 0
SHEET 2 AA3 2 CYS A 102 ARG A 105 -1 O ARG A 105 N GLU A 67
SHEET 1 AA4 2 HIS B 27 ASP B 34 0
SHEET 2 AA4 2 CYS B 51 GLY B 58 -1 O VAL B 52 N VAL B 33
SHEET 1 AA5 3 PHE B 47 LYS B 48 0
SHEET 2 AA5 3 GLU B 67 LYS B 84 -1 O MET B 81 N LYS B 48
SHEET 3 AA5 3 GLY B 88 ARG B 105 -1 O ARG B 105 N GLU B 67
SSBOND 1 CYS A 26 CYS A 68 1555 1555 2.04
SSBOND 2 CYS A 51 CYS B 60 1555 1555 2.08
SSBOND 3 CYS A 57 CYS A 102 1555 1555 2.05
SSBOND 4 CYS A 60 CYS B 51 1555 1555 2.05
SSBOND 5 CYS A 61 CYS A 104 1555 1555 2.05
SSBOND 6 CYS B 26 CYS B 68 1555 1555 2.05
SSBOND 7 CYS B 57 CYS B 102 1555 1555 2.05
SSBOND 8 CYS B 61 CYS B 104 1555 1555 2.04
SSBOND 9 CYS C 10 CYS C 39 1555 1555 2.04
SSBOND 10 CYS D 10 CYS D 39 1555 1555 2.03
LINK C GLU C 8 N XCP C 9 1555 1555 1.44
LINK C XCP C 9 N CYS C 10 1555 1555 1.34
LINK C ASN C 11 N XPC C 12 1555 1555 1.34
LINK C XPC C 12 N ARG C 13 1555 1555 1.31
LINK C GLU C 16 N AIB C 17 1555 1555 1.33
LINK C AIB C 17 N ALA C 18 1555 1555 1.33
LINK C HIS C 29 N AIB C 30 1555 1555 1.33
LINK C AIB C 30 N LYS C 31 1555 1555 1.34
LINK C TRP C 33 N XPC C 34 1555 1555 1.30
LINK C XPC C 34 N ILE C 35 1555 1555 1.52
LINK C ILE C 36 N XCP C 37 1555 1555 1.40
LINK C XCP C 37 N ASP C 38 1555 1555 1.40
LINK C CYS C 39 N NH2 C 40 1555 1555 1.34
LINK C GLU D 8 N XCP D 9 1555 1555 1.39
LINK C XCP D 9 N CYS D 10 1555 1555 1.28
LINK C ASN D 11 N XPC D 12 1555 1555 1.36
LINK C XPC D 12 N ARG D 13 1555 1555 1.37
LINK C GLU D 16 N AIB D 17 1555 1555 1.32
LINK C AIB D 17 N ALA D 18 1555 1555 1.33
LINK C HIS D 29 N AIB D 30 1555 1555 1.33
LINK C AIB D 30 N LYS D 31 1555 1555 1.34
LINK C TRP D 33 N XPC D 34 1555 1555 1.35
LINK C XPC D 34 N ILE D 35 1555 1555 1.43
LINK C ILE D 36 N XCP D 37 1555 1555 1.31
LINK C XCP D 37 N ASP D 38 1555 1555 1.35
LINK C CYS D 39 N NH2 D 40 1555 1555 1.35
CISPEP 1 LYS A 48 PRO A 49 0 2.88
CISPEP 2 LYS B 48 PRO B 49 0 0.47
CRYST1 39.100 78.400 56.500 90.00 102.80 90.00 P 1 21 1 4
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 0.025575 0.000000 0.005811 0.00000
SCALE2 0.000000 0.012755 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018150 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
